ID A0A2G5I0Y1_CERBT Unreviewed; 1289 AA.
AC A0A2G5I0Y1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative ATP-dependent RNA helicase {ECO:0000313|EMBL:PIA98430.1};
GN ORFNames=CB0940_06648 {ECO:0000313|EMBL:PIA98430.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA98430.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA98430.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA98430.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PIA98430.1}.
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DR EMBL; LKMD01000102; PIA98430.1; -; Genomic_DNA.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000230605; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 2.
DR Gene3D; 2.30.30.1160; -; 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 InterPro; IPR040801; Ski2_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF8; HELICASE SKI2W; 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 Pfam; PF17911; Ski2_N; 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:PIA98430.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 322..478
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 610..811
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 200..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1289 AA; 144644 MW; 5DBE4B450C167FB8 CRC64;
MADELHAALE GLSLSSENVH EDIDDLLDQA KPRKRIRKSP EEVKADLERQ FLTPSTSFSP
EWLDRLQQRW EAPTNYNELF ALGPTQTRTI IRFTREGLEG RVTGYKEVTV PANSATAKNS
TSLLRKPANR ADFVRGAAGF YPFAPGGLDA VEATAAYEDE FIQQQQGAED AKKSNKLDKV
INFAAEGGLL EVPPGFSRGL RVNEKPKQDD EAAKEVEEVL DEQSDVPEAF QNGVPLPKEN
GEADEGDEGD EEGEEELDAL LPVEFPALAA HGPLAVARNK QGGREWAHMV DVNRDITNFR
ELVPEMAREW PFELDTFQKE AVYHLENGDS VFVAAHTSAG KTVVAEYAIA LAAKHMTKAI
YTSPIKALSN QKFRDFRQEF DDVGILTGDV QIRPEASCLI MTTEILRSML YRGADLVRDV
EFVIFDEVHY VNDSERGVVW EEVIIMLPEH VTLICLSATV PNTYEFASWV GRTKKKDIYV
ISTPKRPVPL EHYLWADKKM FKIVDANKSF IEKGWKDAND AMSGRDKIIA AEAKAKEKEE
AAVAAGRGGR GGRGAQQGRG GQQRGGGNQR GGPQQRGRGA PATRGQGNIA RTGRGGGRTT
AAQDRNIWVH LVQHLRKEDL LPCTIFVFSK KRCEENADAL SNLDFCTAAE KSAIHMILEK
SLARLKPDDR TLPQIRRTRE LLSRGIAVHH GGMLPIVKEC VEILFSKTLV KVLFATETFA
MGLNLPTRTV IFSGFRKYDN KSFRDLLPGE YTQMAGRAGR RGLDTVGYVI LVSPGADEAP
PAGRLRQMML GEPTKLRSQF RLTYNMILNL LRVEALKIEE MIKRSFSENA TQALLPEHQK
QIKLSEADLE KVVREPCDIC DKDIDACQAA AVEFEKLTAS LHLMMLSTPV GRRMFQPKRL
IVFKGRNDVR TAGVLLRDGA SKGSPPTVQV LEVLYRNQRK RQDADFLPFL PRFRRRFIDL
PQSENEMQLR TVTIPLDNIE ALTGSHIQMD VSGVLQRDPE ALAKAKTELL TTCSSWTSST
WNELDYYKYL KDMSIRTLLD QRSQAATIAS DRECIHCPNL PKHFAMAHDQ WLIRDKINSI
RQLMSDQNLQ LLPDYEQRIS VLKDLGFIDS NSRVELKGKV ACEIHSADEL VLTELVLENV
LADYEPEEIV ALLSSFVFQE KTDAVPNLTP QLEKGQEMII SIAEKVNQYQ TLHQVILSSD
DSNDFVSRPR FGLVEVVYEW ARGMPFSRIT DLTDVLEGTI VRVITRLDET CREVKNAARI
IGDPTLFTKM QTCQELIKRD ICATASLYM
//
