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TRA1_SCHPO
ID   TRA1_SCHPO              Reviewed;        3699 AA.
AC   Q9HFE8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Transcription-associated protein 1;
GN   Name=tra1; ORFNames=SPBP16F5.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Essential component of histone acetyltransferase (HAT)
CC       complexes, which serves as a target for activators during recruitment
CC       of HAT complexes. Essential for vegetative growth. Functions as a
CC       component of the transcription regulatory histone acetylation (HAT)
CC       complexes SAGA, SALSA and SLIK. At the promoters, SAGA is required for
CC       recruitment of the basal transcription machinery. It influences RNA
CC       polymerase II transcriptional activity through different activities
CC       such as TBP interaction and promoter selectivity, interaction with
CC       transcription activators, and chromatin modification through histone
CC       acetylation and deubiquitination. SAGA acetylates nucleosomal histone
CC       H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC       interacts with DNA via upstream activating sequences (UASs). SALSA, an
CC       altered form of SAGA, may be involved in positive transcriptional
CC       regulation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SAGA complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Although strongly related to the PI3/PI4-kinase family,
CC       it lacks the typical motifs that constitute the catalytic site of
CC       PI3/PI4-kinase proteins, suggesting that it may lack such activity.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. TRA1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAC08542.1; -; Genomic_DNA.
DR   RefSeq; NP_595777.1; NM_001021677.2.
DR   SMR; Q9HFE8; -.
DR   BioGRID; 277779; 38.
DR   IntAct; Q9HFE8; 24.
DR   MINT; Q9HFE8; -.
DR   STRING; 4896.SPBP16F5.03c.1; -.
DR   iPTMnet; Q9HFE8; -.
DR   MaxQB; Q9HFE8; -.
DR   PaxDb; Q9HFE8; -.
DR   EnsemblFungi; SPBP16F5.03c.1; SPBP16F5.03c.1:pep; SPBP16F5.03c.
DR   GeneID; 2541265; -.
DR   KEGG; spo:SPBP16F5.03c; -.
DR   PomBase; SPBP16F5.03c; tra1.
DR   VEuPathDB; FungiDB:SPBP16F5.03c; -.
DR   eggNOG; KOG0889; Eukaryota.
DR   HOGENOM; CLU_000129_1_0_1; -.
DR   InParanoid; Q9HFE8; -.
DR   OMA; NPIFAMD; -.
DR   PhylomeDB; Q9HFE8; -.
DR   PRO; PR:Q9HFE8; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0070209; C:ASTRA complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IEA:InterPro.
DR   GO; GO:0010674; P:negative regulation of transcription from RNA polymerase II promoter involved in meiotic cell cycle; IMP:PomBase.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:GOC.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR033317; TRA1/TRRAP.
