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Database: UniProt
Entry: W9CRH1_SCLBF
LinkDB: W9CRH1_SCLBF
Original site: W9CRH1_SCLBF 
ID   W9CRH1_SCLBF            Unreviewed;      1086 AA.
AC   W9CRH1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Putative ATP dependent RNA helicase (Dob1) {ECO:0000313|EMBL:ESZ97090.1};
GN   ORFNames=SBOR_2520 {ECO:0000313|EMBL:ESZ97090.1};
OS   Sclerotinia borealis (strain F-4128).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ97090.1, ECO:0000313|Proteomes:UP000019487};
RN   [1] {ECO:0000313|EMBL:ESZ97090.1, ECO:0000313|Proteomes:UP000019487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX   PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA   Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT   "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT   pathogenic fungus.";
RL   Genome Announc. 2:E0117513-E0117513(2014).
CC   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010140}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESZ97090.1}.
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DR   EMBL; AYSA01000102; ESZ97090.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9CRH1; -.
DR   STRING; 1432307.W9CRH1; -.
DR   HOGENOM; CLU_002902_0_1_1; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000019487; 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, ECO:0000313|EMBL:ESZ97090.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019487}.
FT   DOMAIN          172..328
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          408..612
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..77
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1086 AA;  123382 MW;  008AEACBC329F932 CRC64;
     MDDLFDVFDD KPQTAASSKP KKAKKDKKDK KDRSKKRNAN GDVKPIVDAQ DEDSEMIDAE
     DPAVEADAEE EDIEEVDDNR EAIKAAKRRR KELESEPVVT DAFETAQSRE LAASAGLQGA
     PEEKPLVLQH NIQHQVSLPP DYDYVPISQH KAPEIPAKTW AFELDPFQKV AIASIQRNES
     VLVSAHTSAG KTVTAEYAIA QCLKNNQRVI YTSPIKALSN QKYREFTHEF GDVGLMTGDV
     TINPTATCLV MTTEILRSML YRGSEIMREV AWVVFDEIHY MRDKARGVVW EETIILLPDK
     VRYVFLSATI PNAMQFAEWI TKTHNQPCHI VYTDFRPTPL QHYFFPAGAD GIHLIVDEKG
     NFREDNFSKA MATIEDKKGS DPADINAKQK GRGKDKKTNK GANKEGSDIY KIVRMIMLKH
     YNPVIVFSFS KRECEAYALQ MSSMAFNDQS EKDMVTKVFE SAIESLSVED RTLPQIQHIL
     PLLRRGIGVH HSGLLPILKE TIEILFQENL IKVLFATETF SIGLNMPAKT VVFTSVEKFD
     GEKMRYLTPS EFVQMSGRAG RRGLDDRGIV IMMIDDKMEP ESAKTIVRGE QDKLNSAFYL
     GYNMILNLMR LEGISPEFML EHCFYQFQNT SSVSGLEKEL QDLQIEKDDV QIPDEATIKD
     YYDLRQQLTS YTKDMRDVIN HPNYCLQFMQ PGRVVHIKHQ DHDFGWGAVV KFTPRRPARG
     SAEQFPPQQS YILDVLLLVS SNSTVVTQTQ SDLPLGITPP GEGDKGKMEV VPVLLSCVEA
     IGHVRIFLPK DLHSANERNQ IRKSLEEVKR RFPDGIAVLD PIENMGITDD SFKRLLRKIE
     VLESRLLSNP LHNSPRLPDL YDQYAGKLDI TKQIKEKRKA ITSALSIMQL DELKSRKRVL
     RRLGFINEQE VVELKARVAC EISSTGDGHE LLLSELLFNG YFNDLTPEMC AAVLSVFIFE
     EKSQAPPLSE ELGVKYREIQ AQARIVAKVT AESKLKMNEE EYVTSFKWQL MEVVYVWAQG
     KSFAEICKMT DVYEGSLIRL FRRLEELLRQ MAQAGKVMGS EEVSSKFEEA LKKIRRDIVA
     AQSLYL
//
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