spacer
spacer

SAS results for UniProt accession no. Q13526

Sequence annotated by structure

Key:
Sec. struc: By homology
  Helix Strand  
Residue contacts:   to ligand
Catalytic residues:   (from CSA)
Active sites:   (from PDB SITE records)
PROSITE patterns: Low   High conservation

Secondary structure shown in red comes from a homologous protein structure which is at least 30% sequence identical to the target protein and has an alignment overlap of at least 80 residues or at least three-quarters of the length of the target sequence (whichever overlap is the larger).

Click on annotated residues to get source(s) of each annotation.

 

FASTA alignment for UniProt accession no. Q13526 - coloured by no. of contacts to ligand

Below are the FASTA results from a search of the sequence of UniProt accession no. Q13526 against all protein sequences in the PDB. Identical sequences are grouped together and represented by a single 'consensus' sequence (asterisked) onto which all relevant annotations are mapped. The number of sequences represented by each consensus sequence is shown by the '×n' on the right of the alignment. Use the box below to modify the annotations shown on the alignment. At the bottom of the page are given the FASTA stats for all the sequences. There you can exclude any sequences from the alignment.

Struct

FASTA

The search returned 116 unique sequences (including 22 consensus sequences) giving 159 sequence matches in all. The 124 sequences excluded from the alignment are listed at the end.

Modify alignment: Annotate by:
  Number:  
  Show secondary structure: Yes No  


                1         2         3         4         5         6     
       12345678901234567890123456789012345678901234567890123456789012345    Protein name
       ---------+---------+---------+---------+---------+---------+-----    ------------
Q13526 ----madeeklppgwekrmsrssgrvyyfnhitnasqwerpsgnsssggkngqgeparvrcshll    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1  ...
1nmv:A ----madeeklppgwekrmsrssgrvyyfnhitnasqwerpsgnsssggkngqgeparvrcshll    Solution structure of human pin1
1pin:A ---------KLPPGWEKRMSRSSGRVYYFNHITNASQWERPSG-----GKNGQGEPARVRCSHLL    Pin1 peptidyl-prolyl cis-trans isomerase from homo sapiens
2zr4:A ---------KLPPGWEKRMSRSSGRVYYFNHITNAAQWERPSG-----GKNGQGEPARVRCSHLL    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr5:A ---------KLPPGWEKRMSRSSGRVYYFNHITNASQWERPSG-----GKNGQGEPARVRCSHLL    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqt:A ---------KLPPGWEKRMSRSSGRVYYFNHITNASQWERPSG-----GKNGQGEPARVRCSHLL    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr6:A ---------KLPPGWEKAMSRSSGRVYYFNHITNASQWERPSG-----GKNGQGEPARVRCSHLL    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqv:A ---------KLPPGWEKRMSRSSGRVYYANHITNASQWERPSG-----GKNGQGEPARVRCSHLL    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqs:A ---------KLPPGWEKRMSRSSGRVYYFNHITNASQWERPSG-----GKNGQGEPARVRCSHLL    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqu:A ---------KLPPGWEKRMSRSSGRVYYFNHITNASQAERPSG-----GKNGQGEPARVRCSHLL    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2f21:A ----MADEEKLPPGWEKRMS-ADGRVYYFNHITNASQWERPSG---------QGEPARVRCSHLL    Human pin1 fip mutant
1nmw:A -----------------------------------------------------GEPARVRCSHLL    Solution structure of the ppiase domain of human pin1
2xpa:A*----------LPPGWEKAMSRSSGRVYYFNHITNASQWERPSG-----------EPARVRCSHLL×2  Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3ntp:A ---------KLPPGWEKAMSRSSGRVYYFNHITNASQWERPSG-----------EPARVRCSHLL    Human pin1 complexed with reduced amide inhibitor
1zcn:A ----------LPPGWEKRM--SNGRVYYFNHITNASQWERPS------------EPARVRCSHLL    Human pin1 ng mutant
2xp4:A*----------LPPGWEKAMSRSSGRVYYFNHITNASQWERP-------------EPARVRCSHLL×3  Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
2iti:A*----------LPPGWEKAMSRSSGRVYYFNHITNASQWERPS------------EPARVRCSHLL×11 Human pin1 bound to l-peptide
3kce:A ---------KLPPGWEKAMSRSSGRVYYFNHITNASQWERPS------------EPARVRCSHLL    Structure-guided design of alpha-amino acid-derived pin1  ...
3odk:A ----------LPPGWEKAMSRSSGRVYYFNHITNASQWERPS------------EPARVRCSHLL    Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3oob:A*---------KLPPGWEKAMSRSSGRVYYFNHITNASQWERPS------------EPARVRCSHLL×3  Structural and functional insights of directly targeting  ...
1f8a:B GSHGMADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPS------------EPARVRCSHLL    Structural basis for the phosphoserine-proline recognition  ...

