ID A0A099Z2P7_TINGU Unreviewed; 419 AA.
AC A0A099Z2P7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Carboxypeptidase A2 {ECO:0000313|EMBL:KGL75090.1};
DE Flags: Fragment;
GN ORFNames=N309_07693 {ECO:0000313|EMBL:KGL75090.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL75090.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL75090.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL75090.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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}.
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DR EMBL; KL887646; KGL75090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099Z2P7; -.
DR STRING; 94827.A0A099Z2P7; -.
DR MEROPS; M14.002; -.
DR Proteomes; UP000053641; 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; cd03870; M14_CPA; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR034248; CPA_M14_CPD.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF155; CARBOXYPEPTIDASE A4-RELATED; 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:KGL75090.1};
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:UP000053641};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..419
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001965616"
FT DOMAIN 170..192
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 306..316
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
FT NON_TER 419
FT /evidence="ECO:0000313|EMBL:KGL75090.1"
SQ SEQUENCE 419 AA; 46866 MW; 5FCBAC950DC46536 CRC64;
MKLILVFSAL FGASLCLETF VGHQVLRIRA SNKEQIQKLQ FLETLEHLQL DFWLNPSSPA
LPVDVRIPFH SLQAVKVFLE SNSIEYSILI EDLQVVLDEE KQAMALSQQR ERSSSTFNYG
TYHSLTSIYE ELDNLAHECS GIVSKLTIGE SYEKRPLYVL KFSTGGTNRP AIWIDAGIHS
REWITQASAI WIARKIASDY GSDPSITSLL DKMDIFLLAV ANPDGYEFTH TENRMWRKTR
SRNQGCLCIG VDPNRNWDAG FGGPGASSNP CSDTYHGPSA NSEVEVKSIV DFIENHGNIV
AFLTLHSYSQ LLMYPYGYKC TKPADYAELD SVGKAAASSI HSLYGTTFEV GSICTTIYQA
SGGSIDWSYD YGIKYSFAFE LRDTGTYGFL LPASQIIPTA EETWLGLKTI MEHVRDNPY
//
