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Database: UniProt
Entry: A0A0P6WSD9_9SPHN
LinkDB: A0A0P6WSD9_9SPHN
Original site: A0A0P6WSD9_9SPHN 
ID   A0A0P6WSD9_9SPHN        Unreviewed;       446 AA.
AC   A0A0P6WSD9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Protein-S-isoprenylcysteine methyltransferase {ECO:0000313|EMBL:KPL68131.1};
GN   ORFNames=SZ64_08365 {ECO:0000313|EMBL:KPL68131.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68131.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL68131.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68131.1,
RC   ECO:0000313|Proteomes:UP000049978};
RA   Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA   Pandey G.;
RT   "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT   from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT   of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL   Appl. Environ. Microbiol. 0:0-0(2015).
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:KPL68131.1}.
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DR   EMBL; JXQC01000003; KPL68131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P6WSD9; -.
DR   STRING; 1603897.SZ64_08365; -.
DR   PATRIC; fig|1603897.4.peg.1584; -.
DR   Proteomes; UP000049978; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1630; -; 1.
DR   InterPro; IPR010721; UstE-like.
DR   Pfam; PF06966; DUF1295; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000313|EMBL:KPL68131.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW   Transferase {ECO:0000313|EMBL:KPL68131.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        103..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        228..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   446 AA;  50665 MW;  18C5FF90C473C186 CRC64;
     MAGKKPPRSD VSPRVGLVGL IGLFVWIAIC RNWPHIADAL NLPGPRERMS GAYAALASML
     FIGILMAAWS VLVEKVYLRP STGISWKNPR PLSSVIEVSV TKLAGLWSTW AIIGFLYCVC
     RWYWDGQYLF AMEVIGASAI PLFILSVPYV LWLDRVLVNP HDGAWHFGAM LIGREPWDAE
     QVKKHWRAWT IKAFFGAFMI SILPPGFANI VNADIPALLN DPGRFGGVLF ELLFVIDVQI
     GTVGYLFTLR PLDAHIRSGN PFLAGWLAAL MCYPPFVWGV MSNNGVIGYE YHTADWSYWF
     QGHTALMWVW AGWLGFLTAV YAWATVAFGI RFSNLTYRGV LTNGPYRFTR HPAYLAKNTF
     WWCSTLPFFV TNGSLVDVVR NTFFLACVSG VYYWRARTEE AHLLAEDPKY REYHDWMAEH
     GLITSRLRKL LLRFRRRPPV ALQPAE
//
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