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SAS results for UniProt accession no. P04390

Sequence annotated by structure

Key:
Sec. struc: By homology Predicted
  Helix Strand   Helix Strand
Residue contacts:   to ligand   to DNA/RNA   to metal
Active sites:   (from PDB SITE records)

Predicted secondary structure (green) comes from the DSC program. The lighter the green the less certain the prediction. 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. P04390 - coloured by no. of contacts to ligand

Below are the FASTA results from a search of the sequence of UniProt accession no. P04390 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 50 unique sequences (including 3 consensus sequences) giving 58 sequence matches in all. The 30 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
       ---------+---------+---------+---------+---------+---------+-----   ------------
P04390 mslrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Type-2 restriction enzyme EcoRV OS=Escherichia coli  ...
1b94:A*-slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee×7 Restriction endonuclease ecorv with calcium
1b96:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Analysis of a mutational hot-spot in the ecorv restriction  ...
1stx:A*-slrsdlinalydenqkydvcgiisaegkiyplgsdtavlstifelfsrpiinkiaekhgyivee×2 Structure of the k38a mutant of ecorv bound to cognate DNA  ...
1b97:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Analysis of a mutational hot-spot in the ecorv restriction  ...
1suz:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   The structure of k92a ecorv bound to cognate DNA and mg2+
4rve:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   The crystal structure of ecorv endonuclease and of its  ...
1sx8:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Ecorv bound to cognate DNA and mn2+
1rv5:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Complex of ecorv endonuclease with d(aaagat)/d(atctt)
1eo3:A -SLRSDLINALYDENQKYDVCGIISAEGKIYPLGSDTKVLSTIFELFSRPIINKIAEKHGYIVEE   Inhibition of ecorv endonuclease by deoxyribo-3'-s-  ...
1az0:A*-slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee×2 Ecorv endonuclease/DNA complex
1eop:A -slrsdlinalyde-----vcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Ecorv bound to cognate DNA
1bsu:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Structural and energetic origins of indirect readout in  ...
1eo4:A -SLRSDLINALYDENQKYDVCGIISAEGKIYPLGSDTKVLSTIFELFSRPIINKIAEKHGYIVEE   Ecorv bound to mn2+ and cognate DNA containing a 3's  ...
2b0d:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Ecorv restriction endonuclease/gaattc/ca2+
1eon:A -SLRSDLINALYDENQKYDVCGIISAEGKIYPLGSDTKVLSTIFELFSRPIINKIAEKHGYIVEE   Ecorv bound to 3'-s-phosphorothiolate DNA and ca2+
2ge5:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Ecorv restriction endonucleasE C-terminal deletion  ...
1az4:B -slrsdlinalyd-----dvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Ecorv endonuclease, unliganded, form b, t93a mutant
1az3:B -slrsdlinalyde----dvcgiisaegkiyplgsd-kvlstifelfsrpiinkiaekhgyivee   Ecorv endonuclease, unliganded, form b
1rv5:B -slrsdlinal-------dvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Complex of ecorv endonuclease with d(aaagat)/d(atctt)
2b0e:A -slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgyivee   Ecorv restriction endonuclease/gaautc/ca2+

