ID A0A421JBT2_9ASCO Unreviewed; 1049 AA.
AC A0A421JBT2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=ATP-dependent helicase FUN30 {ECO:0000313|EMBL:RLV86278.1};
GN ORFNames=JA9_004485 {ECO:0000313|EMBL:RLV86278.1};
OS Meyerozyma sp. JA9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV86278.1, ECO:0000313|Proteomes:UP000286412};
RN [1] {ECO:0000313|EMBL:RLV86278.1, ECO:0000313|Proteomes:UP000286412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA9 {ECO:0000313|EMBL:RLV86278.1,
RC ECO:0000313|Proteomes:UP000286412};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RLV86278.1}.
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DR EMBL; NSDU01000010; RLV86278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JBT2; -.
DR STRING; 2028340.A0A421JBT2; -.
DR Proteomes; UP000286412; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd17998; DEXHc_SMARCAD1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:RLV86278.1};
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:UP000286412}.
FT DOMAIN 514..680
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 881..1040
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 119415 MW; 5209975E0915CA55 CRC64;
MSENGSTNPP YVQVPSSSPI QVSMSPNESN GNGESSSGGS SRAVLDEEKQ RDLEAKRMAI
RNHPYYAMLR KGFFYLSESD IFKGFVKGKG NLRDITTWLQ ENFDRDAMVA RYEQERAVQA
AAEYQRQQHQ NANGYNPAAN PATNGVANVA PSTKVEVSKQ KSIAEKYNNT DPQGAIPRFS
YYVFDPVTKK RKLVKGSKYT VPPAPSGYGS TSRVVPAGTI NYMRNQTGPL TAPRFSSQYP
SYSQPYGSAL PQQPVVPARK KSKKAFRDED LSDMIVAEDD LEKIEAKIRR NRRSRAAKSM
KISDDEMEDE DDDLEEEGED EEDENSSDDM SDGDGGDAYE GVTSIDTQVL EFLNSASVDD
IVEICNIPPK TAEIIMSKRP FIDIYQVTSQ EFEAEETEKA DRQTRRRYKK KTLGQRVVEN
TEFSLKGYKA VDSLVKKCSE YGELISKQMK QWGVSVDSNH QDGLDVVEMD PVNDEVVVDE
EGKQSIKYLR ERPALFAEDM ELKNYQQVGI NWLNVLYQNK LSCILADEMG LGKTCQVIAF
MAHLKQVNEP GPHLVIVPSS TLENWLREFK KFCPSLVVKA YYGSQRERED IRYDLESTDY
DVLVTTYNLA TGAPADFKFL KHCDFNMIVY DEGHLLKNST SDRYTKLMRL KAKFRLLLTG
TPLQNNLKEL VSLLSFMLPN LFSERREDLH GLFNKKASTI NADEDYNPLL SQQAIAKAKT
MMTPFVLRRK KSQVLTHLPG KTNQIKYCEL TPAQKEIYLE HLNKGKATRK ERERRKLLTG
KEAEKARDEP ITSSSNVMMA LRKAALHPLL FRKIYNEDKL KQMAKDIMKE PEYVEANEQY
IYEDMEVMSD YELNNLCVKF PTLSKYVLED KEWLNSGKVS LLMDHIKEIM ARKERVLVFS
LFTQMLDILE RVLTIGNIKF LRLDGQTSVD TRQDLIDTFY DDDTIPVFLL STKAGGFGIN
LVAANNVVIF DQSFNPHDDR QAEDRAHRVG QTSEVLVTRF ISKGTIEENM LQLAENKLQL
DQSISSSEVS ESKMEEKAVS MFEKILFDE
//
