ID A0A2K1R329_9PEZI Unreviewed; 617 AA.
AC A0A2K1R329;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Transcription factor {ECO:0000256|PIRNR:PIRNR002595};
GN ORFNames=CAC42_1542 {ECO:0000313|EMBL:PNS21688.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS21688.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS21688.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS21688.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR002595}.
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:PNS21688.1}.
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DR EMBL; NKHZ01000010; PNS21688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1R329; -.
DR STRING; 2082308.A0A2K1R329; -.
DR InParanoid; A0A2K1R329; -.
DR OrthoDB; 1117127at2759; -.
DR Proteomes; UP000243797; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProtKB-UniRule.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR014402; Sig_transdc_resp-reg_Skn7.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF002595; RR_SKN7; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR002595};
KW Nucleus {ECO:0000256|PIRNR:PIRNR002595};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000243797};
KW Transcription {ECO:0000256|PIRNR:PIRNR002595};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR002595}.
FT DOMAIN 365..479
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 206..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 133..167
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 497..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 415
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 617 AA; 68368 MW; 27D548664D6B7723 CRC64;
MDAQGSNNSS DFVRKLYKML ESPQDESVVR WGDQGDSFVV LENEKFTKHI LPKHFKHSNF
ASFVRQLNKY DFHKVRHNNE DNNSSPYGAG AWEFKHPDFR ANNKDALDNI RRKAPAPRKP
NAMGEDILPT QQMDMFNTQV VATQQQLQQL QERYNELSMH HSLLLQELIG VQKTVVNHEH
VMQYVMNFLQ SIDAQRRRES RIANPFAPPL ANGGAPAPAA PAQPAVSEED VPASPLQNAA
KLLGEVNAEH MLNTRNLEQM NEMSMRMNAA LTTPPPDMGF RNGRAAVKGQ PPHSASSSTI
SYGDLDTMVY PVGQTQGIDP MYSEHIHNIP YALPPKGPEQ PSLAPGPEPR KKSAAMDPGW
IRPPQVLLVE DDPTCRRIGS KFLYAFHCNI DSSFDGLEAV NKMNAGQKYD LVLMDIIMPN
LDGVSATHLI RQFDNTPIIA MTSNIRSDDI SMYFQHGMND VLPKPFTKEG LLSMLEKHLG
HLKKGAPGIE MGPPGNLPQS GKQSLKSDES PATSPATWNS PSGHITGISP ASADGEYTAV
QQAAYPMQPS PQAMTFGTSP QGMRQQLPGQ QPHRRQISEI SGGADMGPDV KRQQMYAQQG
PHLGQPMANA MMQQQRR
//
