ID F2KQG4_ARCVS Unreviewed; 233 AA.
AC F2KQG4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN OrderedLocusNames=Arcve_1698 {ECO:0000313|EMBL:AEA47697.1};
OS Archaeoglobus veneficus (strain DSM 11195 / SNP6).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=693661 {ECO:0000313|EMBL:AEA47697.1, ECO:0000313|Proteomes:UP000008136};
RN [1] {ECO:0000313|EMBL:AEA47697.1, ECO:0000313|Proteomes:UP000008136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNP6;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Archaeoglobus veneficus SNP6.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002588; AEA47697.1; -; Genomic_DNA.
DR RefSeq; WP_013684353.1; NC_015320.1.
DR AlphaFoldDB; F2KQG4; -.
DR STRING; 693661.Arcve_1698; -.
DR GeneID; 10394824; -.
DR KEGG; ave:Arcve_1698; -.
DR eggNOG; arCOG04066; Archaea.
DR HOGENOM; CLU_1217517_0_0_2; -.
DR OMA; MATPWHL; -.
DR OrthoDB; 9287at2157; -.
DR Proteomes; UP000008136; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008136};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 30..67
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
SQ SEQUENCE 233 AA; 26566 MW; 17DC183FD1FE736A CRC64;
MRGKTATFGS RKNVVYSEEH WKLLERKREE AKKIMENLVR AGFRPILYGS VARGDVSPTS
DIDIFVPQLC PSYLIELAVD YMDRRIVQAT PNYAIKGELI VDESITVSFP LVKMKDRELD
FYRFGGCIGY DELLKGVRAA GVDKRLVLIL PNERGHEEVP INEMQPSEVA KILNVSIDIV
EERMRVLERR REVGRTGVFL CVSVPPGESF ESVLRDIAKK KPAVRRQIVE RMG
//