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Database: UniProt
Entry: G0VHR4_NAUCC
LinkDB: G0VHR4_NAUCC
Original site: G0VHR4_NAUCC 
ID   G0VHR4_NAUCC            Unreviewed;       471 AA.
AC   G0VHR4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=ATP-dependent RNA helicase DBP5 {ECO:0000256|ARBA:ARBA00039326};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   AltName: Full=ATP-dependent RNA helicase dbp5 {ECO:0000256|ARBA:ARBA00039604};
GN   Name=NCAS0G00610 {ECO:0000313|EMBL:CCC70948.1};
GN   OrderedLocusNames=NCAS_0G00610 {ECO:0000313|EMBL:CCC70948.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC70948.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC70948.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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 membrane {ECO:0000256|ARBA:ARBA00004335};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004335};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004335}. Nucleus, nuclear pore
CC       complex {ECO:0000256|ARBA:ARBA00004567}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
CC       subfamily. {ECO:0000256|ARBA:ARBA00038143}.
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DR   EMBL; HE576758; CCC70948.1; -; Genomic_DNA.
DR   RefSeq; XP_003677301.1; XM_003677253.1.
DR   AlphaFoldDB; G0VHR4; -.
DR   STRING; 1064592.G0VHR4; -.
DR   GeneID; 11527769; -.
DR   KEGG; ncs:NCAS_0G00610; -.
DR   eggNOG; KOG0332; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; G0VHR4; -.
DR   OMA; DPQTYLH; -.
DR   OrthoDB; 1087080at2759; -.
DR   Proteomes; UP000001640; Chromosome 7.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; 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:InterPro.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd17963; DEADc_DDX19_DDX25; 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:SF31; RNA HELICASE; 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   mRNA transport {ECO:0000256|ARBA:ARBA00022816};
KW   Nuclear pore complex {ECO:0000256|ARBA:ARBA00023132};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492}; Nucleus {ECO:0000256|ARBA:ARBA00023132};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW   Translocation {ECO:0000256|ARBA:ARBA00023132};
KW   Transport {ECO:0000256|ARBA:ARBA00022927}.
FT   DOMAIN          81..109
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          114..281
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          292..459
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          15..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           81..109
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        22..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  52581 MW;  25488156A8930A43 CRC64;
     MSNITDKDPA DLLASLKLKE NDQTTTVKKT DDAKKVEEGK KPEEKKETAE PDTNLLASEY
     EVKVKLVDLQ ADPNSPLFSV KSFDDLGLDP ALLKGVYAMK FQKPSKIQEK ALPLLLHNPP
     RNMIAQSQSG TGKTAAFSLA MLSRVNVDEE IPQAICLAPS RELARQTMEV VQDMGKFTKI
     STQLIVPDSF ERNTRINAQI VVGTPGTVLD LMRRKLIDIS KIKIFVLDEA DNMLDKQGLG
     DQCVRVKRFI PKTAQLVLFS ATFADAVREY AKKVVPDANT LELQTNEVNV SAIKQLYMDC
     KSEEHKYEVL SELYGLLTIG SSIIFVATKN TANLLYGQLR KDGHAVSILH GDLQSTERDR
     LIDDFREGKS KVLITTNVLA RGIDIPTVSM VVNYDLPTLR NGEADPATYI HRIGRTGRFG
     RTGVAISFVH DKKTLNTLLT IQKYFGDIEM TRVPTDDWDE VEKIVKKVLK E
//
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