ID G0HP64_THES4 Unreviewed; 234 AA.
AC G0HP64;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN OrderedLocusNames=GQS_10105 {ECO:0000313|EMBL:AEK73914.1};
OS Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK73914.1, ECO:0000313|Proteomes:UP000000874};
RN [1] {ECO:0000313|EMBL:AEK73914.1, ECO:0000313|Proteomes:UP000000874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX PubMed=21914870; DOI=10.1128/JB.05851-11;
RA Wang X., Gao Z., Xu X., Ruan L.;
RT "Complete genome sequence of Thermococcus sp. strain 4557, a
RT hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT area.";
RL J. Bacteriol. 193:5544-5545(2011).
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; CP002920; AEK73914.1; -; Genomic_DNA.
DR RefSeq; WP_014013596.1; NC_015865.1.
DR AlphaFoldDB; G0HP64; -.
DR STRING; 1042877.GQS_10105; -.
DR GeneID; 11016703; -.
DR KEGG; the:GQS_10105; -.
DR PATRIC; fig|1042877.9.peg.1974; -.
DR eggNOG; arCOG04066; Archaea.
DR HOGENOM; CLU_1217517_0_0_2; -.
DR OMA; MATPWHL; -.
DR OrthoDB; 9287at2157; -.
DR Proteomes; UP000000874; Chromosome.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR009185; Nucleotidl_trans.
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 PIRSF; PIRSF005928; Nucleotidltrnsf; 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 Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649};
KW Transferase {ECO:0000313|EMBL:AEK73914.1}.
FT DOMAIN 31..81
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
SQ SEQUENCE 234 AA; 27396 MW; 6105DB55F79CEAC6 CRC64;
MPREKVVRVW DEREVVYPPK RWRYLREKRE KALKIMERLS QFDPQLYGSV ARGDVRRESD
IDIFIPYRVP SYLIELALEG LVSRRKIVMA TPWHLIKGVI EIDEETTVTF PLIDPTDREL
EFYRWGGAVD LRGVKTNERV PGVNKKLILI VPTERGHIER EVVGRESEVA RILSVSIDIV
TERVHVLTRR DAIGRTGIYI NEEVPDWMSF EEALKVIADR DPNVRRKVRE RGGI
//