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InterPro: IPR008979 Galactose-binding domain-like
Protein matches
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UniProtKB Matches: 12614 proteins |
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Accession
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IPR008979 Galactose-bd-like |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR000421 Coagulation factor 5/8 type, C-terminal
IPR001090 Ephrin receptor, ligand binding
IPR002706 DNA-repair protein Xrcc1, N-terminal
IPR003305 Carbohydrate-binding, CenC-like
IPR005084 Carbohydrate binding domain, family 6
IPR005086 Carbohydrate binding domain, family 17/28
IPR005088 Carbohydrate binding domain, family 15
IPR005638 Delta endotoxin, C-terminal
IPR006104 Glycoside hydrolase family 2, carbohydrate-binding
IPR010565 Muskelin, N-terminal
IPR012919 Sad1/UNC-like, C-terminal
IPR013736 Peptidase S15/CocE/NonD, C-terminal
IPR015176 Lyase, N-terminal
IPR015295 Carbohydrate binding module 27
IPR015908 Allantoicase domain
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Found in
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IPR001944 Glycoside hydrolase, family 35
IPR004939 Anaphase-promoting complex, subunit 10
IPR006585 Fucolectin tachylectin-4 pentraxin-1
IPR010900 Nicotine adenine dinucleotide glycohydrolase
IPR012905 PA-IL-like
IPR016257 Tyrosine-protein kinase, ephrin receptor
IPR016590 Rhamnogalacturonase B
IPR016625 Uncharacterised conserved protein UCP014872, subtilisin-related
IPR016901 Anaphase-promoting complex, subunit 10, subgroup
IPR017313 Peptidase S8A, subtilisin-related, clostridia-2
IPR017319 Peptidase S8A, subtilisin-related, prokarya
IPR017323 Lysyl endopeptidase
IPR020694 Tyrosine-protein kinase, ephrin receptor, subgroup
IPR020742 Tyrosine-protein kinase, discoidin domain-containing receptor
IPR020766 Tyrosine-protein kinase, ephrin A10 receptor
IPR020767 Tyrosine-protein kinase, ephrin B6 receptor
IPR020768 Tyrosine-protein kinase, ephrin A receptor
IPR020769 Tyrosine-protein kinase, ephrin B receptor
IPR020770 Tyrosine-protein kinase, ephrin A1/A2 receptor
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Contains
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IPR001426 Tyrosine-protein kinase, receptor class V, conserved site
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Proteins containing a galactose-binding domain-like fold can be found in several different protein families, in both eukaryotes and prokaryotes. The common function of these domains is to bind to specific ligands, such as cell-surface-attached carbohydrate substrates for galactose oxidase and sialidase [1], phospholipids on the outer side of the mammalian cell membrane for coagulation factor Va [2], membrane-anchored ephrin for the Eph family of receptor tyrosine kinases [3], and a complex of broken single-stranded DNA and DNA polymerase beta for XRCC1 [4].
The structure of the galactose-binding domain-like members consists of a beta-sandwich, in which the strands making up the sheets exhibit a jellyroll fold. There is a high degree of similarity in the beta-sandwich and in the loops between different family members, despite an often low level of sequence similarity.
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Structural links
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SCOP:
a.246.1.1
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b.1.18.2
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b.1.4.1
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b.18.1.1
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b.18.1.10
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b.18.1.11
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b.18.1.12
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b.18.1.13
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b.18.1.14
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b.18.1.15
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b.18.1.16
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b.18.1.17
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b.18.1.18
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b.18.1.19
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b.18.1.2
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b.18.1.20
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b.18.1.21
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b.18.1.22
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b.18.1.23
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b.18.1.24
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b.18.1.25
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b.18.1.28
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b.18.1.3
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b.18.1.4
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b.18.1.5
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b.18.1.7
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b.18.1.8
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b.18.1.9
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c.1.8.3
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c.69.1.21
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j.13.1.1
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Example proteins
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O14786 Neuropilin-1
O61460 Ephrin receptor 1
P13134 Kexin
P19137 Laminin subunit alpha-1
P26016 Furin-like protease 1, isoforms 1/1-X/2
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR018031 |
Laminin B, subgroup |
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| IPR001791 |
Laminin G |
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| IPR000421 |
Coagulation factor 5/8 type, C-terminal |
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| IPR000998 |
MAM |
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| IPR017441 |
Protein kinase, ATP binding site |
