BTAF1_ARATH
ID BTAF1_ARATH Reviewed; 2045 AA.
AC B5BT18; Q9M378;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=TATA-binding protein-associated factor BTAF1;
DE Short=AtBTAF1;
DE EC=3.6.4.-;
DE AltName: Full=Protein BTAF1 homolog;
DE AltName: Full=Protein ROOT GROWTH DEFECTIVE 3;
GN Name=BTAF1; Synonyms=RGD3; OrderedLocusNames=At3g54280;
GN ORFNames=F24B22.240;
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF GLY-932.
RX PubMed=19054368; DOI=10.1111/j.1365-313x.2008.03750.x;
RA Tamaki H., Konishi M., Daimon Y., Aida M., Tasaka M., Sugiyama M.;
RT "Identification of novel meristem factors involved in shoot regeneration
RT through the analysis of temperature-sensitive mutants of Arabidopsis.";
RL Plant J. 57:1027-1039(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP MUTANT RGD3-1.
RX PubMed=14522871; DOI=10.1242/dev.00794;
RA Konishi M., Sugiyama M.;
RT "Genetic analysis of adventitious root formation with a novel series of
RT temperature-sensitive mutants of Arabidopsis thaliana.";
RL Development 130:5637-5647(2003).
RN [5]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
CC -!- FUNCTION: Involved in meristem development. Acts as positive regulator
CC of the CUC-STM pathway in shoot apical meristem (SAM) neo-formation.
CC {ECO:0000269|PubMed:19054368}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=B5BT18-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Impaired in root growth and true leaf
CC development. {ECO:0000269|PubMed:19054368}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB71002.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB440793; BAG70033.1; -; mRNA.
DR EMBL; AL132957; CAB71002.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79207.1; -; Genomic_DNA.
DR PIR; T47587; T47587.
DR RefSeq; NP_190996.3; NM_115288.8. [B5BT18-1]
DR AlphaFoldDB; B5BT18; -.
DR SMR; B5BT18; -.
DR STRING; 3702.AT3G54280.2; -.
DR iPTMnet; B5BT18; -.
DR PaxDb; B5BT18; -.
DR PRIDE; B5BT18; -.
DR ProteomicsDB; 239102; -. [B5BT18-1]
DR EnsemblPlants; AT3G54280.1; AT3G54280.1; AT3G54280. [B5BT18-1]
DR GeneID; 824595; -.
DR Gramene; AT3G54280.1; AT3G54280.1; AT3G54280. [B5BT18-1]
DR KEGG; ath:AT3G54280; -.
DR Araport; AT3G54280; -.
DR eggNOG; KOG0392; Eukaryota.
DR HOGENOM; CLU_000315_1_1_1; -.
DR OMA; SYDICRN; -.
DR PhylomeDB; B5BT18; -.
DR PRO; PR:B5BT18; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; B5BT18; baseline and differential.
DR Genevisible; B5BT18; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:1902185; P:positive regulation of shoot apical meristem development; IMP:UniProtKB.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR Gene3D; 1.25.10.10; -; 3.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR36498; PTHR36498; 1.
DR Pfam; PF12054; DUF3535; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..2045
FT /note="TATA-binding protein-associated factor BTAF1"
FT /id="PRO_0000423018"
FT REPEAT 3..40
FT /note="HEAT 1"
FT REPEAT 41..78
FT /note="HEAT 2"
FT REPEAT 584..621
FT /note="HEAT 3"
FT REPEAT 702..739
FT /note="HEAT 4"
FT REPEAT 1288..1325
FT /note="HEAT 5"
FT REPEAT 1367..1405
FT /note="HEAT 6"
FT DOMAIN 1463..1633
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1805..1976
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1990..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1584..1587
FT /note="DEAH box"
FT COMPBIAS 1990..2004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1476..1483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 932
FT /note="G->E: In rgd3-1; impaired in adventitious root
FT formation at the restrictive temperature of 28 degrees
FT Celsius. Impaired in shoot regeneration."