                                         1         1         1         1
           7         8         9         0         1         2         3
       67890123456789012345678901234567890123456789012345678901234567890   Protein name
       ----+---------+---------+---------+---------+---------+---------+   ------------
P04390 pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia   Type-2 restriction enzyme EcoRV OS=Escherichia coli  ...
1b94:A*pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia×7 Restriction endonuclease ecorv with calcium
1b96:A pkqenhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia   Analysis of a mutational hot-spot in the ecorv restriction  ...
1stx:A*pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia×2 Structure of the k38a mutant of ecorv bound to cognate DNA  ...
1b97:A pkqlnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia   Analysis of a mutational hot-spot in the ecorv restriction  ...
1suz:A pkqqnhypdftlykpsepnkkiaidiattytnkenekikftlggytsfirnntknivypfdqyia   The structure of k92a ecorv bound to cognate DNA and mg2+
4rve:A pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia   The crystal structure of ecorv endonuclease and of its  ...
1sx8:A pkqqnhypdftlykpsepnkkiaidiattytnkenekikftlggytsfirnntknivypfdqyia   Ecorv bound to cognate DNA and mn2+
1rv5:A pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia   Complex of ecorv endonuclease with d(aaagat)/d(atctt)
1eo3:A PKQQNHYPDFTLYKPSEPNKKIAIDIKTTYTNKENEKIKFTLGGYTSFIRNNTKNIVYPFDQYIA   Inhibition of ecorv endonuclease by deoxyribo-3'-s-  ...
1az0:A*pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia×2 Ecorv endonuclease/DNA complex
1eop:A pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia   Ecorv bound to cognate DNA
1bsu:A pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia   Structural and energetic origins of indirect readout in  ...
1eo4:A PKQQNHYPDFTLYKPSEPNKKIAIDIKTTYTNKENEKIKFTLGGYTSFIRNNTKNIVYPFDQYIA   Ecorv bound to mn2+ and cognate DNA containing a 3's  ...
2b0d:A pkqqnhypdftlykpsepnkkiaidikttytnke--kikftlggytsfirnntknivypfdqyia   Ecorv restriction endonuclease/gaattc/ca2+
1eon:A PKQQNHYPDFTLYKPSEPNKKIAIDIKTTYTNKENEKIKFTLGGYTSFIRNNTKNIVYPFDQYIA   Ecorv bound to 3'-s-phosphorothiolate DNA and ca2+
2ge5:A pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia   Ecorv restriction endonucleasE C-terminal deletion  ...
1az4:B pkqqnhypdftlykpsepnkkiaidikatytnkenekikftlggytsfirnntknivypfdqyia   Ecorv endonuclease, unliganded, form b, t93a mutant
1az3:B pkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntknivypfdqyia   Ecorv endonuclease, unliganded, form b
1rv5:B pkqqnhypdftlykpsepnkkiaidikttytnk----ikftlggytsfirnntknivypfdqyia   Complex of ecorv endonuclease with d(aaagat)/d(atctt)
2b0e:A pkqqnhypdftlykpsepnkkiaidikttyt-----kikftlggytsfirnntknivypfdqyia   Ecorv restriction endonuclease/gaautc/ca2+

                1         1         1         1         1         1     
                4         5         6         7         8         9     
       12345678901234567890123456789012345678901234567890123456789012345   Protein name
       ---------+---------+---------+---------+---------+---------+-----   ------------
P04390 hwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Type-2 restriction enzyme EcoRV OS=Escherichia coli  ...
1b94:A*hwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah×7 Restriction endonuclease ecorv with calcium
1b96:A hwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Analysis of a mutational hot-spot in the ecorv restriction  ...
1stx:A*hwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah×2 Structure of the k38a mutant of ecorv bound to cognate DNA  ...
1b97:A hwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Analysis of a mutational hot-spot in the ecorv restriction  ...
1suz:A hwiigyvytrvat-ksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   The structure of k92a ecorv bound to cognate DNA and mg2+
4rve:A hwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   The crystal structure of ecorv endonuclease and of its  ...
1sx8:A hwiigyvytrv---ksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Ecorv bound to cognate DNA and mn2+
1rv5:A hwiigyvytrv----sslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Complex of ecorv endonuclease with d(aaagat)/d(atctt)
1eo3:A HWIIGYVYTRVAT-KSSLKTYNI--LNEIPKPYKGVKVFLQDKWVIAGDLAGSGNTTNIGSIHAH   Inhibition of ecorv endonuclease by deoxyribo-3'-s-  ...
1az0:A*hwiigyvytrv-------ktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah×2 Ecorv endonuclease/DNA complex
1eop:A hwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Ecorv bound to cognate DNA
1bsu:A hwiigyvytrv-------ktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Structural and energetic origins of indirect readout in  ...
1eo4:A HWIIGYVYTRV---KSSLKTYNI--LNEIPKPYKGVKVFLQDKWVIAGDLAGSGNTTNIGSIHAH   Ecorv bound to mn2+ and cognate DNA containing a 3's  ...
2b0d:A hwiigyvytrv------lktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Ecorv restriction endonuclease/gaattc/ca2+
1eon:A HWIIGYVYTRV---KSSLKTYNI-----IPKPYKGVKVFLQDKWVIAGDLAGSGNTTNIGSIHAH   Ecorv bound to 3'-s-phosphorothiolate DNA and ca2+
2ge5:A hwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Ecorv restriction endonucleasE C-terminal deletion  ...
1az4:B hwiigyvytrv-------ktyninelneipkpykgvkvflqdkwviagdlag-----nigsihah   Ecorv endonuclease, unliganded, form b, t93a mutant
1az3:B hwiigyvytrv-------ktyninelneipkpykgvkvflqdkwviagdlag-----nigsihah   Ecorv endonuclease, unliganded, form b
1rv5:B hwiigyvytrv------lktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Complex of ecorv endonuclease with d(aaagat)/d(atctt)
2b0e:A hwiigyvytrv------lktyninelneipkpykgvkvflqdkwviagdlagsgnttnigsihah   Ecorv restriction endonuclease/gaautc/ca2+

