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Database: UniProt
Entry: Q8PXQ3_METMA
LinkDB: Q8PXQ3_METMA
Original site: Q8PXQ3_METMA 
ID   Q8PXQ3_METMA            Unreviewed;       102 AA.
AC   Q8PXQ3;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE            EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN   OrderedLocusNames=MM_1163 {ECO:0000313|EMBL:AAM30859.1};
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM30859.1, ECO:0000313|Proteomes:UP000000595};
RN   [1] {ECO:0000313|EMBL:AAM30859.1, ECO:0000313|Proteomes:UP000000595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC   {ECO:0000313|Proteomes:UP000000595};
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA   Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA   Fritz H.J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30859.1; -; Genomic_DNA.
DR   RefSeq; WP_011033112.1; NC_003901.1.
DR   AlphaFoldDB; Q8PXQ3; -.
DR   GeneID; 82160196; -.
DR   KEGG; mma:MM_1163; -.
DR   PATRIC; fig|192952.21.peg.1363; -.
DR   eggNOG; arCOG01206; Archaea.
DR   HOGENOM; CLU_130257_10_0_2; -.
DR   OMA; YMNLKFY; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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   Nucleotidyltransferase {ECO:0000313|EMBL:AAM30859.1};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649};
KW   Transferase {ECO:0000313|EMBL:AAM30859.1}.
FT   DOMAIN          17..93
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
SQ   SEQUENCE   102 AA;  11594 MW;  85F3E3B3C5032DD0 CRC64;
     MKLQSQRGVD IYIKKLQEML PELKKKYPIK YMGIFGSYIR GEQSPSSDLD ILVEFNGSIT
     LLGYARLENE LSDKLGIKVD LVSKTALKPR IGKHILLEVV EI
//
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