ID A0A3D8QGD1_9HELO Unreviewed; 1078 AA.
AC A0A3D8QGD1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=ATP-dependent RNA helicase DOB1 {ECO:0000313|EMBL:RDW60797.1};
GN ORFNames=BP6252_12180 {ECO:0000313|EMBL:RDW60797.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW60797.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW60797.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW60797.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW60797.1}.
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DR EMBL; PDLM01000015; RDW60797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8QGD1; -.
DR STRING; 1849047.A0A3D8QGD1; -.
DR Proteomes; UP000256645; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:RDW60797.1};
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:UP000256645}.
FT DOMAIN 164..320
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 400..604
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 625..652
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 33..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 122487 MW; E2AABE4D8AC60D1A CRC64;
MDDLFDVFDD APKGITSNAA TKRPKKDKKD KIKKRKANGD VKAVSDVHDG DEEMADELPA
VEDDAEEEDD EIQEQQENKR RRRDIEAEPV VTDTFQTEQS RQLAASAGLQ GSKDDGALVL
QHNIQHQVSL PPNYNYIPIS QHKSPETPAR KWPFELDPFQ KVSIASIERG ESVLVSAHTS
AGKTVVAEYA IAQSLRNNQR VIYTSPIKAL SNQKYREFAA EFGDVGLMTG DVTINPTATC
LVMTTEILRS MLYRGSEIMR EVQWVIFDEV HYMRDKTRGV VWEETIILLP DKVRYVFLSA
TIPNSMQFAE WITKTHNQPC HIVYTDFRPT PLQHYFFPAG ADGIHLIVDE KGNFREDNFQ
KAMATIEEKK GADPADINAK RKGKGKDKKT NKGGNKEGSD IYKIVRMIML KHYNPVIVFS
FSKRECEAYA LQMSSMAFND DSEKAMVTKV FESAIESLSE EDKTLPQIQH ILPLLRRGIG
VHHSGLLPIL KETIEILFQE NLIKVLFATE TFSIGLNMPA KTVVFTSVEK FDGVAMRYLT
PSEFIQMSGR AGRRGLDDRG IVIMMIDNKM EPASAKEIVR GEQDKLNSAF YLGYNMILNL
MRVEGISPEF MLEHCFYQFQ NTSSVSGLEL ELQELQNERD SMEIEDEAII KDYYDLRQQL
TSYAKDMRDV INHPNYCLQF MQPGRVVHIK HNDHDFGWGA VVKFTQRRAP KGQVADFPPQ
QSYILDVLLP ISDESSVGTK TDTDLPSGIR PPGPGEKGKM EVVPLLLSCI EAIGHVRIFL
PKELNSIENR TTVRKSLDEV KRRFPDGIAT LDPIENMGIT DDSFKKLLRK IELLESRLLT
NPLHNSPRLA ELYNQYASKI EIGKKIKEKK KAISAALSIM QLDELKSRKR VLRRLDFIND
GEVVQLKARV ACEISSTGDG HELLLSELLF NRFFNELSPE LCAAVLSCFI FEEKSQCPPL
KEELAKPFRE IQAQARIIAK VSQESKIKIN EEEYVQGFKY ELMEVVLSWA TGKSFAEICK
MTDVYEGSLI RLFRRLEELL RQMAQAAKVM GSEELAARFE ESLTKIRRDI VSAQSLYL
//