                                         1         1         1         1
           7         8         9         0         1         2         3
       67890123456789012345678901234567890123456789012345678901234567890    Protein name
       ----+---------+---------+---------+---------+---------+---------+    ------------
Q13526 vkhsqsrrpsswrqekitrtkeealelingyiqkiksgeedfeslasqfsdcssakargdlgafs    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1  ...
1nmv:A vkhsqsrrpsswrqekitrtkeealelingyiqkiksgeedfeslasqfsdcssakargdlgafs    Solution structure of human pin1
1pin:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Pin1 peptidyl-prolyl cis-trans isomerase from homo sapiens
2zr4:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr5:A VAHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqt:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr6:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqv:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqs:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDASSAKARGDLGAFS    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqu:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2f21:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Human pin1 fip mutant
1nmw:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Solution structure of the ppiase domain of human pin1
2xpa:A*VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS×2  Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3ntp:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Human pin1 complexed with reduced amide inhibitor
1zcn:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Human pin1 ng mutant
2xp4:A*VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS×3  Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
2iti:A*VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS×11 Human pin1 bound to l-peptide
3kce:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Structure-guided design of alpha-amino acid-derived pin1  ...
3odk:A VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3oob:A*VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS×3  Structural and functional insights of directly targeting  ...
1f8a:B VKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFS    Structural basis for the phosphoserine-proline recognition  ...

                1         1         1       
                4         5         6       
       1234567890123456789012345678901234567                                Protein name
       ---------+---------+---------+-------                                ------------
Q13526 rgqmqkpfedasfalrtgemsgpvftdsgihiilrte                                Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1  ...
1nmv:A rgqmqkpfedasfalrtgemsgpvftdsgihiilrte                                Solution structure of human pin1
1pin:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Pin1 peptidyl-prolyl cis-trans isomerase from homo sapiens
2zr4:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr5:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqt:A RGQAQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zr6:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqv:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqs:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2zqu:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Crystal structure of a mutant pin1 peptidyl-prolyl  ...
2f21:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Human pin1 fip mutant
1nmw:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Solution structure of the ppiase domain of human pin1
2xpa:A*RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                            ×2  Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3ntp:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Human pin1 complexed with reduced amide inhibitor
1zcn:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Human pin1 ng mutant
2xp4:A*RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                            ×3  Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
2iti:A*RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                            ×11 Human pin1 bound to l-peptide
3kce:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Structure-guided design of alpha-amino acid-derived pin1  ...
3odk:A RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Discovery of cell-active phenyl-imidazole pin1 inhibitors  ...
3oob:A*RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                            ×3  Structural and functional insights of directly targeting  ...
1f8a:B RGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE                                Structural basis for the phosphoserine-proline recognition  ...

Residue colours: black = 0, purple = 1, blue = 2, green = 3, orange = 4, red = 5 or more contacts.

Sequence listing

The listing below shows the FASTA statistics for the PDB entries that matched UniProt accession no. Q13526. Ditto marks indicate identical sequences represented by a single representative sequence in the alignment above. The representative is asterisked and the names of all its duplicate sequences are indented to the right.

Structures whose names are given in purple are those that are annotated above. The parameters defining which sequences can transfer their annotations are shown at the bottom of the page where they can be altered and the alignment regenerated.

Use the checkboxes to the left of the PDB codes to exclude any sequences from the alignment (or to add back any sequences in the Excluded list). Then click the SELECT button at the bottom of the page to redisplay the alignment.

