ID S8BNR1_DACHA Unreviewed; 971 AA.
AC S8BNR1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN ORFNames=H072_5000 {ECO:0000313|EMBL:EPS41133.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS41133.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS41133.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS41133.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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:EPS41133.1}.
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DR EMBL; AQGS01000256; EPS41133.1; -; Genomic_DNA.
DR RefSeq; XP_011110889.1; XM_011112587.1.
DR AlphaFoldDB; S8BNR1; -.
DR STRING; 1284197.S8BNR1; -.
DR eggNOG; ENOG502S85C; Eukaryota.
DR HOGENOM; CLU_305432_0_0_1; -.
DR OMA; WRERWVK; -.
DR OrthoDB; 1406561at2759; -.
DR Proteomes; UP000015100; 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 Gene3D; 1.10.10.2170; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50172; BRCT; 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:UP000015100};
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 12..92
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 207..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..859
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 971 AA; 106770 MW; CAB72BE1FD2952CF CRC64;
MADEEDEPAS TQGGFLFKGL AFHLSNLCPM KSHFQSLLQV NGAKLCKTET GADAIISDHL
KSQGNVPSAV SFTWIEACVK SGELVDIEPY RISALQSNSE APKKTGKATS SSIRKQIAAA
GPTPPIAGTR RAFTKEEDDL LLWWIEHAGL TGGNAVYKSL AEAFPTHSFQ GWRERWVKKL
RKYPEYAKGP FPPKDFDVTK VKGWHEGIHR PNDGSLSSPG GDPPVGTQDT PEMEEEIEDI
SSIMRSVHEE ALKDRLPEIL SKNNEEEINE IFEQIVEKFP EHTVAEYRKL FDEKVLPEHK
KNEANEGRKK KKKQPTKPHT TEKKDQTVVN FEISMIEQKA LFSKFDEIVL GDSKEEQLEI
CQAIADEFPG RSAEEFFGYF LSKMKPAVKH LKLKGKVRPE DLEEAVLSAL NGDKLEEPTA
DGTDKGREQV AIPANPSPGS NKPDTRFERL ATMTPSRKSL GLKVAAEGVD NSPKTKSISK
SPGTKLTSAK TSPDIQINRE AQIAAKGQVL VYSPKNQDNL RTPNKKSSQG SPGAYHTPSS
TKPLTSSVIS VRRNPPSASA SPTPRAKVQV VADPSNDGVT PDPPTQGAQA TFIASVHEHF
NSLSQQQGSD APASSPPALA VIRGVSPHLS AKPRLNSPML TSPMPTSSTT YEESDPIPFQ
EPTKAAASSL RKTARLSSSG SGRPPKRRKA GPGDQRRLVV ESTPESKLFP PPLPVISSSA
FGSSPSTQPR FFNQEPSSPT QSFLVQKSAR KLKGIAHTKR DSISSSQETK MPTIVSEHGD
TTEDEADPMD LDSVTNRNLG MMNDHSPTIL NRRSFTPSFS AESEDVEEPV YSDDDETVPN
SLAPESPEEE EEDEEEESVR TIDQALDAIS PLIDEMTKKY GLEAGCVGLV IERTTADRKL
VELVLRQVVK HLDKNANLDN FVWPIKRGIW TEEDDKALEG DSDQDKIIYL AQKHGDSLIL
LRHQWLEAFR Q
//
