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Database: UniProt
Entry: C3N8Q5_SULIY
LinkDB: C3N8Q5_SULIY
Original site: C3N8Q5_SULIY 
ID   C3N8Q5_SULIY            Unreviewed;       218 AA.
AC   C3N8Q5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE            EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN   OrderedLocusNames=YG5714_2161 {ECO:0000313|EMBL:ACP46410.1};
OS   Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=439386 {ECO:0000313|EMBL:ACP46410.1, ECO:0000313|Proteomes:UP000002308};
RN   [1] {ECO:0000313|EMBL:ACP46410.1, ECO:0000313|Proteomes:UP000002308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.G.57.14 / Yellowstone #1 {ECO:0000313|Proteomes:UP000002308};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001403; ACP46410.1; -; Genomic_DNA.
DR   RefSeq; WP_012714147.1; NC_012622.1.
DR   AlphaFoldDB; C3N8Q5; -.
DR   GeneID; 8762151; -.
DR   KEGG; siy:YG5714_2161; -.
DR   HOGENOM; CLU_1217517_0_0_2; -.
DR   OMA; MATPWHL; -.
DR   Proteomes; UP000002308; 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   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT   DOMAIN          28..60
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
SQ   SEQUENCE   218 AA;  25263 MW;  97844F9C116E6BAF CRC64;
     MQIDYTERHW KILNGKRKIA IEILSLLKQY GMEGYVYGSV ARGDVNEKSD VDVIVFNPNQ
     IVLDTLNVNH KYIVQATPNS APKAYLSIDE EETIVISFPL GRLRRNEIEF YSFGGLVDLK
     DLLENRRVPG VNKKLMLIIP TENGHMEIPL EGNEDYVSKL LKISLDTIME RKRLLTKRIE
     RGHTGIFLRY DLSGNESIYD AFNKMYKSNK FFKRMVDV
//
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