ID A0A1V8V921_9PEZI Unreviewed; 971 AA.
AC A0A1V8V921;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=B0A51_00191 {ECO:0000313|EMBL:OQO32406.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO32406.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000256|ARBA:ARBA00003706}.
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. DDX54/DBP10
CC subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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:OQO32406.1}.
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DR EMBL; NAEU01000004; OQO32406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8V921; -.
DR STRING; 1974281.A0A1V8V921; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17959; DEADc_DDX54; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
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 InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 83..111
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 114..286
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 343..496
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 83..111
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 36..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 971 AA; 105050 MW; DB774B78E3316517 CRC64;
MVRAASPTHS ENDFDISNTL VHDGQVDDGD EDWDTLGEQP QSKRRRVAGK GAQSDDDDQD
EAFIAAAQAA VNRKGDKGGK KAGAFQTMGL SAVVLKAITR KGFSVPTPIQ RKTVPLIMDG
QDVVGMARTG SGKTAAFVIP MIEKLKAHSA KVGARAIVLS PSRELALQTL KVVHELAKGT
DLRTTLLVGG DSLEDQFSSM ASNPDIVIAT PGRFEHLKVE MGLELSSVKY VVFDEADRLF
EMGFAMQLTE IMHSLPPNRQ TLLFSATLPK SLVEFARAGL QDPKLVRLDA ESKIAPGLES
AFFTVKRSDK EGALLHLLQD VLKMPTGETE AAIKAKEPAE GKKRKREHIA PNETPSPHST
VLFAATKHHV EYLAALLKGF GYATSYVYGS LDQTARKLQV DDFRTGMTNI LVVTDVAARG
LDIPVLANVI NYDFPSQPKI FLHRVGRTAR AGKSGWSYSI VSQHDLPYLL DLQLFLGRKL
TVGRRQADPA LFRDTIVLGT LVREPMERYI EEASKIIGED SDLALMRDVA AKGEKQYLRT
RNSASAESVK RAKQLAGTEE MKATNMLFDA EVDQDVEAQR LQMLATVSGF RPQETVFEVG
KRGNANRTEI AEVIQKRRAK QAAKAERAPD TDAADATVPA GDSAVATLAP AQDQSDSEDD
ELVLTQPADM ESADESDLEI TFTQAKSSKR GSSFQDTEHF MSYTPTSFNS AEDRGYGVHT
GGTNATSGPG AHFLTQAKGA TMDLTNDENS GTAEKARGMR WDKKGKKYVS RANDEDGSKG
KKFIVGESGQ KILASFRAGR FEAWRKANKV SHVPRVGELE RPGRFSSDAL AGGGGRRGKH
TLDKAPKEAD KFRDDYYKKK KLVDAAREAR RGRFADGVGV RGRKVESEIR GVDDVRALRR
EQDKRKEKNA RPSREGRGSG SRGGSRGGSS SGGGSRGGSS RGGSRGASSS RGGGRGGGRG
GSGRGRGRGR G
//
