ID Q67Y44_ARATH Unreviewed; 452 AA.
AC Q67Y44;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE SubName: Full=Oxidoreductase, 2OG-Fe(II) oxygenase family protein {ECO:0000313|EMBL:AEE86616.1};
GN Name=ALKBH9C {ECO:0000313|TAIR:AT4G36090};
GN OrderedLocusNames=At4g36090 {ECO:0000313|Araport:AT4G36090,
GN ECO:0000313|EMBL:AEE86616.1};
GN ORFNames=T19K4.220 {ECO:0000313|EMBL:AEE86616.1}, T19K4_220
GN {ECO:0000313|EMBL:AEE86616.1};
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 {ECO:0000313|EMBL:BAD44387.1};
RN [1] {ECO:0000313|EMBL:AEE86616.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=10617198; DOI=10.1038/47134;
RG EU;
RG CSHL and WU Arabidopsis Sequencing Project;
RA Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Kotter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., Van Montagu M., Rogers J.,
RA Cronin A., Quail M., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA Montfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sehkon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L., Nelson J.,
RA Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffmann J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2] {ECO:0000313|EMBL:BAD44387.1}
RP NUCLEOTIDE SEQUENCE.
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AEE86616.1}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AEE86616.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
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DR EMBL; CP002687; AEE86616.1; -; Genomic_DNA.
DR EMBL; AK176624; BAD44387.1; -; mRNA.
DR RefSeq; NP_001031793.1; NM_001036716.2.
DR AlphaFoldDB; Q67Y44; -.
DR SMR; Q67Y44; -.
DR ProteomicsDB; 177104; -.
DR EnsemblPlants; AT4G36090.2; AT4G36090.2; AT4G36090.
DR GeneID; 829765; -.
DR Gramene; AT4G36090.2; AT4G36090.2; AT4G36090.
DR KEGG; ath:AT4G36090; -.
DR Araport; AT4G36090; -.
DR TAIR; AT4G36090; ALKBH9C.
DR OMA; EHEDISM; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q67Y44; baseline and differential.
DR GO; GO:0032451; F:demethylase activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR044842; ALKBH9B/ALKBH10B-like.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR31447:SF29; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR31447; HYDROXYPROLINE-RICH GLYCOPROTEIN FAMILY PROTEIN-RELATED; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q67Y44,
KW ECO:0007829|ProteomicsDB:Q67Y44};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT DOMAIN 253..350
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 78..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 50444 MW; 71F708A2B61468E6 CRC64;
MVDNMESEEV DNMESEEVDN KMDNIYDGKL CVSHSLDSLK AGAFVFGSLS DSVSHAMPSS
QSTVSEAASA QMSWADMGEE DGLEEEDQKE NELGSHGVDV SPSVGDSMKT PEKRKLSREE
RERYRFMNVK KMKVFSCYEK VRGRSVNILE GLELHTGVFS AVEQKKIVDF VYELQEKGRR
GELRERTFTA PHKWMRGKGR VTIQFGCCYN YAPDKAGNPP GILQRGDVDP MPSIFKVIIK
RLVGWHVLPP TCVPDSCIVN IYEEDDCIPP HIDNHDFLRP FCTVSFLSEC NILFGSNLKV
LGPGEFSGSY SIPLPVGSVL VLKGNGADVA KHCVPAVPTK RISITFRKMD ESKRPVGFTP
EPDLEEIKPL PYEHTTPSTP ADAVISSSRS SIDQNGSNHN NRTAHGGGSK YRRSRDYHSE
SRERSSSGQR RETSRHTPNR SYRPKVTSSD NV
//
