HVT1_ARATH
ID HVT1_ARATH Reviewed; 1299 AA.
AC F4INY4; O80847; Q0WVL4; Q38800; Q8RYE1;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=DExH-box ATP-dependent RNA helicase DExH6 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000305};
DE AltName: Full=Protein HELICASE IN VASCULAR TISSUE AND TAPETUM {ECO:0000303|PubMed:9225469};
DE EC=3.6.4.12 {ECO:0000305};
GN Name=HVT1 {ECO:0000303|PubMed:9225469};
GN OrderedLocusNames=At2g30800 {ECO:0000312|Araport:AT2G30800};
GN ORFNames=F7F1.1 {ECO:0000312|EMBL:AAC20715.2},
GN T11J7.19 {ECO:0000312|EMBL:AAM14828.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia {ECO:0000312|EMBL:AAB01660.1};
RC TISSUE=Aerial part {ECO:0000312|EMBL:AAB01660.1};
RX PubMed=9225469; DOI=10.1046/j.1365-313x.1997.11061307.x;
RA Wei W., Twell D., Lindsey K.;
RT "A novel nucleic acid helicase gene identified by promoter trapping in
RT Arabidopsis.";
RL Plant J. 11:1307-1314(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-636.
RC STRAIN=cv. Columbia;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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: May function as an ATP-dependent RNA/DNA helicase.
CC {ECO:0000250|UniProtKB:F4IDQ6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000303|PubMed:9225469}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the tapetum and vascular
CC tissues. {ECO:0000269|PubMed:9225469}.
CC -!- SIMILARITY: Belongs to the DExH box helicase family. {ECO:0000305}.
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DR EMBL; U10245; AAB01660.1; -; mRNA.
DR EMBL; AC002340; AAM14828.1; -; Genomic_DNA.
DR EMBL; AC004669; AAC20715.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08442.1; -; Genomic_DNA.
DR EMBL; AK226731; BAE98834.1; -; mRNA.
DR PIR; H84712; H84712.
DR RefSeq; NP_850154.2; NM_179823.4.
DR AlphaFoldDB; F4INY4; -.
DR SMR; F4INY4; -.
DR STRING; 3702.AT2G30800.1; -.
DR iPTMnet; F4INY4; -.
DR PaxDb; F4INY4; -.
DR PRIDE; F4INY4; -.
DR ProteomicsDB; 232093; -.
DR EnsemblPlants; AT2G30800.1; AT2G30800.1; AT2G30800.
DR GeneID; 817631; -.
DR Gramene; AT2G30800.1; AT2G30800.1; AT2G30800.
DR KEGG; ath:AT2G30800; -.
DR Araport; AT2G30800; -.
DR TAIR; locus:2052841; AT2G30800.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_1_6_1; -.
DR InParanoid; F4INY4; -.
DR OMA; MWSSKRE; -.
DR OrthoDB; 278674at2759; -.
DR PRO; PR:F4INY4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4INY4; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004386; F:helicase activity; ISS:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd06007; R3H_DEXH_helicase; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034083; R3H_DEXH_helicase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF01424; R3H; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51061; R3H; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1299
FT /note="DExH-box ATP-dependent RNA helicase DExH6"
FT /id="PRO_0000435296"
FT DOMAIN 15..82
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT DOMAIN 197..366
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 537..711
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 987..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 313..316
FT /note="DEIH box"
FT /evidence="ECO:0000305"
FT MOTIF 1182..1200
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000303|PubMed:9225469"
FT MOTIF 1267..1283
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000303|PubMed:9225469"
FT COMPBIAS 993..1009
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 1006..1014
FT /note="VAANTNEEV -> A (in Ref. 1; AAB01660)"
FT /evidence="ECO:0000305"
FT CONFLICT 1156
FT /note="H -> P (in Ref. 1; AAB01660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1299 AA; 144479 MW; FE5F93C6B60F8826 CRC64;
MGNKRFRSDN NAGKPTSVEA TRIWATKVIE DFRASGNEVY TFEHNLSNNE RGVIHQMCRK
MGIQSKSSGR GEQRRLSIFK SRHKNGNKNE ANEKSNKEKL KCVSFPPGAD VILQELFTHY
PPCDGDTAAT SFTKYSGNKG KQGQWKDDFF RKPQISSEEI LEKVASLSSR LKKDKALKEI
TKLRSKLPIT SFKDAITSAV ESNQVILISG ETGCGKTTQV PQYLLDHMWS SKRETCKIVC
TQPRRISAMS VSERISCERG ESIGENIGYK VRLQSKGGRH SSVVFCTNGI LLRVLVGKGS
VSSVSDITHI IVDEIHERDC YSDFMLAIIR DLLPSNPHLR LILMSATLDA ERFSGYFGGC
PVVRVPGFTY PVRTLYLEDV LSILKSGGDN HLSSTNLSIS DHKLDLTDED KLALDEAIIL
AWTNDEFDAL LDLVSSRGSH EIYNYQHQST WLTPLMVFAG KGRISDVCML LSFGADWSLK
SKDGMTALEL AEAENQLEAA QIIREHADNS QSNSQQGQQL LDKYMATINP EQVDVSLIQQ
LMRKICGDSE DGAILVFLPG WDDINKTRQR LLENPFFADS AKFDIICLHS MVPAGEQKKV
FNRPPPGCRK IVLATNIAES AVTIDDVVYV IDSGRMKEKS YDPYNNVSTL QSSWVSKANA
KQRQGRAGRC QPGICYHLYS RLRAASMPDF KVPEIKRMPV EELCLQVKIL DPNCKTNDFL
QKLLDPPVDQ SIANALSILQ DIGALTPQEE LTELGEKFGH LPVHPLISKM LFFAVLVNCL
DPALTLACAA DYKEPFTMPM SPVERQKAAA AKLELASLCG GDSDHLAVVA AFECWKNAKG
RGLSAEFCSQ YFVSPSAMKM LDQMRSQLES ELKRHGIIPN DISSCSQNSR DPGILRAVLA
VGLYPMVGRL CPAFGNNRRT IVETASGAKV RVHSLSNNFN LSSKKYDESL LVFDEITRGD
GGMHIRNCTV ARDLPLLLIS TEIAVAPTGS SDSDDSNEEE EDDEEVAANT NEEVAANTNE
EGMDIHKEES RRGAKMMSSP ENSVKLVVDR WLPFRTTALE VAQMYILRER LMASILFKVT
HPREHLPPHL GASMHAIAGI LSYDGHAGLS CPPESMVPKH SRTEMYDTGG WEEKPNSFLN
SLFWSLSLKE NKHPSHTNRN QQHNYNMAPT EAASIPRQQN YKQRNPKATN NTDSGKKKEK
MFVNPTNRIN QPEAASTGKP SKHKSANSSG SSNKKENMPS DQAYGNKQHN TVPREAAAPM
AKNQSSKKTK TRSGNNSDSG KKKEQYIPKR QREDKAEQK
