ID B6K677_SCHJY Unreviewed; 464 AA.
AC B6K677;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Transcriptional adapter 2 {ECO:0000256|PIRNR:PIRNR025024};
GN Name=ada2 {ECO:0000313|JaponicusDB:SJAG_04205};
GN ORFNames=SJAG_04205 {ECO:0000313|EMBL:EEB09031.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB09031.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB09031.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation.
CC {ECO:0000256|PIRNR:PIRNR025024}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR025024}.
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DR EMBL; KE651167; EEB09031.1; -; Genomic_DNA.
DR RefSeq; XP_002175324.1; XM_002175288.2.
DR AlphaFoldDB; B6K677; -.
DR STRING; 402676.B6K677; -.
DR EnsemblFungi; EEB09031; EEB09031; SJAG_04205.
DR GeneID; 7050600; -.
DR JaponicusDB; SJAG_04205; ada2.
DR VEuPathDB; FungiDB:SJAG_04205; -.
DR eggNOG; KOG0457; Eukaryota.
DR HOGENOM; CLU_018273_3_0_1; -.
DR OMA; YNGNHRP; -.
DR OrthoDB; 206414at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0140671; C:ADA complex; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000124; C:SAGA complex; IEA:EnsemblFungi.
DR GO; GO:0070461; C:SAGA-type complex; IBA:GO_Central.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:EnsemblFungi.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IEA:EnsemblFungi.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEA:EnsemblFungi.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0035065; P:regulation of histone acetylation; IEA:InterPro.
DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IEA:EnsemblFungi.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:EnsemblFungi.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02335; ZZ_ADA2; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR041983; ADA2-like_ZZ.
DR InterPro; IPR016827; Ada2/TADA2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12374:SF20; TRANSCRIPTIONAL ADAPTER 2-ALPHA; 1.
DR PANTHER; PTHR12374; TRANSCRIPTIONAL ADAPTOR 2 ADA2 -RELATED; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR025024};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR025024};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR025024}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 3..59
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 61..114
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 66..114
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 66..110
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 347..444
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 439..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 52710 MW; 2141EEF4F680079A CRC64;
MPPQKYHCNV CAQDITRSIH IRCVTCTDFD LCVSCFTSGS SSGDHQPAHP YRVIETNSFP
IFNDDWGADE ELLLIDACET LGLGNWADIA EYVGNCRTKE DCEQHYINTY ILSESYPLPS
MDTVFDVDRT AFAARKRARL EAFTPPPVYP LKLLASTPQC HEIQGYMPGR LEFDQELENE
AEVSVKDMTF DSDESLDLSS PSPEVEVKLA LLEIYNARLT RRALRKNVIF THNLLDFKRI
QANEKRRSKE ERSLLTQAKV FARLLSKEDY AAFVDGLLTQ HSLLKRIEQL QEWRQMGLTT
MEQGHKYERD KAQRILLTKA ASSLDRNDLR KSSLYNSRDL PYRDLSTSSK KQAAPLTFIT
SADRQLLSPE EQTLCTQLHI LPKPYLAIKC TLLTAFLANP KTISLDRAYV LLPKVDQNKV
QRVFEFLQSS GWLSFKATET KTEPNSAASA TLDSSSAVIT EEPQ
//
