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Database: UniProt
Entry: A0A2B7XVV1_9EURO
LinkDB: A0A2B7XVV1_9EURO
Original site: A0A2B7XVV1_9EURO 
ID   A0A2B7XVV1_9EURO        Unreviewed;       616 AA.
AC   A0A2B7XVV1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN   ORFNames=AJ79_03743 {ECO:0000313|EMBL:PGH13326.1};
OS   Helicocarpus griseus UAMH5409.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX   NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH13326.1, ECO:0000313|Proteomes:UP000223968};
RN   [1] {ECO:0000313|EMBL:PGH13326.1, ECO:0000313|Proteomes:UP000223968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH13326.1,
RC   ECO:0000313|Proteomes:UP000223968};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PGH13326.1}.
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DR   EMBL; PDNB01000047; PGH13326.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7XVV1; -.
DR   STRING; 1447875.A0A2B7XVV1; -.
DR   OrthoDB; 1406561at2759; -.
DR   Proteomes; UP000223968; Unassembled WGS sequence.
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   CDD; cd11653; rap1_RCT; 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:UP000223968};
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          20..94
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|Pfam:PF16589"
FT   DOMAIN          116..176
FT                   /note="Rap1 Myb"
FT                   /evidence="ECO:0000259|Pfam:PF08914"
FT   DOMAIN          515..589
FT                   /note="TRF2-interacting telomeric protein/Rap1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11626"
FT   REGION          172..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  69462 MW;  D5310E0EDFA4706F CRC64;
     MAGSTVVYTD VSNPNNVSGD LFKDMKFWLS KTVPSRSWMK QIIEANGGKV VFLEKDADVL
     LVDHMKPNNP PGSTSFQYVE KSIRNGSLEN IEDHRAGPPS DYIRPVGSAM RQKGHRTTFT
     PEDDQTLYDW VKPFEENGGR FRGNKIYQQL AEKYPHHTYQ SWRDHYLKKV RDRPRPVTPE
     RQRSRAAAAS EPARGPSNEE HAQPEEPEDT SRMQRSRSNK TKYEKFTAEE KEDLLKVVKY
     ILNINPGKED EAWAEYAKDT GKSATEWKSF FRDVVLPEYK AEKSKEGSRH RALQAPHRET
     IATSSTSLEM KRIEPPRTDR GGSFRRPSVP NQQPPSPHTH QEVNGNGKRP RTSTDSSPIR
     RESASFQSRK RRIAEPAPQE TVSPSAASGR SRIRASMPRS THSRHPSSTL ETPSKSKPST
     SHNNKPTPTS RAVSATNSDQ FETAPQPEGA LQSHYQTPPQ VLDRRNEFNN SPTPRPTPAR
     AAPTSKPPAK TKAKTADERL AEWFHSKTEG PNACSRDQAF EAMDCTTMIP DLAEIVLEHF
     ARGEGIPSDA RGVWTKEDDE RLQAADSRGV EALLKKHGNE LFNMRFDYLL TRENALEQRN
     GEQSGTEEHQ ACCADS
//
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