ID I1BJA3_RHIO9 Unreviewed; 1061 AA.
AC I1BJA3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=ATP-dependent RNA helicase DOB1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=RO3G_00987 {ECO:0000313|EMBL:EIE76283.1};
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:EIE76283.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE76283.1, 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).
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; CH476732; EIE76283.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BJA3; -.
DR STRING; 246409.I1BJA3; -.
DR VEuPathDB; FungiDB:RO3G_00987; -.
DR eggNOG; KOG0948; Eukaryota.
DR InParanoid; I1BJA3; -.
DR OMA; IMLKNYN; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000009138; 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:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18024; DEXHc_Mtr4-like; 1.
DR CDD; cd13154; KOW_Mtr4; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 2.40.30.300; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT DOMAIN 153..309
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 387..588
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 31..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 120394 MW; 2EAEF5538FC60A04 CRC64;
MFDEESLFNV FSGEAATDNF DDVDDEEILD DVDETTQTKR RNSIIAEDQN AKKQRTESNE
QQKMREEIEQ QPTPIVADTF EQETSRQVAN IAGLQGQAAV AAEGEQIVLS HQVRHQVAVP
PNYPYVPISQ HVPPADPARV YPFTLDPFQR VAVSSIERNE SVLVSAHTSA GKTVVAEYAI
AQCLKNKQRV IYTSPIKALS NQKYREFTEE FGDVGLMTGD VTINPQASCL VMTTEILRSM
LYRGSEVIRE VAWVVYDEIH YMRDSERGVV WEESIILLPD VVRYVFLSAT IPNAMEFAEW
ICKIHQQPCH IVYTDFRPTP LQHYLFPAGG DGIHLVVDEK SRFREDSFQK AIAALSDGKG
DDPSGTRARG KKGKTYKGGN ANDGPADIYR IIKMVMMKNY HPVIVFSFSK KECEANALLM
SKLDFNDENE RDMVSQVFTN AISGLNEDDR QLPQIQQLLP LLRRGIGVHH GGLLPIMKET
IEVLFQEGLL KVLFATETFS IGLNMPAKTV VFTSVRKYDG KGTRWVTSGE YIQMSGRAGR
RGLDERGVVI MMIDEKMEPA VAKGMVKGES DRMNSAFHLS YNMILNLLRV EGVSPEYMLE
KCFYTFQSDS NIPQFEKQLK QLEEEKNSII IKDEEEISGY YELRKQIDTF TQDVHDVMIH
PTYALPFMQP GRLVRVEHDK MDFGWGVILN HQKVFGKKRA SDGEREVNYV VDVLLNCSQD
SSLAKDAAGQ PTGVRPATND DNRNLLVIPV SLRAIQSISH IRLVLPKDLR SSDARKTVYK
SILEVKKRFQ GNIPLLDPIN NMGIKDPSFQ KLVSKILNLE KKVMEHPLSK SEDLPNMYEV
YTKKMEIVDK MKSLKRKLVD AQSIVQLEEL KNRKRVMRRL GFTTSSDVVE MKGRVACEIS
TGDELLLTEM IFQGVFNDLT VDQSVAVLSC FVFDEKVDVK AKLQEELSAP LRLMQETARR
IAKVATECKM PLDEEEYVAK FKPELMDVVF AWCQGAKFSQ ICKMTTVYEG SLIRVFRRLE
ELLRQMCAAA KSIGNTELEN KFSEGINRIH RDIIFAASLY L
//