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Database: UniProt
Entry: A0A1Y2FPV7_9BASI
LinkDB: A0A1Y2FPV7_9BASI
Original site: A0A1Y2FPV7_9BASI 
ID   A0A1Y2FPV7_9BASI        Unreviewed;      1480 AA.
AC   A0A1Y2FPV7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:ORY86023.1};
GN   ORFNames=BCR35DRAFT_302664 {ECO:0000313|EMBL:ORY86023.1};
OS   Leucosporidium creatinivorum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX   NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY86023.1, ECO:0000313|Proteomes:UP000193467};
RN   [1] {ECO:0000313|EMBL:ORY86023.1, ECO:0000313|Proteomes:UP000193467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=62-1032 {ECO:0000313|EMBL:ORY86023.1,
RC   ECO:0000313|Proteomes:UP000193467};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY86023.1}.
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DR   EMBL; MCGR01000015; ORY86023.1; -; Genomic_DNA.
DR   STRING; 106004.A0A1Y2FPV7; -.
DR   InParanoid; A0A1Y2FPV7; -.
DR   OrthoDB; 5399336at2759; -.
DR   Proteomes; UP000193467; 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   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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 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; PS00690; DEAH_ATP_HELICASE; 1.
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:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ORY86023.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193467}.
FT   DOMAIN          648..835
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1028..1183
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1291..1379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..520
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..544
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1318..1334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1348..1379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1480 AA;  166896 MW;  D75190FC68912559 CRC64;
     MAFGSATLPV RTKIKVTTKA TVKTTTTSSS VASTSELPAK GRKLADDSSQ SQPPPKRRES
     LPDPTDSEDD DDPDFGRSAK EKTREEAEDL MQKEAVKRAK EAEKIKKAEC RKQGIEYVPP
     PKVKKARKSR VKDESDDEPL PVVRRPPPRT TASLRARAGD STDSDEDKNV TKSRYDPEAR
     KRELAQRTGY NIGGLGGRDK GKGKAKEKDL DESTTSDEFE GEGYLKKRHS YAGSGKNRRR
     IYPDTERGRA QEIKSHLKRR WVNKKHPERM SAYRKRMEEL HNPLVQLLNV EITVVNSDNE
     SMYDGSDDNN HSFNLRTDSE DDEKPPVARQ APPRPKKPLA TPMLDHVDRK VKRESSSEDV
     KPLNKEEEDV KPFIKREEED VKPVITPMLT LSDDESEPAT EPDNDDDESP SDRLAHRLSL
     VDVKPVIHPS PPPVASTSKL PDTAQDVNML SLVDDSGSEP PTEDEGPILP LPPSNIKKEA
     DPTPMISLSD SEPEPETEVE VEDDGSDAMD LDEDEEMDPT TKMLLDDRRK QLEKKREAEK
     KRIRREDEER IRRKMEEASK GGDSDCEDDN LVTELSHSQA IEQAASQVAS QAIPKEGKPV
     LKGRPKFPIF TQEQLTTGRH RLSSEHEIPT PINRFLRPYQ RDGVDFLHHQ FSKGMGGVLG
     DDMGLGKTIQ VIAFLSAVMN KTGRRQDGGA RSGAIRQIPS GEPLPAPSEH GLTCLIICPA
     SVVHNWEREF QVWSYIDTVV YGGNDKKDRL RMFSMGHKDV VIAGFETARK NIDRLSREDF
     SIVIVDEAHR LKSHKAEVTQ AIHRFDTRLR YGLTGTAVQN RLGELWSILN WAVPTQVGTA
     KQWGDLVTSP LKFTQKSDAT DEQLALGRRR TIALAGSLLP RFWIRRTKES VKLQLPRKID
     NIVLCPLTDT QKEVYRNIMQ LDDVQILLTA DDPCPCGSMD DSGVRYKQGK CCQQDWSKMI
     FKYMDLFRKI SNHLALIYPD KEDKKTNPAK YQQDLAWVQA AFPDDWQNRK LGAVQNDYDP
     ELCGKWKILC DLLDVWKAAG DKVLLFTNTL KILDLLEKRF EAKQYYKWSR LDGKVANDDR
     MALVDEFNDP KGGVDVFLIS TRAGGVGLNL TAANRVVIFD PNWNPSHDLQ AMDRSYRFGQ
     TREVHVYRLV GAGTIEELII NRQQVKRALA NMAYDANAER RLYTGVEGEK EHTGELYGVK
     NIFKYTEHFS LTEKAIKDCA LAEAEYEDPE DEENADGSQR IKEIDENEVV KGLVDIGQQQ
     HLTAAERRKK EEQEAIKRIL TGAYTLESNA TLGNSKAEEE RARRAVQGQT LGSKPRARED
     SPATKRDSKA ADVKPAPKAP KSTAAWDPTA RRGKKRKAPE TGALPPKPKR EVKVKSEQDV
     KVEVKREEVR IKPEPISPPR QASTSASTAA SLSEAVAMLT EIKKRLGISS SVTFKQIVEA
     SYPNRRDFTD WLDELVFMDE AGQKRALERL CLAYKNRRRA
//
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