DR   PANTHER; PTHR11139:SF1; PTHR11139:SF1; 2.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; SSF48371; 3.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 2.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; Nucleus; Reference proteome; Repeat;
KW   TPR repeat; Transcription; Transcription regulation.
FT   CHAIN           1..3699
FT                   /note="Transcription-associated protein 1"
FT                   /id="PRO_0000314773"
FT   REPEAT          314..347
FT                   /note="TPR 1"
FT   REPEAT          2082..2114
FT                   /note="TPR 2"
FT   DOMAIN          2546..3107
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   REPEAT          2610..2643
FT                   /note="TPR 3"
FT   DOMAIN          3333..3669
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          3667..3699
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT                   ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          197..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3339..3345
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          3535..3543
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          3555..3580
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   COMPBIAS        197..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3699 AA;  422339 MW;  1B5810C719C89BAB CRC64;
     MQLALSHNIP IVIVKYLGKR IRVQLEFKKE LAQRSKHLMD VSQCEHWHNR LCDVGLDSKQ
     KANTAIEIRD ALDDVLVTEK TNFETFIPLL EDTLSLLEKE RPVFSSLAAT HRLRIALLEL
     LKKSGSYKGF EAFVNRTFAV LLRIVVNDNE EMAVLALKLV VLLFKDHSSL AKGHVQEFLS
     IVVENYKSMT TVVSEAFPPR SAPNTPSSHP MSAASSASPA EIGMEHAGPK MIPKASSSFK
     VTAEFPIIVF LLFQTYKDLI PKMLPLLAPL VLQFISLRPP PQAEARRLAE SQKEVFIGVV
     PSLRRNHLYN DLISAQIKSF SFLAYLLRSF GAALKQFESS IPICTLQLFM DCPSELYQTR
     RELLVATRHV LSTDYLRGFL PYVDQLLDTK ILVGSGITSQ HSLRPMAFSM LADMLHYVRM
     ELSPQQIYKV ILLYFSILMD DFYTSAIQAM ATKLILNLVE RIVALEDFST SRSLLFAILL
     CLLRKLTSLN FEFMKLRDSL QENADLKQIK IEENKHDLPM FENPTGAAQP SGLDKLKDCI
     FLFKNTLLGI KPVLFGLKQR NIPLANGSIF TAQEWSEKLH LSSTNEVLLF RRLLVESLKG
     FSYYQTDEKT GVFKSSKNLA YSQLDSSLTT NPSKLLEEKE LLEMLATLFL HLDPSVFVEI
     LESEFPNIFE CLVDNLALLH IFQFWMSNEV TSVNCTGIVL SFCCDNLAKI GSGQSTRVSV
     LLRLFKLAFM TVNVFPEKNA EVLRPHISYI ISTSLELTTD AVEPLNYVYL MKALFRNISG
     GKFDSLYKEI LPLLQVMLEC FNRLIFTVTS TSQKELYAEL CLTLPIRLSV LLPHMNFLMK
     PLIVALKGPP EIASQGLRIF ELCLDNLTQE FLDPLLDSIM PDLLICLWNH SRLNQSNNQL
     HQSAVRILGK MGGRNRQIYL GTFGFDFLQD ENIFPSIQFS FQGSSQNFSL EHSKFLMSSC
     AVLNNQNSDL EEKKQAFQMV KNSYLLLFAS AKPDEDFWES IDTMCRAVVD RMDKNLQQVS
     NGRLCPDKDE SYYLQRSIVS NIFKSLVGSM SCVEFVAEAR ETINRSLEWL IVLDLVNYAD
     SLQIKDQNIF DNLQSIKMLD LTTCINGIFE SLCSENENTR SNALSCIDHY LNAHKMLLNT
     TLDISKLPSF QNLVTVFCQS CHKELWYQKN AGFLGLKAIL SYDSHHKLWI QDRLHDILKA
     LFFILKDTPT DYGVLKLTEV RSFIVDITTQ FCILQDVLAP KERANNIINA FSPFFLELLH
     PNDHVRNTVQ QAIENISNNS KLSVVDLLLP IKDRLLSPIF GKPLRALPFT IQIGHIDAIT
