ID C4YSX8_CANAW Unreviewed; 1062 AA.
AC C4YSX8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=ATP-dependent RNA helicase DOB1 {ECO:0000313|EMBL:EEQ47114.1};
GN ORFNames=CAWG_05673 {ECO:0000313|EMBL:EEQ47114.1};
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ47114.1, ECO:0000313|Proteomes:UP000001429};
RN [1] {ECO:0000313|EMBL:EEQ47114.1, ECO:0000313|Proteomes:UP000001429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1 {ECO:0000313|EMBL:EEQ47114.1,
RC ECO:0000313|Proteomes:UP000001429};
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 -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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; CM000313; EEQ47114.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YSX8; -.
DR PaxDb; 5476-C4YSX8; -.
DR VEuPathDB; FungiDB:CAWG_05673; -.
DR HOGENOM; CLU_002902_0_1_1; -.
DR OMA; IMLKNYN; -.
DR Proteomes; UP000001429; Chromosome 7.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18024; DEXHc_Mtr4-like; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 2.40.30.300; -; 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; IPR048392; MTR4-like_stalk.
DR InterPro; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EEQ47114.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 149..305
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 388..589
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 120505 MW; 4CC17E0AF292242B CRC64;
MDDLFDVFDE APQAAPPKIE EIKDEVKPET TDNQTRSTKK RQLDNNNKTT TNSNNSSSSN
NKKHKQAEDI KPVVFDSVEI ETSREVKPSE GLSNSATVDA DNKLKLKHQI RHQVAIPPSY
PYVPIGEHKR KHEARTYPFT LDPFQDTAIS CIDRNESVLV SAHTSAGKTV VAEYAIAQSL
RDKQRVIYTS PIKALSNQKF RELQAIFGDV GLMTGDVTIN PDAGCLVMTT EILRSMLYRG
SEVMREVAWV VFDEVHYMRD KSRGVVWEET IILLPDKVHY VFLSATIPNA MEFAEWIVKI
HNQPCHVVYT DFRPTPLQHY LFPAGGDGIH LVVDEKGTFR EENFQKAMAT ISDNSGDDPA
SSDSGRGNKK GKTNKGRNHQ DGKGDIYKIV KMIYMKKYNP VIVFSFSKRD CESLALKMSK
LDFNTDEERN SLTQIFYNAI ELLPEADREL PQIKNILPLL KRGIGIHHSG LLPILKEIIE
ILFQEGFLKV LFATETFSIG LNMPAKTVVF TSVRKWDGVG FRWVSGGEYI QMSGRAGRRG
LDDRGIVIMM IDEKMEPQVA KGMVKGQADR LDSAFHLGYN MILNLMRVEG ISPEFMLEHS
FFQFQKASSV PILEGKLAQC KQEFADITIE DEPIIKDYYD LKQQLLKYNE DVRKVITHPG
NILPFLQDGR VIKVKIGDLD YGWGMVTTFT KRNRRHQEEF APHDAYVVEV FITTMFIDSP
VNLIKKFNPM LPEGIRPAKS GEQTRAEFIS ITLSSIEKIS TVRLRVPDDY KSSTAKRTLV
KTLKDLPKRL PDGIPLIDPV QSMKITDDDF KKLLQKIDIL DSKIVSNPLN NSARLDDLYA
KYTAKVDLNN QIKKLEEQIF QAKSIIQLDQ LSNMKRVLKK LEFTGSEEVV ELKGRVAAEL
STGDELMITE LLFSGFFNEL TPQQICGLLS AFIFQERAKE LPKLKPELAE PAKVIHETAN
KIAKISKQSG LEIVEKDYIE QFNLALVEVV FVWSNGASFS SICKMTDIYE GSIIRALRRE
IELIKQLVDA SKIIGNQELV DKFEKCIELI NRDFVQVSSL YM
//