           2         2         2         2         2     
           0         1         2         3         4     
       67890123456789012345678901234567890123456789012345                  Protein name
       ----+---------+---------+---------+---------+-----                  ------------
P04390 ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk                  Type-2 restriction enzyme EcoRV OS=Escherichia coli  ...
1b94:A*ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk               ×7 Restriction endonuclease ecorv with calcium
1b96:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk                  Analysis of a mutational hot-spot in the ecorv restriction  ...
1stx:A*ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk               ×2 Structure of the k38a mutant of ecorv bound to cognate DNA  ...
1b97:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk                  Analysis of a mutational hot-spot in the ecorv restriction  ...
1suz:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk                  The structure of k92a ecorv bound to cognate DNA and mg2+
4rve:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy----                  The crystal structure of ecorv endonuclease and of its  ...
1sx8:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk                  Ecorv bound to cognate DNA and mn2+
1rv5:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk                  Complex of ecorv endonuclease with d(aaagat)/d(atctt)
1eo3:A YKDFVEGKGIFDSEDEFLDYWRNYERTSQLRNDKYNNISEYRNWIYRGRK                  Inhibition of ecorv endonuclease by deoxyribo-3'-s-  ...
1az0:A*ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk               ×2 Ecorv endonuclease/DNA complex
1eop:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgr-                  Ecorv bound to cognate DNA
1bsu:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgr-                  Structural and energetic origins of indirect readout in  ...
1eo4:A YKDFVEGKGIFDSEDEFLDYWRNYERTSQ-RNDKYNNISEYRNWIYRGRK                  Ecorv bound to mn2+ and cognate DNA containing a 3's  ...
2b0d:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk                  Ecorv restriction endonuclease/gaattc/ca2+
1eon:A YKDFVEGKGIFDSEDEFLDYWRNYERTSQLRNDKYNNISEYRNWIYRGRK                  Ecorv bound to 3'-s-phosphorothiolate DNA and ca2+
2ge5:A ykdfvegkgifdsedefldywrnye-------------------------                  Ecorv restriction endonucleasE C-terminal deletion  ...
1az4:B ykdfvegkgifdsedefldywrnye--------kynniseyrnwiy----                  Ecorv endonuclease, unliganded, form b, t93a mutant
1az3:B ykdfvegkgifdsedefldywrnye--------kynniseyrnwiy----                  Ecorv endonuclease, unliganded, form b
1rv5:B ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk                  Complex of ecorv endonuclease with d(aaagat)/d(atctt)
2b0e:A ykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiyrgrk                  Ecorv restriction endonuclease/gaautc/ca2+

