ID Q6L0D6_PICTO Unreviewed; 357 AA.
AC Q6L0D6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Xaa-Pro dipeptidase {ECO:0000313|EMBL:AAT43566.1};
DE EC=3.4.13.9 {ECO:0000313|EMBL:AAT43566.1};
GN OrderedLocusNames=PTO0981 {ECO:0000313|EMBL:AAT43566.1};
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828 / KAW 2/3).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=1122961 {ECO:0000313|EMBL:AAT43566.1, ECO:0000313|Proteomes:UP000000438};
RN [1] {ECO:0000313|EMBL:AAT43566.1, ECO:0000313|Proteomes:UP000000438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
RC {ECO:0000313|Proteomes:UP000000438};
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Futterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
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DR EMBL; AE017261; AAT43566.1; -; Genomic_DNA.
DR RefSeq; WP_011177782.1; NC_005877.1.
DR AlphaFoldDB; Q6L0D6; -.
DR STRING; 263820.PTO0981; -.
DR MEROPS; M24.008; -.
DR PaxDb; 263820-PTO0981; -.
DR GeneID; 2844448; -.
DR KEGG; pto:PTO0981; -.
DR eggNOG; arCOG01000; Archaea.
DR HOGENOM; CLU_017266_4_0_2; -.
DR InParanoid; Q6L0D6; -.
DR OrthoDB; 1346at2157; -.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
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:SF2; XAA-PRO AMINOPEPTIDASE P-RELATED; 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:AAT43566.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAT43566.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:AAT43566.1}.
FT DOMAIN 12..132
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 139..341
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 357 AA; 40010 MW; E8C0BE647835F954 CRC64;
MDYKKIFDYT RRADAIIIFN GGEESIDKTF FYLTGARSGI FENSALIVTR DSIKIVTSKL
EESAARETGI ETLIFNKRSE MEDIIRNETK NFDSIGINYS SMTLSLYRDL MRMIPDKDFI
DVSESILEAR KIKEPEELEK IKNAAKIASD ALQDAIKKIK EGITESELAS EVAYSMMKLA
ATGPSFNTIV AFGKNSAIPH YSPGDKRLRP GDFVLIDYGA LYNRYCSDVT RTMVFGRASQ
EQRDIYETVK EAQQKSMDAI KAGKNGRDID AIARSIIDEK YPGKFIHSLG HGVGMDVHDH
PALSPSYDFI LKRNMVVTVE PGIYIPETGG VRIEDDVIVT DSGHTRITTA PRDLIEL
//
