ID   A0A1L7WJX1_9HELO        Unreviewed;      1074 AA.
AC   A0A1L7WJX1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Related to galactonate dehydratase {ECO:0000313|EMBL:CZR53070.1};
GN   ORFNames=PAC_02948 {ECO:0000313|EMBL:CZR53070.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR53070.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR53070.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR53070.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FJOG01000003; CZR53070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7WJX1; -.
DR   STRING; 576137.A0A1L7WJX1; -.
DR   OrthoDB; 1691455at2759; -.
DR   Proteomes; UP000184330; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008869; F:galactonate dehydratase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0034194; P:D-galactonate catabolic process; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd03325; D-galactonate_dehydratase; 1.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR023592; Galactonate_deHydtase.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   PANTHER; PTHR47540; THIAMINE REPRESSIBLE GENES REGULATORY PROTEIN THI5; 1.
DR   PANTHER; PTHR47540:SF3; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00003; D-galactonate_dehydratase; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184330};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        891..910
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          125..227
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   DOMAIN          654..730
FT                   /note="Transcription factor"
FT                   /evidence="ECO:0000259|SMART:SM00906"
FT   REGION          464..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1074 AA;  119288 MW;  9FF9FA6428BA9A17 CRC64;
     MPKIAKIEYF RVPPRWLFVK ITDDAGLEGW GEASLEGHTQ AVEGCLDAYI ERYTGMDADD
     IEHIWQTTWR LGFYRGGPVF MSALAGIDIA LWDLKGKFEV PIYQLLGGKV RDKIKVYAWI
     GGDRPGDVAN QAKARKAQGF TSVKMNGTED LGWLDSPSAL DECVERLKAV KALGMDAGID
     FHGRVHKPMA KQLARVLEPH RPMFIEEPLL SEHIEGIKAL SQQTSIPIAL GERLHSRWDV
     RPFLEAGAVD ILQPDISHCG GISEMRRIAA MAETYDVALA PHCPLGPIAL AANVQVAAAT
     PNFVIQEMSL GIHYNVGGQD LTSYTHNPEV WNVEGGYIKL MTGPGLGIEI DEDQVRKYSE
     SAKAWVSPGF IGPGGEANLC CEFTAAYNRG RLPSVLPDES VQYAPADSSE QNVPGTPDHS
     DQLIEDRRAN YPGMELLLQA SLPSPPGDQR PVTVGRIPRS IQERLDSRMP SSRNSPEPSQ
     TDLQGHYVGP SSGVSFLLRV QKKLHQKVSF SQNSSIFTFG DAPLPEFNPS FFILPAKSDA
     ERLVARYFDF AVPTHRFLHR PTVEAWLEEF YENLGVMRQK DGARERTAVL FMVMAQAKDY
     MPDQGNSPAD TSARYFQAAD HQLSTETGEI RLTSVQARLC QCFYLLSQSR VNHCWSLFGT
     TAHLILAIGI HRKRRIETSN GFDLIELECR KRVFWCAYSL DNYLSAALGR PRTFHDDDID
     QDFPTCVNDS DLSSHRMNPT STKAQSIMMA PVAHARLSRI VSNILRDLYS IRAPSPSARV
     TLTSKYSAAL LSWREGLSRF LGADGIDPSL LLPLYQRQRN VLNLAYHHAL ILVYRPFLLG
     NFASLSNKTS RQRGAPGTPD MDKSVSDCLE AAMNIVGIVN ELSEGKQIFR AYWFTQYFAF
     CAVVVLYVYT TQQRNAPQER YLSYFKAAEK CQSQIGSMAE RESLAQRYSV VLEELRLEAV
     KQTSGHHESQ NGNFSTTYMA GPQSMNHIQD GTNATGSPML DTAGLDFTMA NETSGNDGPN
     GATPSSLMAE LTNWSSFNSL VTAGMGHLDF LFPEEQNLQW DLGVQTDVDG MLLP
//