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. P04390. 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. - - - 245 - - P04390 Type-2 restriction enzyme EcoRV OS=Escherichia coli GN=ecoRVR PE=1 SV=3
2. 1629 100.0% 244 244 2041.4 1e-106 1b94:A * Restriction endonuclease ecorv with calcium
3. " " " " " "  = 1b95:A *
Analysis of a mutational hot-spot in the ecorv restriction endonuclease: a catalytic role for a main chain carbonyl group
4. " " " " " "  = 1eoo:A *
Ecorv bound to cognate DNA
5. " " " " " "  = 1rva:A *
Mg2+ binding to the active site of eco rv endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 angstroms resolution
6. " " " " " "  = 1rvb:A *
Mg2+ binding to the active site of eco rv endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 angstroms resolution
7. " " " " " "  = 1rvc:A *
Mg2+ binding to the active site of eco rv endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 angstroms resolution
8. " " " " " "  = 1rve:A *
The crystal structure of ecorv endonuclease and of its complexes with cognate and non-cognate DNA fragments
9. 1624 99.6% 244 244 2035.1 2.2e-106 1b96:A Analysis of a mutational hot-spot in the ecorv restriction endonuclease: a catalytic role for a main chain carbonyl group
10. 1622 99.6% 244 244 2032.6 3.1e-106 1stx:A * Structure of the k38a mutant of ecorv bound to cognate DNA and mn2+
11. " " " " " "  = 1sx5:A *
K38a ecorv bound to cleaved DNA and mn2+: p1 crystal form
12. 1620 99.6% 244 244 2030.1 4.2e-106 1b97:A Analysis of a mutational hot-spot in the ecorv restriction endonuclease: a catalytic role for a main chain carbonyl group
13. 1603 99.2% 244 243 2008.9 6.4e-105 1suz:A The structure of k92a ecorv bound to cognate DNA and mg2+
14. 1601 100.0% 240 240 2006.4 8.8e-105 4rve:A The crystal structure of ecorv endonuclease and of its complexes with cognate and non-cognate DNA segments
15. 1589 98.4% 244 241 1991.4 6e-104 1sx8:A Ecorv bound to cognate DNA and mn2+
16. 1588 98.4% 244 240 1990.2 7.1e-104 1rv5:A Complex of ecorv endonuclease with d(aaagat)/d(atctt)
17. 1583 98.8% 244 241 1983.9 1.6e-103 1eo3:A Inhibition of ecorv endonuclease by deoxyribo-3'-s- phosphorothiolates: a high resolution x-ray crystallographic study
18. 1567 97.1% 244 237 1964.0 2e-102 1az0:A * Ecorv endonuclease/DNA complex
19. " " " " " "  = 1bgb:A *
Ecorv endonuclease complex with 5'-cgggatatccc DNA
20. 1567 97.9% 243 238 1964.0 2e-102 1eop:A Ecorv bound to cognate DNA
21. 1561 97.1% 243 236 1956.5 5.3e-102 1bsu:A Structural and energetic origins of indirect readout in site-specific DNA cleavage by a restriction endonuclease
22. 1552 97.5% 244 238 1945.2 2.3e-101 1eo4:A Ecorv bound to mn2+ and cognate DNA containing a 3's substition at the cleavage site
23. 1547 96.7% 244 236 1939.0 5e-101 2b0d:A Ecorv restriction endonuclease/gaattc/ca2+
24. 1545 96.7% 244 236 1936.5 6.9e-101 1eon:A Ecorv bound to 3'-s-phosphorothiolate DNA and ca2+
25. 1456 100.0% 219 219 1825.6 1e-94 2ge5:A Ecorv restriction endonucleasE C-terminal deletion mutant/gatatc/ca2+
26. 1353 89.2% 240 215 1342.9 8e-68 1az4:B Ecorv endonuclease, unliganded, form b, t93a mutant
27. 1349 89.6% 240 215 1337.9 1.5e-67 1az3:B Ecorv endonuclease, unliganded, form b
28. 1457 93.0% 244 227 1157.3 1.7e-57 1rv5:B Complex of ecorv endonuclease with d(aaagat)/d(atctt)
29. 1522 95.5% 244 233 1157.2 1.8e-57 2b0e:A Ecorv restriction endonuclease/gaautc/ca2+

