ID A1S187_THEPD Unreviewed; 256 AA.
AC A1S187;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=UBA/THIF-type NAD/FAD binding protein {ECO:0000313|EMBL:ABL79217.1};
GN OrderedLocusNames=Tpen_1822 {ECO:0000313|EMBL:ABL79217.1};
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL79217.1, ECO:0000313|Proteomes:UP000000641};
RN [1] {ECO:0000313|Proteomes:UP000000641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX PubMed=18263724; DOI=10.1128/JB.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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DR EMBL; CP000505; ABL79217.1; -; Genomic_DNA.
DR RefSeq; WP_011753482.1; NC_008698.1.
DR AlphaFoldDB; A1S187; -.
DR STRING; 368408.Tpen_1822; -.
DR EnsemblBacteria; ABL79217; ABL79217; Tpen_1822.
DR GeneID; 4602059; -.
DR KEGG; tpe:Tpen_1822; -.
DR eggNOG; arCOG01676; Archaea.
DR HOGENOM; CLU_013325_10_4_2; -.
DR OrthoDB; 7915at2157; -.
DR Proteomes; UP000000641; Chromosome.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000641}.
FT DOMAIN 12..241
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 256 AA; 27978 MW; 59735234E144ADB6 CRC64;
MKDLSPEELE RYDRQIRVWG VEAQKKLKSS TVLVVGAGGL GSPVAFYLVA AGVGKLIIVD
AEDVELSNLN RQILHWTSDL GKAKVESAKE KLEKLNPHVE VVTLKQKIRS LEDALKLVED
ADVVVDCLDN WSTRFLLNEA CVKLGKPLVH GAVRGLYGQL TVVKPFEGPC LRCILPREPP
EERPFPVAGP TPGVIGSLEA LEVIKILTGY GEPMVGRLLF YDGVRNTFDV VKVERRPDCP
VCGVSVRKVA SGGKTS
//
