ID Q8TWQ0_METKA Unreviewed; 229 AA.
AC Q8TWQ0;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN OrderedLocusNames=MK0982 {ECO:0000313|EMBL:AAM02195.1};
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC Methanopyraceae; Methanopyrus.
OX NCBI_TaxID=190192 {ECO:0000313|EMBL:AAM02195.1, ECO:0000313|Proteomes:UP000001826};
RN [1] {ECO:0000313|EMBL:AAM02195.1, ECO:0000313|Proteomes:UP000001826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938
RC {ECO:0000313|Proteomes:UP000001826};
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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};
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DR EMBL; AE009439; AAM02195.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TWQ0; -.
DR STRING; 190192.MK0982; -.
DR PaxDb; 190192-MK0982; -.
DR EnsemblBacteria; AAM02195; AAM02195; MK0982.
DR KEGG; mka:MK0982; -.
DR PATRIC; fig|190192.8.peg.1029; -.
DR HOGENOM; CLU_1217517_0_0_2; -.
DR InParanoid; Q8TWQ0; -.
DR OMA; MATPWHL; -.
DR Proteomes; UP000001826; 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 Pfam; PF01909; NTP_transf_2; 1.
DR PIRSF; PIRSF005928; Nucleotidltrnsf; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001826}.
FT DOMAIN 22..64
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
SQ SEQUENCE 229 AA; 25771 MW; 7B1A1B5A983E8DE7 CRC64;
MDLREVRYTE EHWELLRTLR DRARKVVETL SQFGLEGWVH GSVARGDVRP GSDVDVFIPT
PVSPHVVDAF MDAAPFEVVG VTAVLPTPRD CVRIKVAMEE DVEVTFPITP PTDRELEFFD
FSGKLTPDSL ERDERVPGVD KRLRMIEPKP WGHVEYSILG REGEVATKLG VSTQLIHERV
RALTRRDKVG VQGVHAKVEG RPGEPVIELL RELGRRNPKA AEKLSELGV
//