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Database: UniProt
Entry: F6BAK5_METIK
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Original site: F6BAK5_METIK 
ID   F6BAK5_METIK            Unreviewed;        45 AA.
AC   F6BAK5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE            EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN   OrderedLocusNames=Metig_1484 {ECO:0000313|EMBL:AEF97018.1};
OS   Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanotorris.
OX   NCBI_TaxID=880724 {ECO:0000313|Proteomes:UP000009227};
RN   [1] {ECO:0000313|EMBL:AEF97018.1, ECO:0000313|Proteomes:UP000009227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5666 / JCM 11834 / Kol 5
RC   {ECO:0000313|Proteomes:UP000009227};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Chertkov O., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M.,
RA   Whitman W., Woyke T.;
RT   "Complete sequence of Methanotorris igneus Kol 5.";
RL   Submitted (MAY-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; CP002737; AEF97018.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6BAK5; -.
DR   STRING; 880724.Metig_1484; -.
DR   KEGG; mig:Metig_1484; -.
DR   HOGENOM; CLU_3194504_0_0_2; -.
DR   Proteomes; UP000009227; 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; 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:UP000009227};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT   DOMAIN          2..41
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
SQ   SEQUENCE   45 AA;  5423 MW;  6B9E9E9DE9BB03AA CRC64;
     MHKKELKEKY KIKSIEIFGS YTRNEQKETS DVDILVEFYE ALDLI
//
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