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Database: UniProt
Entry: G9NMV8_HYPAI
LinkDB: G9NMV8_HYPAI
Original site: G9NMV8_HYPAI 
ID   G9NMV8_HYPAI            Unreviewed;       794 AA.
AC   G9NMV8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN   ORFNames=TRIATDRAFT_81783 {ECO:0000313|EMBL:EHK48238.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK48238.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK48238.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(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}.
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:EHK48238.1}.
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DR   EMBL; ABDG02000019; EHK48238.1; -; Genomic_DNA.
DR   RefSeq; XP_013946400.1; XM_014090925.1.
DR   AlphaFoldDB; G9NMV8; -.
DR   STRING; 452589.G9NMV8; -.
DR   GeneID; 25785624; -.
DR   eggNOG; ENOG502S85C; Eukaryota.
DR   HOGENOM; CLU_006783_1_0_1; -.
DR   OMA; WKYITDS; -.
DR   OrthoDB; 1406561at2759; -.
DR   Proteomes; UP000005426; 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; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR001606; ARID_dom.
DR   InterPro; IPR036431; ARID_dom_sf.
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; PF01388; ARID; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF08914; Myb_DNA-bind_2; 1.
DR   Pfam; PF11626; Rap1_C; 1.
DR   SMART; SM01014; ARID; 1.
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:UP000005426};
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          346..437
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   REGION          198..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..334
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  89951 MW;  AF62F2AE8FF6B254 CRC64;
     MASSITYNGV PSTVGGGNIF QGMKFWVSRL VPSRDWIIDQ IQTNSGTVVV QEKDADMLIA
     DHARKDVPLG SYSWKYITES VKAGFVQVED KYLNGPPPGQ PRPILAGSRA KKTRTPFSEQ
     DDAILAKHVL QKAIDTAGNK MYMELEALYP HHTYQSWRHR WVKILSLRSN HDIDRLARMA
     NLDVDNAPIT ARHIVRRHER EDWPQAPQHA PTVTGRTDQN ARSRTEASSR TAPRDPTRRQ
     QTTPSENLDR KSTTAEATSE QNGDGTENDS TPYHDAPTGE EQAQGQERIE DSEAESEGSQ
     GEKSKENAEE DGGGENVEEG EEPEEEDEEG GGAEDDTGVD RSLPSFTERD QFYSDLQDYC
     EANGRELQKQ CVIRDKRIDL WDLLQAVSTQ NLPLEEVDWR RVARYVGFDR AQSKEIIATL
     LQTSYHRHLA GFVEAMLSFE HDLDEDSEED EETIPQTAEA AAEPTTPSRN GNGTAKATKR
     LPDVQSPTPE QRSKRRRTIG ATIPVTPEAR EKTRRRQSAP APGQLGSIVD DGRVQADNSP
     HSIPMRDGQR QWSPEEPDNT PSQQLRSESN SVASPELGDT RHNQPRSSGY HFNDRGLETI
     MEEEPSASTP TKPKSKKRSL PSSFQQPQTI PPHERRRLVE QEQHQEEGTQ EAQAPEEQQQ
     TEDENWKTKE FHKWTKHYRE AGYSDEHISE AMYRTSWIPG ARMEQVLKSL QKGDEVPKNV
     QGIWTYRDDD KLDYIGQFET LEPVAGDSSE MQRRRAKAAR MLEQLLYKHT KSGVELRSEI
     HEEIAKQGGK KMRR
//
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