ID H2APC0_KAZAF Unreviewed; 768 AA.
AC H2APC0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 08-NOV-2023, entry version 64.
DE RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN Name=KAFR0A07860 {ECO:0000313|EMBL:CCF56220.1};
GN ORFNames=KAFR_0A07860 {ECO:0000313|EMBL:CCF56220.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF56220.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF56220.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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; HE650821; CCF56220.1; -; Genomic_DNA.
DR RefSeq; XP_003955355.1; XM_003955306.1.
DR AlphaFoldDB; H2APC0; -.
DR STRING; 1071382.H2APC0; -.
DR GeneID; 13886229; -.
DR KEGG; kaf:KAFR_0A07860; -.
DR eggNOG; ENOG502S85C; Eukaryota.
DR HOGENOM; CLU_014729_0_0_1; -.
DR InParanoid; H2APC0; -.
DR OrthoDB; 1406561at2759; -.
DR Proteomes; UP000005220; 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; 2.
DR CDD; cd11653; rap1_RCT; 1.
DR Gene3D; 1.10.10.2170; -; 1.
DR Gene3D; 1.20.120.1480; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR021661; Rap1_C.
DR InterPro; IPR038104; Rap1_C_sf.
DR InterPro; IPR015280; Rap1_DNA-bd.
DR InterPro; IPR001005; SANT/Myb.
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; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF09197; Rap1-DNA-bind; 1.
DR Pfam; PF11626; Rap1_C; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_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:UP000005220};
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 71..158
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 300..360
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 300..356
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 26..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 87205 MW; 882AA053F744AA58 CRC64;
MSDADEITKA AEDFVNSLNT EIVVDEETAN GRANNAADEN TTKVTAVEEV SKSVSNDSKK
ASGSVDTDGS ENSEPLVGMK FFLNRDSDAH DSINDIEQLA RLIKSNGGQI LEDVPQSAKT
NVVIVSPYND TNLPTVTPTY IKACVQSKKR LDIGNYLVPY DEFRNVIDTQ LVNSTTQKEE
KIGTDDKTNA GEENKPNESD NEDSFHSVTD NMDPQITESN RNKEDMDKND RQEQERLDQI
RLLEQYSIME NHENGGSNNT NNANNGEVEV TSPPDANVEH ASQSPNDYQS NRTMLARASL
PSHNKASFTE DEDDFILDVV RKNPTRRTTH TLFDEISHYV PNHTGNSIRH RFRVYLAKRL
DFVYKVDQYG KLMRDESGNL IKTTIMPPSL KKKFTADEDY TLALAVKKQF YRDLYQVDPD
TGVSLISQDD SPNAIARRSL TMDSQVTPGS EPPFSTYHAN DRRGPIAREF FKTFAEQNPN
HTENAWRDRF RKFLLVYGID HYIEYFEDET KAGREPEPMK NLTNRPKRPG VPTPGNYNSA
SKRARAYQST TAAAAPATTT LAGASTSSQQ AYTIPENELL DEETMNFISS LRNDLVRNEQ
QLPFEYPPDL AEEIRNDFVN ETNYDNIDPD TIQFPPEIAT VDLFLPTFFQ LSSTREFMDK
LQEVISREYD TSQAEKLVQD LAEEAGIRKT FSTTVLTALS GDLMVFPRYF LNMFKYNANP
PMNVPGIWTR EDDDLLRNGN RDDVKMLIQK HRSARVEMRK KFIERDLI
//
