ID G8YAE5_PICSO Unreviewed; 612 AA.
AC G8YAE5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN Name=Piso0_004106 {ECO:0000313|EMBL:CCE83528.1};
GN ORFNames=GNLVRS01_PISO0K09580g {ECO:0000313|EMBL:CCE83528.1},
GN GNLVRS01_PISO0L09581g {ECO:0000313|EMBL:CCE84559.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE83528.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|EMBL:CCE83528.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
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.
CC {ECO:0000256|RuleBase:RU365068}.
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DR EMBL; FO082049; CCE83528.1; -; Genomic_DNA.
DR EMBL; FO082048; CCE84559.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YAE5; -.
DR STRING; 559304.G8YAE5; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_26_6_1; -.
DR InParanoid; G8YAE5; -.
DR OMA; SCKTIST; -.
DR Proteomes; UP000005222; Chromosome K.
DR Proteomes; UP000005222; Chromosome L.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR24031:SF786; ATP-DEPENDENT RNA HELICASE MSS116, MITOCHONDRIAL; 1.
DR PANTHER; PTHR24031; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 92..275
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 289..465
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 571..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 69585 MW; 4EC873213FBFA271 CRC64;
MLALKPIWKP RTGFRPVVSV GNILTHRSNF SSGIVRYNSV AATTSKDVDL SAFKIETVKD
LAQTGVFDKS ITDSLSKEKF TQLTPVQQQV ILPIVTHDKG LVCRAKTGTG KTLAFALPTL
QDSIKHGRLG KVRTLVIAPT RDLALQIENE YLRLIKHMPV KYKKLLTPTV HIGGKRTIFN
SKRISSIAIA TPGRLNDNLN NEMFKEAFDS LRYRIYDEGD RLLDQGFERE LYEINEKLRE
SRTVDSNLVP LLFSATVNDR VHNFALKSIG RNYDFINTVN ENEPEAHENI EQILVKTDGI
DESFKGALCF SVKTITESNG KVIVFLPTIN AANWFFSAVK EAYFSGDRRK SRNRPAIVLL
HGKKTQSARE IAVSKFRTNA TGILVTTDVA ARGLDFKDVS HVVQMTPSMS LSDYIHKIGR
TARAGAHGQA ILYSTRSEEK YVNALEKEKG IKFSHVVQYS DQAKEEDEVF FEQLGDLSPE
FQDCIRSLLS YYKQVSSVFG IPFRKYLDSL LVYYRSILND SSAKFPFGRK FSLGILSIPD
RVASSYFSDG DRQFRSRDNF NQFTSYNKYG GRGDDRNRYD SRNKFDGRNK FDNGRRFDRP
KKTFKRSNRF DD
//