Aligned sequences

  Smith-
Waterman
score
%-tage
identity
a.a.
overlap
Seq
len
z-score E-
value
  PDB
code
Protein name
1. - - - 163 - - Q13526 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 OS=Homo sapiens GN=PIN1 PE=1 SV=1
2. 1096 100.0% 163 163 1370.0 2.5e-69 1nmv:A Solution structure of human pin1
3. 1014 96.8% 158 153 1268.5 1.1e-63 1pin:A Pin1 peptidyl-prolyl cis-trans isomerase from homo sapiens
4. 1010 96.2% 158 153 1263.5 2.1e-63 2zr4:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
5. 1007 96.2% 158 153 1259.8 3.4e-63 2zr5:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
6. 1006 96.2% 158 153 1258.6 4e-63 2zqt:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
7. 1005 96.2% 158 153 1257.3 4.7e-63 2zr6:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
8. 1003 96.2% 158 153 1254.8 6.4e-63 2zqv:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
9. 1000 96.2% 158 153 1251.1 1e-62 2zqs:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
10. 996 96.2% 158 153 1246.1 2e-62 2zqu:A Crystal structure of a mutant pin1 peptidyl-prolyl cis-trans isomerase
11. 981 92.6% 163 153 960.3 1.6e-46 2f21:A Human pin1 fip mutant
12. 750 100.0% 114 114 942.2 1.7e-45 1nmw:A Solution structure of the ppiase domain of human pin1
13. 943 92.4% 157 146 940.7 2e-45 2xpa:A * Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
14. " " " " " "  = 2xpb:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
15. 949 92.4% 158 147 940.7 2e-45 3ntp:A Human pin1 complexed with reduced amide inhibitor
16. 912 90.4% 157 143 930.9 7.1e-45 1zcn:A Human pin1 ng mutant
17. 926 91.1% 157 144 930.9 7.1e-45 2xp4:A * Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
18. " " " " " "  = 2xp9:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
19. " " " " " "  = 3tc5:A *
Selective targeting of disease-relevant protein binding doma phosphorylated natural product derivatives
20. 933 91.7% 157 145 930.8 7.2e-45 2iti:A * Human pin1 bound to l-peptide
21. " " " " " "  = 2itk:A *
Human pin1 bound to d-peptide
22. " " " " " "  = 2q5a:A *
Human pin1 bound to l-peptide
23. " " " " " "  = 2xp3:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
24. " " " " " "  = 2xp5:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
25. " " " " " "  = 2xp7:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
26. " " " " " "  = 2xp8:A *
Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
27. " " " " " "  = 3kab:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
28. " " " " " "  = 3kag:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
29. " " " " " "  = 3kah:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
30. " " " " " "  = 3kai:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
31. 939 91.8% 158 146 930.8 7.2e-45 3kce:A Structure-guided design of alpha-amino acid-derived pin1 inhibitors
32. 933 91.7% 157 145 930.8 7.2e-45 3odk:A Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
33. 939 91.8% 158 146 930.8 7.2e-45 3oob:A * Structural and functional insights of directly targeting pin epigallocatechin-3-gallate
34. " " " " " "  = 3tcz:A *
Human pin1 bound to cis peptidomimetic inhibitor
35. " " " " " "  = 3tdb:A *
Human pin1 bound to trans peptidomimetic inhibitor
36. 980 92.6% 163 155 930.4 7.5e-45 1f8a:B Structural basis for the phosphoserine-proline recognition b ww domains

