ID U4LX89_PYROM Unreviewed; 827 AA.
AC U4LX89;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Similar to Start control protein cdc10 acc. no. P01129 {ECO:0000313|EMBL:CCX34288.1};
GN ORFNames=PCON_03481 {ECO:0000313|EMBL:CCX34288.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX34288.1};
RN [1] {ECO:0000313|EMBL:CCX34288.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX34288.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX34288.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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DR EMBL; HF936511; CCX34288.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LX89; -.
DR STRING; 1076935.U4LX89; -.
DR eggNOG; ENOG502QPWC; Eukaryota.
DR OMA; RGVEVCR; -.
DR OrthoDB; 3019647at2759; -.
DR Proteomes; UP000018144; Unassembled WGS sequence.
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: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:SF3; REGULATORY PROTEIN SWI6; 1.
DR Pfam; PF13637; Ank_4; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Conidiation {ECO:0000256|ARBA:ARBA00023321};
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 64..170
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REPEAT 364..396
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 504..536
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 749..776
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 89222 MW; 1ACC15F877DEB363 CRC64;
MATTESSPTL QRTGSSVTAN SFAAQGPPPG TVGSFSATAA STPAGTPPPP QLANMDPRGP
PPTIYTAVYS GVAVFEMTIN NVAVMRRRDD SWLNATQILK VAGVEKGKRT KVLEKEILSG
THEKVQGGYG KYQGTWIDFE RGREFCRQYG VEHILAPLLN LDTTSTAGHD STPTKEQAMA
AKRKRMYNPS FGQPNGSNGL FPLNSTAVTS ALTTLGKASA MLESPSNRPG LPAISSSLQG
VMREDSHSQG SWPPPPASMM SDPSFLHSQQ LPDSTYASQI VGHESQNDMH EPPSKRARAS
SPVRDMPDPI HEEGPALPLN LHDIPNVEHA KAILMDVFLR GEEQAIESLE QITPEQVDMP
LDTMGNAAIH WAAALARINV VRALINRGSN IFRVNDSGET ALARSCFSTN NFDQNCFPAL
LNLLHPSIPV QDNNGRTILH HIAVKSGMKG RGQDAKYYLN CLLEFVAKHG VAPSATPNNQ
HEQTLRVMSL GRFISDVVNA QDKTGDTALS ISGRIGNNSI IIPLLDVGAD PSIPNRAGLR
PCDFGVGVQN GQVVPAPNEQ QQVRQLNYTV PQAVVQKRED IVKSMQDLIR SLENDFQKEL
DGKQSTVTTT LSSLRDVTSR LGAERSRAND LRTKVRKISD LRQACRNLKR ALEEQPVTEG
LPTPAEEGIG GTVIAGTAAG PNGTATPAPP AEGRRASIAD EQQEASTADT PYTLQNSLLA
PVHSISNLTT TQLAYIKSLP PSTLLKSRLK GYKRNERSLQ GTAQKLKEKS MDLENNFRRV
VALSTGIEEQ NVDGLIEGLV MAVESDPGEV DTNRVVGFLR KIGEADT
//
