ID A2Q9G8_ASPNC Unreviewed; 848 AA.
AC A2Q9G8;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Contig An01c0270, genomic contig {ECO:0000313|EMBL:CAK43880.1};
GN ORFNames=An01g07820 {ECO:0000313|EMBL:CAK43880.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK43880.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK43880.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM269974; CAK43880.1; -; Genomic_DNA.
DR RefSeq; XP_001389207.1; XM_001389170.2.
DR AlphaFoldDB; A2Q9G8; -.
DR EnsemblFungi; CAK43880; CAK43880; An01g07820.
DR GeneID; 4977954; -.
DR KEGG; ang:An01g07820; -.
DR VEuPathDB; FungiDB:An01g07820; -.
DR HOGENOM; CLU_015602_0_0_1; -.
DR OrthoDB; 1333597at2759; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0031213; C:RSF complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR028938; Rsf1-like.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14296; REMODELING AND SPACING FACTOR 1; 1.
DR PANTHER; PTHR14296:SF3; REMODELING AND SPACING FACTOR 1; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 431..487
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 95761 MW; E4B08C6662B2B088 CRC64;
MVSRKRTRSE VDTAPEQPPE EPGLLQKLRN CWEFASLMQY IAIFGKVMKI DEDFGIEDLE
TECLKPTPSE KLLEIGLCLL KWVSSHRGLT FDNFDEYTRR QYNAKAPHIP NPFGYEEVPK
RFLDFDVFLK LRVLHQLSIW TFWNPDRIRE KMPEQRESDQ TEWRIEEVGY DREGRYYYIL
DDNRLYRRTD PPIPPPKPAK SKSRRKSARA MRASKRRRVT GADPIEESDE EDNVVNGDAS
EDPLQAMTWE CIAITLDDYK QFLESIRKTR DPDEKILRDR IDEQVMPIIE KEEEAQERQK
QKREKELFNM QLLAGAKRSS RIAGKAEKER QEREAAEAAR KRETELAAAR KEEERVKKLE
AERRSRIMTR EQRTKDRERK RILHESELQR IKEEQEKVAR GESRASERHL QAEMEKYRKN
LEDLSQEDQW IFDCSGCGVH GQNLDDGSHS VACESCNVWQ HSKCLGIPKS EAEREDFHFV
CNDCKRREEE AKLPKLPPLK FRVGSSTSPS SAAPDGDTKI KVPDPEQSPI SSIKTAQHTF
QLPLTGSPQK QPPSMPSVPL QNPPQAVSFP PLSPERRPQS AHTTSFSPPR APFSPSKGLN
GHTPSSKDQI PKLPSIHQAM HLPPHSRESF SGGSFPARRP SSSHSTQSPT LPSPIQNRPS
MSPTQGNRDV GPLAGFPPVA STDHSAPWTP YAQHQTPRPN TGNHSSFSSL HNGRPSFMAT
PTATRSSPPQ SSHGVPLSGI SPTKQSPRPM TSGSVTGAPV LPPIQKLEPS PKLMGRSSPD
APIPPPVKCM TPEQEERRQR ENAMLQAQLH GTNGPHSVMS SPSLNRIPPL GPSAVAQQPA
PSPQSGSK
//
