ID A0A8J5YE53_9ROSI Unreviewed; 1760 AA.
AC A0A8J5YE53;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 15.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=CXB51_026381 {ECO:0000313|EMBL:KAG8481558.1};
OS Gossypium anomalum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=47600 {ECO:0000313|EMBL:KAG8481558.1, ECO:0000313|Proteomes:UP000701853};
RN [1] {ECO:0000313|EMBL:KAG8481558.1, ECO:0000313|Proteomes:UP000701853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JFW-Udall {ECO:0000313|EMBL:KAG8481558.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG8481558.1};
RA Grover C.E., Yuan D., Arick M.A., Miller E.R., Hu G., Peterson D.G.,
RA Wendel J.F., Udall J.A.;
RT "The Gossypium anomalum genome as a resource for cotton improvement and
RT evolutionary analysis of hybrid incompatibility.";
RL bioRxiv 0:0-0(2021).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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:ARBA00047984};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG8481558.1}.
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DR EMBL; JAHUZN010000010; KAG8481558.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000701853; Chromosome 10.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:TreeGrafter.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:TreeGrafter.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd22585; Rcat_RBR_DEAH12-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR FunFam; 1.20.120.1750:FF:000020; ATP-dependent RNA helicase DEAH12 chloroplastic; 1.
DR FunFam; 3.40.50.300:FF:001279; ATP-dependent RNA helicase DEAH12 chloroplastic; 1.
DR FunFam; 3.40.50.300:FF:002114; ATP-dependent RNA helicase DEAH12 chloroplastic; 1.
DR FunFam; 1.20.120.1080:FF:000033; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR056245; KH_DEAH11/12.
DR InterPro; IPR056246; KH_DEAH11/12_1st.
DR InterPro; IPR056247; KH_DEAH11/12_2nd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR056248; RBD_DEAH11/12.
DR InterPro; IPR056244; RRM_DEAH11/12.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF81; ATP-DEPENDENT RNA HELICASE DEAH11, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF24471; KH_DEAH11; 1.
DR Pfam; PF24638; KH_DEAH11_1st; 1.
DR Pfam; PF24641; KH_DEAH11_2nd; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF24475; RBD_DEAH11; 1.
DR Pfam; PF24637; RRM_DEAH11; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000701853};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 302..466
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 499..667
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1547..1755
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1551..1593
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1760 AA; 197786 MW; 09C10EE822ED2707 CRC64;
MKNFSSSSNH RHPPPPGGHK PYLQRQHQQS SYPNSFRCVP NFQAVNNKYY RRRFPSPAST
TDGSVNSNAL HCPNFIIQLV HDFSSSPSKP NDLQTLISQL DPSPQHSHIY TTGKIAASLI
FQEWSKTLSS VLHFWRSRLD GSIHYTPKLI SNVIVPSDTE ELNQNLKTLF SSHITGLMEG
ALVRKWQEKI NEKSDEIADL VGQMGKRKSS LGRFYELDDK KKALKAERSA ISKRLKEFKG
GMSSLLRCLE TWEIGNEEGD EGVKVYRVEG ELDWKLIHQL ILRECRRLED GLPIYAYRQE
ILTRIHGQQV MVLIGETGSG KSTQLVQFLS DSGIAANESI VCTQPRKIAA ISLAKRVREE
SIGCYSDNSV ICYPTFSSSQ QFDSKVIYMT DHCLLQHYMK DKNLSGISCI IVDEAHERSL
NTDLLLALVK DLLGRRFDLR LVIMSATANA NQLSDYFFGC GIFHLEGRNF PVDIKYVPCA
TEGTSGSGMV ATYVSDVLRM AAEIHKTEKE GNILAFLTSQ MEVEWACDHF EAPNAIVLPL
HGKLSFEEQC HVFQNYPGKR KIVFATNIAE TSLTIPGVKY VIDSGMVKES KFEPGTGMNV
LEVCWISQSS ANQRAGRAGR TEPGRCYRLY TESDFELMTS NQEPEIRRVH LGIAVLRIVA
LGIKNIQTFD FVDAPSSKAI DSATRNLIQL GAIVEKNGVF ELTDEGRYLV KLGIEPRLGK
LIISCFHCGL RREGLVLAAV MANASSIFCR VGNDDDKVKA DCLKVQFCHQ NGDLFTLLSV
YKEWEALPSD RKNKWCWENS INAKSMRRCQ DTVTELENCL KKEFAVIIPS YLIWDPHKST
ERDKTLKAII LSSLAENVAM YCGHDQLGYE VALTGQYVQL HPSCSLLIFG QKPSWVVFSE
LLSVTKQYLV CVTAFDYESL ATLDPPPLFD ASQMESRKLQ VKALTGFGST LLKKFCGKSN
HNIRSLSSRI KTICKDERIG VEVNVDQNEI LLFASSVDMQ KVLDFVTDVL ECEKKWLHNE
CMEKPLFHGR SASPSMALFG AGAEIKHLEV DKRYLAVDVF HSNLNAIDDK ELLMFFEKHS
NGGICSVHKS QANGQEIDDR EKWGKIMFLT PGAARKAAEL DGVDFSGSAL KVLPSQTSFG
GDHKMFSFPR VKAKLSWPRR LSKGIGIVKC DRLDVQNILY DFSSRLVIAG KYVNCEVSRK
CDDSVLIYGI DKELSDAEVR DILHSATERE IHDFFLVRGD AVENPTCGAC EEALWREISP
FMPKGNPYTN CCWVQVFEPE PKETFMKALI TFDGRLHLEA AKALEQLEGK VLPGCLSWQK
IRCQQLFHSS ISCSSSVYAV IKKQLDSLLA SFRHVKGADC FLETNENGSC RVRISANATK
TVAELRRPVE ELMNGRTVKH ASLTPSILQH LFSRDGINLM RSLQRETRTY ILFNRHSLNI
RIFGLPDDAA VAQKKLMQSL LSYHESKQLE VRLRGRGLPP DMMKEVVKKF GPDLHGLKEK
IPGAEFTLNT RHHIISICGN KEMKQKVEEI VLQIAEAGRD LAVRSDNEVS CPICLCEVED
GYRLDGCSHF FCRSCLLEQC ESAIKNLDSF PLCCAQQGCK APILLTDLKS LLSTEKLEEL
FRASLGAFVA SSGGAYRFCP SPDCPSVYRV AGPEAFGEPF VCGACYAETC TRCHLEYHPY
LSCEKYREFK EDPDLSLKEW CKGKEQVKTC PVCGYTIEKI DGCNHVECKC GRHVCWVCLE
FFSSSDDCYG HLRAVHMAII
//
