ID A5DF98_PICGU Unreviewed; 1248 AA.
AC A5DF98;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Antiviral helicase SKI2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PGUG_01949 {ECO:0000313|EMBL:EDK37851.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK37851.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK37851.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
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}.
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DR EMBL; CH408156; EDK37851.2; -; Genomic_DNA.
DR RefSeq; XP_001486278.1; XM_001486228.1.
DR AlphaFoldDB; A5DF98; -.
DR STRING; 294746.A5DF98; -.
DR GeneID; 5127725; -.
DR KEGG; pgu:PGUG_01949; -.
DR VEuPathDB; FungiDB:PGUG_01949; -.
DR eggNOG; KOG0947; Eukaryota.
DR HOGENOM; CLU_002902_1_4_1; -.
DR InParanoid; A5DF98; -.
DR OMA; CGSDITR; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 2.
DR Gene3D; 2.30.30.1160; -; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR InterPro; IPR048727; Ski2_beta-barrel.
DR InterPro; IPR040801; Ski2_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF8; HELICASE SKI2W; 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; PF21409; Ski2_beta-barrel; 1.
DR Pfam; PF17911; Ski2_N; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 303..461
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 576..775
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1248 AA; 140923 MW; D9041826FFDC0921 CRC64;
MVAEASGETA VSIKNNTALP GTGLDPSFQL ELPEDEIDAE TSLKTEFLTP SSQLSWDLLD
LMQVTPDVDV TKLSQNLVTI PKSAGRTSFR FKRHGISGSI TGYKEETKRS DIDNANSGNS
LSITRKYTSK NDSLKGKTTF LPFQPGGLMT QTAAKDESAF LHRNDLGLFD IPQGFERGLV
IAGESDKKEV SAQLQELDDK SNEDIHGKDD EEPSAGGTKL IVEEEGEVEE VIPREDEDLD
DIDDIIPMNY SAIREKMKNE SERKKTWAHV VDLSHRVDNF KDVVPNMARE WPFELDTFQQ
EAVYHLEQGD SVFVAAHTSA GKTVVAEYAI AMATRNMTKA IYTSPIKALS NQKFRDFKET
FKDIDVGLIT GDVQINPDAN CLIMTTEILR SMLYRGADLI RDVEFVIFDE VHYVNDIDRG
VVWEEVIIML PDHVKYILLS ATVPNTFEFA NWVGRTKQKD IYVISTPKRP VPLEISIWAK
QHLYKVVDAQ RNFSDLEFRK HKEALESGKN KGRPNVVLGP GSRGGRGGTA RGGNRGGGRG
GGGSGRGGSN GGQVSTRPSG RAGFSRDGPN KNTWLQLVQY LKQHNLLPAV VFVFSKKRCE
EYADTLSSVD FCTAKEKSEI HMFVDRAVSR LKKEDRELPQ ILKIRDLLSR GIAVHHGGLL
PIVKECIEIL FSRTLVKVLF ATETFAMGLN LPTRTVVFNQ LRKHDGRGFR NLLPGEFTQM
SGRAGRRGLD DTGTVIVMSY NEPLSPMDFK EVALGVPTKL SSQFRLTYNM ILNLLRIEAL
RVEEMIKHSF SENSTQSLLP EHQKTVEKLS KELQTVHLEP CSVCNLEFTE ETYDLMKEYE
HVYGEILRNV QQSPLLKNNY LRAGRLFCFR DEETRQRVGF LVRVSMDNDS VLLLTFDPGD
NQDDVSKLPY IATKDYLQHY FGQITFNGSF KVVAVPIDKV NFIGQKMVKI YMKDLIHGNK
NEIAHASAQV KTLLRFQTAW RELSFDSAVQ ISLHELLVRK REIVEKISIL RSYECPNFAL
HYKQLSQQDE LKTQISSLQR LISDENLELL PDYEQRLRVL ETLGFIDANH NVGLKGRVGC
EINSGWELAI TELILDNFLG DFEPEEIVAL LSCFVYEGKT NDEEDPPLTP RLERGKQKIM
DISKHVLDVC SDNQIALTSE ETEFLERKRF ALMNVVYEWA RGLSFNEIMQ MSTEAEGTIV
RVITRLDEIC RQVKSAALIV GDSTLHSKMS EAQERIKRDI VFCASLYL
//
