ID C5A5T5_THEGJ Unreviewed; 359 AA.
AC C5A5T5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Xaa-Pro dipeptidase (PepQ) {ECO:0000313|EMBL:ACS33597.1};
DE EC=3.4.13.9 {ECO:0000313|EMBL:ACS33597.1};
GN Name=pepQ-1 {ECO:0000313|EMBL:ACS33597.1};
GN OrderedLocusNames=TGAM_1095 {ECO:0000313|EMBL:ACS33597.1};
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117 {ECO:0000313|EMBL:ACS33597.1, ECO:0000313|Proteomes:UP000001488};
RN [1] {ECO:0000313|EMBL:ACS33597.1, ECO:0000313|Proteomes:UP000001488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3
RC {ECO:0000313|Proteomes:UP000001488};
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
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DR EMBL; CP001398; ACS33597.1; -; Genomic_DNA.
DR AlphaFoldDB; C5A5T5; -.
DR STRING; 593117.TGAM_1095; -.
DR MEROPS; M24.008; -.
DR PaxDb; 593117-TGAM_1095; -.
DR KEGG; tga:TGAM_1095; -.
DR PATRIC; fig|593117.10.peg.1094; -.
DR eggNOG; arCOG01000; Archaea.
DR HOGENOM; CLU_017266_4_2_2; -.
DR Proteomes; UP000001488; 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 NCBIfam; NF040821; dipep_PepQ_Arch; 1.
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:ACS33597.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACS33597.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:ACS33597.1}.
FT DOMAIN 13..135
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 143..345
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 359 AA; 40527 MW; 2429345650B8FFD9 CRC64;
MTLSDTRLVI QMRIERLREF IAEKELDGVI ITHRPNIYYF TGSAPVLGGY LIITADDALF
LVPQLEYEEA RETSRVPVEA FKRGPELFER LKSFRLKKLG IEGRTAYSTV QSYREKLGVE
EFVTVDDVIK ELRMIKTKEE LEVIQAACEI ADQAMLTAIE EISEGKRERE IAAKMEYVMK
MKGAEKPAFD TIIASGWRSA LPHGVASDKR IERGELVVID EGALYNHYNS DTTRTIVVGS
PNEKQKDIYQ AVLEAQKKGV EMARPGITAK ELDTIVRDVI KEYGYGDYFI HSTGHGVGLE
IHEWPGVNQS DETVLKPGMV ITVEPGIYIP KFGGVRIEDT IVITENGARR LTKTERELI
//
