MOT1_ASPFU
ID MOT1_ASPFU Reviewed; 1891 AA.
AC Q4WJI7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=TATA-binding protein-associated factor mot1 {ECO:0000250|UniProtKB:P32333};
DE Short=TBP-associated factor mot1 {ECO:0000250|UniProtKB:P32333};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P32333};
DE AltName: Full=Modifier of transcription 1 {ECO:0000250|UniProtKB:P32333};
DE AltName: Full=NCT transcriptional regulatory complex subunit mot1 {ECO:0000303|PubMed:31969561};
GN Name=mot1 {ECO:0000303|PubMed:31969561}; ORFNames=AFUA_1G05830;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, INTERACTION WITH NCTA AND NCTB, AND SUBCELLULAR LOCATION.
RX PubMed=31969561; DOI=10.1038/s41467-019-14191-1;
RA Furukawa T., van Rhijn N., Fraczek M., Gsaller F., Davies E., Carr P.,
RA Gago S., Fortune-Grant R., Rahman S., Gilsenan J.M., Houlder E.,
RA Kowalski C.H., Raj S., Paul S., Cook P., Parker J.E., Kelly S.,
RA Cramer R.A., Latge J.P., Moye-Rowley S., Bignell E., Bowyer P.,
RA Bromley M.J.;
RT "The negative cofactor 2 complex is a key regulator of drug resistance in
RT Aspergillus fumigatus.";
RL Nat. Commun. 11:427-427(2020).
CC -!- FUNCTION: Regulates transcription in association with TATA binding
CC protein (TBP). Removes TBP from the TATA box via its C-terminal ATPase
CC activity. Both transcription activation and repression require its
CC ATPase activity (By similarity). Part of the NCT transcriptional
CC regulatory complex that acts as a key regulator of ergosterol
CC biosynthesis and the azole exporter cdr1B (PubMed:31969561). The NCT
CC complex binds the promoters of genes linked to azole susceptibility,
CC and especially represses the expression of cdr1B transporter
CC (PubMed:31969561). {ECO:0000250|UniProtKB:P32333,
CC ECO:0000269|PubMed:31969561}.
CC -!- SUBUNIT: Forms the NCT transcriptional regulatory complex with nctA and
CC nctB. {ECO:0000269|PubMed:31969561}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:31969561}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AAHF01000007; EAL88295.1; -; Genomic_DNA.
DR RefSeq; XP_750333.1; XM_745240.1.
DR AlphaFoldDB; Q4WJI7; -.
DR SMR; Q4WJI7; -.
DR STRING; 746128.CADAFUBP00000610; -.
DR EnsemblFungi; EAL88295; EAL88295; AFUA_1G05830.
DR GeneID; 3507592; -.
DR KEGG; afm:AFUA_1G05830; -.
DR eggNOG; KOG0392; Eukaryota.
DR HOGENOM; CLU_000315_1_0_1; -.
DR InParanoid; Q4WJI7; -.
DR OMA; SYDICRN; -.
DR OrthoDB; 61251at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0000228; C:nuclear chromosome; IEA:EnsemblFungi.
DR GO; GO:0005667; C:transcription regulator complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:EnsemblFungi.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:EnsemblFungi.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0045898; P:regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR000330; SNF2_N.
