ID D1PVM1_9BACT Unreviewed; 711 AA.
AC D1PVM1;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Peptidase family M3 {ECO:0000313|EMBL:EFA44591.1};
DE EC=3.4.-.- {ECO:0000313|EMBL:EFA44591.1};
GN Name=dcp {ECO:0000313|EMBL:EFA44591.1};
GN ORFNames=HMPREF0645_1006 {ECO:0000313|EMBL:EFA44591.1};
OS Hallella bergensis DSM 17361.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hallella.
OX NCBI_TaxID=585502 {ECO:0000313|EMBL:EFA44591.1, ECO:0000313|Proteomes:UP000003160};
RN [1] {ECO:0000313|EMBL:EFA44591.1, ECO:0000313|Proteomes:UP000003160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17361 {ECO:0000313|EMBL:EFA44591.1,
RC ECO:0000313|Proteomes:UP000003160};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (OCT-2009) 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}.
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:EFA44591.1}.
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DR EMBL; ACKS01000039; EFA44591.1; -; Genomic_DNA.
DR RefSeq; WP_007173120.1; NZ_GG704780.1.
DR AlphaFoldDB; D1PVM1; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_0_10; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000003160; 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 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:UP000003160};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 258..710
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 711 AA; 80291 MW; 83619D345B66CAD1 CRC64;
MNSNLKKTLL SATLASAVMI TGTDSASAQS GNSNPLLQKS TLPYGAPDFS KIKYEHYLPA
LKEGVRQQRA EIQRIVDNKE KPTFANTVLA LERTGVLLDR VTSVFYGLVS ADKTPEIAAT
EKVITPLLTD LENEISFNAK LFERVKYVYD HEYTTLQGEN KKLLEETYKN FVRSGALLPA
DKKARMEQIN KRISALQQDW GNRLPDATNN AVVWVNSKDE LAGLSDADIA QCRKDAESRG
GKAPYCIVIV NTTQQAILTN LENRDLRRRV FEASIHRADG SGKFNTFPIV VEMAKLRAEK
GELMGYKDFA SYSLERTMAK TSDNVYAFLK QLISAYSPKA DAETQAIETY ARKTMGNNFK
LQPYDRFYYS AKMKNEQFNF SEDDVKPYFN IDSVLTNGVF YAAHRVYGLS FNERTDIPTY
HKDMKVYEVF DKDGKPMGLF YCDYFRRPTK RGGAWMSTFA KQSHERNQLP VIYNVCNYAK
APEGQPTLIT WDEVTTLFHE FGHALHGFLS NCQYNSLSGT AVARDFVEMP SQFNESFATI
PEVFNNFARH TETGRHMPEE LKNKMLNSIN FHSAYALGEN LAATCLDLAW HTLTSQNIPS
ADKASEFETR VLKEIGLLNR QIPPRYSTSY FNHVWGGGYA AGYYSYLWTE VLADNIAQCF
AKRGALKPEV GQAFRDIILS RGNTRDLMKS FTEFTGLQSP DASALLKARG L
//