ID D9Q1M9_ACIS3 Unreviewed; 227 AA.
AC D9Q1M9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN OrderedLocusNames=ASAC_0811 {ECO:0000313|EMBL:ADL19217.1};
OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS 345-15).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus.
OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL19217.1, ECO:0000313|Proteomes:UP000000346};
RN [1] {ECO:0000313|EMBL:ADL19217.1, ECO:0000313|Proteomes:UP000000346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC {ECO:0000313|Proteomes:UP000000346};
RX PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT a new order, Acidilobales, and suggests an important ecological role in
RT terrestrial acidic hot springs.";
RL Appl. Environ. Microbiol. 76:5652-5657(2010).
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; CP001742; ADL19217.1; -; Genomic_DNA.
DR RefSeq; WP_013266729.1; NC_014374.1.
DR AlphaFoldDB; D9Q1M9; -.
DR STRING; 666510.ASAC_0811; -.
DR GeneID; 9499046; -.
DR KEGG; asc:ASAC_0811; -.
DR eggNOG; arCOG04066; Archaea.
DR HOGENOM; CLU_1217517_0_0_2; -.
DR InParanoid; D9Q1M9; -.
DR OMA; MATPWHL; -.
DR OrthoDB; 9287at2157; -.
DR Proteomes; UP000000346; 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 Reference proteome {ECO:0000313|Proteomes:UP000000346};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649};
KW Transferase {ECO:0000313|EMBL:ADL19217.1}.
FT DOMAIN 23..100
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
SQ SEQUENCE 227 AA; 25568 MW; E6778E044356F711 CRC64;
MIQGVRVKYD SERWEILRGK RALAEVLLRA LGGLSAFVYG SVARGDVRPS SDVDVVVLDN
VSPFMVEVRL EAAGLRPYAK EIVQATPNYV PKAYIYLDPD LKVTVSFPLG RMRKREAEFY
SWGGKLDLDG LRKGLRVPGV NKELNLIVPT EDGHIEYPVA GHEAEVARLL NISLDTVEER
LRVLSRRREV GRTGTFLKVE VPPDEPIEDA VRRIAGRNEF FRRAVDL
//