Number of sequences: 36

Excluded sequences

  Smith-
Waterman
score
%-tage
identity
a.a.
overlap
Seq
len
z-score E-
value
  PDB
code
Protein name
1. 734 98.2% 113 113 922.3 2.1e-44 3i6c:A * Structure-based design of novel pin1 inhibitors (ii)
2. " " " " " "  = 3ik8:A *
Structure-based design of novel pin1 inhibitors (i)
3. " " " " " "  = 3ikd:A *
Structure-based design of novel pin1 inhibitors (i)
4. " " " " " "  = 3ikg:A *
Structure-based design of novel pin1 inhibitors (i)
5. " " " " " "  = 3jyj:A *
Structure-based design of novel pin1 inhibitors (ii)
6. " " " " " "  = 3kac:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
7. 925 91.1% 157 145 920.9 2.6e-44 2xp6:A * Discovery of cell-active phenyl-imidazole pin1 inhibitors by structure-guided fragment evolution
8. " " " " " "  = 3kad:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
9. " " " " " "  = 3kaf:A *
Structure-guided design of alpha-amino acid-derived pin1 inhibitors
10. 381 51.3% 113 120 483.3 6e-20 1j6y:A Solution structure of pin1at from arabidopsis thaliana
11. 471 43.2% 169 177 481.0 8.1e-20 1yw5:A Peptidyl-prolyl isomerase ess1 from candida albicans
12. 319 51.8% 110 115 406.5 1.1e-15 2lj4:A Solution structure of the tbpin1
13. 278 100.0% 39 39 361.9 3.5e-13 1i6c:A * Solution structure of pin1 ww domain
14. " " " " " "  = 1i8g:B *
Solution structure of pin1 ww domain complexed with cdc25 phosphothreonine peptide
15. " " " " " "  = 1i8h:B *
Solution structure of pin1 ww domain complexed with human tau phosphothreonine peptide
16. 260 100.0% 36 36 340.0 5.8e-12 2lb3:A Structure of the ww domain of pin1 in complex with a human phosphorylated smad3 derived peptide
17. 248 100.0% 34 36 325.1 3.9e-11 2kcf:A The nmr solution structure of the isolated apo pin1 ww domain
18. 240 100.0% 33 33 315.7 1.3e-10 4gwt:A * Structure of racemic pin1 ww domain cocrystallized with dl-m
19. " " " " " "  = 4gwv:A *
Structure of racemic pin1 ww domain cocrystallized with tri- citrate
20. 214 88.2% 34 34 283.2 8.4e-09 2m9i:A * Nmr solution structure of pin1 ww domain variant 6-1
21. " " " " " "  = 2m9j:A *
Nmr solution structure of pin1 ww domain mutant 6-1g
22. 211 52.1% 71 91 273.7 2.9e-08 1zk6:A Nmr solution structure of b. Subtilis prsa ppiase
23. 214 40.4% 109 97 269.6 4.9e-08 2m1i:A * High resolution structure and dynamics of cspina parvulin at physiological temperature
24. " " " " " "  = 2rqs:A *
3d structure of pin from the psychrophilic archeon cenarchea symbiosum (cspin)
25. 192 85.3% 34 30 256.4 2.6e-07 2kbu:A Nmr solution structure of pin1 ww domain mutant with beta turn mimic at position 12
26. 191 82.4% 34 33 254.8 3.2e-07 2m9e:A * Nmr solution structure of pin1 ww domain mutant 5-1
27. " " " " " "  = 2m9f:A *
Nmr solution structure of pin1 ww domain mutant 5-1g
28. 178 43.6% 78 92 232.6 5.6e-06 1jns:A * Nmr structure of the e. Coli peptidyl-prolyl cis/trans- isomerase parvulin 10
29. " " " " " "  = 1jnt:A *
Nmr structure of the e. Coli peptidyl-prolyl cis/trans- isomerase parvulin 10
30. 174 43.2% 74 96 227.4 1.1e-05 1eq3:A Nmr structure of human parvulin hpar14
31. 174 43.2% 74 101 227.1 1.1e-05 3ui4:A * 0.8 a resolution crystal structure of human parvulin 14
32. " " " " " "  = 3ui5:A *
Crystal structure of human parvulin 14
33. " " " " " "  = 3ui6:A *
0.89 a resolution crystal structure of human parvulin 14 in with oxidized dtt
34. 174 43.2% 74 104 226.9 1.2e-05 1fjd:A Human parvulin-like peptidyl prolyl cis/trans isomerase, hpar14
