ID K1VA94_TRIAC Unreviewed; 1701 AA.
AC K1VA94;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=RNA helicase {ECO:0000313|EMBL:EKD00945.1};
GN ORFNames=A1Q2_04818 {ECO:0000313|EMBL:EKD00945.1};
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:EKD00945.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD00945.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD00945.1,
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 -!- 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:EKD00945.1}.
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DR EMBL; AMBO01000331; EKD00945.1; -; Genomic_DNA.
DR STRING; 1220162.K1VA94; -.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_2_2_1; -.
DR InParanoid; K1VA94; -.
DR OMA; SKFEDIG; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0010467; P:gene expression; IEA:UniProt.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR CDD; cd18020; DEXHc_ASCC3_1; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF6; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EKD00945.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT DOMAIN 290..476
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 512..710
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1144..1311
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 139..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1701 AA; 189835 MW; DBBBA76CAE6356EA CRC64;
MSADAYLDSL VGDPGPSTTA HREWESLLAG WDGQLTPWPT LQSVLNSDKV VNDVAEKIST
VRIVEPEPEH EEPDLNTSAL LARLHRHLQP GAYISLMELL ASPRGEMDIQ SELVETLGFE
GEGLSLVEEL LRPGVRQALV SSSKGKKKGA TPSASGHATP RKRKGKIDIT DVIGTAEDIE
RRIQEQLNRP KAMFVEESQQ RSLQQAEKLP NVFTSSSTMP ALSYGGKIAL PQGTEREQTD
AFEEVTVPPP TMVPPKMGEK PVMINSLSPL AQRCFPKYVS LNRMQSVVHP TAMGTNENML
VCAPTGAGKT DVALMSILRV LESHLLPGPG FKIDKDKFKI IYVAPMKALA AEITRKFGKR
LQWLGIHVRE LTGDMQLTRA EINETQIIVT TPEKWDVVTR KPTGEGELAS KVRLLIIDEV
HLLNEERGAV IETIVARTLR QVESSQSLIR IVGLSATLPN YIDVSDFLRV NRYQGLFFFD
ASFRPVPLEQ HFIGVKGKAR SQTQIRNMDN VVFDKVLEMV REGHQVMVFV HARKETVKTA
QKLKEMATEE GALDVFDTRD HPKFQLYRRD VGTSRNKEMK ELFDYGFGIH HAGMLRSDRN
MMERMFEDNA IKVLCCTSTL AWGVNLPAHA VIIKGTQVYD SNKGSFQDLS VLDVLQIFGR
AGRPGYETSG VGYICTTQDK LDHYLYSIMS QQPIESKFIP GMVDALNAEI SLGTIANVRE
AISWIGYTYL FVRMRREPFI YGMSHDEPKD DPQLGNKRSD LVTQAARTLA AAKMATFDES
NNSFAITDLG RIAARYYLRH QTVEVFNEKF NPRMKNADIF AMLSQATEFA QIQIRDNEVD
ELTNIMNSDN CPMEVNGGAT SAQGKVNILL QAYISKVFIE DFALVSDSAY VAQNAGRIIR
ALLEIALSRN WANCALLLID LSKAIEKRMW PYDHPLGQLN TLQRDTLYNL RRWADDTEIQ
ELREMEPKEL GELVHLNPIH GAALRNAALM FPTIGVSYAL RPLAHDLLQI SVTVEPQFTW
NTKVSGSSEP FYVWVQDEEG LHILQWRSIL LRQTSTAMDI DFVIPWSGEH QSLSIVTASD
RWLGSDSQTS VSLADLVMPA AFDERTPPLD LPFLSISAVD DPDIEKQYRP YITMFNTLQS
QSFWSVYHTQ NNILISAPVA SGKSLMGEMA MWHALRHQSD AFILAIVPGN RSSAEAAARL
RHVLGKRAKV ILARNSKEFE AGAEETGARV LVATPGAFDD IVGEKLTSLA TRLSLIVLED
LHLLDASYEL SIIKLLTIAK PARTRIVGLT CSLSNPSDLA SWLGVEYNYR YCFTPQDRSS
PLVVSTRVFN LPHGLGLLKS MIKPTYDLIK STGSAIVFTP SASSARAVAA DLVTQSGTEF
DLNGFLSAPR ADVEPLLANL ADSELLEPLL HGVGYVVPTM RARDLALVLE LYAAGIVRAL
IAPRTQAWKL PVRAETVVLA GAQYLHFRGE ERMLRNYSKH ELVKMQGFAA QSASPTSPAG
RMVVMCQAEQ VVSIRRLLND GLSLESALPS VLDPALAPLI PSPVSANTGR GRDGHASIEE
HERHVLGRML VSRPKPRPIQ PHRPRDVDLR ARDLMDLLSW SYLVRRIRTN PSFYDAREGE
ERELVSRWID AFFVNREERE RGHAQKPAKD RPKLEVVEGY GQPQEKKDKD DEHEEKVLVP
RVLAEEEYVI EDGDEDEGDS D
//