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| IPR000859 |
CUB |
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| IPR000209 |
Peptidase S8/S53, subtilisin/kexin/sedolisin |
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| IPR009030 |
Growth factor, receptor |
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| IPR002884 |
Proprotein convertase, P |
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| IPR009020 |
Proteinase inhibitor, propeptide |
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| IPR011009 |
Protein kinase-like domain |
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| IPR008957 |
Fibronectin, type III-like fold |
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| IPR008979 |
Galactose-binding domain-like |
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| IPR000719 |
Protein kinase, catalytic domain |
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| IPR020635 |
Tyrosine-protein kinase, subgroup, catalytic domain |
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| IPR010307 |
Laminin II |
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| IPR008211 |
Laminin, N-terminal |
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| IPR013032 |
EGF-like region, conserved site |
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| IPR003961 |
Fibronectin, type III |
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| IPR014648 |
Neuropilin |
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| IPR009254 |
Laminin I |
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| IPR013320 |
Concanavalin A-like lectin/glucanase, subgroup |
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| IPR001245 |
Tyrosine-protein kinase, catalytic domain |
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| IPR002049 |
EGF-like, laminin |
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| IPR012679 |
Laminin G, subdomain 1 |
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| IPR001090 |
Ephrin receptor, ligand binding |
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| IPR020685 |
Tyrosine-protein kinase |
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| IPR015500 |
Peptidase S8, subtilisin-related |
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| IPR000034 |
Laminin B type IV |
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| IPR008985 |
Concanavalin A-like lectin/glucanase |
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ModBase |
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SWISS-MODEL |
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PDB Chain |
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CATH Domain |
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SCOP Domain |
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Publications
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1.
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Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF.
Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase.
Nature 350 87-90 1991
[PubMed: 2002850]
http://dx.doi.org/10.1038/350087a0
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2.
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Macedo-Ribeiro S, Bode W, Huber R, Quinn-Allen MA, Kim SW, Ortel TL, Bourenkov GP, Bartunik HD, Stubbs MT, Kane WH, Fuentes-Prior P.
Crystal structures of the membrane-binding C2 domain of human coagulation factor V.
Nature 402 434-9 1999
[PubMed: 10586886]
http://dx.doi.org/10.1038/46594
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3.
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Himanen JP, Rajashankar KR, Lackmann M, Cowan CA, Henkemeyer M, Nikolov DB.
Crystal structure of an Eph receptor-ephrin complex.
Nature 414 933-8 2001
[PubMed: 11780069]
http://dx.doi.org/10.1038/414933a
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4.
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Marintchev A, Mullen MA, Maciejewski MW, Pan B, Gryk MR, Mullen GP.
Solution structure of the single-strand break repair protein XRCC1 N-terminal domain.
Nat. Struct. Biol. 6 884-93 1999
[PubMed: 10467102]
http://dx.doi.org/10.1038/12347
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Additional Reading
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Shao C, Novakovic VA, Head JF, Seaton BA, Gilbert GE.
Crystal structure of lactadherin C2 domain at 1.7A resolution with mutational and computational analyses of its membrane-binding motif.
J. Biol. Chem. 283 2008 7230-41
[PubMed: 18160406]
http://dx.doi.org/10.1074/jbc.M705195200
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Ramelot TA, Raman S, Kuzin AP, Xiao R, Ma LC, Acton TB, Hunt JF, Montelione GT, Baker D, Kennedy MA.
Improving NMR protein structure quality by Rosetta refinement: a molecular replacement study.
Proteins 75 2009 147-67
[PubMed: 18816799]
http://dx.doi.org/10.1002/prot.22229
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Tailford LE, Offen WA, Smith NL, Dumon C, Morland C, Gratien J, Heck MP, Stick RV, Bleriot Y, Vasella A, Gilbert HJ, Davies GJ.
Structural and biochemical evidence for a boat-like transition state in beta-mannosidases.
Nat. Chem. Biol. 4 2008 306-12
[PubMed: 18408714]
http://dx.doi.org/10.1038/nchembio.81
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Rogers MS, Hurtado-Guerrero R, Firbank SJ, Halcrow MA, Dooley DM, Phillips SE, Knowles PF, McPherson MJ.
Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen.
Biochemistry 47 2008 10428-39
[PubMed: 18771294]
http://dx.doi.org/10.1021/bi8010835
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Blanchard B, Nurisso A, Hollville E, Tetaud C, Wiels J, Pokorna M, Wimmerova M, Varrot A, Imberty A.
Structural basis of the preferential binding for globo-series glycosphingolipids displayed by Pseudomonas aeruginosa lectin I.
J. Mol. Biol. 383 2008 837-53
[PubMed: 18762193]
http://dx.doi.org/10.1016/j.jmb.2008.08.028
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