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Database: UniProt
Entry: A0A094IGI2_9PEZI
LinkDB: A0A094IGI2_9PEZI
Original site: A0A094IGI2_9PEZI 
ID   A0A094IGI2_9PEZI        Unreviewed;       798 AA.
AC   A0A094IGI2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=V498_03203 {ECO:0000313|EMBL:KFY95692.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY95692.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY95692.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent RNA helicase required for ribosome biogenesis.
CC       Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC       Required for pre-rRNA cleavage at site A2.
CC       {ECO:0000256|ARBA:ARBA00037374}.
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|RuleBase:RU365068};
CC   -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC       ribosomal complexes. {ECO:0000256|ARBA:ARBA00038587}.
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. DDX10/DBP4
CC       subfamily. {ECO:0000256|ARBA:ARBA00038084}.
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:KFY95692.1}.
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DR   EMBL; JPKA01000529; KFY95692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094IGI2; -.
DR   HOGENOM; CLU_003041_26_1_1; -.
DR   Proteomes; UP000029270; 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; cd17941; DEADc_DDX10; 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; 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:SF54; ATP-DEPENDENT RNA HELICASE DDX10-RELATED; 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; 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, 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   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          50..78
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          81..255
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          281..430
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           50..78
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        495..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..727
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..782
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   798 AA;  89586 MW;  898D6088E1C7DF92 CRC64;
     MAPPNARKTA GKFAKPKNDA RSLKRKRIVD DHERLEKEIK ELDPKTADIK DFQHLPLSEP
     TSKGLEASHF KTLTDIQSKA IPLALKGKDI LGAAKTGSGK TLAFLVPVLE NLYRQKWTEL
     DGLGALIISP TRELAIQIFE VLRKIGRYHS FSAGLVIGGR SLQEERERLG RMNILVCTPG
     RMLQHMDQTA AFEVDNLQML VLDEADRILD MGFQTSVDAI LDHLPKDRQT MLFSATQTKK
     VSDLARLSLK EPEYVAVHEA ATSATPTTLQ QHYIVVPLAE KLNTLYSFIR ANLKAKIVVF
     MSSGKQVRFV YESFRHIQPG IPLLHLHGRQ KQTARLDITS KFSSSQNSCL FATDVVARGL
     DFPAVDWVIQ MDCPEDADTY IHRVGRTARY ERAGRGVMFL DPTEEEGMLA RLKHKKVPIE
     KIKVRTNKQQ SVQKQLQVMC FQDPELKYLG QKAFVSYTRS VYLQKDKEIF KIDEIDLEGF
     ASSMGLPGAP KIKFQKGNDA KKLKNAPRAT LESSDEESGS EAGGKKGKKE VRTKYDRMFE
     MQNQNVLSGH YTKMIAEDGE GEADAGSDEE GDFMSVKRLI PVDSELPEDM EEVASAGPQP
     LVVKGANDTE LVIDSKRREK MLKSKKKMLK LKGHGTKTVY DSDGNAHDIY ELEDEDDFKA
     RGTAEAQRAK FVEEEASKVK QADVEDKQLA KDKRREKKDK RKARERGDMD EDDEAPALHD
     AGSDAEDPLE FLKSLPMAGE SEAEDERPQK RAKKWFENDS EDESKAAATK KSRRHIIEAA
     DEPETLEDLE ALASGLLG
//
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