ID A0A9P8DEF4_9HYPO Unreviewed; 1275 AA.
AC A0A9P8DEF4;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=J7337_008917 {ECO:0000313|EMBL:KAG9500439.1};
OS Fusarium musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1042133 {ECO:0000313|EMBL:KAG9500439.1, ECO:0000313|Proteomes:UP000827133};
RN [1] {ECO:0000313|EMBL:KAG9500439.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F31 {ECO:0000313|EMBL:KAG9500439.1};
RX PubMed=34388352;
RA Degradi L., Tava V., Kunova A., Cortesi P., Saracchi M., Pasquali M.;
RT "Telomere to telomere genome assembly of Fusarium musae F31, causal agent
RT of crown rot disease of banana.";
RL Mol. Plant Microbe Interact. 0:0-0(2021).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KAG9500439.1}.
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DR EMBL; JAHBCI010000006; KAG9500439.1; -; Genomic_DNA.
DR RefSeq; XP_044679439.1; XM_044826522.1.
DR AlphaFoldDB; A0A9P8DEF4; -.
DR GeneID; 68316773; -.
DR KEGG; fmu:J7337_008917; -.
DR Proteomes; UP000827133; Unassembled WGS sequence.
DR GO; GO:0055087; C:Ski complex; IEA:TreeGrafter.
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:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IEA:TreeGrafter.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR FunFam; 3.40.50.300:FF:000354; ATP-dependent RNA helicase SKI2; 1.
DR FunFam; 3.40.50.300:FF:000987; DEAD/DEAH box RNA helicase; 1.
DR FunFam; 1.10.3380.30:FF:000001; Ski2 ATP-dependent RNA helicase; 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; IPR025696; Beta-barrel_MTR4.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR050699; RNA-DNA_Helicase.
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:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL-RELATED; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000827133};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 310..466
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 597..799
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..233
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..554
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..575
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 142422 MW; 2CE797AA67668616 CRC64;
MAGIDALLER GPEETGQRQP ATKDPEELKR HLEELLLSPS AEFSPDWLNR LQQRWDYEAD
YTSLYKVAPP HTRTLTRFQR HGLEGRVTGY KNVTVPANSA TAKNSTSLSR KPANRADFVR
GAAGFFPFAP GGLEGIEATA AFEDQVHTGA TGGPTETSGS GNKLERVIQL GSEGGLLEKA
PGMSRGIDFT KKKTSISQED ANAVKEVLEE DPEDAKVEEG GNAASTDATT PDATPDETAE
DGDDIDDILP VEFPALEPHG VLAASSARKA GREWAHMVDI NHDMSNFREL VPDMAREWPF
ELDTFQKEAV YHLENGDSVF VAAHTSAGKT VVAEYAIALA AKHMTKAIYT SPIKALSNQK
FRDFRQTFDE VGILTGDVQI NPEASCLIMT TEILRSMLYR GADLIRDVEF VIFDEVHYVN
DFERGVVWEE VIIMLPEHVS LILLSATVPN TKEFASWVGR TKQKDIYVIS TPKRPVPLEH
YLWAGKNIHK IVDSEKKFIE KGWKDAHFAI QGKDKLKPAE TTVATRGGNP RGNQRGGTQR
GGPQRGGRGG GQQQRGGNQQ RGRGGPPRAS HAPGHMGRGG RAGGFTSVAQ DKNLWVHLVQ
YLKKSTLLPA CIFVFSKKRC EENADALSNQ DFCTAAEKSH IHMIIEKSVA RLKPDDRQLP
QIIRLRELLS RGIAVHHGGL LPIVKELVEI LFAQTLVKVL FATETFAMGL NLPTRTVVFS
GYRKHDGHSF RNLLPGEYTQ MAGRAGRRGL DTVGSVIIVP PGGLDDAPPV ADLRNMILGE
PSKLRSQFRL TYNMILNLLR VEALKIEEMI KRSFSEHATQ QLLPEHEKDV KLAQADLAKV
KRDSCEICDV SMDECHQASQ DFKRLTFELY KGLLSIPIGR RMFSQHRLVV FNWDGIRSIG
ILLADGISNK GTTEDPTLHV CAIKSLRDRR DATDQLPFIP AFRKYLHELP KSKKRVQTKT
LHVPLSDVEC LTRWVTKGII PEIFQGGDGY QQAKDKLQEL CGSWDDRWEE LDLSRIKQLQ
LQEIVEKRVE LVKTISNSPA EKCPEFLKHF AMCHDEWLIK DHISQLKQSL SDQNLQLLPD
YEQRVQVLKE LGFIDDATRI QLKGKVACEI HSGDELVLTE LILDNVLADY EPAEIAALLS
AFVFQEKTDI EPSLTGNLER GKEKIVAISE KVNDVQTRLQ VIQSADDSND FVSRPRFGIM
EVVYEWARGM SFKNITGLTD VLEGTIVRTI TRLDETCREV KNAARIVGDP ELYQKMQQAQ
EMIKRDITAV ASLYM
//
