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Database: UniProt
Entry: A0A4D9EFT9_9SAUR
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ID   A0A4D9EFT9_9SAUR        Unreviewed;       419 AA.
AC   A0A4D9EFT9;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Carboxypeptidase A6 {ECO:0000313|EMBL:TFK05294.1};
GN   ORFNames=DR999_PMT12077 {ECO:0000313|EMBL:TFK05294.1};
OS   Platysternon megacephalum (big-headed turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Platysternidae; Platysternon.
OX   NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK05294.1, ECO:0000313|Proteomes:UP000297703};
RN   [1] {ECO:0000313|EMBL:TFK05294.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK05294.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK05294.1};
RA   Gong S.;
RT   "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TFK05294.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK05294.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK05294.1};
RA   Gong S.;
RT   "The genome sequence of big-headed turtle.";
RL   Submitted (APR-2019) 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:TFK05294.1}.
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DR   EMBL; QXTE01000117; TFK05294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4D9EFT9; -.
DR   STRING; 55544.A0A4D9EFT9; -.
DR   Proteomes; UP000297703; 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   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF65; MAST CELL CARBOXYPEPTIDASE A; 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:TFK05294.1};
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:UP000297703};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..419
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020038078"
FT   DOMAIN          168..190
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;  48116 MW;  262FED5745932E12 CRC64;
     MKSMVPLGLI VATFALTSSR CFDSAKVFRV KPQNEKQVNF LKYLASIKQL DFWHPDSAPH
     IVTQMQVDFH VSAHQSRSVQ TLMEQNEIQY EILLHNLQEE IEKQFDGKRN FTSRHSYTKY
     NDWDKIAAWT ARIAKIYPKL VSRIQIGNTF EKQPMYLLKV GKKSGRKKAI FMDCGIHARE
     WISPAFCQWF VKQAASTYGK DKIMTHLLDS LNFYVLPVFN IDGYVWSWTQ DRMWRKNRSK
     NSSTNCTGTD LNRNFAAAWG TTGFISDDPC DETYYGPAPE SEDETKAVAT FIRNHLSSIK
     AYLNIHAYSQ MLLFPYGYTF HKAPNHDELT EVAKAAMEAL SSLYSTKYEY GASATLIYPT
     SGSSVDWAYD QGIKYSFVFE LRDKGRYGFL LPESKIKSTC KETMLAVKSI ANYILSYAS
//
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