ID A0A3L8R9E2_CHLGU Unreviewed; 235 AA.
AC A0A3L8R9E2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132};
GN ORFNames=DV515_00017103 {ECO:0000313|EMBL:RLV76316.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV76316.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV76316.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV76316.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV76316.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV76316.1}.
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DR EMBL; QUSF01000737; RLV76316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8R9E2; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF48; ADIPOCYTE ENHANCER-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT DOMAIN 90..112
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 235 AA; 25652 MW; FEFB92ABE6CDAE7F CRC64;
MALSVAVGTS VVLGTFTGWD PPWAWDSLQG VGSSPQALPP SLPTPQLMKV VNEECPTITR
IYNIGKSSRG LKIYAMEISD NPGEHETGEP EFRYTAGLHG NEALGRELLL LLMQFLCKEY
QDGNPRVRGL VTDTRIHLVP SLNPDGYELA HEALTGALGH PQGSELGNWA LGHWTEEGFD
LFENFPDLAS ALWAAEERRL VPHQFPNHHI PIPEHYLSED AAVSAAQGRG EGGRG
//
