ID A0A3N4JN35_9PEZI Unreviewed; 1248 AA.
AC A0A3N4JN35;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Antiviral helicase {ECO:0000313|EMBL:RPA97840.1};
GN ORFNames=L873DRAFT_1770701 {ECO:0000313|EMBL:RPA97840.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA97840.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA97840.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA97840.1,
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; ML120401; RPA97840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4JN35; -.
DR STRING; 1336337.A0A3N4JN35; -.
DR Proteomes; UP000276215; Unassembled WGS sequence.
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; -; 1.
DR Gene3D; 1.20.1500.20; -; 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:RPA97840.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000276215};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 307..463
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 575..775
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 192..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1248 AA; 140792 MW; 407E681BDDB99ACC CRC64;
MTSSEDLVDA INQLSLVNFD KPDGWIDDIL NKRLPRKRVK PDPSELREQL QQEFLTPSPE
FSNEWLNKLQ KRWDDPPDYT SLMGLAPSMS RTVIRFTREG LEGRVTGYKE VTVPAHSITA
KNSTSLLRKP ASKADFVRGK AGFFPFRPGG VDIGAANERP EELELQEALM EEKIGKDGLL
RVAPGMSRGL MFEEAPGDNE VSKEVDDDGF KFGDVEPKRR PKGGTDDNAR KKAKEPLAEL
DTIDDLLPVE FPMLAPKGNL PSVLKPKTRE WAHMVNMNQE ITNFRELVPN MAKEWPFELD
GFQKEAVFHL ENGDSVFVAA HTSAGKTVVA EYAIALATKH MTKAIYTSPI KALSNQKFRD
FRHVFEDVGI LTGDVQINPE ASCLIMTTEI LRSMLYRGAD LIRDVEFVIF DEVHYVNDSE
RGVVWEEVII MLPEHVNLIL LSATVPNPYE FASWVGRTKK KDIYVISTPK RPVPLEHYIW
ANKAMYKIVN SEKKFLEEGL KDANNALKKK EPDRPQQGGG GQRGGGQNQR GGRGGPQRGG
RGGVQRGGQS TAGFSRSGRG GMRTTTAQDK NIWVHLVHHL KKETLLPAVI FVFSKKRCEE
NADALSAVDF SNQTEKSAIH MIIEKSVARL KPEDRLLPQI LRMRELLARG LAVHHGGLLP
IVKEIVEILF AKSLVKVLFA TETFAMGLNL PTRTVVFSGY RKHDGKSFRD LQPGEYIQMA
GRAGRRGLDE RGIVIIVSPM DEAPPAATLK QMLLGQPTKL QSQFRLTYNM ILNLLRVEAL
KIEEMIKRSF SENSTQTLLP KHEQQVQESQ EKLKLLQSEN CETCNSDLSL FVLAAEQLKK
FSREVIKGGS MTTTGRKYFT KGRLVAIGRK DAHRTIGFLA AEGTSGGPQP VVQVLALVSR
DAVKPLVDNL PFIIACSKGL TSPPYKEWKL RLQTVRISDI EFLGSMVTRL NIARAHQGSR
EDVQAIEEEL RALYGRWTHA EWTEVDWSRI KDLTTLEHLE HRKSKEKEID QFQCLECNDF
ATHFALGYKK YLLELEVANL KHLISDQNLQ LLPDYEQRVL VLKDLDFIDE NMNVQLKGRV
ACEINSANEL VLTELILENV FAEYEPEEIV ALLSAFVFSE KTDVVPTITA RLEKGKAKII
EISKRVNQVQ IDRQIIMSPE NDDFENRPRF GLMEVVYEWA KGMSFSQITD LTDVLEGTIV
RAITRLDEAC REVKNSARII GDPSLFVKMQ ECQELIKRDV CHCASLYL
//
