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Database: UniProt
Entry: A3LW54_PICST
LinkDB: A3LW54_PICST
Original site: A3LW54_PICST 
ID   A3LW54_PICST            Unreviewed;       661 AA.
AC   A3LW54;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN   Name=RAP1 {ECO:0000313|EMBL:ABN66909.2};
GN   ORFNames=PICST_67919 {ECO:0000313|EMBL:ABN66909.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN66909.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN66909.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000499; ABN66909.2; -; Genomic_DNA.
DR   RefSeq; XP_001384938.2; XM_001384901.1.
DR   AlphaFoldDB; A3LW54; -.
DR   STRING; 322104.A3LW54; -.
DR   GeneID; 4839646; -.
DR   KEGG; pic:PICST_67919; -.
DR   eggNOG; ENOG502S85C; Eukaryota.
DR   HOGENOM; CLU_507258_0_0_1; -.
DR   InParanoid; A3LW54; -.
DR   OMA; TSHKFFE; -.
DR   OrthoDB; 1406561at2759; -.
DR   Proteomes; UP000002258; Chromosome 5.
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   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR021661; Rap1_C.
DR   InterPro; IPR015280; Rap1_DNA-bd.
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; PF09197; Rap1-DNA-bind; 1.
DR   Pfam; PF11626; Rap1_C; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367107};
KW   DNA-binding {ECO:0000313|EMBL:ABN66909.2};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367107};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
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          44..120
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|Pfam:PF16589"
FT   DOMAIN          285..401
FT                   /note="Rap1 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF09197"
FT   DOMAIN          567..659
FT                   /note="TRF2-interacting telomeric protein/Rap1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11626"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   661 AA;  75288 MW;  A058A77FDC5B24D9 CRC64;
     MTFSTLHFEG ENTPRRTDRN LPLSMNSPQR SPYNSRLGLE KSTLFTNREG RSIRFYMEYS
     EPRRLHYKAL IETHGGVLLD HSVTDCFWLS TNPLTGRRSY RVQYIDDCVR LVTLQDIRIY
     SHPDFNIDTN LLHRGAGDTT SGMEMDPTSV AAAVVYGDAQ PNPNLSSAAD LPSDFALATA
     STSLSPGTAP KVRTHNRFTP QKDAFILEEV RKHPRARHSH EFFRNLAKNE ILKGHTGNSV
     RSRFRKHLEA DLQYVYQQES DGNPSKDAHG NYIPTKELPQ TLKNKYTAED DYYLCTEAKK
     YILAKESAKD GGEGRGSGKL PELKVLLPYS FFSNLCRPDR GGQDEVADSE NNPDKRNKKH
     IGQRHTLHSW RDRYRKFVGD GTIEKYIKSY EASENPKPLE RRGVINSSSL NNMTGELREI
     VGSNARNREE RALDEEIGQT KSSLIGVPDL NMSAGDVLES LEPIERPTMR EIEEDEEIIE
     DIEVDDIEDI EDFQDASTQL SSIQANFEDA VNPGSQDSQS VMKYIGKGVK FEDLFTDPSV
     LNYDLVSKLN TALRSISDDV QELAECLEEL GFKQALVEHL LYSTCCDKTR LFFLFRHIYN
     NLQDNLVSDG HIPVYELLQP PDEGGFWTKE QDDLLQAGRD DALEVQNKRQ IRTRREFLNK
     L
//
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