ID A0A0P1FCV3_THAGE Unreviewed; 671 AA.
AC A0A0P1FCV3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Peptidyl-dipeptidase dcp {ECO:0000313|EMBL:CUH66005.1};
DE EC=3.4.15.5 {ECO:0000313|EMBL:CUH66005.1};
GN Name=dcp {ECO:0000313|EMBL:CUH66005.1};
GN ORFNames=TG4357_02183 {ECO:0000313|EMBL:CUH66005.1};
OS Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH66005.1, ECO:0000313|Proteomes:UP000051587};
RN [1] {ECO:0000313|EMBL:CUH66005.1, ECO:0000313|Proteomes:UP000051587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH66005.1,
RC ECO:0000313|Proteomes:UP000051587};
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CYSA01000019; CUH66005.1; -; Genomic_DNA.
DR RefSeq; WP_058262919.1; NZ_FOFW01000008.1.
DR AlphaFoldDB; A0A0P1FCV3; -.
DR STRING; 53501.SAMN04488043_108132; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000051587; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CUH66005.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000051587};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 226..667
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 671 AA; 74148 MW; B9160809C9D55011 CRC64;
MTNPLLSHWD TPFEIAPFDR IEDADFAPAF DIALAEHNAE IAAISGNPEA PTFANTIEAL
EAAGEGMHKV LSVFYTVAGA DSNPVREGLQ RDFSPKLAAH YAAISSNKPL FQRVEDLWQR
KDDLGLNAEQ ERVLMLTRRG FVRAGAALEG AADARMAAIK GRLATLGTEF TQNLLADERE
WFMEVAEDDL EGLPDFVTGA MRAAGKEKGV DGPIVTTSRS IITPFLQFSP RRNLREQAYR
AFVSRGANGG QHDNRAIAAE ILKLREERAQ LLGYDNFAAY KLETEMAKTP EKVEDLLLAV
WQPAKTQAEA DAKVLEQMMH DDGINGDLEA WDWHYYAARR RKAEHDLDEA ALKPYLQLDR
MIEAAFDCAN RLFGLEFKPL DAALYHPDCR AWNVTRGGKH VAVFIGDYFA RGSKRSGAWC
SAMRAQAKFP KDQTPVVINV CNFAKADPAL LSYDDARTLF HEFGHALHQM LSNVTYESIS
GTSVARDFVE LPSQLFEHWL EVPEVLSQFA THAETGEPMP QEMLDKVLGA ANFDQGFQTV
EYVASALVDL AFHKGAAPAD PMAMQADILD RLGMPKQIAM RHATPQFAHV FSGDGYSSGY
YSYMWSEVMD ADAFAAFEEV GNPFDPEMAR ALEANILSTG GSQEAEALYT AFRGRMPGVE
ALLKGRGLAA V
//
