GenomeNet

Database: UniProt
Entry: I2H388_TETBL
LinkDB: I2H388_TETBL
Original site: I2H388_TETBL 
ID   I2H388_TETBL            Unreviewed;       775 AA.
AC   I2H388;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   Name=TBLA0D03400 {ECO:0000313|EMBL:CCH60840.1};
GN   ORFNames=TBLA_0D03400 {ECO:0000313|EMBL:CCH60840.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60840.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH60840.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE806319; CCH60840.1; -; Genomic_DNA.
DR   RefSeq; XP_004180359.1; XM_004180311.1.
DR   AlphaFoldDB; I2H388; -.
DR   STRING; 1071380.I2H388; -.
DR   GeneID; 14495876; -.
DR   KEGG; tbl:TBLA_0D03400; -.
DR   eggNOG; KOG0343; Eukaryota.
DR   HOGENOM; CLU_003041_26_1_1; -.
DR   InParanoid; I2H388; -.
DR   OMA; YDKMFER; -.
DR   OrthoDB; 149428at2759; -.
DR   Proteomes; UP000002866; Chromosome 4.
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; 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; 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:UP000002866};
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          42..70
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          73..247
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          279..438
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           42..70
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        520..538
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..746
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  88456 MW;  7312DE07B524475E CRC64;
     MAKKEQKSKT SQRKEQRKRE QDYIRELETR IEEYNPKNSN AVFFKDLPIS NATLRGLKEA
     SFVKLTEIQK NSIPISLKGY DVLGAAKTGS GKTLAFLIPV LEKLYRENWT EFDGLGALII
     SPTRELAIQI YEVLLKIGSR TSFSAGLVIG GKDVKFESER ISRINILIGT PGRILQHMDQ
     AVGLNLNNLQ MLVLDEADRC LDMGFKKTLD AIVNNLPISR QTLLFSATQS QSLDDLARLS
     LTDYKSIGTL DIVKENETGA SATPETLQQS YIDVPLQDKL DTLFSFIKTH LKNKMIIFLS
     SSKQVHFVYE TFRKLQPGIS LMHLHGRQKQ KARTETLDKF SRAQQVCLFA TDVVARGIDF
     PSVDWVVQVD CPEDVDTYIH RVGRCARYGK QGKSLIMLTP TEEAGFLKRL ASKKIEPKKL
     VIKQSKKRSI KPQLQSILFQ DPELKYLGQK AFISYVKSIY IQKDKEVFKF DELPVEEYAN
     SLGLPGAPKI KIKGMKSIER AKQKKNASRS LMALSKMNED GEPENIDKST DEAKQETKVR
     TKYDKMFERK NQTILSEHYL NITKQQANDD EDDDFMTIKR QDHKLVEEEL PDLIVPTSKR
     SQKKALSKKA SLSSKGNATK MVFDDDGQAH PIYELEGEEE FINKGSAEDQ KKEFLAKETE
     VMNEVDIEDK QVAKEKKQEK KRKRLEMLRK EIEDEYAEEY GINEEPENEA FLGTGNLSDD
     MESDSDDDSR TKKEVSYKRN NESDYEGEYD DNIIEMEEPN TLEDLESLTA KLIGN
//
DBGET integrated database retrieval system