ID A0A2T7NRZ2_POMCA Unreviewed; 1133 AA.
AC A0A2T7NRZ2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Cytosolic carboxypeptidase-like protein 5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=C0Q70_17221 {ECO:0000313|EMBL:PVD23945.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD23945.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD23945.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD23945.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD23945.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) 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:PVD23945.1}.
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DR EMBL; PZQS01000010; PVD23945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7NRZ2; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg10.
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:InterPro.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR12756:SF12; CYTOSOLIC CARBOXYPEPTIDASE-LIKE PROTEIN 5; 1.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT DOMAIN 10..151
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 239..314
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 355..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 125784 MW; 50C17BB0AAA10007 CRC64;
MEARFGNLTF TSKFDSGNLA RVEKVSKEDD EEVSNANVNY YLGDLRHDAE FNLWTKPDCA
GSPAENSNRS WFYFGVRGWV PNRLIKFNIM NMNRQGKLYG QGYTPLTRLL PSRPKWERIR
DKPTFEVIDN QFILTFTYRF PDLKGGTCYF AFSYPWSYTE SQEQLQILDK RFEHCLHMSP
GSPPERLYYH RELLCYSLDK LRVDLLTITS CHGNTFCRET RFDKHLFPDQ DTPRCYKFKD
KRVFLLSSRV HPGETPGSFV FNGFLDFILR ENDLRAAQLR QQYVFKLIPM LNPDGVMRGH
YRTDQRGMNL NRMYLDPSPI LHPSIYAAKS LLVYHHVMNQ LPRLGGEPLK IHINFPCDEQ
SSGKDGPGVP NSPQERSGGD QDVLQSGEHD ITLSSDSHKQ TTRRQNETKT KSYQHPLVSA
SLKHVPAIQS NSEKWLEANI AGGTTSLELL SQQESAKVEP LNLTDLYMSD ESASDSCPPA
GLENNQIFHV SSSSSSVVSL DKLHLPATGM VNGQAEMHHV DSELCLHLSE LNMSEDLCSN
TLADDASFDS DTEATERLGN EGSEDEEASP VTLEGLSGNC SPHLSDAQLL EIHPHDSGVA
FYMDLHGHAS KRGCFIYGNY FDNEDIQLES ILYAKLIALN SAHFDFGACN FSERNMYLKD
KRDGFSKEGS GRVAIYKAIG IIHSYTLECN YNMGRLVNSV PPAFRDDGRA TPPPLAGFPP
KFTQAHYEEV GRAVAVAVLD MRDTNPWSRV SLSEYNSIHG LRDWVRRYLR SLRGGPRIPR
NPSLKSMNKN GNNGLPGKSD LTPVQNTTRV SAGRVIGLDS SSRASAIRQT SQNSATTGRR
ELAPVKEATR NTTFSNMRTQ MRRHSSTSSS PPKLSSLSGP SLPVPPVQTQ GNSEHYSMMT
TSSIAADTKV AIARRGGPTS RIPLPTSQSR LTLTAQANSL SDAGLTSADA SLSRTLPASL
LQSTMQNQPL AQVHIVGSQM LQASAPPPSP THSQAQEAPQ PSRALMSLAG APSLSSTHSL
LHKDQLQPPT GLKSLTGIGE SKSPRRRYWN VRRRTQVASP KPGVAKGQNK GAVSGGGDVE
PAKSHRCKRR GPRKPIVVNE APVVVSSKMT AVQEEEMGQG ISSFLFYFHK NLF
//