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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU00741


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00741
General rule information [?]

Accession PRU00741
Dates 17-DEC-2008 (Created)
19-NOV-2022 (Last updated, Version 14)
Data class Domain;
Predictors PROSITE; PS51408; TRANSFERRIN_LIKE_4
Name Transferrin-like domain
Function The transferrin family is a group of glycosylated proteins found in both vertebrates and invertebrates. Most family members contain two transferrin-like domains of around 340 amino acids, the result of an ancient duplication event.
Scope(s) Eukaryota
Example(s) P02788;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTGroup:1>
Protein name + RecName: EC=3.4.21.-;
end case

Comments [?]

SIMILARITYBelongs to the transferrin family.

Keywords [?]

case <FTGroup:1>
Hydrolase
Protease
Serine protease
end case
case <FTGroup:2>
Iron
Metal-binding
end case
case <FTTag:disulf>
Disulfide bond
end case

Gene Ontology [?]

case <FTGroup:1>
GO:0016787; Molecular function:hydrolase activity
GO:0008233; Molecular function:peptidase activity
GO:0004252; Molecular function:serine-type endopeptidase activity
end case
case <FTGroup:2>
GO:0005506; Molecular function:iron ion binding
GO:0046872; Molecular function:metal ion binding
end case

Cross-references [?]

PROSITE PS00205; TRANSFERRIN_LIKE_1; 1;
PROSITE PS00206; TRANSFERRIN_LIKE_2; 1;
PROSITE PS00207; TRANSFERRIN_LIKE_3; 1;

Features [?]

From: PS51408
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Transferrin-like #"
ACT_SITE 68 68 K 1
ACT_SITE 256 256 /note="Nucleophile" S 1
BINDING 56 56 /ligand="Fe(3+)"
/ligand_id="ChEBI:CHEBI:29034"
/ligand_label="#1"		 D 2
BINDING 85 85 /ligand="Fe(3+)"
/ligand_id="ChEBI:CHEBI:29034"
/ligand_label="#1"		 Y 2
BINDING 184 184 /ligand="Fe(3+)"
/ligand_id="ChEBI:CHEBI:29034"
/ligand_label="#1"		 Y 2
BINDING 249 249 /ligand="Fe(3+)"
/ligand_id="ChEBI:CHEBI:29034"
/ligand_label="#1"		 H 2
BINDING 111 111 /ligand="hydrogencarbonate"
/ligand_id="ChEBI:CHEBI:17544"
/ligand_label="#1"		 T 2
BINDING 115 115 /ligand="hydrogencarbonate"
/ligand_id="ChEBI:CHEBI:17544"
/ligand_label="#1"		 R 2
BINDING 117 117 /ligand="hydrogencarbonate"
/ligand_id="ChEBI:CHEBI:17544"
/ligand_label="#1"		 A 2
BINDING 118 118 /ligand="hydrogencarbonate"
/ligand_id="ChEBI:CHEBI:17544"
/ligand_label="#1"		 G 2
DISULFID 4 41 disulf C-x*-C
DISULFID 14 32 disulf C-x*-C
DISULFID 109 190 disulf C-x*-C
DISULFID 151 169 disulf C-x*-C
DISULFID 154 175 disulf C-x*-C
DISULFID 166 173 disulf C-x*-C
DISULFID 227 241 disulf C-x*-C

Additional information [?]

Size range 245-610 amino acids
Related rules None
Fusion None
Repeats 1-2
Topology Not cytoplasmic

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

UniProtKB rule member sequences [?]