ID A0A316W494_9BASI Unreviewed; 601 AA.
AC A0A316W494;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN ORFNames=IE81DRAFT_364735 {ECO:0000313|EMBL:PWN44747.1};
OS Ceraceosorus guamensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN44747.1, ECO:0000313|Proteomes:UP000245783};
RN [1] {ECO:0000313|EMBL:PWN44747.1, ECO:0000313|Proteomes:UP000245783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN44747.1,
RC ECO:0000313|Proteomes:UP000245783};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ819359; PWN44747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316W494; -.
DR STRING; 1522189.A0A316W494; -.
DR InParanoid; A0A316W494; -.
DR OrthoDB; 852805at2759; -.
DR Proteomes; UP000245783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF35; MITOCHONDRIAL CYSTEINE SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000245783};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 142..483
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 67..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 65622 MW; E9F021CFFFF58A54 CRC64;
MSFTRSYTPE WLVEIYARAS RNKSTFFLGV LSGLTLSLAS LSTALIASQL RDARRREIQR
RLRLAAARRE RGANAGQRSK RRRRRRRSAS GLQSDEWEQE DTGSSGYSNE SSNESDDSEE
DDSRDSWVDI EVKNGHVVRG VEGLIGNTPL MRINSLSELT GCEILGKAEF LNPGGSPKDR
VALQILQDAE AARLLHPHTG SCIFEGTVGS TGISLATLAK AKGYRCSIVM PDDVALEKRQ
LLKCLGAEIT LVRPRGIADP KHFVNEARKL AKAFGMTSIK GDAAENRSSR KEQDLVVSSK
AKGGASEDPD ALEERPRGFF ADQFESESNY RAHYRGTGPE IWRQTGGFVS AFVCGAGTGG
TLSGVSTYLK RRDAKVRIVL ADPQGSSLFN RVKYGVLYSS TEAEGTRRRH QVDTVVEGIG
LNRLTRNFSH GLNDDAVDDA ERVTDQEAVK MSRFIARHDG LFLGSSSAVN LVAAVRTAVK
LKQQTKHQQD HSSSSFSARL TFAFPMLGSG STTAQSPGAS HTYQGSSQSY DYNSSIYAPE
EGEGQRAGLA QNAPVVVTIL CDSGSRHLSR FWNDEALREL GLNPEDEDIA EMLQTGTTSP
L
//
