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
//