ID S2Y809_9BACL Unreviewed; 353 AA.
AC S2Y809;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Xaa-Pro dipeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1210_00445 {ECO:0000313|EMBL:EPD53622.1};
OS Paenisporosarcina sp. HGH0030.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae;
OC Paenisporosarcina.
OX NCBI_TaxID=1078085 {ECO:0000313|EMBL:EPD53622.1, ECO:0000313|Proteomes:UP000014412};
RN [1] {ECO:0000313|EMBL:EPD53622.1, ECO:0000313|Proteomes:UP000014412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGH0030 {ECO:0000313|EMBL:EPD53622.1,
RC ECO:0000313|Proteomes:UP000014412};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Paenisporosarcina sp. HGH0030.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:EPD53622.1}.
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DR EMBL; AGEQ01000004; EPD53622.1; -; Genomic_DNA.
DR RefSeq; WP_016426959.1; NZ_KE150421.1.
DR AlphaFoldDB; S2Y809; -.
DR STRING; 1078085.HMPREF1210_00445; -.
DR PATRIC; fig|1078085.3.peg.422; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_0_9; -.
DR Proteomes; UP000014412; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProt.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProt.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
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; IPR001714; Pept_M24_MAP.
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 PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000014412}.
FT DOMAIN 4..127
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 136..337
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 353 AA; 38765 MW; 5A5CDBF91F404A09 CRC64;
MEKLSKLREA LGEHQIDALL ITSGYNRRYI TDFTGTAGIA IVSKDQAVFI TDFRYTEQAA
KQIKNFEIVQ HTKTILEEVS VQLEKMNVRK VGFEKDDMSY AMYESYKKAV NTELVPVSGL
IEKIRLIKTP QEITIIKAAA DIAEAAFEHI LTFIAPGKTE LEVSNELEFF MRKQGASSSS
FDIIVASGLR SALPHGVATD KVIEKGDFVT LDFGALYNGY VSDVTRTVAI GEPSEQLKEI
YQIVLDSQLL SLEKIKPGMT GIEADAIARD YIKSKGYGEA FGHSLGHGIG LEVHEGPGLS
FRSETVLEEG MVITIEPGIY LPGVGGVRIE DDAIVTATGL EKLTHSTKEL LIL
//
