ID A0A2C9V5D8_MANES Unreviewed; 1446 AA.
AC A0A2C9V5D8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=MANES_10G119700 {ECO:0000313|EMBL:OAY39763.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY39763.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY39763.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY39763.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) 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};
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DR EMBL; CM004396; OAY39763.1; -; Genomic_DNA.
DR EnsemblPlants; OAY39763; OAY39763; MANES_10G119700.
DR Gramene; OAY39763; OAY39763; MANES_10G119700.
DR Proteomes; UP000091857; Chromosome lg10.
DR GO; GO:0005524; F:ATP binding; 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; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd00048; DSRM_SF; 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; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857}.
FT DOMAIN 623..799
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 899..1074
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1446 AA; 161317 MW; 2A5F24415A963778 CRC64;
MAPKKKQQKH NNKANSSSSK SKSQSSSSGP RLQISAENEN RLRRLLLNSD RSTHPASAAS
VQDNLSKTQK AKRLKNVYEK LSCEGFSNDQ IELALTSLKD NATFESALDW LCLNLPGNEL
PLKFSSGISL HTNQGSVSVV STARGDWTPP VNPIKTEVDV QPVSVRIKGR WDDDDTLDSR
QPSQADWIRQ YMEQQEEDDS QMWEDYAVDG SFSNKDPALR SYDIIAKEYY AARLEATKAK
EEGDKKSQEQ AGHIIRKLKQ ELSSLGLSDE ILAQEFSHNR GFGSGSEGTL TSTIPHEQLQ
AKTSSSTIGQ SNFVAFPKES PVNVLDMENS SSKEFPEKPV LSCESAQGTI VIVDDARDVE
LGGLFFEDAA SNEALPPEVL ELQKKEKMRE LSSGKNLEKL DGIWKKGDPQ KIPKAVLHQL
CQKSGWEAPK FNKILERKKG FSYSVSILRK ASGRGKSRKS GGLITLQLPE QDEAYESAED
AQNRVAAFAL HQLFPDIPIH LIVTDPYASL ILQWKEGESS IKAENTLEDR KAGFVDWLLN
ADGSTETVAT RLSETLDNSH VEDINNSRDA AIDPVAGREN HTRDVESSHL RQEQEKKKKM
QKYKEMLKTR SALPIAGLKD DILQMLKENN FLVVCGETGS GKTTQVPQFI LDDMIESGRG
GQCNIICTQP RRIAAISVAE RVSDERCEAS PGLNGSLVGY QVRLDSARSE KTKLLFCTTG
ILLRRLAGDR NLTGITHVIV DEVHERSILG DFLLIVLKNL IEKQSDHGNP KLKVILMSAT
VDSTLFSSYF GHCPVLTAQG RTHPVTTYFL EDIYESINYH LASDSPAALR YETSTINKSG
PVNNRRGKKN LVLSGWGDDS LLSEDYVNPH YVSSTYCSYG EQTQQNLKRL NEDVIDYDLL
EDLICHVDET FDEGAILVFL PGVSEIYMLF DRLAASYRFG GESADWILPL HSSIASIDQK
KVFLRPPENI RKVIIATNIA ETSITIDDVV YVIDCGKHKE NRYNPQKKLT SMVEDWISQA
NARQRRGRAG RVKPGTCFCL YTCHRYEKVM RPYQVPEMLR MPLVELCLQI KILSLGHIKP
FLSKALEPPK DEAMTSAISL LYEVGALEGD EELTPLGHHL AKLPVDLLIG KMMLYGAIFG
CLSPILSISA FLSHKSPFVY PKDERQNVER AKLALLTDKL DGSSDSNESD RQSDHIVMMV
AYKKWEKILN EKGVKAAQQF CSSYFLSSSV MFMIRDMRIQ FGTLLADIGF INVPKKYQNL
GKNKENLGSW LSDKSQPFNM YSHHSSIVKA ILCAGLYPNV AATEQGITTT AINSLKQSSS
PAIKGHPVWY DGRREVHIHP SSINSNLRAF QHPFLVFLEK VETNKVFLRD TTIISPFSIL
LFGGVINIQH QTGLVTIDGW LKLAAPAQSA VLFKELRSAL HSLLKELIQK PKNQGSHGSV
PGRHEN
//
