GenomeNet

Database: UniProt
Entry: M1VYW0_CLAP2
LinkDB: M1VYW0_CLAP2
Original site: M1VYW0_CLAP2 
ID   M1VYW0_CLAP2            Unreviewed;       871 AA.
AC   M1VYW0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN   ORFNames=CPUR_08354 {ECO:0000313|EMBL:CCE34422.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE34422.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE34422.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE34422.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE34422.1}.
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DR   EMBL; CAGA01000088; CCE34422.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1VYW0; -.
DR   STRING; 1111077.M1VYW0; -.
DR   VEuPathDB; FungiDB:CPUR_08354; -.
DR   eggNOG; ENOG502S85C; Eukaryota.
DR   HOGENOM; CLU_006783_0_0_1; -.
DR   OrthoDB; 1406561at2759; -.
DR   Proteomes; UP000016801; 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; cd16100; ARID; 1.
DR   CDD; cd11655; rap1_myb-like; 1.
DR   Gene3D; 1.10.10.2170; -; 1.
DR   Gene3D; 1.10.150.60; ARID DNA-binding domain; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR001606; ARID_dom.
DR   InterPro; IPR036431; ARID_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; PF01388; ARID; 2.
DR   Pfam; PF08914; Myb_DNA-bind_2; 1.
DR   Pfam; PF11626; Rap1_C; 1.
DR   SMART; SM01014; ARID; 2.
DR   SMART; SM00501; BRIGHT; 1.
DR   SUPFAM; SSF46774; ARID-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS51011; ARID; 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:UP000016801};
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          275..365
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   REGION          165..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..210
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..594
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..667
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..706
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   871 AA;  97153 MW;  823A3092C0BE40D0 CRC64;
     MASSMRNGAQ AATGGQLFKD KTFWVARTKN GGVVTHLENE ADFRIADHCR KKKEVIPDSI
     SYEFITDSVK NGVTQLPDRY LIHPPFDQGT QESRKRTRTM FSPAEDAALL IYVESHTKDR
     TGNHIYKVFA ESNPRHTWQS WRNRYMKTLF HYPSYQREKL RSLGTKAPAP APAPAPAPAP
     APAPAPAPAP APAPAPAPAP APAPAPAPAP APAPVPVPVP VPVPADPATT LAACPSPQRK
     LTMSASAKGN PRQPSASPDS TLAERKEHEA EIEDQNNRNH FENEIRTFIE ESRRSVSLYP
     EVEGQSFHLY ELARAVVAQK VANEQVDWRR VAEDLGYDLK QNQGVANGLK KCFEKNLATF
     FEACRLIQAK LNERESSPSQ SEEDGSSPAQ SEEDGTPPAQ SEEDGTPPAQ SEEDGTSPAQ
     SEEDGTESEA HDEDRFYQDL EDYQDRSGLP IKRESEVGGK RLEFWHLGHA VLEHRESNGE
     VDWRSVAEDL EAKYDWRQDQ EVVDELKECF KENLAALFEK VFGDLEKGEA AQEHEEDEFQ
     SNLDSPERQL YPSSPPVGPS GHKRPLDDDD DDDDPVYLPE KSAKRRRLDR TAEIPSTPEE
     ILGIPSSCTP TGSKFRQQKE DEEEDEEDIE EIYGYAPPVM SSSDLTPPPG TSHSDFADVT
     PSPEPNFQAL NVEPIPLDLV PSRSVGRPQQ SDHAEPLQQR QSASDANKAS EIKRRFLPSS
     FYKRPSQDSP AQEAGNTSQQ PSQPESPDRR ASSSEPTILE CIGNYEAQGF SRDIVMEALR
     RTSLRPCRRA EHLMELLSMN EEVPFDIGGV WTDRDDLGLR WADCALARGS SATEFMKARA
     KEQLECLVRK HTEKEIDLRR RYLESFTREK A
//
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