ID C4Y6M0_CLAL4 Unreviewed; 573 AA.
AC C4Y6M0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=CLUG_03804 {ECO:0000313|EMBL:EEQ39676.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ39676.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ39676.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ39676.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: ATP-binding RNA helicase involved in mitochondrial RNA
CC metabolism. Required for maintenance of mitochondrial DNA.
CC {ECO:0000256|ARBA:ARBA00037267}.
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 -!- 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. MRH4 subfamily.
CC {ECO:0000256|ARBA:ARBA00038507}.
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DR EMBL; CH408079; EEQ39676.1; -; Genomic_DNA.
DR RefSeq; XP_002616563.1; XM_002616517.1.
DR AlphaFoldDB; C4Y6M0; -.
DR STRING; 306902.C4Y6M0; -.
DR GeneID; 8496640; -.
DR KEGG; clu:CLUG_03804; -.
DR VEuPathDB; FungiDB:CLUG_03804; -.
DR HOGENOM; CLU_003041_18_0_1; -.
DR InParanoid; C4Y6M0; -.
DR OMA; HSTIDFI; -.
DR OrthoDB; 1333884at2759; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
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:SF421; ATP-DEPENDENT RNA HELICASE DDX28-RELATED; 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:UP000007703};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 157..379
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 413..573
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 573 AA; 64344 MW; 65F3A6C8AC1F1795 CRC64;
MRCLNPIIRW PFGLNYSLAR TQLRFFRTKK KQPNSRQGKL LDAPATEKKS KLFAFGNFAS
LQRPAKNEIS KSETVIEKIS SFNSLRIFPT VRAAMIKEIK EGYNLKSTYV KSKEELEIKP
SPVQVAAIRK INQPRKVSAK QSTAANGNEI LKELILENES KKLKVFTVAA ETGSGKTWAY
LASVFSKLKE DDANLFNRSK KLYSEAKQFE TIRAVILLPT HELVDQVYDT AFRASTLPID
LEEDVGAKML QSSGFKSFLE AEGTKNLGLK VVKWGSGDSH ERLFQSAQKG RIDVLVTTPA
KIQGLAKLTN IPRQFRLFNF VEYCVVDEAD TLMDNSWFPD TSTVLRRFNK LKDLIMCSAT
IPKEFNKTMK SMFKDENSVI SIVTPSVHKI PKQIVLKVID AQQAPYHGSK SRCLAQALYA
IYNDGTEAGY VKRILVFVNE KKDVEPLVET LITKYGHRQA DIVAVTGKDS AVERGEKIDS
FIRPATLLED DPDGSKIKVL VTTDLLARGL NFSGIKNVIL MDIPRSSVDL IHRVGRTGRM
KQSGRVFIII DKKSKKSWIK GLPRAIKEGT TIG
//
