ID A0A1V4KGI1_PATFA Unreviewed; 432 AA.
AC A0A1V4KGI1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Carboxypeptidase A6 {ECO:0000313|EMBL:OPJ83538.1};
GN Name=CPA6 {ECO:0000313|EMBL:OPJ83538.1};
GN ORFNames=AV530_006411 {ECO:0000313|EMBL:OPJ83538.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ83538.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ83538.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ83538.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ83538.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:OPJ83538.1}.
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DR EMBL; LSYS01003169; OPJ83538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KGI1; -.
DR STRING; 372326.A0A1V4KGI1; -.
DR Proteomes; UP000190648; 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:UniProtKB-KW.
DR CDD; cd03872; M14_CPA6; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR033843; CPAH.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF18; CARBOXYPEPTIDASE A6; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:OPJ83538.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..432
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013025466"
FT DOMAIN 182..204
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 319..329
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 432 AA; 50111 MW; D17EAE204B0B7808 CRC64;
MPLRGRPAGL LPLCLLCLQA ALPLRGHRGR YAGDKVIRIV PESERETQIL RAAFNRLKVD
LWQPSSPFHI VEGMVTDVRV PRNASQSLLP YLQQANIPYT ILISDLQKAI ENQTGQRPYR
NRRSLSGYNY EMYHSLEEIQ DWMDHLNKTH SDLVHMFSVG ESYEGRPLFV LKLGKRSRPY
KKAVWIDCGI HAREWIGPAF CQWFVKEALQ TYQTDPAMRK MLTQLYFYIM PVFNVDGYHF
SWTNDRFWRK TRSKNTRFRC HGVDANRNWK VKWCDEGASL HPCDDTYCGP FPESEPEVKA
VAHFLRKHRK QIKAYLSFHA YAQMLLYPYS YKYATIPNFS CVELAAYNAV NALQSAYGVR
YRYGPASTTL YVSSGSSMDW AYKNGIPYAF AFELRDTGHF GFLLPETLIK PTCTETMLAV
KNITLHLLKK CH
//
