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Database: UniProt
Entry: D1PVM1_9BACT
LinkDB: D1PVM1_9BACT
Original site: D1PVM1_9BACT 
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
//
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