ID V9D6N3_9EURO Unreviewed; 1069 AA.
AC V9D6N3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=ATP-dependent RNA helicase DOB1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=G647_06395 {ECO:0000313|EMBL:ETI22321.1};
OS Cladophialophora carrionii CBS 160.54.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI22321.1, ECO:0000313|Proteomes:UP000030678};
RN [1] {ECO:0000313|EMBL:ETI22321.1, ECO:0000313|Proteomes:UP000030678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI22321.1,
RC ECO:0000313|Proteomes:UP000030678};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; KB822706; ETI22321.1; -; Genomic_DNA.
DR RefSeq; XP_008728938.1; XM_008730716.1.
DR AlphaFoldDB; V9D6N3; -.
DR GeneID; 19984888; -.
DR VEuPathDB; FungiDB:G647_06395; -.
DR HOGENOM; CLU_002902_0_1_1; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000030678; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 158..314
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 394..592
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 121525 MW; 4C73FBE46AD01077 CRC64;
MDELFDVFDD NGQAPPANRP TRTDRKRLKR QANGEVKDDA NGEDAHASST DGPSPSPAEV
DQEMTDGHEP DAKRIRTEEE PEPVITDTFE TEQSREVAAS AGLLGAKEEE KVILSHQVRH
QVALPPDYDY VPISEHKPPA EPARTWKFEL DPFQQVSIAS IERNESVLVS AHTSAGKTVV
AEYAIAQCLK NNQRVIYTSP IKALSNQKYR EFQADFGDVG LMTGDVTINP TATCLVMTTE
ILRSMLYRGS EIMREVGWVI FDEIHYLRDK VRGVVWEETI ILLPDKVRYV FLSATIPNAM
QFAEWITKTH NQPCHVVYTD FRPTPLQHYF FPAGADGIHL VVDEKGVFRE ENFQKAMSSI
ADKQGDDPAN AMARRKGRGK DKRMNKGGTK GPSDIYKIVR MIMTKNYNPV IVFSFSKRDC
EAYAIQMSSM SFNEDSEKAM VSKVFDSALE MLSPEDKNLP QIQHLLPLLR RGIGIHHSGL
LPILKETIEI LFQEGLIKVL FATETFSIGL NMPAKTVVFT SVRKFDGISQ RWITGGEFIQ
MSGRAGRRGL DERGIVIMMI NEQMEPQIAK DIVRGQQDNL DSAFYLGYNM ILNLLRVEGI
SPEFMLERCF HQFQNTASVS GLEKELQQLE AEKSAMVIAD ESNIRAYYEL RKQLDVYAED
MRMVIVHPNY CLPFMQPGRL VEIKDGGHDF GWGAVLNFSR RSQGRSTEKL APQEEWVLDV
ALEVADGPTP ATKTHQSLPP GIRPPQPGEK SKVEVVPVLL KCVHKISHVR IYPPSDMTVS
EEKRKVQQAL QEVARRFPDG LAVLDPIENM KITDNSFREL LRKIEIMESR LVANPLHHSP
RLEGLYNQYA DKMVLTTKIR NLKKQIQDAH AITQLEELKC RKRVLRRLQF INEDEVVQLK
ARVACEISTG DELMLSELLF NRFFNDLTPE QTAAVMSCFV FEEKVNENPV LPEDMARCLR
EIQKQARNIA KVSIESKLTM NEEEYVQGFK WHLMPVIYAW ATGKSFGDIC KMTDVYEGSL
IRTFRRLEEA LRQMAEASKV MGSEELEKKF EEALNKVRRD IVAAQSLYL
//
