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Database: UniProt
Entry: G7WPU6_METH6
LinkDB: G7WPU6_METH6
Original site: G7WPU6_METH6 
ID   G7WPU6_METH6            Unreviewed;       120 AA.
AC   G7WPU6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE            EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN   OrderedLocusNames=Mhar_2103 {ECO:0000313|EMBL:AET65458.1};
OS   Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET65458.1, ECO:0000313|Proteomes:UP000005877};
RN   [1] {ECO:0000313|EMBL:AET65458.1, ECO:0000313|Proteomes:UP000005877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6Ac {ECO:0000313|EMBL:AET65458.1,
RC   ECO:0000313|Proteomes:UP000005877};
RX   PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA   Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT   "The genome characteristics and predicted function of methyl-group
RT   oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT   spp.";
RL   PLoS ONE 7:E36756-E36756(2012).
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; CP003117; AET65458.1; -; Genomic_DNA.
DR   RefSeq; WP_014587634.1; NC_017527.1.
DR   AlphaFoldDB; G7WPU6; -.
DR   STRING; 1110509.Mhar_2103; -.
DR   GeneID; 12511277; -.
DR   KEGG; mhi:Mhar_2103; -.
DR   PATRIC; fig|1110509.7.peg.2334; -.
DR   HOGENOM; CLU_130257_10_0_2; -.
DR   OrthoDB; 61846at2157; -.
DR   Proteomes; UP000005877; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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: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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005877};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649};
KW   Transferase {ECO:0000313|EMBL:AET65458.1}.
FT   DOMAIN          36..118
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
SQ   SEQUENCE   120 AA;  13355 MW;  B104F55AA319659C CRC64;
     MEVELSISAK KKTRSVSQRG VKTAEEIAEI LRSQMPELSR RYKVASIGIF GSYLRGEADE
     ESDIDLLVDL EDGDEPLTLL EFIALENHLS DLLGAKVDLV EKSALKPAIG RRILEEVQMV
//
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