     YCLHRSPSFL DLTDELYRLF RETIALADAE DEALVTMLKT SQSKDSSSLR KLRATCLHLL
     FASLVAHKFD QPQHAQTRTK IIAIFFKDLY SPHKEIYSVA IDALRHVLSQ NQKLPKELLQ
     SGLRPILMNL SDHNKLSVNG LEGLSRLLRL LTNYFKVEIG RKLLQHLNVL SDSKVLETAS
     LSLLKTNPRI EIIVSLVNVF RDLPPLSAQF LGDLLSSVVN IEAVLRKYSN SPLRKPLYSF
     MDLHANDTWM YILNNARNGD LITRFVGALN DPMSEKLRET AGNYWGKLLE LISQPVSVEN
     LAPMYAVDII ATVFPYISAN VDAGVISAKF IVLSKSLYGM LSSYNEYLFL PIRRCISSIT
     KMLLSSLKKI EKKLEFSLEV FRFKADDDND FLPEYIDSLC GCLITSTSAA EKKSIFLVCC
     SIVGDKSVRP FFKAFLLDKV INPLVFKSCG ENNFIDKDVV HSVYTHVWRV SIRDFAEVSG
     ATDSFYMGIM CLTTALCKYH SALLNDYRKS VIMSAWNYIK LEDPMVKQAA YATIACFISA
     YDTPAKIVTP VYVSILKTYQ PEVRAFIEFS LASLLSVLTA RLSSPSDSTF PLWAKLPRLV
     ISEDVQGISQ PLTVYQFICK APDLFFSCCS HFIVPMVNAL PKLVSFSSAS TEPRKLALDI
     VQTFINWQRK QNESENSETT LFSNSHIEAI LTFLIKFLSL FPEPVEENPL SKKGLSLFND
     LFSFPRWKDC QLNSNFFEKI LVDMDFNDNN YRTVANTLFV FGVILKNRGM EYIQREYSHI
     IALIDKSLRC GKLPVTHSLE QIILLLLQSH PTQAEEEEDT NEADDFKQLL LSVIHDNLAA
     ATNIESAICY LQIVKSSNPE ALDGLLLPLN KCFQKVARDH IVACMQSAIQ ASGKVTLPSA
     SDTVSKLLIS FIEIIRVRMA SLGDQRRWFL SVVVQLLEKS SSFELCEHIL NVTKEWVIVK
     RDSFLTVKEK TALLLKMRTF EGRFDNKLYI EACDLLSTIY RDPIFAHTEL TARLKQAFLL
     ATASKDTKIR MDFMDIFDSS MSRNVYSRLT FILDATSWDT IPSIYWIKQA NYILLGAINA
     KQPVRLTDNS LRFAPVPMTK PILSSLPEVF SKHNGSAIPL GRFTFFKQLD LFLKRNKELT
     VQKIIFPLAH IQMLSDADAN KLWQYIFPLA WKILSSDNRS DLSKSLIYLL TRDYHIKQVN
     NRPNVISTLV SSFVKCAAKL ELPPHLVKYL GKLYGVYHES VSLLEIQLSD KYDMYQNAKV
     QESRADAVAE LYASLNEDDM FYGHWRRNCK YLQTQVALSY EQLGMWGRAQ QLYEQAQTKA
     RSEAIPFSES EYNLWEDQWV MCAQKLQQWD VLTELAKHEG SSELLLECAW RISDWSNNRE
     SLEVAIKSLS DVPTPRKLTF QCFMTLQKSV SQPLAIKEFQ QVLSEAIQLA LIKWHQLPEK
     VNQSHYSLLH LFQQFVELQE AATIYSHLNA INFQNLPTNV QLIKSALQVW QERLPNVWDD
     INLWRDLISW RQIVFSMINR VYLPLVPTIQ ANSSADSSNP PNTSFLFRGY HETAWLINRF
     AHVARKHKLP SVCLNQLTKI YTLPNIEIQE AFYKLREQVL CYLQNPRDLK TGLEVVTNTN
     LMYFNSRQKS EFVTLKGKFL EKLNRGEEAN QMYAAAVQID LGLPKAWAEW GRYNDLLFNK
     SPDNLSAACN AISCYLQAAG TYQSSKARKM LARVLWLLSL NDSAGTIVKA FESYKGDIPV
     WHWLTFIPQL LNSLSKGDTK CAPVVLKKIA KSYPQALFFT LRTAREDIAQ VKRTEMAAWK
     SNTTDENKRN EDILSIQSNF LSTNQSTNAP ATNKEDGLSK KVWEYIDEIM SILKTAYPLL
     ALTMETLVDQ IQAKFKCKND GDAFRLVVAL LNDAVQHSIR LGIVTDEMKL PSSTESNLSL
     FADNILPDYC KQLFKEDFIV NSNGLKSYIF KLRKWRSYFE RLLSKVPKKQ YLEQYSSFLC
     EFHHQKFDEI EVPGQYLLHK DNNNSFSCIE RFLPEVELIV GHGVCYRRLS IRSNGGTIHP
     FVIQYPSARN SRREERFMQL TRYLNDALAL NCETRRRCLK FYIPAVIPLS SHIRLLEDQP
     SSITLQKIYE IYSERNNFSR DDPKELFTNE LSKHMMELNS QISQESTDAE KLANRKQLFS
     RRIGMFENIQ KLYSPSTILK DYFSSIFTNY SDLWLFRKNF SYQYACFSFI TYILSINNRI
     PAKLVFSRDS GGVWTTEALP SMVSSTPVYH NGEIVPFRFT PNIKEFIGKT CTEGLLGPSI
     MAIARALSKP DFDLDMYLGI FIRDDLFWWL AQQTKGVPAD FSMLNKVNSN TDLIMRRVAS
     LSQVAYGNLP VNQTAIDYLA QASSSKVLAQ MDVLWAPWL
 
 
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