ID A0A1B7P897_9EURO Unreviewed; 589 AA.
AC A0A1B7P897;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN ORFNames=ACJ72_00402 {ECO:0000313|EMBL:OAX85209.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX85209.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX85209.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX85209.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-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:OAX85209.1}.
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DR EMBL; LGUA01000021; OAX85209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7P897; -.
DR STRING; 1658172.A0A1B7P897; -.
DR OrthoDB; 1406561at2759; -.
DR Proteomes; UP000091918; 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:UP000091918};
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..94
FT /note="BRCT"
FT /evidence="ECO:0000259|Pfam:PF16589"
FT DOMAIN 117..177
FT /note="Rap1 Myb"
FT /evidence="ECO:0000259|Pfam:PF08914"
FT DOMAIN 498..573
FT /note="TRF2-interacting telomeric protein/Rap1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11626"
FT REGION 92..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 65451 MW; 108398A8D4CE2705 CRC64;
MAGPAVVYSR VSNPTDMSGS LFKDTKFWLS RTVPSRSWII QQIQANGGKI APLEKDADVL
LVDHMRGNNP PGSTSFQYIE KSIQNGKLEN LEDHHAGPQP GYVRPVGSTT TRQKSRRSAF
TAKDDQILYD WVKPFEEKGG QIGGNKIYQQ LAEKYPQHTF QSWRDRYLKK VKDRPRPVTP
ERGKSNEAAA LEPGGDARGE RDHPASASRT RALASGSKGY DNFTEEEKED LLTHAKYILN
IEEGKEDEAW SRMPKMSRRS KTISSRHTQL ANRVEPIATS SANTTSLRTH RSESYSHASP
SRIEKRQHPT THAEQQTTGK RLRHATGSPP TDTESSFVLS SKREAVEHIP QAMAYPSTTS
QQSDEATVST PRPTNSRRSS IREAGALANP NPPSPSNYKT SVSESLSISP TNSTSEDRFE
TAPQFQQETV ENGYQAPPEI INARNEVNGS PTPQPTQIMP ARADAHPSNS SSSSTDDQPT
VERMDEWINS KTTGRNAYSQ QQVIEALACT TMDADLADTV LKAMAAGKGI PNNVKGVWTK
EDDERLEASD SRDIEALLHK HGNELFNARF EYIMTRKEVM MQMERGVEG
//
