ID R5TCG7_9FIRM Unreviewed; 351 AA.
AC R5TCG7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Xaa-Pro dipeptidase {ECO:0000313|EMBL:CCZ54817.1};
GN ORFNames=BN540_00858 {ECO:0000313|EMBL:CCZ54817.1};
OS Dialister invisus CAG:218.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Dialister.
OX NCBI_TaxID=1263072 {ECO:0000313|EMBL:CCZ54817.1, ECO:0000313|Proteomes:UP000017966};
RN [1] {ECO:0000313|EMBL:CCZ54817.1, ECO:0000313|Proteomes:UP000017966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:218 {ECO:0000313|Proteomes:UP000017966};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {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:CCZ54817.1}.
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DR EMBL; CBAF010000115; CCZ54817.1; -; Genomic_DNA.
DR AlphaFoldDB; R5TCG7; -.
DR Proteomes; UP000017966; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01092; APP-like; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
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; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000017966}.
FT DOMAIN 6..123
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 133..334
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 351 AA; 40064 MW; 064292890EDB2288 CRC64;
MTEKMKIIDF LRENQLDAIF VQKDENCRYL SKFTGSDSYL LLTKEELYLL TDSRYTEQAR
KESADYTVVD YKGHLAEIVA KLAGEYHIKT MGVETVFSYQ MYLSFHEYMP NIEFRFSQID
RLRQIKSEEE IFCIKEACRI SDAGFKATLP FIRAGITEAR LRTILECAML EEGSEGKSFD
TIVASGERSA YPHGVATGKV LEDGDLVTFD FGAIYKGYHS DITRTVAIGD VSERLQKIYD
SVLYCNEHIE MQLKEGIICS EVDKSAREYL KKDGFESYFV HSLGHSVGLE IHESPFLSAR
DHTVLKENMI ETVEPGVYIP GIGGVRIEDT VVIKKDGIEV LTKFPKKFLR M
//
