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Database: UniProt
Entry: F2KQG4_ARCVS
LinkDB: F2KQG4_ARCVS
Original site: F2KQG4_ARCVS 
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
//
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