Number of sequences: 29

Excluded sequences

  Smith-
Waterman
score
%-tage
identity
a.a.
overlap
Seq
len
z-score E-
value
  PDB
code
Protein name
1. 1479 94.2% 243 229 1149.8 4.6e-57 1bua:B Structural and energetic origins of indirect readout in site-specific DNA cleavage by a restriction endonuclease
2. 1487 94.2% 243 230 1148.5 5.4e-57 1bss:A Ecorv-t93a/DNA/ca2+
3. 1499 95.1% 243 231 1148.5 5.4e-57 1bua:A Structural and energetic origins of indirect readout in site-specific DNA cleavage by a restriction endonuclease
4. 1341 89.1% 239 213 1085.2 1.8e-53 2rve:A The crystal structure of ecorv endonuclease and of its complexes with cognate and non-cognate DNA segments
5. 1135 86.1% 216 186 903.5 2.4e-43 1az3:A Ecorv endonuclease, unliganded, form b
6. 1126 86.1% 216 187 900.9 3.3e-43 1az4:A Ecorv endonuclease, unliganded, form b, t93a mutant
7. 119 25.4% 169 264 151.7 0.18 4i0n:A Pore forming protein
8. 102 22.1% 226 267 130.4 2.8 4h56:A Crystal structure of the clostridium perfringens netb toxin membrane inserted form
9. 98 24.4% 164 212 126.9 4.3 1ajk:A Circularly permuted (1-3,1-4)-beta-d-glucan 4- glucanohydrolase cpa16m-84
10. 93 36.2% 80 127 124.1 6.2 1ljb:A Transthyretin [precursor]
11. 94 25.6% 90 238 121.1 9 3fiu:A Structure of nmn synthetase from francisella tularensis
12. 93 24.7% 166 214 120.6 9.7 1cpm:A Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis
13. 90 22.7% 198 253 115.7 18 4bf2:A Crystal structures of ask1-inhibitor complexes
14. 90 23.6% 203 260 115.5 18 4bic:A Crystal structures of ask1-inhibitor complexes
15. 88 23.6% 106 254 113.2 25 2wfl:A Crystal structure of polyneuridine aldehyde esterase
16. 88 23.6% 106 255 113.2 25 2wfm:A Crystal structure of polyneuridine aldehyde esterase mutant (h244a)
17. 88 23.6% 106 254 113.2 25 3gzj:A Crystal structure of polyneuridine aldehyde esterase complexed with 16-epi-vellosimine
18. 88 22.1% 163 318 111.7 30 4n0a:H Crystal structure of lsm2-3-pat1c complex from saccharomyces cerevisiae
19. 87 22.3% 157 279 111.3 32 4c8q:H Crystal structure of the yeast lsm1-7-pat1 complex
20. 82 22.7% 75 120 110.7 34 3egn:A C-terminal RNA recognition motif of the u11/u12 65k protein
21. 85 25.0% 132 213 110.6 35 3o5s:A Crystal structure of the endo-beta-1,3-1,4 glucanase from ba subtilis (strain 168)
22. 86 22.0% 200 257 110.6 35 4bie:A Crystal structures of ask1-inhibitor complexes
23. 84 26.1% 115 205 109.6 39 1wm5:A Crystal structure of the n-terminal tpr domain (1-203) of p67phox
24. 92 25.6% 121 943 109.4 41 3sze:A Crystal structure of the passenger domain of the e. Coli autotransporter espp
25. 84 23.4% 128 214 109.3 41 1gbg:A Bacillus licheniformis beta-glucanase
26. 84 25.5% 102 226 109.0 43 3ne8:A The crystal structure of a domain from n-acetylmuramoyl-l-al amidase of bartonella henselae str. Houston-1
27. 83 26.1% 115 192 108.8 44 1hh8:A The active n-terminal region of p67phox: structure at 1.8 angstrom resolution and biochemical characterizations of the a128v mutant implicated in chronic granulomatous disease
28. 86 21.2% 156 345 108.6 45 4am1:A Crystal structure of the marine crustacean decapod shrimp (litopenaeus vannamei) arginine kinase in the absence of su or ligands.
29. 85 19.7% 157 300 108.3 47 4n8y:A Crystal structure of a trap periplasmic solute binding prote bradyrhizobium sp. Btai1 b (bbta_0128), target efi-510056 (bbta_0128), complex with alpha/beta-d-galacturonate
30. 84 23.3% 202 255 108.2 48 3vw6:A Crystal structure of human apoptosis signal-regulating kinas with imidazopyridine inhibitor

Number of sequences: 30

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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

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