ID G5SWX6_9BACT Unreviewed; 610 AA.
AC G5SWX6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Creatinase {ECO:0000313|EMBL:EHG98357.1};
GN ORFNames=HMPREF9441_03904 {ECO:0000313|EMBL:EHG98357.1};
OS Paraprevotella clara YIT 11840.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHG98357.1, ECO:0000313|Proteomes:UP000003598};
RN [1] {ECO:0000313|EMBL:EHG98357.1, ECO:0000313|Proteomes:UP000003598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHG98357.1,
RC ECO:0000313|Proteomes:UP000003598};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
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:EHG98357.1}.
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DR EMBL; AFFY01000098; EHG98357.1; -; Genomic_DNA.
DR RefSeq; WP_008623189.1; NZ_JH376661.1.
DR AlphaFoldDB; G5SWX6; -.
DR STRING; 762968.HMPREF9441_03904; -.
DR GeneID; 78584571; -.
DR PATRIC; fig|762968.3.peg.3408; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_011781_2_4_10; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000003598; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}.
FT DOMAIN 16..140
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 319..531
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 541..600
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 610 AA; 69098 MW; FF6B92232E87C78C CRC64;
MHKWQNSIMN KNINKRVAEL RLHLRKNGLA AYIFPSTDPH HSEYPPEYWK TREWISGFNG
SAGTAVVTSD DAALWTDSRY FIAAEEQLKD TPFRLMKERL EGTPSVTQWL AEVLPPGSTV
GMDAWTNSAD EIRIIREELT HCGLHLEIAD QPADTLWKNR PALPDSPVRI QPPAFAGRSI
TEKLALIREA MAGRQADGLI LSTLDEIAWT LNLRGTDVHC TPVFVAYTWI TPSRCTLYIN
KVKLTEEVSA HLKEYGVETQ NYTDILPDLS RFDGKRIWTD CQTTNYALCR SLPETCSVVD
AASPVGLLKA VKHPAEVEGY RRAMLRDGVA MVKFLKWLIP AVQAGGQTEL SISRKLEELR
SEQDLFCGNS FDTIAGYAHH GAVVHYEPTP ETDLELLPKG LLLLDSGAQY EDGTTDITRT
IALGPVNEEE RHDYTLVLKG HIRLARAKFP QGCSGTQLDA CARYAMWQEG INYLHGTGHG
VGSCLCVHEG PHQIRMNYMP SPLLPYMTVT NEPGIYKEGR HGIRIENTQI ILPYRETEFG
TFLQFDPLTL CPIDMKPIDW SLLDTEEIEW LNRYHSRVYD QLAPLLDHEH RTWLREATRP
YEYTKPSQKS
//
