ID B2ARH4_PODAN Unreviewed; 626 AA.
AC B2ARH4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 18-JUN-2025, entry version 74.
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 4, supercontig 4 {ECO:0000313|EMBL:CAP66752.1};
GN ORFNames=PODANS_4_7490 {ECO:0000313|EMBL:CAP66752.1};
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 {ECO:0000313|EMBL:CAP66752.1};
RN [1] {ECO:0000313|EMBL:CAP66752.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP66752.1};
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] {ECO:0000313|EMBL:CAP66752.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP66752.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
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).
RN [4] {ECO:0000313|EMBL:CDP28487.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., 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 Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CU633895; CAP66752.1; -; Genomic_DNA.
DR EMBL; FO904939; CDP28487.1; -; Genomic_DNA.
DR RefSeq; XP_001906086.1; XM_001906051.1.
DR AlphaFoldDB; B2ARH4; -.
DR FunCoup; B2ARH4; 123.
DR STRING; 515849.B2ARH4; -.
DR GeneID; 6190316; -.
DR KEGG; pan:PODANSg3114; -.
DR VEuPathDB; FungiDB:PODANS_4_7490; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_017715_0_0_1; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000001197; Chromosome 4.
DR GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:TreeGrafter.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IEA:TreeGrafter.
DR GO; GO:1901987; P:regulation of cell cycle phase transition; IEA:TreeGrafter.
DR CDD; cd00882; Ras_like_GTPase; 1.
DR FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR055116; DBF4_BRCT.
DR InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR InterPro; IPR051590; Replication_Regulatory_Kinase.
DR InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
DR PANTHER; PTHR15375; ACTIVATOR OF S-PHASE KINASE-RELATED; 1.
DR PANTHER; PTHR15375:SF26; PROTEIN CHIFFON; 1.
DR Pfam; PF22437; DBF4_BRCT; 1.
DR Pfam; PF08630; Dfp1_Him1_M; 1.
DR Pfam; PF07535; zf-DBF; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 565..614
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 70152 MW; 1C3A987997569C8E CRC64;
MSTARRVPLS NNPNVANSPM RTSAALNGAK KVRSHAELLR EEPYGQPPPA KRQMIERGVA
SPSRTKPSRT IVHRGTTTRA AVTTSQKTSQ GAVEKASQLE LAEWRATYSA RFPTWVFYFE
SVPDEQRSRL AKRVNNLGAR EEKFFSIDVT HVITTRPIPR AEKNSAHDQE NAAESHGSEQ
PKTIDPSLLN RVAEAPPVRR KLVFDTSRRM PVPGQDAKPQ KSRSTDILLR AQDMKMKLWS
VDKLTRFLEA LEAEPHKSTN HGRTGTGKTT DRSNLRHLLQ QERVHGPSDR DPTVATKEMH
HFKGPYIYIY DMEEKTKPVM AREYAKVADK KDGEWPQFRV ASAGRCPFVQ DYEIPEKENR
EKTKTKERAA KAAAAENAAK LQPPEVPAPK PATGKRTLAV MEDGQNRGTP PVAAADALDR
SRVSNPPQME FRTQNAFMSH AKAGRLLAGE PVASGLQQSA VTSAIRSQMI SSTSGVLGAK
AGTSKEIHGL QRKVLAKAGP PAVSQDLSSR RMAEMSHDST TFVRSASASR ATHRKLETVD
EEEAAKQREK LRRTVSLPVA QRQKRDPKPG YCENCMDKFD DFDEHILTRK HRKFAENDDN
WVQLDALLAL LKRRPRHRHE VDNDEW
//
