ID A0A0B0NLR6_GOSAR Unreviewed; 1335 AA.
AC A0A0B0NLR6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=F383_17074 {ECO:0000313|EMBL:KHG12734.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG12734.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN398233; KHG12734.1; -; Genomic_DNA.
DR Proteomes; UP000032142; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17982; DEXHc_DHX37; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KHG12734.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000032142}.
FT DOMAIN 290..482
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 657..840
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 46..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..621
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 149398 MW; FBE0D18696B205C8 CRC64;
MENSCPPVEL KTGQDALSIG IDINRMLFAY ICSLEASDSN ALILPTKRSK KRRGKDQELQ
RVKEKQNPKL SKSQIRKLKK IEEEKEKELF LSKSIEALEK YKIPEDVYSL LQSSKTIGQA
ETTREKRRTA IQFSKVGLEV PQCAKSSKVG DGDLLSSSEP EIELEELNPR KGISQNQIEQ
SIKVEKEVAK HAGDSLASSQ KLAFCKDLSA SCNYVDTLPT MEAFCKNNDA PLEEGMETCI
PKLPVDGGRK STISMGPLSA PTVVVHVSRP DEIENKRKDL PIVMMEQEIM EAINENSTVI
ICGETGCGKT TQVPQFLYEA GFGSNQSTIR SGVIGITQPR RVAVLATAQR VAFELGLHLG
KEVGFQVRHD KKIGGRCSIK FMTDGILLRE VQNDVLLKRY SVIVLDEAHE RSLNTDILIG
MLSRVIRLRQ DLYEKQQQMI LSGQSINPEN MIYPLNLVLM SATLRVEDFI SGRRLFCVPP
PVIEVPTRQY PVTIHFSKRT ELVDYIGQAF KKVMSIHKRL PPGGILVFVT GQREVEYLCR
RLRKASKGVI TNISKGDKRT EAAPNSQISS VEDINMKDIS DAFETNEDSA HQKTDRLSSY
DEDQYDYHED DSDASYDSET DSELETFDED GNTLDKKSME NSGNLVDVLG GDGSLASLKA
AFEALSGKNG LDSNPEGQEA VSINPESSLE QHSAPIEKVS EGNIGLNTGA LRVLPLYAML
PAAAQLRVFE EVKDGERLVV VATNVAETSL TIPGIKYVVD TGREKVKNYN PTNGMETYEI
QWISKASAAQ RAGRAGRTGP GHCYRLYSSA VFSNILPDFS CAEISKIPVD GVVLLMKSMG
IDKVANFPFP TSPGPTALVE AERCLKALEA LDGSGRLTSL GKAMAHYPMS PRHSRMLLTV
IQIMRRVKSY ARANLVLGYA VAAAAVLSST NPFVIQYEES HNQTDEPKRD DGSNPLDSEK
VLNKKEKSQK RKLKELAKMS RAKFSNPSSD TLTVAYALQC FELSESQVDF CNANALHLKI
MEEMSKLRKQ LLQLIFNQNV HCDVGQDFLW THGTMEDVEQ SWRVASSKYP LLQNEEELLG
QALCAGWADR VAKRIRGVSR SSEGDRKVNT VRYQACLVTE TVFLHRASSL SSSAPEFLVY
SELLQTKRPY MHGATSVKSD WLVKYAKSYC TFSAPLTDPR PYYDPQTDEV YCWVVPTFGP
HLWQLPMHNL QISSNAHRAT VFAYALLEGQ VLPCLKSVKQ FMSASPDIIL KPESYGQSRV
GNLLHKFKTW RIDSCGQLRK IWEDDSRALH SVILDWFQES FHKHFEMLWS EMLSEVLLDP
QERFPKRLKR DKRKK
//
