ID A0A2G5I7Z3_CERBT Unreviewed; 901 AA.
AC A0A2G5I7Z3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN ORFNames=CB0940_01744 {ECO:0000313|EMBL:PIB00624.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIB00624.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIB00624.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIB00624.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) 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:PIB00624.1}.
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DR EMBL; LKMD01000100; PIB00624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5I7Z3; -.
DR OrthoDB; 1406561at2759; -.
DR Proteomes; UP000230605; Chromosome 1.
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 Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU367107};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 22..93
FT /note="BRCT"
FT /evidence="ECO:0000259|Pfam:PF16589"
FT DOMAIN 117..174
FT /note="Rap1 Myb"
FT /evidence="ECO:0000259|Pfam:PF08914"
FT DOMAIN 814..895
FT /note="TRF2-interacting telomeric protein/Rap1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11626"
FT REGION 104..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 901 AA; 99373 MW; 481184DEEB62CA31 CRC64;
MAGASIVVSD ASAEHRRTGA ATLFANLSFF CLQKLPARSQ LIRDIEANGG RVVKNEKLAD
YVIADHVRKD VPAGSYSWTL ITTAIANGAL PDPADHYAGP RPGTIRDVGS AAPGKATRTP
FTHEEDKQLW QWVEQEKTRG GQFKGNDIYK RLEQINPRHT FQSWRDRYLK KLMNNPPAGV
QPTVPANAPP SPSTALDGEM EEEQASTPPA KRRRVEIVDE KDQGPEHSED QSADTVHAED
HGKKETDVDL LMPHAADIDN VLEDQWLPAW ELWAEAYPHR SAQEWAKFWQ EDVRPIYQAQ
LRDKGNTERP SVRPSDAGEN RRKRKRHFDV VPTNGESHFE PGSPQPRSQN HSPSRSSDVH
RIDHTTKAAT ATASESLGPF AELLTSDENR AAAQQITNES LVAFDESASR AGLVEASGEG
EDLIKLLTHE NNQLEHRPYI SDGPEIEDLR SSEVQQRPTE DDIGAIMPED DLASDFESQL
SGGTALTEAN LAAQEARHKA PLLRGADLPE DDANNDQSDF VKYLQQSLMP SHNQPELSQE
RNVSGSHSNA GKARSIEDES DHDVDEVILS NLEWPSSPHR PQVTAMPSNT QAEDIENVPL
AEAKGLTAGS PLAASSTARP DAIARSGGLE ARNMEPSDDL DQEVDLSVAF PEVGGGFDPS
SDRDSTPAMA EEEALDLGDY YDEVDGPNPH EYETPRKASQ LIEISSTSIP SSPLPDSPGS
QDGTRGRQIP RPLETQDFYN AETQQADLTM PLPLDTDDED GDGEQNDEHD QTAHDLTETI
EQYASSQAMR AESPSADLNS EDESERLESW MATMKVRGHD ESAIIEAVKC TSLRLDLAEF
VLMHVRAGKG IPTDVPGVWN EDEDEQLEGG NARAIRLLEK KHGWDACRAR LNYLEQYRDT
E
//
