ID I1NRZ0_ORYGL Unreviewed; 1227 AA.
AC I1NRZ0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA01G0263000.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA01G0263000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 AlphaFoldDB; I1NRZ0; -.
DR STRING; 4538.I1NRZ0; -.
DR EnsemblPlants; ORGLA01G0263000.1; ORGLA01G0263000.1; ORGLA01G0263000.
DR Gramene; ORGLA01G0263000.1; ORGLA01G0263000.1; ORGLA01G0263000.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_1_6_1; -.
DR OMA; HMECGSA; -.
DR Proteomes; UP000007306; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd06007; R3H_DEXH_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
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; 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 InterPro; IPR034083; R3H_DEXH_helicase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR PANTHER; PTHR18934:SF213; 3'-5' RNA HELICASE YTHDC2; 1.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 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 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; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51061; R3H; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 49..112
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 220..400
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REPEAT 483..515
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 570..744
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1037
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 134955 MW; ABD7F24202E14BDD CRC64;
MVRRGRKGKD AAAGAGGTGG RGGGAGRGGG RGGSGGGGGG GGGGGGVREA TLVRVSKVLE
DFQASDAQVY KFEPGISKQE RAAIHEMCRK MGMISKSSGN GERRCLSVYK RKQNQGLETE
EGPSHLGFSV EARNVLQDLF MHYPPDDAEL NGHTVRNSSD KAVKIQWKPD GAFCRPALRK
QDILKKVEML ASKVNKSEQL RKIVQDRSKL PISSYKDAIS STLENHQVVL ISGETGCGKT
TQVPQYILDH MWGKGESCKI VCTQPRRISA ISVAERISAE RGESVGDTVG YKIRLESKGG
KNSSIMFCTN GVLLRLLIGR VTNISKEQNQ KRSFDDAVTG ITHIIVDEIH ERDRFSDFML
AILRDLLPLY PHLRLVLMSA TIDAERFSNY FSGCPFIQVP GFTHPVKTFY LEDVLSILQS
VGDNHLDPTT DDLKQSSLLT DDYKSSMDEA INLALDNDEF DPLLELISGE QNQEIFNYQH
SETGVTPLMV LAGKGQVGDI CMLLSFGVDC STRDHDGKSA LDWAEQGNQQ EVCEVIKKHM
ECGSAKLTEE NELLNKYLAT INPEHIDTVL IERLLRKICV DSNEGAILVF LPGWEDINQT
RERLLASPFF QDSSKFLVLS LHSMIPSSEQ KKVFKRPPAG SRKIILSTNI AETAVTIDDV
VFVIDSGRMK EKSYDPYNNV STLHSSWVSK ANARQRQGRA GRCQPGTCYH LYSRFRAASL
LEYQIPEIKR MPIEELCLQV KLLDPNCRIA DFLRKTLDPP VPETVRNAIT VLQDLGALTQ
DEQLTELGEK LGSLPVHPST SKMLLFGILM NCLDPALTLA CAADYRDPFL LPMAPDERKR
AAAAKVELAS LYGGYSDQLA VVAAMDCWRR AKDRGQEAQF CSKYFVSSNT MNMLSNMRKQ
LQNELAQRGF VPVDASACSL NARDPGIIRA VLMAGAYPMV GRLLPPRKNT RRAVIETASG
AKVRLHPHSC NFNLSFRKTS GNPLVIYDEI TRGDGGMYIK NSSVVGSYPL IILATEMVVA
PPEDDDSDEE DGDSSEDETE KVTLGQHKEI MSSPDNSVSV VIDRWLRFDA TALDVAQIYC
LRERLASAIL FKVKHPQDVL PPDLGATMYA IACILSYDGL PAMITSDDVA TSQGSNQSSA
ESSRFSQGRR VGYIPPGGFL MSLLSDKPLN APHFQKSFNH PDGASGHIRS SRTSVGRFDQ
SRHPQRNNSG PGSSAARTFK RQRNGAQ
//