ID A0A087R8J1_APTFO Unreviewed; 419 AA.
AC A0A087R8J1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Carboxypeptidase A2 {ECO:0000313|EMBL:KFM09795.1};
GN ORFNames=AS27_08693 {ECO:0000313|EMBL:KFM09795.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM09795.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM09795.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM09795.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL226211; KFM09795.1; -; Genomic_DNA.
DR RefSeq; XP_009280937.1; XM_009282662.2.
DR AlphaFoldDB; A0A087R8J1; -.
DR STRING; 9233.A0A087R8J1; -.
DR MEROPS; M14.002; -.
DR GeneID; 103901735; -.
DR KEGG; afor:103901735; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000053286; 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:KFM09795.1};
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:UP000053286};
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_5001828526"
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"
SQ SEQUENCE 419 AA; 46909 MW; FFBBB8C293A4EA08 CRC64;
MKLILIFSAL FGASLCLETF VGHQVLRIKT RNEEEVQKLQ LLESLEHLGL DFWINPSTPA
LPVDVRIPAN SVQAVKAFLE SHGIEYAILI EDLQVVLDKE KQDMAYSQQR DRSSNSFNYG
TYHSLDSIYA ELDHLASEYS NIVSKLQIGQ SYEKRPLYVL KFSTGGSNRP AIWLDAGIHS
REWVTQASAI WIAKKIASDY GKDPSLTSLL NKMDIFLLTV SNPDGYVFTH TTNRMWRKTR
SKNRGSQCVG VDPNRNWDAG FGGPGASSNP CSDSYRGPSA NSEVEVKSVV NFIKNHGNIR
AFLTLHSYSQ LLMYPYGYKC TEPADYAELD ALGRAAASSI QSLYGTTFTV GSICTTIYQA
SGGSIDWSYD YGIKYSFAFE LRDTGRYGFL LPASQIIPTA EETWLGLKKI MEHVRDNPY
//
