EFG1_CANAX
ID EFG1_CANAX Reviewed; 552 AA.
AC P43064;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Enhanced filamentous growth protein;
GN Name=EFG1; Synonyms=EFG;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX PubMed=9155024; DOI=10.1093/emboj/16.8.1982;
RA Stoldt V.R., Sonneborn A., Leuker C.E., Ernst J.F.;
RT "Efg1p, an essential regulator of morphogenesis of the human pathogen
RT Candida albicans, is a member of a conserved class of bHLH proteins
RT regulating morphogenetic processes in fungi.";
RL EMBO J. 16:1982-1991(1997).
CC -!- FUNCTION: Putative transcription factor that stimulates pseudohyphal
CC morphogenesis.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00630}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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DR EMBL; Z32687; CAA83640.1; -; Genomic_DNA.
DR PIR; S49338; S49338.
DR AlphaFoldDB; P43064; -.
DR SMR; P43064; -.
DR VEuPathDB; FungiDB:CAWG_02083; -.
DR VEuPathDB; FungiDB:CR_07890W_A; -.
DR PHI-base; PHI:87; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR029790; EFG1/Phd1/StuA.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR47792; PTHR47792; 1.
DR Pfam; PF04383; KilA-N; 1.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 3: Inferred from homology;
KW DNA-binding; Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..552
FT /note="Enhanced filamentous growth protein"
FT /id="PRO_0000086939"
FT DOMAIN 204..310
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 238..259
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 17..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 59964 MW; F94FD94FC2E06EB7 CRC64;
MSTYSIPYYN QMNGNYNNGM PQQTTAANQQ AFPQQQQPTT TGNASQQQQQ AAATAAAVQQ
PYNYMFYQQQ GQPGQQTGQT AGQQQQQQQQ QQQYDYNTYN RYQYPAATSQ GNYYQQTIPN
QLSQPQPQHY NGSNRNYTSA PSGAPIPSNS TSGPSQQPPL PGQQAVPIPP HVSTMQQPTP
VQDTLNASST STVGQFQPPG IRPRVTTTMW EDEKTLCYQV DANNVSVVRR ADNNMINGTK
LLNVAQMTRG RRDGILKSEK VRHVVKIGSM HLKGVWIPFE RALAMAQREQ IVDMLYPLFV
RDIKRVIQTG VTPNAAAATA AAAATATSAS APPPPPPPVA AATTTAATAI SKSSSGNGNS
ISATSGGSNV SGASGAGSTT SPVNTKAATA AGIPQGNYYQ TYNQQQYPQQ YGQYNAPGKN
QNTPASQPGS TTNDQYLQQQ QQQQQQMYGY QSNYYQGGAA NSSYYPNYYQ QQQPNYASSY
PYQQQQQKQQ QQQPNQQQQS DQQQTSTPSG GAGTRSVHQS PQVQSLTQGS VHPSPQQHQA
NQSASTVAKE EK
