YZ38_AQUAE
ID YZ38_AQUAE Reviewed; 320 AA.
AC O66426;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Probable protein adenylyltransferase aq_aa38;
DE EC=2.7.7.n1;
GN OrderedLocusNames=aq_aa38;
OS Aquifex aeolicus (strain VF5).
OG Plasmid ece1.
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Probable adenylyltransferase that mediates the addition of
CC adenosine 5'-monophosphate (AMP) to specific residues of target
CC proteins. {ECO:0000250}.
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.n1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1;
CC -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
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DR EMBL; AE000667; AAC07978.1; -; Genomic_DNA.
DR RefSeq; NP_046426.1; NC_001880.1.
DR RefSeq; WP_010890572.1; NC_001880.1.
DR AlphaFoldDB; O66426; -.
DR SMR; O66426; -.
DR EnsemblBacteria; AAC07978; AAC07978; aq_aa38.
DR KEGG; aae:aq_aa38; -.
DR eggNOG; COG3177; Bacteria.
DR HOGENOM; CLU_064957_0_0_0; -.
DR InParanoid; O66426; -.
DR OrthoDB; 1232677at2; -.
DR Proteomes; UP000000798; Plasmid ece1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3290.10; -; 1.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR InterPro; IPR040198; Fido_containing.
DR InterPro; IPR041657; HTH_17.
DR InterPro; IPR010093; SinI_DNA-bd.
DR PANTHER; PTHR13504; PTHR13504; 1.
DR Pfam; PF02661; Fic; 1.
DR Pfam; PF12728; HTH_17; 1.
DR SUPFAM; SSF140931; SSF140931; 1.
DR TIGRFAMs; TIGR01764; excise; 1.
DR PROSITE; PS51459; FIDO; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Nucleotidyltransferase; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..320
FT /note="Probable protein adenylyltransferase aq_aa38"
FT /id="PRO_0000187004"
FT DOMAIN 76..206
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT BINDING 100..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 157..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 320 AA; 37061 MW; A395DC9B53D8647A CRC64;
MTYQNGVEVL LEEFLDYLTK EETICSLEIE KLKVSIDELE KETDEPRVLQ GINYFRTAKE
VYQLSRKAYE TKEEVVSEAL ILWIYENLWK GFNVPKGYRK SDMVIFGAKF SPPPPYVVPN
LIRTIVNWLR NEKTIDVVKK SIIFHTLFEV IHPFPDGNGR VGRILLNAIL VENGLLNVAF
RNREKYISAL REAEEGAIVV VEKLSRGRKI DYSSITETVE YYGNLNVFDE LIRTEMMHSL
KVYSNIKQVF LTPEEAAKLL GLKNKDYVRV LIHRGKLKAV KEEGKWKIPL SEVVKNFEHK
LKGEEFKLAN NLFKGKLSPS
