ID S7QLY2_GLOTA Unreviewed; 793 AA.
AC S7QLY2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN ORFNames=GLOTRDRAFT_135238 {ECO:0000313|EMBL:EPQ60571.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ60571.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ60571.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ60571.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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.
CC {ECO:0000256|RuleBase:RU367107}.
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DR EMBL; KB469296; EPQ60571.1; -; Genomic_DNA.
DR RefSeq; XP_007860953.1; XM_007862762.1.
DR AlphaFoldDB; S7QLY2; -.
DR STRING; 670483.S7QLY2; -.
DR GeneID; 19303280; -.
DR KEGG; gtr:GLOTRDRAFT_135238; -.
DR eggNOG; ENOG502SQ9M; Eukaryota.
DR HOGENOM; CLU_343578_0_0_1; -.
DR OMA; AVRPQWV; -.
DR OrthoDB; 1539412at2759; -.
DR Proteomes; UP000030669; Unassembled WGS sequence.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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 SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|RuleBase:RU367107};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367107};
KW Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW Telomere {ECO:0000256|RuleBase:RU367107}.
FT DOMAIN 471..542
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 157..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 85899 MW; AD8E2B195E350DD7 CRC64;
MDWIGVHATF LRCFEHSSLS TMAAAMQAPF EHAMSLSQST APPTNIFTLS AQPIRVFVEA
SGVQSRPKLI RSLRNAGAHI SLSPNDAQVI LVDSSTLEGV QFVREWTADS GKVVLEAIWA
RKCMKAGRLL WDADNWGGCL CALSSDGQSV VIATPQEEPN HLPTPSPTPT RPVPGPSARP
AAPPAPAAES RPLSSSGTAH SNGAAAVAQS SRRSSSVQLN HVPSPGPSSY PPPPPPSQGT
PQLPYPQLQT PAQLLALQQQ MQQIPPNILP ELLNMYALQR MTYPGLPMMP YNPMFYPSQP
DQAQNIPYNP LQPHPSQPLP QPQQQQQQPY SPLRMSNMSP PPPVARPPSA RPPYSSSSQT
SRDAQSPFSR PVSSSHKRKT PPSLSPSSYS PSPSPSASAA SVSTPMRSKG KEPADSHRDA
TPDLSQPSQT ASSSRGSPPR RTILSHRRPG EIFISDAGEP LLFHVQVDLK NRMQVLQAIK
KNGGKITPDI ENADYIILYT RSKTFNALYD STEANGKVPV QPTFVLDCVE ENALLDPENY
ILEHPDPKRR RKKAKNKTKA NGKGTPAKSK AASAKRTRRT RIVPVSGDDD GGGVGDSPPP
PTNTILLPTG KYLFTDEERE YARDYIELCL TRDPTTSGTR IAQKLAAKMP NHTPSSWSTV
VGRMNAWTDS VRKRVSASRM QPQSAADAPT PDGVSHGTGG GGGEVSQAGG SADDIYHQEL
NYLVHFLMTN DPNESEEQTF QRLENQAPCR TSASWIQFYD EHVEDITRAL GFDAGGVAPE
SGHMNPEPKV EET
//
