ID Q8TR86_METAC Unreviewed; 106 AA.
AC Q8TR86;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN OrderedLocusNames=MA_1295 {ECO:0000313|EMBL:AAM04714.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM04714.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM04714.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108;
CC Evidence={ECO:0000256|ARBA:ARBA00034429};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + O-(5'-adenylyl)-L-tyrosyl-[protein] = diphosphate + O-
CC [5'-(adenylyl-(5'->3')-adenylyl)]-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:66528, Rhea:RHEA-COMP:13846, Rhea:RHEA-COMP:17046,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83624,
CC ChEBI:CHEBI:167160; Evidence={ECO:0000256|ARBA:ARBA00035071};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the MntA antitoxin family.
CC {ECO:0000256|ARBA:ARBA00038276}.
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DR EMBL; AE010299; AAM04714.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TR86; -.
DR STRING; 188937.MA_1295; -.
DR EnsemblBacteria; AAM04714; AAM04714; MA_1295.
DR KEGG; mac:MA_1295; -.
DR HOGENOM; CLU_130257_10_2_2; -.
DR InParanoid; Q8TR86; -.
DR OMA; IEVIYNV; -.
DR PhylomeDB; Q8TR86; -.
DR Proteomes; UP000002487; Chromosome.
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:SF14; PROTEIN ADENYLYLTRANSFERASE MJ0128-RELATED; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002487};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 21..103
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
SQ SEQUENCE 106 AA; 12232 MW; CEE1BBB8C47BA2C6 CRC64;
MKKTRYINMH TVEEREDLFR KISSFLKKYG ATKVSVFGSY VRGEEKPESD IDVLVEFAER
KSLLTLVNIE LELSDYLGIK VDLLTEKSIS PYLIDGIKKE ARVISE
//