ID K1VCI5_TRIAC Unreviewed; 1065 AA.
AC K1VCI5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=ATP-dependent RNA helicase DOB1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1Q2_07197 {ECO:0000313|EMBL:EKC98515.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98515.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC98515.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98515.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKC98515.1}.
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DR EMBL; AMBO01000388; EKC98515.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VCI5; -.
DR STRING; 1220162.K1VCI5; -.
DR eggNOG; KOG0948; Eukaryota.
DR HOGENOM; CLU_002902_0_1_1; -.
DR InParanoid; K1VCI5; -.
DR OMA; IMLKNYN; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000006757; 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; cd13154; KOW_Mtr4; 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; 2.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT DOMAIN 171..313
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 392..596
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 118874 MW; C022A8AC1AFDC7EA CRC64;
MARASAAAGP STPRKKTKKR AAEDGTPAAK KTKAPRIDDE EAQEEPAQND DPMAALEEAQ
KDPMETLDEN LKGETSEDGP VEESKDGHIP GQAPVRADEY ELKAEREVDA SKGLGGGDAA
DEGKLKLVHE VRHQVAIPPG FPYVPISQHK RLDPPARTYK FELDPFQYVA TSCIERSETV
LVSAHTSAGK TVVAEFAIAT ALKSGMRVVY TSPIKKFRDF QEDFGQENVG LMTGDVTINP
TASCLVMTTE VMREVGWVIF DEVHYMRDKE RGVVWEETLI LLPHKVRCVF LSATIPNSME
FAEWWCQTHE QPCHIVYTDF RPTPLQHYLF PAGSEGIYLV VDERSNFRED NFQKAMAALA
AGQGEDPADP NSGRNKKGKT KKGGAMKGGV SDIYKIVKLI MSRNLNPVII FAFSKRECEA
LAMQMSKLDF NTEDEAATVQ QVFENAIGAL SEDDRKLPQI EQILPLLKRG IGIHHGGLLP
ILKEVIEILF QEGLLKALFA TETFSIGLNM PAKTVVFTSV RKFDGKEFRT LSGGEYIQMS
GRAGRRGLDA RGIVIMMCDE KIEPEAAKGM VKGQADRLDS AFHLGYNMII NLMRVEGISP
EYMLERCFYQ FQNSLSVPVL EKQLKAAEEE RDEIKIEDED DIAEYYDLRD QLKVLEGDFK
SVITHPQYVL PFMQPGRMVE IRDGGRDFGW AVVVGYNKVV NPKGRPPIVT ENDPPQKGYV
IDVLVKVASG SQVPRDKNAE GIQPPGPGDN GETAIIGVLL STVQAVSTVR LHLPKDLRSQ
SDKDTAFRAV NEVKKRFPKG IALLDPVVNM GIKDDSFKKL VKDRIQTLPI TSSPDLPQKY
DEYDRKQKAI ASVRSLKKRI SSVHDVLQLE ELKGRKRVLR RLGFTTSEDV VEMKGRVACE
ISTGDELLLT EMMFGGTFNP LTPEQCAALL SCFVFQEKSE AKVKIREELA APLRVLQETA
RRIAKVSNES KIPVVEDEYV QSFKVEMMEP VLQWCKGASF AELCKLTDVY EGSIIRCFRR
LQELLRQMGQ AANAIGNKEL EEKFTKALEM LEKPNSIIFS PSLYL
//