35. 175 35.8% 120 252 218.0 3.6e-05 3rfw:A The virulence factor peb4 and the periplasmic protein cj1289 structurally-related sura-like chaperones in the human path campylobacter jejuni
36. 156 55.6% 36 43 209.8 0.0001 2dmv:A Solution structure of the second ww domain of itchy homolog e3 ubiquitin protein ligase (itch)
37. 157 31.4% 105 111 205.4 0.00018 2jzv:A Solution structure of s. Aureus prsa-ppiase
38. 147 64.5% 31 31 200.5 0.00034 2jo9:A Mouse itch 3rd ww domain complex with the epstein-barr virus latent membrane protein 2a derived peptide eeppppyed
39. 147 64.5% 31 37 199.5 0.00039 1yiu:A Itch e3 ubiquitin ligase ww3 domain
40. 144 64.5% 31 36 195.7 0.00063 2joc:A Mouse itch 3rd domain phosphorylated in t30
41. 139 50.0% 32 39 189.2 0.0015 2kyk:A The sandwich region between two lmp2a py motif regulates the interaction between aip4ww2domain and py motif
42. 148 33.0% 112 388 186.9 0.002 1m5y:A Crystallographic structure of sura, a molecular chaperone that facilitates outer membrane porin folding
43. 135 53.1% 32 36 184.7 0.0026 1wr3:A Solution structure of the first ww domain of nedd4-2
44. 133 48.6% 35 50 180.3 0.0046 1i5h:W Solution structure of the rnedd4 wwiii domain-renac bp2 peptide complex
45. 131 52.9% 34 40 179.1 0.0053 2ysh:A Solution structure of the ww domain from the human growth- arrest-specific protein 7, gas-7
46. 130 56.2% 32 37 178.3 0.0059 1ymz:A Cc45, an artificial ww domain designed using statistical coupling analysis
47. 136 32.1% 106 108 177.0 0.007 4g2p:A Crystal structure of peptidyl-prolyl cis-trans isomerase dom molecular chaperone sura from salmonella enterica subsp. En serovar typhimurium str. 14028s
48. 125 55.9% 34 47 170.7 0.016 2jx8:A Solution structure of hpcif1 ww domain
49. 124 34.8% 69 88 165.8 0.029 1tk7:A Nmr structure of ww domains (ww3-4) from suppressor of deltex
50. 118 48.5% 33 34 163.9 0.037 2lty:A Nedd4l ww2 domain in complex with a smad7 derived peptide
51. 119 45.0% 40 49 163.0 0.042 2dwv:A Solution structure of the second ww domain from mouse salvador homolog 1 protein (mww45)
52. 118 45.2% 31 40 163.0 0.042 2laj:A Third ww domain of human nedd4l in complex with doubly phosp human smad3 derived peptide
53. 117 42.9% 35 37 162.2 0.047 1e0m:A Prototype ww domain
54. 118 45.2% 42 49 161.8 0.049 2zaj:A Solution structure of the short-isoform of the second ww domain from the human membrane-associated guanylate kinase, ww and pdz domain-containing protein 1 (magi-1)
55. 114 45.2% 31 41 157.8 0.081 1wr7:A Solution structure of the third ww domain of nedd4-2
56. 115 53.1% 32 53 157.6 0.084 2jm7:A * Solution structure of group iv ww domain: a. Nidulans pina
57. " " " " " "  = 2jv4:A *
Structure characterisation of pina ww domain and comparison with other group iv ww domains, pin1 and ess1
58. 113 48.4% 31 35 157.5 0.085 2lb2:A Structure of the second domain of human nedd4l in complex wi phosphorylated ptpy motif derived from human smad3
59. 113 48.4% 31 36 157.4 0.086 1wr4:A Solution structure of the second ww domain of nedd4-2
60. 111 42.1% 38 40 154.3 0.13 1k9q:A * Yap65 ww domain complexed to n-(n-octyl)-gpppy-nh2
61. " " " " " "  = 1k9r:A *
Yap65 ww domain complexed to acetyl-plppy
62. 111 47.4% 38 49 153.1 0.15 2ysb:A Solution structure of the first ww domain from the mouse salvador homolog 1 protein (sav1)
63. 114 28.4% 67 108 152.1 0.17 3gpk:A Crystal structure of ppic-type peptidyl-prolyl cis-trans iso domain at 1.55a resolution.
64. 108 48.4% 31 35 151.3 0.19 2lb1:A Structure of the second domain of human smurf1 in complex wi smad1 derived peptide