DR PANTHER; PTHR36498; PTHR36498; 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; SSF48371; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1891
FT /note="TATA-binding protein-associated factor mot1"
FT /id="PRO_0000449616"
FT REPEAT 30..68
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 473..511
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 569..606
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 957..996
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 1139..1177
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 1181..1216
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 1219..1257
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT DOMAIN 1316..1489
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REPEAT 1526..1565
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT DOMAIN 1663..1813
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 184..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1440..1443
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 188..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1329..1336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1891 AA; 210167 MW; 29F5E577251C99D6 CRC64;
MTSRLLETGS TPFIRNTAAQ QLADVQKQHP DELFNLLGRI LPYLRSKSWD TRAAAAKAIG
LIVANADTFD PNQDDGQEIK KAENDDLDVD IKSEEELLSP MDDSLLQLER LDLPSILKYG
KRLLGSAGKE YEYSLAAMDP ASRLQHQKKT LTSRLGLAGE YIEEDLINDN DLVSKPVVKE
EPSFVASREH SIQGTSQPLA SPIEPANGEE SGLSKRQLNQ LKRKNKQSAR MGANKVRVVD
LSSRRASENV TTPSVATPYP IKSENGEERN GDSKPDYFSL DRSAGDDESK IVSEFKGASV
PENPLLQPES TEEGPNPNWP FELMCDILMV DLFDPNWEIR HGAAMALREV IRIQGAGAGR
VQGKSRAEND ILNRKWLDDL ACRLLCVLML DRFGDYISDN VVAPIRETVG QTLGALLSQL
PSRSVISVYK CLYRIIMQTD LGLERPIWEV CHGGMIGLRY LVAVRKDLLI KDSKLMDGVL
EAVMKGLGDY DDDVRAVSAA TLVPIAEEFV KTRQSTLGTL MTIVWDCLSN LQDDLSASTG
SVMDLLAKLC TFQEVLDAMK ANAAVNPESS FGKLVPRLYP FLRHTITSVR SAVLRALMTF
LQLEGEGTDE WVDGKTVRLI FQNLLVERNE GVLKQSLQVW SELLNSLETR GSFKSESDLL
SHIKPLITLS MGPFGVPRYP VPMDASLFIK PSGLPFPSSA AAPARSSPAS NTPEGTKGRR
RKSEKKEAPP PSAHNVDGHM LQGDIDLVGA DTMLRSKIYA ARALGQLLFV WDQNQLPSLW
QSILEGLNHS ASTSQLASAM IVEEYAKLSG PSGRYASTLC ENLRPIIEGE RPPWYSDIAC
YLHVARAQCH SLLNTFRDHA HVPGSRLPVL AVIVQGDPEA GPNAFSLSDA EKVIGPDFER
LKKGLTPAQR ITALQVLNDT RATAESAVNE ARNAREQRDL RVRAAAAGAL VALSDIPKKP
SHIIKGMMDS IKKEENAELQ QRSATAITSL VEYYTTSAKR GPVDKVIGNL VKYCCVDTSE
TPEFHHNAML EKSILSLRKE EDRRDHPDAA KFEREAKEAR IMRRGAKEAL EQLAVKFGSE
LMAKVPNLAS LIERPLKEAL AADELPANIR DPENELGQEV VDGLSTLRAI LPKFHSGLYP
WVVDLLPLVV KALQCNLSVI RYAAAKCFAT ICSVITVEGM TMLVEKVLPM INDALDVHHR
QGAVECIYHL IHVMEDGILP YVIFLVVPVL GRMSDSDNEV RLLATTSFAT LVKLVPLEAG
IPDPPGLSEE LLKGRDRERQ FMAQMLDVRK VEEFKIPVAI KAELRPYQQE GVNWLAFLNR
YNLHGILCDD MGLGKTLQTI CIVASDHHMR AEEFARTQKP EVRKLPSLIV CPPSLSGHWQ
QELKQYAPFL NCVAYVGPPA ERSRLQSALP NADIVVTSYD ICRNDNEVLN PINWNYCVLD
EGHLIKNPKA KATIAVKRLL SNHRLILSGT PIQNNVLELW SLFDFLMPGF LGTEKVFLDR
FAKPIAASRF SKSSSKEQEA GALAIEALHK QVLPFLLRRL KEEVLNDLPP KIIQNYYCDP
SELQRKLFED FTKKEQKALQ DKVGSTEKAD KEHIFQALQY MRRLCNSPAL VVKEGHKQYN
EVQQYLAAKH SNIRDVAHAP KLSALRDLLI DCGIGVDSPS EGDLSGASYV SPHRALIFCQ
MKEMLDIVQS EVFNKLLPSV QFLRLDGSVE ATRRQDIVNR FNTDPSYDVL LLTTSVGGLG
LNLTGADTVI FVEHDWNPQK DIQAMDRAHR IGQKKVVNVY RLITRGTLEE KILNLQRFKI
DVASTVVNQQ NAGLGTMDTD QLLDLFNLGE TAETAEKPSD AAGNEVDMVD IDGNVKEKGK
KGWLDDLGEL WDDRQYQEEY NLDSFLATMK G
