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Database: UniProt
Entry: I1BJA3_RHIO9
LinkDB: I1BJA3_RHIO9
Original site: I1BJA3_RHIO9 
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
//
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