ID A0A0D2DJP8_9EURO Unreviewed; 399 AA.
AC A0A0D2DJP8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PV04_10739 {ECO:0000313|EMBL:KIW62577.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW62577.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW62577.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW62577.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC sites A0, A1, and A2, leading to mature 18S rRNA.
CC {ECO:0000256|ARBA:ARBA00024310}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX48/FAL1
CC subfamily. {ECO:0000256|ARBA:ARBA00037945}.
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DR EMBL; KN846963; KIW62577.1; -; Genomic_DNA.
DR EMBL; KN846963; KIW62578.1; -; Genomic_DNA.
DR STRING; 5601.A0A0D2DJP8; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR OrthoDB; 1087080at2759; -.
DR Proteomes; UP000054266; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; 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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd18045; DEADc_EIF4AIII_DDX48; 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 InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF26; EUKARYOTIC INITIATION FACTOR 4A-III; 1.
DR Pfam; PF00270; DEAD; 1.
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.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492}.
FT DOMAIN 25..53
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 56..226
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 237..398
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 25..53
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 399 AA; 45442 MW; 34D03C71EB8FF80E CRC64;
MAEGIDRTAD DRMEFSTSKE VTVAPTFEDM HLKENLLRGI YAYGYESPSA VQSRAIVQIC
KGRDTIAQAQ SGTGKTATFS ISILQIIETS VRETQALVLS PTRELATQIQ SVIMALGDYM
NVQCHACIGG TNVGEDIRKL DYGQHVVSGT PGRVADMIRR RNLRTRHIKM LVLDEADELL
NRGFREQIYD VYRYLPPATQ VVVVSATLPY DVLDMTTKFM TDPVRILVKR DELTLEGLKQ
YFIAVEKEEW KFDTLCDLYD TLTITQAVIF CNTRRKVDWL TDKMREANFT VSSMHGEMPQ
KERDSIMSDF RQGNSRVLIS TDVWARGIDV QQVSLVINYD LPSNRENYIH RIGRSGRFGR
KGVAINFVTS EDVRILRDIE LYYSTQIDEM PMNVADLLT
//
