ID G5HA64_9BACT Unreviewed; 737 AA.
AC G5HA64;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN ORFNames=HMPREF9450_01529 {ECO:0000313|EMBL:EHB91480.1};
OS Alistipes indistinctus YIT 12060.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=742725 {ECO:0000313|EMBL:EHB91480.1, ECO:0000313|Proteomes:UP000006008};
RN [1] {ECO:0000313|EMBL:EHB91480.1, ECO:0000313|Proteomes:UP000006008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12060 {ECO:0000313|EMBL:EHB91480.1,
RC ECO:0000313|Proteomes:UP000006008};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Alistipes indistinctus YIT 12060.";
RL Submitted (AUG-2011) 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:EHB91480.1}.
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DR EMBL; ADLD01000013; EHB91480.1; -; Genomic_DNA.
DR RefSeq; WP_009134335.1; NZ_JH370372.1.
DR AlphaFoldDB; G5HA64; -.
DR STRING; 742725.HMPREF9450_01529; -.
DR PATRIC; fig|742725.3.peg.1621; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_0_10; -.
DR Proteomes; UP000006008; 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:UP000006008};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 286..733
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT REGION 20..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 82753 MW; 1AAF24C59D5D4CB2 CRC64;
MAFYPPYTAA LGSAVSGMNA PAGEQDGSTG ISSASSTRSS TDIASPDDSI SGGLLPCDSL
SCNPLLQRWP GPHATPAFDR IRNEHYLPAF RHALREARAE VAAIAGNPGE PTFANTVEAL
EFSGRRLDDI GNIFFNLNEA CTDDEMQRIA LEVSPLLTAF GNDISLDPVL FARVRAVYDN
RDSLELTVEQ TRLLEKTYKW FTRGGAALEE ADKETFRALT AELSQLSLQF TQNVLAATNA
FVLHLTDPGQ VDELPASVRD GAAAEARERG LDGWVITLQA PSMVPFMTYS SDRKLKERLW
RAYNSRCYGD AYDNTEIVTR IVALRLRLAN LLGYPTYADY VLEERMARTP QRVREFLDEL
LERAIVPARG DVREVVDFAR SAGAAYELMP WDYGYWQERL KRARYTLDEE QLKPYFRLEN
VQHGAFLLAG KLYGLTFHEN PDIPVYHPDV RAFEVCDGDG TFLAVLYMDY FPRASKRGGA
WMTEFRPQYV EQGCEIRPLI SIVCNFTKPT DRQPSLLTFN EVTTLLHEFG HALHGMLACG
RYPALTGTNV YRDFVELPSQ LMENWATEKE FLDLWAVHYR TGEKIPADLV QKIVDAKNFQ
AAYLHIRQVS FGLSDMAWHT VTAPVEGGVA EFERRAIGKA QLLPYVAGQC MATAFGHIFS
GGYAAGYYGY KWAEVLDADA FSLFRERGIF NPDVAEAFRT NILEKGGAEH PMTLYVRFRG
REPDSRALFE RMGIRDK
//
