ID A0A0D1C1L3_USTMA Unreviewed; 2115 AA.
AC A0A0D1C1L3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=MOT1-transcriptional accessory protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=UMAG_04230 {ECO:0000313|EMBL:KIS67732.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS67732.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS67732.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM003151; KIS67732.1; -; Genomic_DNA.
DR RefSeq; XP_011390709.1; XM_011392407.1.
DR STRING; 237631.A0A0D1C1L3; -.
DR EnsemblFungi; KIS67732; KIS67732; UMAG_04230.
DR GeneID; 23564480; -.
DR KEGG; uma:UMAG_04230; -.
DR VEuPathDB; FungiDB:UMAG_04230; -.
DR eggNOG; KOG0392; Eukaryota.
DR InParanoid; A0A0D1C1L3; -.
DR OMA; WYSDIAC; -.
DR OrthoDB; 180798at2759; -.
DR Proteomes; UP000000561; Chromosome 12.
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:UP000000561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1530..1703
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1889..2046
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 40..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2060..2115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2115 AA; 228060 MW; 794388F33C4C9913 CRC64;
MAATRLDRLV SLLDTGSTPA IRATAAKQLG QIAAVRIRGQ STAQQAAAHA RPQKVESSTQ
SNAIVSGTST PTIDPEADGL VKSEDASSSA SKKQTAKFGT SEQINKQHNF SGPSVDDQFG
IYRGTDGDWD EITSYLARVV PFLRSKSWDT RVAAALAIES ICHAAGIWDP DIQPSKPGES
SKSILTDDDD DIKDEKPDLS ELLATESLLT FDAFSLPTVL ATGTKLLSSA GKEFEQASLA
VGGDRLAQAK KDVASKLGLG FGIDEMDIGM DVEAELKTGE SATISSVPHS SQGSVDWRTA
AGGASKSKLP APRFTGGSSP AVSSLPPLRF ANNGASASPS PVTPTFAPAI SAPSPSPLPV
ASGSEAPADE IDMSKLSARE RNALKRKRKI EGKNGPSDAK TRVIDSTDFA SQSAAGGLRV
KTPSGAFVQT PATPANAETA GDYLAAGPPP TPKHPAGGPG SLPAVTGSVS TPTPISEVPG
SPAAASSPAV GVAGAPAYSS SADPFQVRPG EWPFRLVVDT LSVDLFSPTW ETRHGAALGL
RELLKTQGSG GGKVQLASQQ DNAKMHKAWC DDMSIKLLCV FALDRLGDFV FDQVVAPVRE
TASQTLACLL PHMPESSILL VHNVLLQMIR QDHAAEGATT DFNAGFAAKR GKKGYVWEVR
HAGLLGLKYE VVVKKDLLMS SESVKSEIAD IKTEVPDHKP ISEETAIIDT AKMLRDVVEV
AILGLKDDDD DVRAVAASVL VPIVDVILEK LPTEVGRLLN QLWDCLGDLK DDLASSIGGV
MDLLAKLVEH PGIVIHLRAE AQEQRALSLL IPRLFPFFRH TITSVRLSVL NALRVFLTVP
SLPKDWIDER VLRLLFQNLV VEEKLPIRRA SADAWRHALA HVAGDAATVQ SLLGPYIVDF
FRIIMTPLGS PIDFTLFYNA SFGSSGHADT NRHNVDKSIL TQDLSLVGVD AVIRGRLSAA
EALGDALARF PRAEDELTFG AVLREYLEST SALQKCLSAA IIQEWAQACA TLGIDLKDSS
TIVPDIAGRL ISALETPAPP TYAEMTVMLQ RIQAECQGLY NSFQRDAKVA KAKIPALPAT
VDPLGMMADA FTVDTAKAVA STGFDSLLTH AGSKAKKAAL PLLEDRRRKL IAAIGFYQAN
KEKQDTQVFA SIASAVISLK VLPSKLNPVI RSIMNSVKFE ENMDLQTRSA RSVARLVEYC
VSPTAKSNPS DKIVKNLCAF VCQDTTRVAI FAASKNVREG ILSMNEPTVV PRGPGRTSVK
DETVESEEVL QGKLIRRGAA AALAQLADLF GDTLFDVVPM LWQCMSSSLV GTFGSTSADA
DALIEKQDDL GQSILDACAV LDVNLPNLKG SLCDKVVELL PALTLAIQSE FAVIRSAAAK
CFAVVASCLT EVALKHIVEK VVPLVGDPAS ITNRQGAVEL IYHTVQQLDL KILPYVIFLI
VPVLGRMSDN DEMVRLVATN TFASLVKMVP LEAGLPDPPG FPSELLERRE TERKFLMQLL
DGSKVEPYQI PVKINAKLRK YQQDGVNWMA FLAKYQLHGI LCDDMGLGKT LQSICILSSK
HFERAERYRL TQAADAKPLP SLIICPPTLT GHWCHEIKQY ANNLRPLLYS GLPAERARLQ
GEIHRYDAVV MSYDVVRNDI AALSQISWNY CILDEGHVIR SAKTKTTKAV KMIRANHRLL
LSGTPIQNNV LELWSLFDFL MPGFLGTERS FHERFGKPII ASRDGKLGAK EQEAAALALE
ALHKQVLPFL LRRLKEDVLD DLPPKIIQDI ECDLGEIQKQ LYDDFSKDQN EDEAEAFASS
EASLAGKEPN SEKQHVFKAL QYMRKLVNHP SLVLTDDNPK HVAIKHKLNK SGGSLNDISH
SPKLQALRQL LLDCGIGASG AAAAAGSGGV SDLNGDIGGE SAVSQHRVLI FCQLKQMIDI
IQRDLFAALM PSVSYMRLDG SVSAEKRHSI VQTFNADPSI DVLLLTTQVG GLGLTLTGAD
TVIFVEHDWN PMKDLQAMDR AHRLGQKKVV NVYRLITRNT LEAKIMGLQR FKLNVANSVV
NQQNAGMDSM ETDQILDLFN AQGGTSGTDG GANGDPAKKK GFAKLTQKQI LEGAHRGPEN
EEQEYSQMSG WRPDQ
//
