ID W7IHS4_9PSEU Unreviewed; 344 AA.
AC W7IHS4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Putative Xaa-Pro dipeptidase {ECO:0000313|EMBL:EWC59898.1};
DE EC=3.4.13.9 {ECO:0000313|EMBL:EWC59898.1};
GN ORFNames=UO65_4901 {ECO:0000313|EMBL:EWC59898.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC59898.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC59898.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC59898.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
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:EWC59898.1}.
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DR EMBL; AYXG01000184; EWC59898.1; -; Genomic_DNA.
DR AlphaFoldDB; W7IHS4; -.
DR STRING; 909613.UO65_4901; -.
DR PATRIC; fig|909613.9.peg.4899; -.
DR eggNOG; COG0006; Bacteria.
DR Proteomes; UP000019277; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
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 Dipeptidase {ECO:0000313|EMBL:EWC59898.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EWC59898.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:EWC59898.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019277}.
FT DOMAIN 2..115
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 123..327
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 344 AA; 35683 MW; 3DF2DD84312F7087 CRC64;
MIAPGSDLRY LLGGTVVSHE RFTGLVLPAE GEPVLVVPKL EAAGYDPYDL PGLGVDTATW
VDGEDPYGLV ARLVGGPGVV AVGDMLPAVH VLGLRGALPG AEQALAGPVL RGLRMRKDAA
EVEQLRRAGA AIDRVHARMG EWLRAGRTEA EVAADIGAAI VAEGHASAEF VIVGSGPNGA
SPHHEVSDRV ITAGDVVVVD IGGPLPSGYC SDSTRTYAVG EPRDADVVES YEVLRRAQAA
SVASVRPGVS AESVDAAGRG VLADAGLAEF FIHRTGHGIG LDVHEHPYIV AGNELVLEPG
MAFSVEPGVY LPGRWGARIE DIVVVTDTGV EPLNTRPHEL VVLG
//
