ID B2AC39_PODAN Unreviewed; 711 AA.
AC B2AC39;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Cell division cycle-related protein res2/pct1 {ECO:0000313|EMBL:CDP26413.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 2, supercontig 3 {ECO:0000313|EMBL:CAP61014.1};
GN ORFNames=PODANS_2_14120 {ECO:0000313|EMBL:CAP61014.1};
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:CAP61014.1};
RN [1] {ECO:0000313|EMBL:CAP61014.1, 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:CAP61014.1};
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:CAP61014.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP61014.1};
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:CDP26413.1}
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 (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CU633447; CAP61014.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP26413.1; -; Genomic_DNA.
DR RefSeq; XP_001903242.1; XM_001903207.1.
DR AlphaFoldDB; B2AC39; -.
DR STRING; 515849.B2AC39; -.
DR GeneID; 6187288; -.
DR KEGG; pan:PODANSg254; -.
DR VEuPathDB; FungiDB:PODANS_2_14120; -.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_009666_3_1_1; -.
DR OrthoDB; 3019647at2759; -.
DR Proteomes; UP000001197; Chromosome 2.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:UniProt.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR43828; ASPARAGINASE; 1.
DR PANTHER; PTHR43828:SF15; TRANSCRIPTION FACTOR MBP1; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF04383; KilA-N; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cell cycle {ECO:0000313|EMBL:CDP26413.1};
KW Cell division {ECO:0000313|EMBL:CDP26413.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Conidiation {ECO:0000256|ARBA:ARBA00023321};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 10..119
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REPEAT 266..298
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 388..420
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 111..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 496..561
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 142..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 79386 MW; 6CC6DF3C17C3F49B CRC64;
MAKGAAPAGV YSATYSGVPV YEFQFGTDLK EHVMRRRADN WVNATHILKA AGFDKPARTR
ILEREVQKEE HEKVQGGYGK YQGTWIPLEQ GEALAQRNNI YERLRPIFEY EPGSESPPPA
PRHASKPKAP KAKPAVPKWG SKSQNRKGSL SQPAVFSHSH AQQGVPIQEE YESVASQMHE
DDTPDNMTVA SASYMAEDDR AYDMSHFSTG HRKRKREEEM RDMTAQQHAM YGDELLDYFL
LSTNQQAAIR PDPPTNFQPD WPIDTDRHTS LHWASAMGDT DVIKQLKRFD ANLMAQNIRG
ETPLMWAVNF TNCYMKKTFP TVLNELFKSV DARDHSGCTV IHHAAVMKRG RVQSSTCARY
YLDIILNKLV EVRQPEEVQA LLDAQDEEGN TALHLAARVN ARKCIRSLLG RGAATDIENN
EGVRAEDLIK EINTTRSLAR TGPQRSSSPF APETARRNGF RDALGEDPTS KLQLSYQSEA
ANTVQSRITP LVLQKLQDLS QSYDSEFNET DEAEKEARHI LANTQAELNN LRASIAELES
RIEADDQASK TEEEVAAAKK QVLALFRRQT QLAIEKAIEQ NLASVTNGQQ QEEEDDSPEE
RLKLAAQLHA MLVEQEAAEV EYVEARGMLG TGKKIDQYRH LLCSCLPPED QDMLDQNLED
MISMMEDEAE SNSAALLPPG TNPDGVMEGM GMLGGMALAM AEAAEPMEIT G
//
