ID A0A0S6WVI5_9SPHN Unreviewed; 692 AA.
AC A0A0S6WVI5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE SubName: Full=Peptidyl-dipeptidase DCP {ECO:0000313|EMBL:GAM03120.1};
GN ORFNames=MBENS4_0119 {ECO:0000313|EMBL:GAM03120.1};
OS Novosphingobium sp. MBES04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1206458 {ECO:0000313|EMBL:GAM03120.1};
RN [1] {ECO:0000313|EMBL:GAM03120.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBES04 {ECO:0000313|EMBL:GAM03120.1};
RA Ohta Y., Nishi S., Kobayashi K., Tsubouchi T., Iida K., Tanizaki A.,
RA Kurosawa K., Adachi A., Nishihara M., Sato R., Hasegawa R., Hatada Y.;
RT "Draft Genome Sequence of Novosphingobium sp. Strain MBES04, Isolated from
RT Sunken Wood from Suruga Bay, Japan.";
RL Genome Announc. 3:e01373-14(2015).
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; DF850488; GAM03120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S6WVI5; -.
DR STRING; 1206458.MBENS4_0119; -.
DR HOGENOM; CLU_001805_4_0_5; -.
DR Proteomes; UP000053513; Unassembled WGS sequence.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 241..688
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT COILED 162..189
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 692 AA; 76800 MW; 6B7328FC8662A02E CRC64;
MTISTAHAAS DTAYDGIFAQ PSTLPFQAPD FTKIRDTDWQ PAIEAGIAQK RAEMKAIADN
PEAPTFENTL VAMQRAGVLY DRVYNVFGQL TSAATNDTLD AIDTAVSPQI SSMQDDIYLD
PKLFARVKAV HDSAAGQALT GEDAMLLKTE YAKFVHRGAL LSAAKKAELK AMNTQISKLE
TEFAQQLTQA NNAHAVVFDS AEELAGLTEG QISSAAKRAK EEGKPGKYVL PLINFTQQPV
LASLTNRDSR RRVFEESINR ASSGDEFDTT GIVTKLATLR AKKAELLGQP NFGTFQMYDR
MINTPEKAMA FMTGFTPALR TTQDREAALL LDAAKADGVT TLQPWDWTYY AEKVRKAKYD
LDESAIKPYF EVYNVLENGV FYAASQTYGL SFKRRTDIPV YHETMRVYEV TDKDGSALGL
FYFDPFSRPS KRGGAWMNNF VEQSDLLGNT PVIANTLNID PPAEGEPALA SWDNVTTMFH
EFGHALHGFF ASQTYPALSG TNTARDFVEF PSQFNENFAT VPEVLAHYAK HYETGAPLPE
GTIDKINAAS KFNQSVGFGE TLEAAMLDIK WHTLSPQEAA QDPMAFEKQA LYSMGLRSDL
IPPRYRTPYF RHIWDNGYAS GYYSYIWTEL LAHDGWDWVA KHGGMTRANG DHIRASFLGQ
GHSKDLDVLY RDFTGHDPEI GPMLEARGLS EK
//