65. 108 48.4% 31 35 151.3 0.19 2ltx:A Smurf1 ww2 domain in complex with a smad7 derived peptide
66. 108 39.5% 38 39 150.4 0.21 1k5r:A Yap65 ww domain s24-amino-ethylsulfanyl-acetic acid mutant
67. 105 41.9% 31 34 147.8 0.3 2law:A Structure of the second ww domain from human yap in complex human smad1 derived peptide
68. 105 41.9% 31 36 147.4 0.31 2ltv:A Yap ww2 in complex with a smad7 derived peptide
69. 105 45.2% 31 37 147.3 0.32 2ltz:A Smurf2 ww3 domain in complex with a smad7 derived peptide
70. 106 42.1% 38 46 147.2 0.32 1jmq:A Yap65 (l30k mutant) ww domain in complex with gtppppytvg peptide
71. 105 45.2% 31 42 146.5 0.35 2djy:A Solution structure of smurf2 ww3 domain-smad7 py peptide complex
72. 104 46.9% 32 36 146.2 0.36 2lax:A * Structure of first ww domain of human yap in complex with a smad1 doubly-phosphorilated derived peptide.
73. " " " " " "  = 2lay:A *
Structure of the first ww domain of human yap in complex wit phosphorylated human smad1 derived peptide
74. " " " " " "  = 2ltw:A *
Yap ww1 in complex with a smad7 derived peptide
75. 105 45.2% 31 90 142.0 0.62 2kxq:A Solution structure of smurf2 ww2 and ww3 bound to smad7 py m containing peptide
76. 99 41.9% 31 33 140.5 0.75 4n7h:A Crystal structure of the complex of 3rd ww domain of human n 1st ppxy motif of arrdc3
77. 99 41.9% 31 34 140.3 0.77 2kpz:A Human nedd4 3rd ww domain complex with the human t-cell leuk 1 gag-pro poliprotein derived peptide sdpqipppyvep
78. 99 41.9% 31 35 140.1 0.79 2kq0:A Human nedd4 3rd ww domain complex with ebola zaire virus mat protein vp40 derived peptide ilptappeymea
79. 99 41.9% 31 37 139.8 0.82 4n7f:A Crystal structure of 3rd ww domain of human nedd4-1
80. 110 41.7% 36 412 139.3 0.88 3olm:A Structure and function of a ubiquitin binding site within th catalytic domain of a hect ubiquitin ligase
81. 110 41.7% 36 419 139.2 0.89 4lcd:A Structure of an rsp5xubxsna3 complex: mechanism of ubiquitin and lysine prioritization by a hect e3
82. 99 41.9% 31 43 138.9 0.92 2m3o:W Structure and dynamics of a human nedd4 ww domain-enac compl
83. 98 37.5% 40 39 138.3 1 2op7:A Ww4
84. 98 37.5% 32 39 138.3 1 2ysc:A Solution structure of the ww domain from the human amyloid beta a4 precursor protein-binding family b member 3, apbb3
85. 100 48.1% 27 75 136.9 1.2 1o6w:A Solution structure of the prp40 ww domain pair of the yeast splicing factor prp40
86. 97 38.7% 31 46 136.0 1.3 2l4j:A Yap ww2
87. 97 40.5% 37 60 134.5 1.6 2yse:A Solution structure of the second ww domain from the human membrane-associated guanylate kinase, ww and pdz domain- containing protein 1. Magi-1
88. 95 35.1% 37 43 134.0 1.7 2jmf:A Solution structure of the su(dx) ww4- notch py peptide complex
89. 95 29.3% 41 46 133.6 1.8 2ez5:W Solution structure of the dnedd4 ww3 Domain- comm lpsy peptide complex
90. 95 37.2% 43 50 133.1 2 2dk1:A Solution structure of ww domain in ww domain binding protein 4 (wbp-4)
91. 93 38.7% 31 40 131.9 2.3 2ysg:A Solution structure of the ww domain from the human syntaxin- binding protein 4
92. 93 44.8% 29 75 128.2 3.6 2jxw:A Solution structure of the tandem ww domains of fbp21
93. 90 43.2% 37 50 126.9 4.3 2e45:A Solution structure of fe65 ww domain
94. 93 28.0% 93 102 126.4 4.6 2kgj:A Solution structure of parvulin domain of ppid from e.Coli
95. 88 44.4% 36 37 126.1 4.7 2oei:A Crystal structure of human fe65-ww domain in complex with human mena peptide
96. 85 45.2% 31 30 123.7 6.5 2idh:A Crystal structure of human fe65 ww domain
