ACUK_PODAN
ID ACUK_PODAN Reviewed; 682 AA.
AC B2AR36; A0A090CQ30;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Transcription activator of gluconeogenesis PODANS_4_8760;
GN OrderedLocusNames=Pa_4_8760; ORFNames=PODANS_4_8760;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
CC -!- FUNCTION: Transcription factor which regulates nonfermentable carbon
CC utilization. Activator of gluconeogenetic genes (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- SIMILARITY: Belongs to the ERT1/acuK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP66614.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU633895; CAP66614.1; ALT_FRAME; Genomic_DNA.
DR EMBL; FO904939; CDP28349.1; -; Genomic_DNA.
DR RefSeq; XP_001905948.1; XM_001905913.1.
DR AlphaFoldDB; B2AR36; -.
DR SMR; B2AR36; -.
DR STRING; 515849.B2AR36; -.
DR EnsemblFungi; CAP66614; CAP66614; PODANS_4_8760.
DR GeneID; 6190033; -.
DR KEGG; pan:PODANSg2976; -.
DR eggNOG; ENOG502R1M5; Eukaryota.
DR HOGENOM; CLU_010748_1_0_1; -.
DR OrthoDB; 681770at2759; -.
DR Proteomes; UP000001197; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Gluconeogenesis; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..682
FT /note="Transcription activator of gluconeogenesis
FT PODANS_4_8760"
FT /id="PRO_0000406449"
FT DNA_BIND 77..105
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 75181 MW; 4C7FCBFF40A62B9F CRC64;
MPEDGGPFGS EAAEASGAMS ETENEYDDHE PHHKDEDDRM SEQNTTPDGV DAGGEVKKKY
DPKDPLRPRR KKARRACYAC QRAHLTCGDE RPCQRCIKRG LQDSCQDGVR KKAKYLHDAP
PEALRPVLGP NYNPNAPSSR HGGQRHHSVS TDASTVRTFF SHSNASQYPV YSSTQSIPHG
LTESLPFNSQ QSPVSPTFQQ TSSNPPISGM VAPPVSSPMT PFGLPFDPSD PNIFNFNIDG
LNFGSHYGAM EFGMLGHMSS SAADTPPQES GMGQQPGDVH FGAGLFGSHF DNRMLPEFLG
LDAGANGIYS QGNLQHGLPH AYAIPAGPTS LQSPSTENNS PQPTTFGFDD RPSPTMSQYP
NAPGAKSSSN SRPSKLRKLD KVAILQKRQR DPSYIYDTVK KSFDYVGSFH KLFEVLSSRF
SQPHAARIAK SLAAIRPALL ASTRNLTTQD LIFMEQCFQR TLFEYEDFMT QSSSPTLACR
RTGEIAGVNK EFTALTGWTK DVLLGKEPNR NTNLGGTGVR TTPRLKSLNE SSAENGGAAS
GPRPVFLAEL MDHESAVEFY EDYSQLAFGD SRGRMTRKCR LLKYRTDKPA AGGGGGAGEE
ERKPDPSAAP RQQEKDSRHS ILSNRVAKID GEHGISKLER DGKLECSYTW TIKRDMFDMP
MLFVINVRFF FFFDDYYGRR HC
