ID   S7VS90_9FLAO            Unreviewed;       676 AA.
AC   S7VS90;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Dipeptidyl carboxypeptidase Dcp {ECO:0000313|EMBL:EPR73120.1};
DE            EC=3.4.15.5 {ECO:0000313|EMBL:EPR73120.1};
GN   ORFNames=ADIWIN_1901 {ECO:0000313|EMBL:EPR73120.1};
OS   Winogradskyella psychrotolerans RS-3.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR73120.1, ECO:0000313|Proteomes:UP000014962};
RN   [1] {ECO:0000313|EMBL:EPR73120.1, ECO:0000313|Proteomes:UP000014962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-3 {ECO:0000313|EMBL:EPR73120.1,
RC   ECO:0000313|Proteomes:UP000014962};
RX   PubMed=23950132;
RA   Kumar Pinnaka A., Ara S., Singh A., Shivaji S.;
RT   "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, Isolated
RT   from the Marine Transect of Kongsfjorden, Ny-Alesund, Svalbard, Arctic
RT   Ocean.";
RL   Genome Announc. 1:e00630-e00613(2013).
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}.
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:EPR73120.1}.
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DR   EMBL; ATMR01000095; EPR73120.1; -; Genomic_DNA.
DR   RefSeq; WP_020897715.1; NZ_ATMR01000095.1.
DR   AlphaFoldDB; S7VS90; -.
DR   STRING; 641526.ADIWIN_1901; -.
DR   PATRIC; fig|641526.4.peg.1885; -.
DR   eggNOG; COG0339; Bacteria.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000014962; 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:EPR73120.1};
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:UP000014962};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          225..673
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   676 AA;  77098 MW;  7A5BB8C988A77D5B CRC64;
     MAVLNKPFNT PYNTAPFSEI KTEDYLPAFK EGIKKAKSEI DAITANTEAP TFENTIEALD
     YSGEELDRLS SIFFNLNSAE TNDEIQKIAQ DVSPLLSEFS NDITLNEDLF KRVKAVYDSK
     ARLDLTTEQE TLLDKKYKGF SRNGANLPED KKEKLRAIDK ELSQLKLKFG EHILAETNKF
     EMHLTDESDL SGLPEGAKEA AKQLAESKDK DGWLITLDYP SYIPFMTYAD NRALREELSK
     AFGRKGFQND ELDNQNIVLK IAQLRFERAQ LLGYKTHAHF VLEERMAETP AKVTSFLNEL
     LEKAKPAAKD EFEELESFAK ELDGIDQLQK WDSGYYSEKL KQKLFDLDDE QLKPYFKLEN
     VINGAFTVAE KLFGLQFEEI NTIDKYHDDV LTYKVTDADG ELVSIFYADF FPRAGKRNGA
     WMTSYKPQMI KDGKNERPHI SNVCNFTKPT KSKPSLLTFN EVTTLFHEFG HALHGMLANT
     TYPSISGTSV YWDFVELPSQ VLENWCYEKE ALELFATHYE TGEVIPMELV EKIKASATFH
     EGMQTLRQLS FGLLDMSWHG IDPSNITNVK SHEVEAFGDT SLYPDVAENC MSTSFSHIFQ
     GGYSSGYYSY KWAEVLDADA FEYFKEEGIF NKTVADKFKT FVLSQGGTDN PMTLYKKFRG
     QEPKPEALLR RAGLLK
//