ID A0A010RZ21_9PEZI Unreviewed; 703 AA.
AC A0A010RZ21;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 02-APR-2025, entry version 36.
DE SubName: Full=KilA-N domain-containing protein {ECO:0000313|EMBL:EXF83484.1};
GN ORFNames=CFIO01_13346 {ECO:0000313|EMBL:EXF83484.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF83484.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF83484.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF83484.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family.
CC {ECO:0000256|ARBA:ARBA00007247}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF83484.1}.
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DR EMBL; JARH01000234; EXF83484.1; -; Genomic_DNA.
DR RefSeq; XP_007592872.1; XM_007592810.1.
DR AlphaFoldDB; A0A010RZ21; -.
DR STRING; 1445577.A0A010RZ21; -.
DR KEGG; cfj:CFIO01_13346; -.
DR eggNOG; ENOG502QW2C; Eukaryota.
DR HOGENOM; CLU_016460_0_0_1; -.
DR OrthoDB; 5407653at2759; -.
DR Proteomes; UP000020467; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:TreeGrafter.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:TreeGrafter.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR FunFam; 3.10.260.10:FF:000003; Ascospore maturation 1 protein; 1.
DR Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR InterPro; IPR029790; EFG1/Phd1/StuA.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR47792; PROTEIN SOK2-RELATED; 1.
DR PANTHER; PTHR47792:SF1; PROTEIN SOK2-RELATED; 1.
DR Pfam; PF04383; KilA-N; 1.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 3: Inferred from homology;
KW Conidiation {ECO:0000256|ARBA:ARBA00023321};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 190..296
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..50
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..141
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..385
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..430
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..496
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 74974 MW; 68F70382CD5CF733 CRC64;
MNSERVPSLP LPNLHQAYSS GTSSPRVSSI GSASSSHAGS QSSFTSAASS HGPKTPSPTL
PINAAIPGSS GQPIGGYEHY PAMNQPAADM YYQQHISAGQ APPPQTVTSG AMSYHSQPPP
LQPSHLPQYQ QQTQYGQPYG YANGLTSPQS APVNNGMGGQ NVLPLPGVNP GGFQGFDTTG
QVAPPGMKPR VTATLWEDEG SLCFQVEARG ICVARREDNH MINGTKLLNV AGMTRGRRDG
ILKSEKVRHV VKIGPMHLKG VWIPFERALD FANKEKITEL LYPLFVHNIG ALLYHPTNQT
RTNQVMAAAE RRKAEQSQMR GAPQNGAPGL PSIQQHHHHS MGLPGPQQPL PSHANMGRPT
LDRAHTFPTP PTSASSVMGG SMGASDNGFQ WAQSQGMTNA QPQNPMSIDT GLSNARSMPA
TPASTPPGST IQNMQPYQTG TQQYDSSRAM YNQSSQQSPY QTSQGSQDRS VYGQTDPYAK
SDMGPPSARP AATSASQDQK PSNGIMHPDS NASQPAGEEE ADHEHDAEYT HDSGAYDANR
GSYNYSTPAV GTLSTEHQHL SPEMTGSPSH PPASGRATPR TATAPQPYYS QQAGYSTPPR
VAQQSSSNLF NVITDRNSAA AGGNNVYQPQ SDMNSMANGY PSQMNGASSG IKRGRDDDDD
LQRPLSGGGM DMKRRKTLMN SAVPTYDTMA RAPPVMAQQQ QGR
//
