ID N4TDQ1_FUSC1 Unreviewed; 901 AA.
AC N4TDQ1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=FOC1_g10016243 {ECO:0000313|EMBL:ENH61428.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH61428.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC subfamily. {ECO:0000256|ARBA:ARBA00038200}.
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DR EMBL; KB731261; ENH61428.1; -; Genomic_DNA.
DR AlphaFoldDB; N4TDQ1; -.
DR STRING; 1229664.N4TDQ1; -.
DR VEuPathDB; FungiDB:FOC1_g10016243; -.
DR HOGENOM; CLU_003041_15_2_1; -.
DR OMA; HLEWLVI; -.
DR Proteomes; UP000016928; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd17956; DEADc_DDX51; 1.
DR CDD; cd18787; SF2_C_DEAD; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR PANTHER; PTHR24031:SF68; ATP-DEPENDENT RNA HELICASE DDX51; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 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, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 373..622
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 733..896
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 901 AA; 100855 MW; 3DC9D2D55E9D2138 CRC64;
MYPRYVPHSK GGSNSNASPP HSSSKTTNST APTPATNAFS FSRYVPPSAK PIPQSMHIET
PQVQYFDDTP PKNTKRKLDA SDESKGTPGP DSKKPKTEEP TTQKDGEDAP KKKKKVRRGK
RRTGATNDER DDDDIKPAQE APEVKSKEAD ATPEESQTLD EDSAKDKEKP KRDVKEKKEK
RKRKSKNEEQ ESKVPHRPAP EDEDRNEDVS MTDAAEPIEE VENIPEPTEP AADEEDKRQK
RREKKKKEKE TEPAEEQEDE LQTNQRHKTV MSKLEKSLKL ASELPADERD EEDQGELHGL
EPLPQPEPIS SLTTSKPNYK ILPSWLEDPI RVSQDTRTPF AELDIIPKAC RVLEEKGFRD
AFAVQTAAIP LLLPTSKQRG DVLISAATGS GKTLAYALPV VRDISQGCLT RLRALVVLPT
RELVKQAQET FELCARAFDG GDRKRVRVGI SIGSQSLEVE QKAFMDQELR YDPDTYKKLK
EETQRRNQLK WGLSASENLQ DLDMEDTDPR LSHMNGYVVD YLSKIDVLIC TPGRLVEHME
QTRGFNLDYV RWLVVDEADK LLAQSFQGWL DLVMEKFRIN KFTARHFHDM DFSGVRKVIL
SATLTRDLSL LNQLGLQRPR LIVLESDGDI QIAEHSLPVS LKEHAIRVHD TNLKPLYLLD
LLRSQDMLMA SPNKDEEEPK AEEAEDSATS SDSSSSSDSD SDSDATSDTS SDTSSDSDSD
TATNTKLKVS GRTLKSHIPV SLIFTKSNES ALRLSRLLAL LDPSLADHIG TLTSTTPTHI
RRKTLRAFST ASSPIRLLIA SDLVARGIDL PNLDHVINYD LPPSVAGYVH RVGRTARAGR
SGCAWTLVGD DESGWFWGKI AKGAGVKRVQ KVERTRIEEI DEKRVEEYEA ALEKLGKEAG
R
//