ID C6A1H9_THESM Unreviewed; 514 AA.
AC C6A1H9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Predicted metal-dependent hydrolase with the TIM-barrel fold {ECO:0000313|EMBL:ACS89474.1};
GN OrderedLocusNames=TSIB_0408 {ECO:0000313|EMBL:ACS89474.1};
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS89474.1, ECO:0000313|Proteomes:UP000009079};
RN [1] {ECO:0000313|EMBL:ACS89474.1, ECO:0000313|Proteomes:UP000009079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12597 / MM 739 {ECO:0000313|Proteomes:UP000009079};
RX PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(2009).
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DR EMBL; CP001463; ACS89474.1; -; Genomic_DNA.
DR AlphaFoldDB; C6A1H9; -.
DR STRING; 604354.TSIB_0408; -.
DR KEGG; tsi:TSIB_0408; -.
DR eggNOG; arCOG00691; Archaea.
DR HOGENOM; CLU_009942_3_1_2; -.
DR OrthoDB; 8791at2157; -.
DR Proteomes; UP000009079; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 3.10.310.70; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR033932; YtcJ-like.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS01137; TATD_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ACS89474.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009079}.
FT DOMAIN 57..511
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 514 AA; 58187 MW; ACA41C5DFB38583C CRC64;
MKKLWVSKLI HAFVNGKIYT SFQPKKVADG IVIAHEKILY VGDSKKATKI VKELGGEIID
LQGKTILPGF IDSHTHLNSL GQSLHMLDLN GTTSIDEFKE KLKKYAESVK TTWILGFGWD
QEDLGRYPTK EDIDEVIKDR PVFLSRTCFH AAVLNTKAIE LIGLEEGEDV DLERGIVKEN
ALERVRDVIN QNLTIEDYKQ FIEEGAKFAL SQGVTSIGFV SVNEKSLRAL LELDSEGKLP
IRVFVYLNPS LLEELKKLGL TKNIGSKRVK IMGIKILADG SLGARTAWLS KPYEDAPTSG
HPNISKEELE TIVQEAQQLG LQMAVHAIGD RTIDMVLDIY EKFGEERYRI EHASIIREDQ
IERMKKLGVV VSVQPRFVIS DWWAVQRVGK ERAKWIYPFN SMLKKGIPIG FGTDSPIEVV
NPWETVYAAV TRGKFEGIET YKYTEEECVS LEEALHLYIY GSAYIMHSEN ELGTLEEEKL
ADFIIVDKDP FEVEERELKN IKVLEAYVGG SKLY
//