97. 88 31.8% 44 57 123.6 6.6 2ysd:A Solution structure of the first ww domain from the human membrane-associated guanylate kinase, ww and pdz domain- containing protein 1. Magi-1
98. 85 45.2% 31 31 123.5 6.7 2idh:B Crystal structure of human fe65 ww domain
99. 85 45.2% 31 33 123.1 7 2ho2:A Structure of human fe65-ww domain in complex with hmena pept
100. 85 45.2% 31 33 123.1 7 2idh:H Crystal structure of human fe65 ww domain
101. 85 45.2% 31 34 122.9 7.2 2idh:D Crystal structure of human fe65 ww domain
102. 83 44.4% 27 28 121.6 8.5 1ywi:A * Structure of the fbp11ww1 domain complexed to the peptide apptppplpp
103. " " " " " "  = 1ywj:A *
Structure of the fbp11ww1 domain
104. 83 44.4% 27 30 121.2 9 1zr7:A * Solution structure of the first ww domain of fbp11
105. " " " " " "  = 2dyf:A *
Solution structure of the first ww domain of fbp11 / hypa (fbp11 ww1) complexed with a pl (pplp) motif peptide ligand
106. 82 37.5% 32 33 119.4 11 2laz:A * Structure of the first ww domain of human smurf1 in complex mono-phosphorylated human smad1 derived peptide
107. " " " " " "  = 2lb0:A *
Structure of the first ww domain of human smurf1 in complex phosphorylated human smad1 derived peptide
108. 85 38.1% 42 108 116.1 17 1lv6:A 3d structure of human resistin
109. 78 57.9% 19 29 115.2 19 2mdu:A Circular permutant of the ww domain with loop 1 excised
110. 90 22.5% 102 103 115.1 19 2pv1:A * Crystallographic structure of sura first peptidyl-prolyl isomerase domain complexed with peptide weyipnv
111. " " " " " "  = 2pv2:A *
Crystallographic structure of sura first peptidyl-prolyl isomerase domain complexed with peptide nftlkfwdifrk
112. 84 40.7% 27 92 114.6 21 2l5f:A Solution structure of the tandem ww domains from hypa/fbp11
113. 79 50.0% 20 40 114.5 21 2ysi:A Solution structure of the first ww domain from the mouse transcription elongation regulator 1, transcription factor ca150
114. 90 23.6% 106 449 113.9 23 2osx:A Endo-glycoceramidase ii from rhodococcus sp.: Ganglioside gm
115. 76 37.0% 27 37 111.2 32 1e0l:A * Fbp28ww domain from mus musculus
116. " " " " " "  = 2jup:W *
Fbp28ww2 domain in complex with the pplipppp peptide
117. " " " " " "  = 2rly:W *
Fbp28ww2 domain in complex with ptppplpp peptide
118. " " " " " "  = 2rm0:W *
Fbp28ww2 domain in complex with a ppplipppp peptide
119. 82 28.0% 82 163 109.9 38 4lzp:C Structure of the tir domain of the immunosuppressor btpa fro
120. 81 32.2% 59 147 109.3 41 2gmy:A Crystal structure of a protein of unknown function atu0492 f agrobacterium tumefaciens, putative antioxidant defence pro
121. 83 23.5% 115 244 108.8 44 2huc:A Structural studies examining the substrate specificity profiles of pc-plcbc protein variants
122. 82 26.9% 104 225 108.0 48 4byn:y * Cryo-em reconstruction of the 80s-eif5b-met-itrnamet eukaryo translation initiation complex
123. " " " " " "  = 4byq:L *
Cryo-em reconstruction of the 80s-eif5b-met-itrnamet eukaryotic translation initiation complex
124. 82 26.9% 104 225 108.0 48 4jux:C Crystal structure of the ribosome bound to elongation factor guanosine triphosphatase state (this file contains the 50s

Number of sequences: 124

Select or deselect any sequence by clicking its checkbox.
Selection shortcuts : select all/none invert selection

Then click to effect selection changes.

Annotation parameters

The parameters below were used in determining which structural annotations could be transferred on to the target sequence. You can change the parameters and regenerate the SAS alignments and annotation by pressing the Rerun button.

Min. seq. identity:   Min. seq. overlap   Max. E-value

  spacer

spacer