GenomeNet

Database: UniProt
Entry: V2XN75_MONRO
LinkDB: V2XN75_MONRO
Original site: V2XN75_MONRO 
ID   V2XN75_MONRO            Unreviewed;      1875 AA.
AC   V2XN75;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Tbp associated factor {ECO:0000313|EMBL:ESK94301.1};
GN   ORFNames=Moror_8286 {ECO:0000313|EMBL:ESK94301.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK94301.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK94301.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK94301.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK94301.1}.
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DR   EMBL; AWSO01000147; ESK94301.1; -; Genomic_DNA.
DR   RefSeq; XP_007846445.1; XM_007848254.1.
DR   STRING; 1381753.V2XN75; -.
DR   KEGG; mrr:Moror_8286; -.
DR   HOGENOM; CLU_000315_1_1_1; -.
DR   OrthoDB; 180798at2759; -.
DR   Proteomes; UP000017559; 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:UP000017559};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1297..1470
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1649..1808
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          123..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1014..1040
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1015..1040
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1875 AA;  206821 MW;  F749B840A5E90C96 CRC64;
     MSVVARIIPF LHSKSYETRT AASVALSQIF TLTPLWQPTY DPSVMSTDST TIPVPEYPPF
     SVQELIAQGK LLLASSGKEF VKPAVLSSPA EVKKARKEAM GRLGLEFLDD VAEEMDLDKE
     LGADLEGNGD VDMDQVKSEV PPSPMDVCPP KKEPESGPTS RSATPADVPP TTPSEPEQQD
     LSAMSARERN RLKRKRKPGN NAFVAAPPPQ SAGAKYSASA AGNNKARLVA PEENTQEKSR
     VGSPNAGSSP DKVVIDPSKG GAVSAKDVKP SKALEVGPGV WVWDGLVKVL EVDLFSAAWE
     VRHGAAMALR ELLKIQGKHG GMHGGATPEE NEIAHERWCN DLSAKFLCVF VLDRFGDFVS
     DQVVAPVREM VSQTLASLLI HMPRRSVLHV HSILLQMIKQ EFAIPKSTET RKLSKKRNGE
     AEQKAHVWEV RHAGLLGIKY EVAVRSDLFE ADSIKQGVKQ EENAEFDDDG KAILRDVVDA
     AVLGLGDKDD DVRSVAASCL LPIAGHFVNN LPDSLDRVLL VLWNCLSDMK DDLSSSVGAV
     MELLGKLVAY DQVIKILADE SVSLPLTTLA PTLYPFFRHT ISNVRFSVVN TLHSFLTVES
     LPRDWIGLPF LQLLFQNLIV EERADIRDAS LQAWRTTLSI VSSIPGWVES QISQQAILDW
     YAIVMTPLGM PIDPSTFYRP SVTVEGDVPE RHNVDKNMLA QDLALITMEV VYKARIAAST
     ALATLMTFWP QEPQSADAMF QPILLHYIES TSMLQKLLSA VIAEEWACEY NKNPTSSALI
     DISPLAKELS QKASSFLQAT PPAAYHEMAY SLARIHADCI ALLHSFSTDC KLPSSSIPTL
     GSEIDITGSR PGCFTIETAQ AAVGLMFTRL KDSLGRAKKK ELNAIVEKRV LVVASIDRYN
     EVKAQNDIRV SATFAAAYVA FRGTPDKFSP IVKGIMNGVK NEENLDLQTR SAVAVASFID
     FCRQHQLPQP PEKIVKNLCT FLCQDIEQTP TFAYTRKFTD GILSYQAVSA AQHNGKEAAK
     EKDKDKEKEA PRADDSAKSR ISRRGAGLAF NQLSARFGAD LLVVVPNMWA SMVGGLESAF
     SKSSSPEQSD TLMEKQFGQD VIDSLSVLEA VAPTLHEDLW PKVSETFPML LLALRSKFAI
     IRQSAARCFA TICDIMTAEA MRFVIENVVP LLGDALSLEN RQGAAELIYH IVQRLDIKAL
     PYVIFMVVPV LGRMSDNNDD IRSTATNTFA SLVKMVPLEA GLPDPPGFPE ELLKRRDDER
     QFLAQLLDGS KVEPYTIPIP IKAELRKYQQ DGVNWLAFLA KYQLHGILCD DMGLGKTLQS
     ICILASKHSE RAQRYKETGS PDSVHLPSLI ICPPTLTGHW YYEILKYVDN LKPVLYTGNS
     RERTKLLSQL KSYDVVITSY EVVRNDINNL EGIRWLYCIL DEGHIIKNAK TKLTKAVKSI
     QSQHRIILSG TPIQNNVLEL WSLFDFLMPG FLGTESSFNE RFGKPILSNR DGKAKNGEAA
     ALALEALHKQ VLPFLLRRLK EDVLNDLPPK IIQDYYCELS EIQKNLYDDF SKSQAHHDAE
     NAVQSAQNKE GKEQQHVFQS LQYLRKLCNH PALVLKDAEA VSAALDRVGA KAEGLNDIQH
     APKLLALKQL LLDCGIGGGT PNTSTLDQGK SELIDTVPES NGAFSQHRCL IFCQMKQMLD
     IIESDLFKQH MPSVTYMRLD GGTEANKRHA IVQTFNSDPS IDCLLLTTHV GGLGLTLTGA
     DTVIFVEHDW NPMKDLQAMD RAHRIGQKKV VNVYRLITKG TLEEKIMGLQ RFKLNIANSV
     VTQQNSGLSS MDTDLVLDLF KRTNDGDAAA ALKKKAKEAN VPVSQKNLLV GLEDLPPEDE
     YEGLDLSSFM GSLGK
//
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