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Database: UniProt
Entry: F9X9I1_ZYMTI
LinkDB: F9X9I1_ZYMTI
Original site: F9X9I1_ZYMTI 
ID   F9X9I1_ZYMTI            Unreviewed;       410 AA.
AC   F9X9I1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN   ORFNames=MYCGRDRAFT_71018 {ECO:0000313|EMBL:EGP88428.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP88428.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP88428.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
CC   -!- FUNCTION: Involved in the regulation of telomere length, clustering and
CC       has a specific role in telomere position effect (TPE).
CC       {ECO:0000256|RuleBase:RU367107}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367107}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367107}.
CC       Chromosome, telomere {ECO:0000256|RuleBase:RU367107}.
CC   -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000256|ARBA:ARBA00010467,
CC       ECO:0000256|RuleBase:RU367107}.
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DR   EMBL; CM001199; EGP88428.1; -; Genomic_DNA.
DR   RefSeq; XP_003853452.1; XM_003853404.1.
DR   AlphaFoldDB; F9X9I1; -.
DR   STRING; 336722.F9X9I1; -.
DR   EnsemblFungi; Mycgr3T71018; Mycgr3P71018; Mycgr3G71018.
DR   GeneID; 13400422; -.
DR   KEGG; ztr:MYCGRDRAFT_71018; -.
DR   eggNOG; ENOG502S85C; Eukaryota.
DR   HOGENOM; CLU_006783_2_0_1; -.
DR   InParanoid; F9X9I1; -.
DR   OMA; FQGARFW; -.
DR   OrthoDB; 1406561at2759; -.
DR   Proteomes; UP000008062; Chromosome 4.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0010833; P:telomere maintenance via telomere lengthening; IEA:UniProtKB-UniRule.
DR   CDD; cd11655; rap1_myb-like; 1.
DR   Gene3D; 1.10.10.2170; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR021661; Rap1_C.
DR   InterPro; IPR038104; Rap1_C_sf.
DR   InterPro; IPR015010; Rap1_Myb_dom.
DR   InterPro; IPR039595; TE2IP/Rap1.
DR   PANTHER; PTHR16466; TELOMERE REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR16466:SF6; TELOMERIC REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF08914; Myb_DNA-bind_2; 1.
DR   Pfam; PF11626; Rap1_C; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367107};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367107};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU367107};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          21..89
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|Pfam:PF16589"
FT   DOMAIN          116..173
FT                   /note="Rap1 Myb"
FT                   /evidence="ECO:0000259|Pfam:PF08914"
FT   DOMAIN          324..405
FT                   /note="TRF2-interacting telomeric protein/Rap1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11626"
FT   REGION          177..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  44518 MW;  777BA6EEE540F16F CRC64;
     MADAPVLVTN GAGGSPAVGR LLEGKSFFLV QRLPARSHLI ADIESNAGRI VKLETNADYV
     IADHARKDAP AGSLSYTFVE QAIRKGALPD PLEHPAGPQV GTAREAGSVI PGKSFRTPFS
     AADDKILWRW VETAKANGEA SKGNDVYKRL EAVNPRHTWQ SWRDRYVKKL LGKPPAGVMV
     AANAPPSPPT APDNDQISNG RSARETTPRP SPKRRKVTAS PEKQVAGRSG PVFEQADFDT
     ATSSRPLDTQ DILDAQTQYA DLNVALPLSD DDDDLDDDSS EDSQIPAKPA TKHKVRPGRT
     VESQALTGDP EQIADKLDEW IATQEVRGYN NEASMRAMLC TSMRPDLAEL VLLGEKGGTG
     LPHDVSGIWS EREDRAVEGG DAAAIRRLEA KHGWDECKAR LKFLADWREV
//
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