GenomeNet

Database: UniProt
Entry: D9Q1M9_ACIS3
LinkDB: D9Q1M9_ACIS3
Original site: D9Q1M9_ACIS3 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system