ID A0A1J7ID39_9PEZI Unreviewed; 575 AA.
AC A0A1J7ID39;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JUN-2023, entry version 22.
DE SubName: Full=PAP1-domain-containing protein {ECO:0000313|EMBL:OIW25203.1};
GN ORFNames=CONLIGDRAFT_583669 {ECO:0000313|EMBL:OIW25203.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW25203.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW25203.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW25203.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV875102; OIW25203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7ID39; -.
DR STRING; 1408157.A0A1J7ID39; -.
DR InParanoid; A0A1J7ID39; -.
DR OrthoDB; 1363150at2759; -.
DR Proteomes; UP000182658; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd14688; bZIP_YAP; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.10.238.100; YAP1 redox domain. Chain B; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013910; TF_PAP1.
DR InterPro; IPR023167; Yap1_redox_dom_sf.
DR PANTHER; PTHR40621:SF6; AP-1-LIKE TRANSCRIPTION FACTOR YAP1-RELATED; 1.
DR PANTHER; PTHR40621; TRANSCRIPTION FACTOR KAPC-RELATED; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF08601; PAP1; 2.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR SUPFAM; SSF111430; YAP1 redox domain; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000182658}.
FT DOMAIN 147..210
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 28..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 62802 MW; 21DA7C6E3FC635BD CRC64;
MTSIRNPLGE LILTPQQQSL LFAALNSNKA NGSPANNALT MSPSTFDSSP THTHGLPPTD
SPLLDFDYDY NNADSSFDFS FDNGNDDSRM IGDLPGAPST ARSESASDQD SPDKRSHPDD
DEEENGAKRR ESEDKVSKKP GRKPLTTEPT SKRKAQNRAA QRVFRERKER HLKDLETKVQ
ELEKASQAAN HENELLKQKV EKMTVELSEY KKRVTIAGTS GRPAMLSNSN SRPFGQPIVN
NINDVNFQFE FPKFGVLPGP TPVSNQVPAK SSISPPIKRS SSDPSRQPSQ SPGNSSSYSQ
IGLDSQMKED LANIGANLFN PLMPSSNGSR TSFDSHPATT TSSPSASSNS HMGASSSCGT
SPEPLTQSPT AFKPVDTLTT IGEEPATLHD SNQDMDHFAN VNVTDFNWLP QNNFQFDPQL
FGDYREPQDN ILSTGVFDDS FFNDAFDADF LTPYNVPVTT NGGNPKKPGL IEQIDAAKNT
DELDSNGNLL TCNKIWSKLQ NCPKVQNGDF DLDGLCSELQ KKAKCSGSGA VVDERDFKTV
MRKYLGSSEK DIAECEARDQ AQKELDGRKA LGQTA
//
