ID A0A2B4RSX0_STYPI Unreviewed; 477 AA.
AC A0A2B4RSX0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carboxypeptidase D {ECO:0000313|EMBL:PFX20701.1};
GN Name=CPD {ECO:0000313|EMBL:PFX20701.1};
GN ORFNames=AWC38_SpisGene14843 {ECO:0000313|EMBL:PFX20701.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX20701.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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:PFX20701.1}.
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DR EMBL; LSMT01000307; PFX20701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4RSX0; -.
DR STRING; 50429.A0A2B4RSX0; -.
DR EnsemblMetazoa; XM_022942670.1; XP_022798405.1; LOC111336557.
DR OrthoDB; 5490979at2759; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd03858; M14_CP_N-E_like; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF57; PEPTIDASE_M14 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 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:0000313|EMBL:PFX20701.1};
KW Hydrolase {ECO:0000313|EMBL:PFX20701.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:PFX20701.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..477
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012089408"
FT TRANSMEM 432..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..106
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 209..219
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 477 AA; 53050 MW; EBD7093F68542C40 CRC64;
MMAVYRRVLS LIVLLSLNVL ETRQHGVVDF THHDYDQMTS ILNDLQAAYP SITRLFSLGK
SVEGRELWVL QISDNPEIHE PGEPEFKYIG NMHGNEVVSR EILLHFIEHL LQGYNNDDEI
TNLIDTTRIS IMPSMNPDGY EKAKSDSSKP SVKCSGVVGR ANAKGVDLNR NFPDQFSGEM
SDESQLATET LLVKKWIDEV PFVLSANLHG GSLVANYPYD NRPDGKSDYS ETPDDDVFRS
LAQTYSSNHP KMHLPRAACV GDHFKDGITN GAEWYSVAGG MQDYNYVNSN SFELTMDVSC
CKFPDASTLQ GFWNDNKQSL LEYLKRVHTG LTGFVRDQNG QGIEGADINI GSRNHPVRSA
RDGDYWRLLL PGDYIVTVSK RGYDPVKRTV TIPKGLAKKE VFVLTSNGQA MDETGAQLEE
VVPDKEKKPV PISLVIGLTI VCVVSLLLAL ALAILIAKKY RGKESAQGEY SQVHTCP
//
