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Database: UniProt
Entry: A0A0D2IVZ7_9EURO
LinkDB: A0A0D2IVZ7_9EURO
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ID   A0A0D2IVZ7_9EURO        Unreviewed;       649 AA.
AC   A0A0D2IVZ7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=Z518_09930 {ECO:0000313|EMBL:KIX00865.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX00865.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX00865.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX00865.1,
RC   ECO:0000313|Proteomes:UP000053617};
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 Rhinocladiella mackenzie CBS 650.93.";
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   -!- 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   -!- SUBUNIT: Associates in the nucleolus with the 60S and pre-60S ribosomal
CC       subunits. {ECO:0000256|ARBA:ARBA00024365}.
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; KN847482; KIX00865.1; -; Genomic_DNA.
DR   RefSeq; XP_013268001.1; XM_013412547.1.
DR   AlphaFoldDB; A0A0D2IVZ7; -.
DR   STRING; 1442369.A0A0D2IVZ7; -.
DR   GeneID; 25298001; -.
DR   VEuPathDB; FungiDB:Z518_09930; -.
DR   HOGENOM; CLU_003041_26_5_1; -.
DR   OrthoDB; 149428at2759; -.
DR   Proteomes; UP000053617; 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:UniProtKB-EC.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053617};
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          128..156
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          159..335
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          349..519
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           128..156
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        37..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..92
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  72643 MW;  F7A2C5FD75CD0ADB CRC64;
     MELHVEKSKK RKRKHGKFTT VAAEAPPAAS LSNDKILISE LKEKGLKRRK TSHTSEDEDD
     VEPENVQKAV EDAQGEEPPT ETDDDEDSEE GSRLEETLNI SHGNTQATTT DLPTDSVPTL
     PGANTPPQKF SELSLSEKTM KAITEMKFET MTEIQRRGIP PLMAGRDVLG AAKTGSGKTL
     AFLIPAAEML HALRFKPRNG TGVIVVSPTR ELALQIFGVA RDLMQFHSQT FGIVIGGANR
     SAEAEKLTKG VNLLIATPGR LLDHLQNTKG FVYKNVKALV IDEADRILEV GFEDEMRQIV
     KILPKENRQT MLFSATQTTK VEDLARISLR PGPLYINVDQ TKTHSTVEGL EQGYVICESD
     KRFLLLFSFL KRNLKKKVIV FMSSCNCVKY HAELLNYIDL PVLELHGNLK QQKRTNTFFE
     FCNATAGTMV CTDVAARGLD IPAVDWIVQF DPPDDPRDYI HRVGRTARGA NGKGRSLMFL
     QPNEVGFLSQ LKEARVPVVE FDFPAKKLVN IQSQLEKLIA QNYYLNKVSR RRPESHSRPP
     RIKNVTDILF RRGEDLLTNE PTHIQSAKDG YRSYLQAYAS HSLRSVFDVN KLDLVKVAKS
     FGFATPPRVD IQLGASMQRD KKQGARRSYG SQPKQNGHGI KFKRTHGRG
//
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