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Database: UniProt
Entry: Q6AS20_DESPS
LinkDB: Q6AS20_DESPS
Original site: Q6AS20_DESPS 
ID   Q6AS20_DESPS            Unreviewed;       366 AA.
AC   Q6AS20;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   SubName: Full=Related to Xaa-Pro dipeptidase {ECO:0000313|EMBL:CAG34855.1};
GN   OrderedLocusNames=DP0126 {ECO:0000313|EMBL:CAG34855.1};
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG34855.1, ECO:0000313|Proteomes:UP000000602};
RN   [1] {ECO:0000313|Proteomes:UP000000602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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DR   EMBL; CR522870; CAG34855.1; -; Genomic_DNA.
DR   RefSeq; WP_011187371.1; NC_006138.1.
DR   AlphaFoldDB; Q6AS20; -.
DR   STRING; 177439.DP0126; -.
DR   KEGG; dps:DP0126; -.
DR   eggNOG; COG0006; Bacteria.
DR   HOGENOM; CLU_017266_4_2_7; -.
DR   OrthoDB; 9806388at2; -.
DR   Proteomes; UP000000602; Chromosome.
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:UP000000602}.
FT   DOMAIN          6..141
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          149..350
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
SQ   SEQUENCE   366 AA;  40637 MW;  62AC0C6FB6C63642 CRC64;
     MNYAKRIKKI QKTLSRKNLD ALLVSQPENR RYLSGYTGGD HGIGETSGVL IIPAKGKVHL
     LTDFRYQLQA EQDASWTKVL IYTKGLIPLL LKLLPELGIK TLAFESDYTL HSFAKSLREK
     LGTVGVTTTP SLNLIEKMRL IKDEDEIDAI RRSVLLNEAV FQEVYADLKP GITETELAIK
     IEATMRRRGA ERPSFDTIVA SGKNSALPHA VPGMDKIRKE SPLTIDMGLI LDGYCSDMTR
     TFVLGKPGKK YLKYHRLVRR AQLAGMKAVR AGVTGQEVDA VARKIISDAG YGEYFGHSLG
     HGVGLAVHEN PRLSFSNNKK LREGMIVTVE PGIYIPGWGG IRLENMVVVR KDGCENLNQD
     TTFLDL
//
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