ID I1CAS9_RHIO9 Unreviewed; 1045 AA.
AC I1CAS9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=RO3G_10269 {ECO:0000313|EMBL:EIE85559.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE85559.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE85559.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
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DR EMBL; CH476739; EIE85559.1; -; Genomic_DNA.
DR AlphaFoldDB; I1CAS9; -.
DR STRING; 246409.I1CAS9; -.
DR VEuPathDB; FungiDB:RO3G_10269; -.
DR eggNOG; KOG0922; Eukaryota.
DR InParanoid; I1CAS9; -.
DR OMA; DPMVAPE; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd21691; GH2-like_DHX8; 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; IPR049588; DHX8_GH2-like.
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:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EIE85559.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT DOMAIN 393..556
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 574..754
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 80..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..180
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 118744 MW; F5954C0D85CBD386 CRC64;
MDELEQLEHL SLVQKVVSEL YNHTGLHEKV LAEFIIHLHD QANGSISTFK KLLKDADADF
PESFIENLDR IIKTMKPKNR KFNSAETSID EKTQAFPGLA VQDDPEWQKK REEDIEVADD
MLAQLQGISN NSRHRHERSS SPDNRRHNRR RSPRRSSPYR RYRSRSPSPS RHRRHHESSS
GRRRSREAER TRNPDRPSIR QKPSVTGGGI MVEDVPSRSI KRMSSPERWE LKQLIASGVV
DPADYPELNE DLDFHGSVEP EEEIDVEVRE EEPPFLRGQT KKSLDLSPVK VIKIPDGTLN
RSALAGASLA KERRELRQQQ QQQEMDAVPQ DVTTPWLDPM AGPAGRQFAQ DARGGSRPER
VSEWKKATFN NATSFGKVTN LSIQEQRESL PVFKLRSDLI NAVREANTGS GKTTQMTQYL
AEEGFANNGR IGCTQPRRVA AMSVAKRVAE EVGCRVGQEV GYTIRFEDCT SPETRIKYMT
DGMLLRECLI DPAMSQYSVV ILDEAHERTI STDVLFGLLK RAAKKRPDLK LIITSATLDA
DKFATYFNNC PIFTIPGRTY PVEVLYTKDP ESDYLDAALI TVMQIHLSEP PGDILLFLTG
QEEIDTAAEI LFERMKALGN DVPELIILPV YSALPSEMQS RIFDPAPLGS RKVVIATNIA
ETSITIDGIY YVIDPGFVKQ NKWDAKLGMD SLVVVPISQA AARQRAGRAG RTGPGKCYRL
YTEAAYRNEM LPNTIPEIQL LNLSMTVLTL KAMGVNDLLH FDFMDPPPEN NLIQALEQLY
ALQALDDEGL LTRLGRKMAE FPLEPQLSKM LIQSVDLGCS EEILTIVAML TAQNVFYRPK
EKQAQADQKK AKFHQPEGDH LTLLTVYNGW KNSKFSTVWC FENFIQQRSM KRAQDVRKQL
LGIMDRYRHD IVSCGRNYTK VCKALVSGYF RNAAKKDPQE GYKTLLEGTP VYIHPSSALF
NKGPEWVIYH EIVFTSKEYM REVTAIDPKW LTEAAPTFFR IADANKISKR KKQEKIEPLF
NRYEKPNEWR LSRARRGGRI SQTFG
//
