ID A0A090MXE4_STRRB Unreviewed; 1054 AA.
AC A0A090MXE4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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};
GN ORFNames=SRAE_1000354200 {ECO:0000313|EMBL:CEF65289.1,
GN ECO:0000313|WBParaSite:SRAE_1000354200.1,
GN ECO:0000313|WormBase:SRAE_1000354200};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF65289.1};
RN [1] {ECO:0000313|Proteomes:UP000035682, ECO:0000313|WBParaSite:SRAE_1000354200.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000354200.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CEF65289.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 Heterogonic {ECO:0000313|EMBL:CEF65289.1};
RA Aslett A.Martin.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:SRAE_1000354200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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}.
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DR EMBL; LN609528; CEF65289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090MXE4; -.
DR STRING; 34506.A0A090MXE4; -.
DR MEROPS; M14.A29; -.
DR EnsemblMetazoa; SRAE_1000354200.1; SRAE_1000354200.1; WBGene00260159.
DR WBParaSite; SRAE_1000354200.1; SRAE_1000354200.1; WBGene00260159.
DR WormBase; SRAE_1000354200; SRP06973; WBGene00260159; -.
DR eggNOG; KOG2637; Eukaryota.
DR eggNOG; KOG2649; Eukaryota.
DR OMA; QLNCHDY; -.
DR OrthoDB; 2873395at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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 NCBIfam; TIGR01167; LPXTG_anchor; 1.
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:CEF65289.1};
KW Hydrolase {ECO:0000313|EMBL:CEF65289.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CEF65289.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1054
FT /note="Carboxypeptidase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015031370"
FT TRANSMEM 980..998
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..153
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 252..262
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 1054 AA; 121172 MW; 0B1A088F5FB8259C CRC64;
MIIKFLLISI WFINLKVNCE LSWDSDIIAS DDDIEKSKSD ALIKYFGDRA ENSSIFLTYE
NISNIIGNYQ NVDKNRFHHH DYYSLTKFVK KINSTYSDIT HLYSIGHSVE DRELWVLIIS
KNPRKHELLK PEFKYVANMH GNEVLGRECL IYLTYFLCKN YGKNDYLTKL MNDVRIHLLF
SMNPDGYERS QIGDKMSGNG RSNANSIDLN RNFPANHPEH VELSGGVEIE EETKHVMSWI
KSFPFVLSAN LHGGSLVANY PFDDSESGKD GIYTPSLDDK LFVQLSYQYA RAHKDMWKTG
RRCGLGINGD TFYHGITNGA AWYHLAGGMQ DWQYLHTNTL EITIEMGCYK FPLSYMYEKL
WNDNMFALIA YIDMVRYGLK GIVKDIDGKP LINATVEIIG DKKGKIITTT DQGEYWRLLA
PGKYKIKFSH GYHISKIIDI FIKPRELIIN DIILENPPCN YSDNFKQEVY YRGFTEYTTM
IIGVDQFGKK IITNLLETLC NISLPYIKEL FKNTKIIALP EYIQGEHLPY IKAHSPTILI
YFGMGETKSI IYIPMDEVPK GFNKNILDES LNNYFGKYND NSCTGILNDE KLSEMAVDMK
LKKSFILGLG LGCNINITNN DDYIKNIILI INNIVYRAKK DSVEEYSVVP SVNPLDHFTP
QDVIASTSAG LNRIEESKYC NTKVKMLENM RIIEIGQQES GPRTLIMSIE ARTEHMIYQM
LSYLCEVSPT DHDYRVKRFM ENSKLIVIPE IPGTQLNCHD YSTIQPFEPL LSIIIKVYPD
IDYVIFMASG GLKVRYVNAS NTDMAYQLSE IYVKKHKLMV DGVWNICSKN NKMTYVNGEF
KWNNTNNDNW IKPDALLVQT GCCYEASGDG HLFEENKNSL FDLLENRLQG ISGRVIKRKK
YVGIKIKINI LKEGKLYKQV ETNPKVEGYY HVWLPVGDYT LETIDSSYPK TEIDFHISSA
TSVIIDINID TGDDSGNNSI LIIGIIIFIL ALGIYYYFKK HNSYKYFILD NRNEGFERIP
LRDNIDEDSD IDEDDNGEKL LSFKVEHGIT NGFS
//
