ID I7KE08_METBM Unreviewed; 101 AA.
AC I7KE08;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Nucleotidyltransferases {ECO:0000313|EMBL:CCJ37366.1};
GN OrderedLocusNames=BN140_2443 {ECO:0000313|EMBL:CCJ37366.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ37366.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(2012).
CC -!- SIMILARITY: Belongs to the MntA antitoxin family.
CC {ECO:0000256|ARBA:ARBA00038276}.
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DR EMBL; HE964772; CCJ37366.1; -; Genomic_DNA.
DR AlphaFoldDB; I7KE08; -.
DR STRING; 1201294.BN140_2443; -.
DR KEGG; mbg:BN140_2443; -.
DR PATRIC; fig|1201294.9.peg.2726; -.
DR HOGENOM; CLU_130257_10_0_2; -.
DR BioCyc; MBOU1201294:BN140_RS12115-MONOMER; -.
DR Proteomes; UP000009007; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR CDD; cd05403; NT_KNTase_like; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR33571:SF18; BSL3053 PROTEIN; 1.
DR PANTHER; PTHR33571; SSL8005 PROTEIN; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009007};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649};
KW Transferase {ECO:0000313|EMBL:CCJ37366.1}.
FT DOMAIN 16..94
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
SQ SEQUENCE 101 AA; 11172 MW; 6A3954B78CC66BD0 CRC64;
MRVSMQSREE IVATLQRLKD DIAARFSVSR IGTFGSVARG EQTEASDIDI LVEFSRLVGF
FAFLELEEYL SLHLGAPVDL VTPDALKPAI RERVAAEVAY A
//
