ID J6F1K5_TRIAS Unreviewed; 1063 AA.
AC J6F1K5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJT49032.1};
GN ORFNames=A1Q1_01889 {ECO:0000313|EMBL:EJT49032.1};
OS Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 /
OS KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1186058 {ECO:0000313|EMBL:EJT49032.1, ECO:0000313|Proteomes:UP000002748};
RN [1] {ECO:0000313|EMBL:EJT49032.1, ECO:0000313|Proteomes:UP000002748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NCYC 2677 / UAMH
RC 7654 {ECO:0000313|Proteomes:UP000002748};
RX PubMed=23104369; DOI=10.1128/EC.00237-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Draft genome sequence of CBS 2479, the standard type strain of
RT Trichosporon asahii.";
RL Eukaryot. Cell 11:1415-1416(2012).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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:EJT49032.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ALBS01000181; EJT49032.1; -; Genomic_DNA.
DR RefSeq; XP_014180372.1; XM_014324897.1.
DR AlphaFoldDB; J6F1K5; -.
DR GeneID; 25985403; -.
DR KEGG; tasa:A1Q1_01889; -.
DR VEuPathDB; FungiDB:A1Q1_01889; -.
DR HOGENOM; CLU_288884_0_0_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000002748; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 443..594
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 773..828
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 877..1043
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 60..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..218
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 73..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 116894 MW; CC258A6AC520FE9F CRC64;
MNAPGERPSP SRVEEVARKA IELEDESESV PSFLWNAISD FLTTNPADFN FLLEIKAGDS
GNPFGTATFP SAGLHEQKLS QPASSPFASS SFPGPSSTQS STPTNHRPSP HSRPSISSFP
LVKPEPLQGE SQRVNMSSPT VSATSKGKNK HKQPTIISLL DSDDDEDIVL VGSSKPAVKA
GPPQSEQVWK KMNITEKMDA LKRERKCLRK ACDSCTNEGH KKLIMARRNE LRGLSAGLVF
RIWEPPNPSL FKAIPFHKYD MSEALRATIK PPAPTAPDSA EPSSEPSGGG GALRSTPPSS
AAIVSGGIPP SGDRAPSDMS GRATDALQAV NSTFEGLVNS MKSFAEGAGN LFNPLAQRLA
AGGIGPTITG LPGPSVFPGG FDFADLQARR AQIEEEFGYD LNAFFKDSLE DFSEDATVDE
GLKILKLNSL QDKLPGANFV LLPHQRETIR GGLLCDAMGL GKTVQCIGLM LARDERPDDF
KGCPQLIIAP LALLNHAESG LKTKNQRKQA RDRRREQGSD YESEDEVPNK KGPLFRTKWF
RVTIDEAHQI RNRQTKTAKS VLALDCLHPW ILTGTPIVNT LADLGPPLVF TGKVDFEEFH
KKIVSVERKL ASKRAQAALR GVMLRRNKDT EVDGKRILNL PPKTTNMDPL HFEAEERAIY
AAIEQRARVR VNKFIKQHYS VVLVLLTRLR QCVNHPWLLR RKEGEAGRDD DMLVDDDVFT
GNMTDTRDND ADEYGRAVAL LGKETVDKMA KKLEDRHNAM CSDASGDDID MECSICYEPF
VNNEFITACS HLYCRTCLDN LFVQPARDGS LLSDEEAQRG CRACPLCRTL IEPGRVFRAK
ALWQPPSDEK PDVDEALEDD EPGPSEVRDK GKKRAASVDL DFFEKKPRLE KGKGKEKVID
IDMDEEKDEL ADKNEVVIPP STKMRRILMS QNERDESIRR FSMPSSIADP INVILISTKA
GGVGLNLTMA TKVIMADLAY SPTTEAQAVD RAHRIGQTKE VTVERLVISD TVEDRLLEIQ
ERKGLLADGA LGEGAIGKLG KLSVKDISFL FGIGAEMQRD DDD
//
