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ALKBH_ARATH
ID   ALKBH_ARATH             Reviewed;         345 AA.
AC   Q9SA98; A2RVV6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB;
DE            EC=1.14.11.-;
DE   AltName: Full=Alkylated DNA repair protein alkB homolog;
GN   OrderedLocusNames=At1g11780; ORFNames=F25C20.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative dioxygenase that may repair alkylated DNA or RNA by
CC       oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate
CC       and iron (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD30244.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007296; AAD30244.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28784.1; -; Genomic_DNA.
DR   EMBL; BT030097; ABN04835.1; -; mRNA.
DR   PIR; G86251; G86251.
DR   RefSeq; NP_172643.1; NM_101050.4.
DR   AlphaFoldDB; Q9SA98; -.
DR   SMR; Q9SA98; -.
DR   STRING; 3702.AT1G11780.1; -.
DR   PaxDb; Q9SA98; -.
DR   PRIDE; Q9SA98; -.
DR   ProteomicsDB; 245024; -.
DR   DNASU; 837723; -.
DR   EnsemblPlants; AT1G11780.1; AT1G11780.1; AT1G11780.
DR   GeneID; 837723; -.
DR   Gramene; AT1G11780.1; AT1G11780.1; AT1G11780.
DR   KEGG; ath:AT1G11780; -.
DR   Araport; AT1G11780; -.
DR   TAIR; locus:2027347; AT1G11780.
DR   eggNOG; KOG2731; Eukaryota.
DR   HOGENOM; CLU_029471_2_0_1; -.
DR   InParanoid; Q9SA98; -.
DR   OMA; WDTKKYS; -.
DR   OrthoDB; 1045321at2759; -.
DR   PhylomeDB; Q9SA98; -.
DR   PRO; PR:Q9SA98; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SA98; baseline and differential.
DR   Genevisible; Q9SA98; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0035516; F:oxidative DNA demethylase activity; IBA:GO_Central.
DR   GO; GO:0035515; F:oxidative RNA demethylase activity; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0035513; P:oxidative RNA demethylation; IBA:GO_Central.
DR   GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IBA:GO_Central.
DR   Gene3D; 2.60.120.590; -; 1.
DR   InterPro; IPR004574; Alkb.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR16557; PTHR16557; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; DNA damage; DNA repair; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..345
FT                   /note="Alpha-ketoglutarate-dependent dioxygenase alkB"
FT                   /id="PRO_0000066670"
FT   DOMAIN          225..345
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         232..234
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         245
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         299
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         336..342
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         336
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   345 AA;  39020 MW;  42882F3B7EA9376D CRC64;
     MYESANVSDD ADRTAFRRAE KKYKLYYEQD SKFSRKKKLP KPIDLSELLD FNLISQNFNN
     DGVLPDGIRV SKVDSSPVFC IDNRPGFYFI PDALSLKEQC KWIKESLTSF PQPPNRTNHN
     AIYGPIDDLF DSAKENKVLV QDDLTNNKWK FYEEVDIEKA TRSSCKSVSA SVLLRKLRWS
     TLGLQFDWSK RNYDVSLPHN NIPDALCQLA KTHAAIAMPD GEEFRPEGAI VNYFGIGDTL
     GGHLDDMEAD WSKPIVSMSL GCKAIFLLGG KSKDDPPHAM YLRSGDVVLM AGEARECFHG
     IPRIFTGEEN ADIGALESEL SHESGHFFAE YIKTSRININ IRQVF
 
 
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