ID G3AXS5_CANTC Unreviewed; 1063 AA.
AC G3AXS5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Antiviral helicase {ECO:0000313|EMBL:EGV65684.1};
GN ORFNames=CANTEDRAFT_118199 {ECO:0000313|EMBL:EGV65684.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV65684.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; GL996512; EGV65684.1; -; Genomic_DNA.
DR RefSeq; XP_006684258.1; XM_006684195.1.
DR AlphaFoldDB; G3AXS5; -.
DR STRING; 590646.G3AXS5; -.
DR GeneID; 18248625; -.
DR KEGG; cten:CANTEDRAFT_118199; -.
DR eggNOG; KOG0948; Eukaryota.
DR HOGENOM; CLU_002902_0_1_1; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000000707; Unassembled WGS sequence.
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; 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:EGV65684.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT DOMAIN 150..306
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 387..588
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 120266 MW; 9CF4694E0C01F503 CRC64;
MDDLFDVFDE APVEVPEPPI APVNNPDTVK NTAEVVEPQE DSESQKRKLA DDSASHKLKK
QTTRKPSIKA VVSDALEIEA SREVAISDGL LASKPDPNGH PSGQLKLKHQ VRHQVAIPPG
FPYVPISEHK RQNDARRYPF KLDPFQDTSI SCIDRNESVL VSAHTSAGKT VVAEYAIAQS
LRDKQRVIYT SPIKALSNQK YRELQAEFGD VGLMTGDVTI NPDAGCLVMT TEILRSMLYR
GSEVMREVAW VIFDEVHYMR DKSRGVVWEE TMILLPDKVH YVFLSATIPN AMEFAEWIVK
IHEQPCHVVY TDFRPTPLQH YLFPAGGDGI HLVVDEKGTF REENFQKAMA QISDGMGEDP
GAVDGKKGKK GQTWKGGNND GKTDIYKIVK MIYMKRYNPV IVFSFSKRDC ETLALKMSRL
DFNNDDERDA LTKIFNNAIG LLPESDRELP QIKNILPLLR RGIGIHHSGL LPILKEIIEI
LFQEGLLKVL FATETFSIGL NMPAKTVVFT SVRKWDGVGF RWVSGGEYIQ MSGRAGRRGL
DDRGIVIMMI DEKMEPQVAK GMVKGQADRL DSAFHLGYNM LLNLMRVEGI SPEFMLESSF
FQFQSASSVP KMESQLVELT NQLSTINIDD ENLIKEYYEF KVQLSKLQED SQKIITHPGH
ILPYLQSGRV IKVKIGDMDY GWGMVQSFSK RANKRNSSAI YSDHESYLVQ VFIYSLFVDS
PVNLIKSFNP DLPEGIRPSK SGEQSRAEYI PITLSSIEKI SSVRLKVPAD FKSSSAKRNL
LKTLKDLPKK LPDGIPIMDP VNSMKIDDDE FKTLLRKIDV VESKLLGNPL HGSVRLDELY
QKYDSKVKIE TQIKALKDQI LETKAVIQLD DLKHRKRVLR RLGFTTQNDI IELKGRVACE
ISTGDELLLT ELIFNGTFND LTPEQCAALL SCCVFQEKAK ETPRLKPELA EPLKNLQEMA
LKIAKISKEC KIEMVEKDYI ESFRPELMEV TYAWCKNATF TQICKMTDVY EGSIIRTFKR
LEEMIRQMVS AAKTIGNMEL ETKMDKALEL VHRDIVSAGS LYL
//
