ID A0A3N4J067_9PEZI Unreviewed; 1073 AA.
AC A0A3N4J067;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=ATP-dependent RNA helicase-like protein DOB1 {ECO:0000313|EMBL:RPA90647.1};
GN ORFNames=L873DRAFT_1838934 {ECO:0000313|EMBL:RPA90647.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA90647.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA90647.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA90647.1,
RC ECO:0000313|Proteomes:UP000276215};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; ML120518; RPA90647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4J067; -.
DR STRING; 1336337.A0A3N4J067; -.
DR Proteomes; UP000276215; 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:RPA90647.1};
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:UP000276215}.
FT DOMAIN 159..315
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 398..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1073 AA; 121621 MW; 6CD241151A4C58B6 CRC64;
MYGEQELFDV FDAENVKNDA RPSKSMKERP EHRKKRFSNG GDSRADAMSV DSIPTAGEEK
VTTTSPGNSP LAKRQRRESG ADPIATDAFE IDAVREVPAS SGLTSQDTEG KSIIIPHQVR
HQVSLPTDYQ YKPIENHIFA DPPARAYGFT LDPFQKTSVA AIERGESVLV SAHTSAGKTV
VAEYAIAQSL RDNQRVIYTS PIKALSNQKY REFSAEFGDV GLMTGDTTIN PNATCLVMTT
EILRSMLYRG SEVMREVQWV VFDEIHYMRD KARGVVWEET IILLPDKVRY VFLSATIPNA
MQFAEWICKT HNQPCHVVYT DFRPTPLQTY LFPAGSDGMH LVVDEKGVFR EDNFQKAMNF
IAEKQGDDPG DINGRKGRGR GDRKHKTNTG GNKSGPSDIY KIVKMIMLKN YNPVIVFSFS
KRECESLALQ MSSLAFNDDT EKDMVKKVFD NAISSLSEED RGLLQIRHVL PLLRRGIGIH
HSGLLPILKE VIEILFQEGL IKVLFATETF SIGLNMPAKT VVFTNVRKFD GKEQRWVSPS
EFVQMSGRAG RRGLDDRGIV ILMLDQTLEP ATAREIVKGE QDRLNSAFYL GYNMILNLMR
VEGISPEYML EKCFFQFQNT AGAAGLEKEL GELETEKINT IIEDEPTVRE YHDLRQKLDG
YTKDMREVIN HPNYCLQFMQ PGRLVKVKYL NYDFGWGAVV NYTKRLRSKS GEEFSPQESY
VVDVLLNIAS DASSFTRPGQ ELPTGVKPPS EGDNGKMEVV PVLLSCLAGI SGIRIFLPKD
MKSQDQRNSA RKNLEEVKRR FADGISVLDP IENMGIVDDS FKNLLRKIEV LESRLLSNPL
HNSPRLKVLY NLYNHKVELQ EKIKAVKKKI TLAHSVMQLE ELKYRKRVLR RLGFIDDLDI
IQLKARVACE ISSGDELLIS ELLFNRVFNE LSPEQTAALL SCFVFEEKSN TEARLKPELE
KPYKELQAQA KLIAKISIES KLPVVVEEYC QKFKNQLMEV VYAWSEGASF ASICKMTDVY
EGSLIRMFRR LEELLRQMIM AAKVMGSEEL EKKFEDAMSK IRRDIVNSGS LYL
//
