ID A0A0V1CEM0_TRIBR Unreviewed; 971 AA.
AC A0A0V1CEM0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Carboxypeptidase D {ECO:0000256|ARBA:ARBA00014107};
DE EC=3.4.17.22 {ECO:0000256|ARBA:ARBA00012811};
DE AltName: Full=Metallocarboxypeptidase D {ECO:0000256|ARBA:ARBA00030819};
DE Flags: Fragment;
GN Name=CPD {ECO:0000313|EMBL:KRY47438.1};
GN ORFNames=T03_6964 {ECO:0000313|EMBL:KRY47438.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY47438.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY47438.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY47438.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Releases C-terminal Arg and Lys from polypeptides.;
CC EC=3.4.17.22; Evidence={ECO:0000256|ARBA:ARBA00000614};
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:KRY47438.1}.
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DR EMBL; JYDI01000243; KRY47438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CEM0; -.
DR Proteomes; UP000054653; 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 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:SF73; CARBOXYPEPTIDASE D; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 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:KRY47438.1};
KW Hydrolase {ECO:0000313|EMBL:KRY47438.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KRY47438.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..971
FT /note="Carboxypeptidase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006875811"
FT TRANSMEM 930..948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..150
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 247..257
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
FT NON_TER 971
FT /evidence="ECO:0000313|EMBL:KRY47438.1"
SQ SEQUENCE 971 AA; 111718 MW; 3BE9EC0A5809955E CRC64;
MIQEQFFFII LFSLFAAIHS KLKFSSNKPA EFIFNFQHFE RKHEKSEDLY NNVKYFTHTG
SKIFIGKFKE PTDFRHHHYD DLVQWMHRFS IKFPKITHLY SIGQSVEGRE LLVMAISDFP
KIHEPGEPEF KYIGNMHGNE VVGRECLLYL IHVLCENYGE NSFITHLIDN TRIHIMPSMN
PDGYENAVEG DIMDYTGRNN SNNVDLNRNF PCRFPHLCQD AAPMQPEVKA VINWSHRIPF
VLSANLHGGS TIVNYPYDDN VNNISQDTPA PDAAVFKTIG YSYARAHPNM WMSGYRCGFQ
GYGQYMPDGL INGAVWYPLS GGMQDWNYLH TNNFELTIEM NCYKYPFAST LQNYWNDHKY
SLLLFINEVH SSLSGFVVDS SGSPLSGVTI FVQGIEHNVT SNKDGDYWRK FDFAPNPSPS
IIQMTRLNLK NISSTEIMRA MQLLASDESI HLIILLHDFA NQAIISNKAA IMLANNKLIT
QVSAFLMDYT NHASEIGCFM TTDTQIIDKI LPNKIMENFP MVILGIQASQ CSKVLPALPF
EFVDKFYPGM KNLLTAFVAV EWQGFYGKFK SSPFSSHPVL RLRRLFTHQI IVTPLNETYI
FPVPSGVYDI QVSDSSEKIY YSTTKYVPPS LWIEMDLLSL TMDRHTTASS RLTIRVSEIC
PTAVHVKGFK SGFHKNIFKS GEGPIRITWI SVDNFGQEML INLMKYFCSF SNDFMPNEIM
KNFTMYFVFY SSDKENCKAT PASESENDWI EVLSKSIIEP FLIKMNSFEI TDMQCSSSES
QGRKTVEIEP TTLKVQDANN GILTCSFCFM LQIACCNDTL NTDLWFENFD YLKEFLKRVS
QGIQGRIVSN KAYKNDVYYN LTVKNRMYNR SFRWNVTSNF YLPLLPGIYE MKITKKLGKY
ILKTAKISNT TRNLMQIDFF MEEDSSNANI FIFVALLLTI GIIAAFVYHN YSRKMHAMSP
YGYKNVPLID F
//