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Database: UniProt
Entry: A0A179ULP1_BLAGS
LinkDB: A0A179ULP1_BLAGS
Original site: A0A179ULP1_BLAGS 
ID   A0A179ULP1_BLAGS        Unreviewed;      1919 AA.
AC   A0A179ULP1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=TBP associated factor {ECO:0000313|EMBL:OAT08800.1};
GN   ORFNames=BDBG_05027 {ECO:0000313|EMBL:OAT08800.1};
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT08800.1, ECO:0000313|Proteomes:UP000002038};
RN   [1] {ECO:0000313|Proteomes:UP000002038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; GG657455; OAT08800.1; -; Genomic_DNA.
DR   STRING; 559298.A0A179ULP1; -.
DR   VEuPathDB; FungiDB:BDBG_05027; -.
DR   OrthoDB; 180798at2759; -.
DR   Proteomes; UP000002038; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   CDD; cd17999; DEXHc_Mot1; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR044972; Mot1.
DR   InterPro; IPR044078; Mot1_ATP-bd.
DR   InterPro; IPR022707; Mot1_central_dom.
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; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   Pfam; PF12054; DUF3535; 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; SSF48371; ARM repeat; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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:UP000002038};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1340..1513
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1687..1838
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          76..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1919 AA;  213351 MW;  C3A5FD02EB11F036 CRC64;
     MTSRLDRLVT LLETGSTPLI RNTAAQQLAD VQKQHPDELF NLLGRILPYL RSRSWDTRTA
     AAKAIGGIVG YAERFDPNAD EGPKSAEDVV GEDDDVSPAV KKEEDKEVAE NAVSEDLLDV
     DTLDISSILK FGHKLLGSAG KEYEYSLAGL DAASRLQHQK KTLASRLGLG GEYMQEDLVN
     EADFATQPQH KVSGPKLEIA IPSVSRKSST QSNPSCAMAS PHDPMQATPT NGDDQGLSKR
     QLNQLKRKNK QNAKMGANKI RVVDLAVRKH SDAISTPITA STPHAVKKEE DGDDSNGDKK
     LDYFSLERTE PDDDSKIVSE FKGPVIPEKP VIQTDAEEEG LEWPYERMCE FLMVDLFDPS
     WEIRHGAAMG LREVIRVQGA GAGRVRGKSR RQNDMFNHRW LNDLACRLLC VFLLDRFGDY
     ISDNVVAPIR ETVGQTLAAL LLHLPTRSLA SVYRILYRMI MQNDLGLSSP IWEVCHGGMI
     GLKYLVAVRT DVLLKEPEIL DGVIAAVMKG LGDYDDDVRA VSAATLVPIA EDFVRLRPGS
     LNSLINIVWE CLSNLQDDLS ASTGSVMDLL SKLCTFPQVL KAMKTNAAQD SESSFGNLVP
     RLFPFLRHTI TSVRSAVLRA LLTFLKLDSE RQNAWADGKA MRLIFQNLLV ERNEGVLKLS
     LQVWVELLQA LEDRGLFRTD DELLPSLQPL ITLTMSPFGV PRYPIPMDAS LFIRPSGLPY
     TSAGVPPRKP SPTTIAPEPS VKGRRRKAEK KDTTAVFTHN VDGHMLQGDI DLVGVETVIR
     SKIYAATALG RFLSTWDSND RSNIWQTILP YLKAPGSSSQ LVAAMVTVEY AKIQGAKTRY
     VSLLSQSLNP VIENERPSWY SDIASYLHIA RAQCHSLLNA FRDHAHVSQF SLPMLAVIVQ
     GDQDAGPSAF SISDAEKVLG PDFEKLKRSL SPAQRMTALQ VLNDSRASAL TAVEEAKEVK
     DQRDMRIRAA AASALVALHD IPRKPSQIIK GMMDSVKKEE NVELQQRSAS AVASLVQYYT
     SASRRGPVDK VIGNLVKFCC IDTSETPEFH HNAGLETAIL SLRKEEDKKD HLDATRFEQE
     SREARIMRRG AKEALEQLAC RFGAELLDKV PNLASLIEGP LRRALTGDLP PDITDPNSQT
     GQEVVDGLST LRALVPKFHP GIYPWIISLM PIIAKSLQCK LSVIRYAAAK CFATICSVIT
     VEGMTMLVEK VLPNINNALD VHCRQGVIEC IYHLIHVMED NILPYVIFLI VPVLGRMSDS
     DNDVRLLATT AFATLVKLVP LEAGIPDPPG LSEELLKGRD RERQFMAQML DVHKIEPFEI
     PVAIKAELRS YQQEGVNWLA FLNRYHLHGI LCDDMGLGKT LQTLCIVASD HHMRKEEFAR
     SGAPEARRLP SLIICPPTLS GHWQQEIKQY APFLSCLAYV GPPAERSRLQ NSLGSVDVVI
     TSYDICRNDN DVFAPLNWNY CVLDEGHLIK NPKAKITLAV KRLKSNHRLI LSGTPIQNNV
     LELWSLFDFL MPGFLGTEKV FLDRFAKPIA ASRFSKSSSK EQEAGALAIE ALHKQVLPFL
     LRRLKEEVLN DLPPKILQNY YCDLSDLQRQ LFEDFTKKEQ KDIAKIVGST DKEAKQHIFQ
     ALQYMRRLCN SPALVVKENH KRYDEIQKSL AGKNSHIRDV AHAPKLTALR DLLVDCGIGV
     DPSTEGELDT GASYVSPHRA LVFCQMKEML DIVQNDVLKK LLPSVQYLRL DGSVEATKRQ
     NIVNQFNTDP SYDVLLLTTS VGGLGLNLTG ADTVIFVEHD WNPQKDIQAM DRAHRIGQKK
     VVNVYRLITR GTLEEKILNL QRFKIDVAST VVNQQNAGLS TMDTDQLLDL FNLGETAEGA
     EKPSQDGGVG GNEIDMVDID GEVKEKGKKG WLDDLGELWD DRQYQEEYNL DSFLATMKG
//
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