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Database: UniProt
Entry: N4TDQ1_FUSC1
LinkDB: N4TDQ1_FUSC1
Original site: N4TDQ1_FUSC1 
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
//
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