ID B8GK24_METPE Unreviewed; 109 AA.
AC B8GK24;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN OrderedLocusNames=Mpal_1789 {ECO:0000313|EMBL:ACL17095.1};
OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX NCBI_TaxID=521011 {ECO:0000313|EMBL:ACL17095.1, ECO:0000313|Proteomes:UP000002457};
RN [1] {ECO:0000313|EMBL:ACL17095.1, ECO:0000313|Proteomes:UP000002457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c
RC {ECO:0000313|Proteomes:UP000002457};
RX PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA Yavitt J.B., Zinder S.H.;
RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL Genome Announc. 3:e01280-15(2015).
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; CP001338; ACL17095.1; -; Genomic_DNA.
DR AlphaFoldDB; B8GK24; -.
DR STRING; 521011.Mpal_1789; -.
DR KEGG; mpl:Mpal_1789; -.
DR eggNOG; arCOG01206; Archaea.
DR HOGENOM; CLU_130257_10_0_2; -.
DR OrthoDB; 61846at2157; -.
DR Proteomes; UP000002457; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002457};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 25..106
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
SQ SEQUENCE 109 AA; 12650 MW; 4D0F2B0A11A28CD8 CRC64;
MKRMIHRTRM TRSLEDMKGL LRERLPELRR TYGVTSMKIF GSWVRDEQTT RSDLDILIAF
DPVQKISLFN LVALEQELSA YLGVPVDLVE EETIKPALRH RILGEAVPL
//
