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Database: UniProt
Entry: A0A256ICH0_9EURY
LinkDB: A0A256ICH0_9EURY
Original site: A0A256ICH0_9EURY 
ID   A0A256ICH0_9EURY        Unreviewed;        97 AA.
AC   A0A256ICH0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE            EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN   ORFNames=DJ70_15210 {ECO:0000313|EMBL:OYR54006.1};
OS   Halorubrum halodurans.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halorubrum.
OX   NCBI_TaxID=1383851 {ECO:0000313|EMBL:OYR54006.1, ECO:0000313|Proteomes:UP000216308};
RN   [1] {ECO:0000313|EMBL:OYR54006.1, ECO:0000313|Proteomes:UP000216308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cb34 {ECO:0000313|EMBL:OYR54006.1,
RC   ECO:0000313|Proteomes:UP000216308};
RX   PubMed=24782836; DOI=10.3389/fmicb.2014.00140;
RA   Fullmer M.S., Soucy S.M., Swithers K.S., Makkay A.M., Wheeler R.,
RA   Ventosa A., Gogarten J.P., Papke R.T.;
RT   "Population and genomic analysis of the genus Halorubrum.";
RL   Front. Microbiol. 5:140-140(2014).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYR54006.1}.
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DR   EMBL; NHPJ01000132; OYR54006.1; -; Genomic_DNA.
DR   RefSeq; WP_066414377.1; NZ_NHPJ01000132.1.
DR   AlphaFoldDB; A0A256ICH0; -.
DR   OrthoDB; 9287at2157; -.
DR   Proteomes; UP000216308; Unassembled WGS sequence.
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; 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   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:UP000216308};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT   DOMAIN          12..96
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
SQ   SEQUENCE   97 AA;  10994 MW;  6DF91FCAC0AF402F CRC64;
     MPSTEDIPTR LAQLKPQLER EYPISELGIF GSYARGEQRS DSDLDVLVAF DQPVTLFDLV
     RLENELTDEL GVEVDLVTKD SLKPRIEARV TDDLVYV
//
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