ID D8PN65_SCHCM Unreviewed; 528 AA.
AC D8PN65;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=SCHCODRAFT_46575 {ECO:0000313|EMBL:EFJ03562.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ03562.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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 -!- 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|ARBA:ARBA00001556,
CC ECO:0000256|RuleBase:RU365068};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
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. DDX18/HAS1
CC subfamily. {ECO:0000256|ARBA:ARBA00024357}.
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DR EMBL; GL377302; EFJ03562.1; -; Genomic_DNA.
DR RefSeq; XP_003038464.1; XM_003038418.1.
DR AlphaFoldDB; D8PN65; -.
DR STRING; 578458.D8PN65; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02612747; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_26_5_1; -.
DR InParanoid; D8PN65; -.
DR OMA; LMEFHSQ; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd17942; DEADc_DDX18; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR044773; DDX18/Has1_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
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; PTHR24031:SF301; ATP-DEPENDENT RNA HELICASE DDX18; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT DOMAIN 13..41
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 44..220
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 234..403
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 461..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 13..41
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 464..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 59395 MW; 04905181AE86A1F8 CRC64;
MAAEGSSQPE ERVPFSTLEL SEPTMRGLTD MGFSTMTPVQ AKSIPVLLAG KDVLGAARTG
SGKTLAFLIP AIEMLHRLKF KPMNGTGIII ITPTRELALQ IFGVAKDLMA HHSQTYGIVM
GGANRRAEME KLQKGVNLLI ATPGRLLDHL QNSKGFVFRN LKALVIDEAD RILEVGFEEE
MKRIISILPN ENRQSMLFSA TQTTKVQDLA RISLRPGPVS IDVDKEEATS TVSTLSQGYV
VCPSDRRFLL LFTFLKKHLK KKIIVFFSSC NSVKYHAELL NYIDTPVLDL HGKQKQQKRT
NTFFEFINAE SGILLCTDVA ARGLDIPRVD WIIQYDPPDD PRDYIHRVGR TARAGKVGKS
LLFLLPSELG FLRFLKESKV PLNEYSFPAN KIANVQSQLE KLLQKNYFLH QSAKDGYRSY
LQAYASYSLK KIFDVNALDL AKVGKAFGFT VPPRVNVNIG EGKGNATKKR KRAEGEEFEP
ELEPVETSSW RQSKERRVET LGRKKVEKEV YKKNKERQKM GANGQWSR
//