ID A0A1R3RZ25_ASPC5 Unreviewed; 520 AA.
AC A0A1R3RZ25;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Transcriptional adapter 2 {ECO:0000256|PIRNR:PIRNR025024};
GN ORFNames=ASPCADRAFT_203513 {ECO:0000313|EMBL:OOF99733.1};
OS Aspergillus carbonarius (strain ITEM 5010).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=602072 {ECO:0000313|EMBL:OOF99733.1, ECO:0000313|Proteomes:UP000188318};
RN [1] {ECO:0000313|Proteomes:UP000188318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 5010 {ECO:0000313|Proteomes:UP000188318};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV907494; OOF99733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3RZ25; -.
DR STRING; 602072.A0A1R3RZ25; -.
DR VEuPathDB; FungiDB:ASPCADRAFT_203513; -.
DR OMA; YNGNHRP; -.
DR OrthoDB; 206414at2759; -.
DR Proteomes; UP000188318; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0035065; P:regulation of histone acetylation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
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; 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; 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:UP000188318};
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 16..75
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 77..130
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 82..126
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 432..520
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 131..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 58728 MW; C7212C043E6D50E5 CRC64;
MGVIRKKTAS RGTEAGTKYH CDICSVDVTS TVRVSCAHPV CHEYDLCVPC FAAGEKSKNH
DPSAHPFQVI EQNSVPIFEE DWGADEELLL LEGAEIYGLG SWADIADHIG GYRTKEEVRD
HYVSAYIDSP NFPLPERADP DDKRLSEAIS KEEFQSRKKR RIEERKEAAK AAPPTTPKQK
PTASVPACHE VQGYMPGRLE FETEFMNEAE EAVQHMTFEP GAGETANGET DAEMELKMTV
VDIYNSRLTA RTERKKVLFE HSLLEYRKNT ALEKKRTKEE RDLLNKAKPF ARMMNHDDFE
EFNKGLEYEH NLRLAITQLQ EWRQMGIGDL KGGEKYEQEK QQRAQRLVPQ GSFDRFASTR
PAKQAQQPEQ PTAASQLTTP ELPLRLQKVS GTPKAPEPVN QPMNDFDRAF AASNGDGVST
PQPAKTKFVI PPLNGVIPWK LENEGAPDLH LLTKEEVEVC NVLHMQPKPY LVIKETMLKE
SMKQGGSLKK KDARTICKID STKSSRIYDF MVHSGWINKG
//
