PHM2_PYRSX
ID PHM2_PYRSX Reviewed; 747 AA.
AC A0A2Z5XAS1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Transcription factor phm2 {ECO:0000303|PubMed:29972614};
DE AltName: Full=Phomasetin biosynthesis cluster protein 2 {ECO:0000303|PubMed:29972614};
GN Name=phm2 {ECO:0000303|PubMed:29972614};
OS Pyrenochaetopsis sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pyrenochaetopsidaceae;
OC Pyrenochaetopsis; unclassified Pyrenochaetopsis.
OX NCBI_TaxID=1756125;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=RK10-F058;
RX PubMed=29972614; DOI=10.1002/anie.201805050;
RA Kato N., Nogawa T., Takita R., Kinugasa K., Kanai M., Uchiyama M.,
RA Osada H., Takahashi S.;
RT "Control of the stereochemical course of [4+2] cycloaddition during trans-
RT decalin formation by Fsa2-family enzymes.";
RL Angew. Chem. Int. Ed. 57:9754-9758(2018).
CC -!- FUNCTION: Transcription factor that regulates the expression of the
CC gene cluster that mediates the biosynthesis of the trans-fused decalin-
CC containing tetramic acid phomasetin. {ECO:0000269|PubMed:29972614}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BBC43185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; LC361337; BBC43185.1; ALT_SEQ; Genomic_DNA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Metal-binding; Nucleus; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..747
FT /note="Transcription factor phm2"
FT /id="PRO_0000453353"
FT DNA_BIND 21..50
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 112..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 83066 MW; A5E0088839ABE20A CRC64;
MSDTASTATG HRKRDKPQLS CNACRKRKRV RCDRLHPCSN CASRGLGSTC TFAAISSPTN
MPPSHGHSIP VQHRVESARP GPTNSMQTRI NQLENLVIEL MNQNNTPGMR TGLQNQGSDA
RSDARCQPTP LSSETEFEYP VAPSPSDHGS INTRLARPTY VSSSHWAAIF DSITELRNHF
VQEDIEHGAS TVLPSSTVPK PQILYGAWTS ETPHAIISSL PPRTTVDRLI SRYFNVLDIA
PGVVHSTQFL REYENFWMAP QDAPIMWVGL LFAMMCLSAQ LQQASLPAHD SRPSSSRASQ
QDSIAIYREK TIQCLQLGHY TMGGTHALET LILYFLGECF NLKDMEIGIW ILSGTILQIA
IHMGYHRDAK NFPSITPFAG EMRRRVWAMI VQLDFSISAQ LGLPTLIKAS QTDTAEPRNL
YDTDFDEDSS ALPESRPETE VTPTLYVLAK LRLISIGLRV TNVASESRTR SYSDVLELDR
QLREARDALP SSLKWIDLGT SLNVSSQTIL QRIWLEVTIQ QLTIVLHKKF LGVSGLQKDF
KTSRAACLNA AVKILELQRL VDDETQPDGL LYQSRWRVSS AFSNDFLLAT SILCYCLQNR
PEGTISNFDE SVSVGLDQIR ALLETSKSIW SRQCAESKEA HKAVAALRYV LGHSGADVDS
GYTVAERQPL PMPTAALSYF PDLTSDYNFA GFDFGSSDTT RWTAFASDEL GEENWSRGAG
FQQMDMSLKL EAFDRVVPNS IPSRCLS
