ID A0A0G4MWZ0_9PEZI Unreviewed; 977 AA.
AC A0A0G4MWZ0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=ATP-dependent RNA helicase DBP3 {ECO:0000256|ARBA:ARBA00039328};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=ATP-dependent RNA helicase dbp3 {ECO:0000256|ARBA:ARBA00039606};
GN ORFNames=BN1708_007882 {ECO:0000313|EMBL:CRK38728.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK38728.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK38728.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK38728.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent RNA helicase required for 60S ribosomal subunit
CC synthesis. Involved in efficient pre-rRNA processing, predominantly at
CC site A3, which is necessary for the normal formation of 25S and 5.8S
CC rRNAs. {ECO:0000256|ARBA:ARBA00037449}.
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|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC subfamily. {ECO:0000256|ARBA:ARBA00009334}.
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DR EMBL; CVQH01025638; CRK38728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4MWZ0; -.
DR STRING; 100787.A0A0G4MWZ0; -.
DR OrthoDB; 5477821at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006153; Cation/H_exchanger.
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; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF57; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00999; Na_H_Exchanger; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 588..761
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 794..947
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 347..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 107145 MW; 798AB6B5D65C5865 CRC64;
MLATYLIRHA EGVSVQSMTG ESDGGLHRRA GDVERQGGGV SVAMGNWFLE TLLYYVIMGA
VYGAVAGTLT RFAVKFSLKR KWIDSESYLL IPLALGFLMI GSAGLVGTND LIACFAAGSA
LNWDGEYLAE TLKRHDEVNS SIDVILNFGG FMYLGSIFPW AGFQNAETGI TYGRLFGLGF
LVLLFRRIPA IMITYKLMPH SIRNWKEALF VGYFGPIGVG AAFYVEHTKH LFPHLDETND
TEVNDLLRAL SPVVYWLALF SIVVHGLSIP ILNALYGYFG VQPIQDDAVE MRRKSVHVAA
PPNAIEGDKE TFIAYNRFSR PMFDNNQLPD WRDENPEPSL DVDLERQKSE AALSAPRTPR
TPRNRSRSRS TIRFMDRRGA NTGMGMMAAT KRLLAESEDH SAADDAAPSK KQKVKDLPEG
DDEAAALKKQ RKKEKKAAKA AKEGGGEDKD EKKKRKEEKR EKKRLREEAE KAAAGEDAPM
ADVDADAETK PKKEKKDKKE KKAKSQNGAA APGAAVASAS YTQSAALTAL PQADIDAYLA
EQSIVIGDDK STNLRPVLAF NQLPVTDLLA KSPFAAYTKP TPIQAASWPF TLSGRDAIGV
AETGSGKTMA FALPLVESIS KMKKRCIKAV VVSPTRELAM QTHEQTAQLA AHLGLKSVCV
YGGASKDEQR SLLQRGADII VATPGRLKDF MSDGTVDLSH SRFAVLDEAD RMLDKGFEDD
IKAILGAMPA REDRQTLMFT ATWPASVRLL ASSFMVDPVK ITIGSGGKET ASGSVELQAN
ARITQRVEVV DGRDKEQRLL QILRQYQAGK GRHDRILVFC LYKKEATRVE GFLQQRGIHV
CGIHGDLRQD QRTRSLEAFK SGSTSVMVAT DVAARGLDIP EVKLVVNVTF PLTIEDYVHR
IGRTGRAGKT GEAITLFTVQ DKAHSGSLIN ILKGANQPVP DELFKFGTTV KKKAHDTYGA
FFKDVDMSKK ATKIVFD
//
