MOT1_SCHPO
ID MOT1_SCHPO Reviewed; 1953 AA.
AC O43065; O74784; O94734;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 4.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable helicase mot1;
DE EC=3.6.4.-;
DE AltName: Full=Modifier of transcription 1;
DE AltName: Full=TBP-associated factor mot1;
GN Name=mot1 {ECO:0000312|PomBase:SPBC1826.01c};
GN ORFNames=SPBC1826.01c, SPBC25B2.12.c, SPBC6B1.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA87285.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 564-761, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Regulates transcription in association with TATA binding
CC protein (TBP). Removes TBP from the TATA box via its ATPase activity
CC (By similarity). {ECO:0000250|UniProtKB:P32333}.
CC -!- SUBUNIT: Forms a complex with TBP which binds TATA DNA.
CC {ECO:0000250|UniProtKB:P32333}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC Note=Localized on chromatin.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000255}.
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DR EMBL; AB027981; BAA87285.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21270.1; -; Genomic_DNA.
DR PIR; T39739; T40642.
DR RefSeq; NP_596080.2; NM_001021992.3.
DR AlphaFoldDB; O43065; -.
DR SMR; O43065; -.
DR BioGRID; 276189; 3.
DR STRING; 4896.SPBC1826.01c.1; -.
DR iPTMnet; O43065; -.
DR MaxQB; O43065; -.
DR PaxDb; O43065; -.
DR PRIDE; O43065; -.
DR EnsemblFungi; SPBC1826.01c.1; SPBC1826.01c.1:pep; SPBC1826.01c.
DR GeneID; 2539633; -.
DR KEGG; spo:SPBC1826.01c; -.
DR PomBase; SPBC1826.01c; mot1.
DR VEuPathDB; FungiDB:SPBC1826.01c; -.
DR eggNOG; KOG0392; Eukaryota.
DR HOGENOM; CLU_000315_1_2_1; -.
DR InParanoid; O43065; -.
DR OMA; SYDICRN; -.
DR PhylomeDB; O43065; -.
DR PRO; PR:O43065; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; ISO:PomBase.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; NAS:PomBase.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:PomBase.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR Gene3D; 1.25.10.10; -; 3.
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 Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1953
FT /note="Probable helicase mot1"
FT /id="PRO_0000074334"
FT REPEAT 36..74
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 358..396
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 513..551
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 554..592
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 608..646
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 1191..1229
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 1270..1311
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT DOMAIN 1370..1543
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REPEAT 1580..1623
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT DOMAIN 1725..1877
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 79..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1901..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1494..1497
FT /note="DEGH box"
FT /evidence="ECO:0000255"
FT COMPBIAS 82..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1383..1390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1953 AA; 217632 MW; 0F53BB674ECC3038 CRC64;
MTTRLDRLVV LLDSGSTSVV RETAAKQIGD IQKVHPDELY NLLGRVVPYL KSKNWDTRVA
AAKAIGGIVE NVPVWNPNRT SPVKKEETED LPSFNGDTEE KPFIKTEEGA PASSQSQVVV
SSNLTSNSEV SKLEEERLST RSHSQEIKPI VDFGPDEETA KELNTELKGK FENSLLSFES
FDIANVLKAG KKLLGSASRD YDVNPANYST HYLQQLSNLK SRLDLAGEYL DDSIMNDLGD
NVGSNSKGSP TTSIPEHKTS INNNKPEDTP TPSENVHLSA RQRNALKRKA RQMKNSQKVR
VIDVAPTLVH QQNSTSSADK KTGADYNFTA QSRSDRLVVE HKAPIVPSAA VAVTSDSVWP
FETLVELLLI DMFDPSWEIR HGACMGLREI IRYAGFGYGR VVGKSEAENE QLNKKYFDDL
LCRIACVFAL DRFGDYLADQ VVAPIRESVS QVLGVALIYV PNDSVFSMYK VLHSLVFQNE
LGLTNTVWEA AHGGMLGIKY LVAVKYPLFF SHSDYLDSLI NTVIHGLANH DDDVRAVSAL
TLLPIADKLV QEKLSSCKNL LKVLWDCLDD VKDDLSSSTS CVMDLLSSLC SFTEVMNLMQ
ETANSDPEFS FETLVPRLFH LMRYTLTGVR RSVVYALTKF ISVQTSCSWI TGLTLRLCFQ
NVLLEQQEDI SKSSCELAQR VMDILYRDGP ESFSKLLYSH IEPMLKVSIT PIGSFRRPYP
LDTTLIVKPS GQPYAPSTSR ERNNNISELS NSRTKHRAKD DPKGSFCFSV DEPMLNGDVE
FVGEERMLKA RLRASSLLGR IIGRWKRDEI LLFFKPFLQA CLTSSFSTPV VLGSRLIESF
FEVEDNDLTI QKDELYHLLC DQFATVPREN YANLVSQLHV VRAQCNALLN TFLDVGRLSR
SKIPSLAVVV KGDPEAGPIA FGIADAEKLV GPTYENLCKL LSPSQKAQSS KALNEIKYLI
IDEISIYKIA KERQDIQCSA SIASAMVTYD KLPKKLNSII KGIMESIKKE QFSCLQMHSA
SAMMKLISAC YKESRQVISE KIVRNLCAYV CMDTTETPIF HDSGKNGILS LHSIGTSDDN
DEQVSGKLVD DSDDVSNDRK SSLSSVSDKD AAVLQRMGAQ LTLQQMAQNF GSSLFSRVPV
LSQCLFVPLQ QYAESGFPSE VDQASCTVGQ DLLDAMSILR FLVAYLDSGL QSEIVSTLPH
LLATLQSNYS AVRNMASKCF AAITESNAAG SKALHLLVED VVPLLGDASS TIHRQGAIEC
IYHVVQRLGV RILPYILYLI IPLLGRMSDA DQDVRVLATT SFATLVKLVP LEAGLPDPPD
LPQYLLDSRE KERKFLEQML NPSKVEAFSI PVPISADLRK YQQEGVNWLA FLNKYELHGI
LCDDMGLGKT LQTICIVASD HYNRQKLFEE SGSPKFAHVP SLIVCPSTLA GHWQQELSTY
APFLKVSAYV GPPAERAKIR SKMKKSDVVV TSYDICRNDV DELVKIDWNY CVLDEGHVIK
NARAKLTKAV KSLRSYHRLI LSGTPIQNNV LELWSLFDFL MPGFLGTEKT FQERFVRPIA
ASRDAKSSSK ERERGTLALE AIHKQVLPFM LRRLKEDVLA DLPPKIIQDY YCDMSDLQRK
LLNDFVSQLN INEELEDDET EKTQGTRKKK SQKAHIFQAL QYMRKLCNHP ALILTEKHPK
RNAIVKQLAK ENSGLHDLKH APKLTALGQL LRDCGLGNSS VNSNGIDSAL TNAVSEHRVL
IFCQLKDMLD MVEKDLLQAT MPDVTYMRLD GSVEPTKRQE AVTKFNNDPS IDVLLLTTHV
GGLGLNLTGA DTVIFVEHDW NPMRDLQAMD RAHRIGQKKV VNVYRLITRG CLEEKIMGLQ
RFKMNVASTV VNQQNAGLSS IGTDQILDLF NTTADEQQTV QNIDKEESED AAGRGLSGTS
KKALEGLPEM WDESQYDEFN LDGFISTLPK DAS
