AC   PRU00741;
DC   Domain;
TR   PROSITE; PS51408; TRANSFERRIN_LIKE_4; 1; level=0
XX
Names: 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.
XX
case <FTGroup:1>
DE   + RecName: EC=3.4.21.-;
end case
CC   -!- SIMILARITY: Belongs to the transferrin family.
case <FTGroup:1>
DR   PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1; trigger=no
DR   PROSITE; PS00206; TRANSFERRIN_LIKE_2; 1; trigger=no
DR   PROSITE; PS00207; TRANSFERRIN_LIKE_3; 1; trigger=no
end case
XX
case <FTGroup:1>
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
GO   GO:0004252; F:serine-type endopeptidase activity
end case
case <FTGroup:2>
GO   GO:0005506; F:iron ion binding
GO   GO:0046872; F:metal ion binding
end case
XX
case <FTGroup:1>
KW   Hydrolase
KW   Protease
KW   Serine protease
end case
case <FTGroup:2>
KW   Iron
KW   Metal-binding
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS51408
FT   DOMAIN          from..to
FT                   /note="Transferrin-like #"
FT   ACT_SITE        68
FT   Group: 1; Condition: K
FT   ACT_SITE        256
FT                   /note="Nucleophile"
FT   Group: 1; Condition: S
FT   BINDING         56
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="#1"
FT   Group: 2; Condition: D
FT   BINDING         85
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="#1"
FT   Group: 2; Condition: Y
FT   BINDING         184
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="#1"
FT   Group: 2; Condition: Y
FT   BINDING         249
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="#1"
FT   Group: 2; Condition: H
FT   BINDING         111
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="#1"
FT   Group: 2; Condition: T
FT   BINDING         115
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="#1"
FT   Group: 2; Condition: R
FT   BINDING         117
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="#1"
FT   Group: 2; Condition: A
FT   BINDING         118
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="#1"
FT   Group: 2; Condition: G
FT   DISULFID        4..41
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID        14..32
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID        109..190
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID        151..169
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID        154..175
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID        166..173
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID        227..241
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 245-610;
Related: None;
Repeats: 1-2;
Topology: Not cytoplasmic;
Example: P02788;
Scope:
 Eukaryota
Comments: None;
XX
# Revision 1.13 2022/11/19
//