FT /evidence="ECO:0000269|PubMed:19054368"
SQ SEQUENCE 2045 AA; 227055 MW; D3D8D42603F71DE6 CRC64;
MAQQQSSRLN RLLTLLDTGS TQATRLTAAK QIGDIAKSHP QDLSSLLRKV LHHLRSKKWD
TRVAAAHAIG AIVLNVKHPS LSELLNSLAT KLGEAGISDN VDEVVAFRNL QSKILANAPF
RSFEMNKVLE FGALLASGGQ EYDILNDNSK NPRDRVARQK KNLRRRLGLD MCEQFMDVNE
MIRDEDLIEQ KSNVPANGVG NRLYANCSPH HIQQFVSRMV PRVNSRRPSA RELNLLKRKA
KISSKDQAKG SCEVADVEMS SSHVASTSKR ILSDSLDSSK ADIGNEDDIE PDGDGKWPFH
SFVEQLILDM FDPAWEIRHG SVMALREILM LHGGSAGVST EEFSSDNGFE LKDVLNKVTR
EREIDLNMQV SENELEPLRK RPKIEDPSKS FIDNTVLEVI GGDYDINVKD EDAEFLLPPV
KVNGQTDCSS TKLEPQSSMD DSTSHSEINH VAEVNNHFED KSFIEEPVIP KQQEENLEVL
DLVKQARHSW IKNFEFLQDC TIRFLCVLSL DRFGDYISDQ VVAPVREACA QALGATFKYM
NPSLIYETLN ILLQMQRRPE WEIRHGSLLG IKYLVAVRQE MLQDLLGYIL PACKAGLEDS
DDDVRAVAAD ALIPAAAAIV SLRGQTLLSI VMLLWDILLE LDDLSPSTSS IMNLLAEIYS
QDDMTLVMHE ELSLGEEQNI ELNEMGHIES IGERRDVKES PYALSGLAPR LWPFTRHDIT
SVRFSAIRTL ERLLEAGCRK NISGQSKSSF WPSSILGDTL RIVFQNLLLE STEEILECSE
RVWRLLVQCP VDDLEDTAKF YMASWIELAA TPYGSTLDAT KMFWPVAPPR KSHFKAAAKM
KAVKLENEAS SILGFDYARS SASLEKQEDA SARSTKIIVG SDMEMSVTRT RVVTASALGI
FASRLREGSM QFVVDPLSST LTSMSGVQRQ VGSIVLISWF RETKCKAPSD GSGSLPGFPS
PLKKWLLDLL ACADPAFPTK DIFLPYAELS RTYTKMRNEA SQLLHTVETC HCFDKLLSTN
KLNVESVTAD ETIDFASTLD LWNKESAGNE SLEKQVFEDV ESSRQQLLST AGYLKCVQSN
LHITVTSLVA AAVVWMSEFP ARLNPIILPL MASIKREQEQ ILQQIAAEAL AELIAYCVDR
KPSPNDKLIK NICSLTCMDP SETPQASIIS SMDIVDDMDF LSSRSNTGKQ KAKVVLASGE
DRSKVEGFIT RRGSELALKH LSLKFGGSLF DKLPKLWECL TEVLVPEIPS DQQKIDLKIE
SISDPQVLIN NIQVVRSIAP VMEETLKPRL LSLLPCIFKC VRHSHVAVRL AASRCVMTMA
KSMTTDVMAA VVESAIPMLG DLTCISGRQG AGMLIGLLVQ GLGVELVPYS PLLVVPLLRC
MSDVDSSVRQ SVTRSFAALV PMLPLARGVP PPVGLSKDLS SNAEDAKFLE QLLDNSHIDD
YKLCTELKVQ LRRYQQEGIN WLGFLKRFKL HGILCDDMGL GKTLQASAIV ASDAAERRGS
TDELDVFPSI IVCPSTLVGH WAFEIEKYID LSLLSVLQYV GSAQDRVSLR EQFNNHNVII
TSYDVVRKDV DYLTQFSWNY CILDEGHIIK NAKSKITAAV KQLKAQHRLI LSGTPIQNNI
MELWSLFDFL MPGFLGTERQ FQASYGKPLL AARDPKCSAK DAEAGVLAME ALHKQVMPFL
LRRTKEEVLS DLPEKIIQDR YCDLSPVQLK LYEQFSGSSA KQEISSIIKV DGSADSGNAD
VAPTKASTHV FQALQYLLKL CSHPLLVLGD KVTEPVASDL AAMINGCSDI ITELHKVQHS
PKLVALQEIL EECGIGSDAS SSDGTLSVGQ HRVLIFAQHK ALLDIIEKDL FQAHMKSVTY
MRLDGSVVPE KRFEIVKAFN SDPTIDVLLL TTHVGGLGLN LTSADTLVFM EHDWNPMRDH
QAMDRAHRLG QKRVVNVHRL IMRGTLEEKV MSLQKFKVSV ANTVINAENA SMKTMNTDQL
LDLFASAETS KKGGGSSKKG SEDNDQIAGT GKGMKAILGN LEELWDQSQY TEEYNLSQFL
TKLNG
