GenomeNet

Database: UniProt
Entry: S7UYL2_DESML
LinkDB: S7UYL2_DESML
Original site: S7UYL2_DESML 
ID   S7UYL2_DESML            Unreviewed;       238 AA.
AC   S7UYL2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Precorrin-2 C20-methyltransferase {ECO:0000313|EMBL:EPR39319.1};
GN   ORFNames=dsmv_2661 {ECO:0000313|EMBL:EPR39319.1};
OS   Desulfococcus multivorans DSM 2059.
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfococcaceae; Desulfococcus.
OX   NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR39319.1, ECO:0000313|Proteomes:UP000014977};
RN   [1] {ECO:0000313|EMBL:EPR39319.1, ECO:0000313|Proteomes:UP000014977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR39319.1,
RC   ECO:0000313|Proteomes:UP000014977};
RX   PubMed=23950126;
RA   Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT   "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT   bacteria.";
RL   Genome Announc. 1:e00618-e00613(2013).
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|PIRNR:PIRNR036427}.
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:EPR39319.1}.
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; ATHJ01000090; EPR39319.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7UYL2; -.
DR   STRING; 897.B2D07_03490; -.
DR   PATRIC; fig|1121405.3.peg.2316; -.
DR   eggNOG; COG2243; Bacteria.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000014977; Unassembled WGS sequence.
DR   GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11645; Precorrin_2_C20_MT; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR012382; CobI/CbiL.
DR   InterPro; IPR006364; CobI/CbiL/CobIJ_dom.
DR   NCBIfam; TIGR01467; cobI_cbiL; 1.
DR   PANTHER; PTHR43467; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43467:SF2; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036427; Precrrn-2_mtase; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EPR39319.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014977};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPR39319.1}.
FT   DOMAIN          7..216
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   238 AA;  25934 MW;  D33BE975F71FDED5 CRC64;
     MMTATGKLYG IGVGPGDPEL IPLKAVRILG GVDVVFAASS SKNTYSMAVD IARNHIPENT
     PIIKLPFPMT RDKIETEKAW RENAQTIIAH VSAGKQAAFI TLGDPMTYST YGYVLKSILA
     IRPDLPIETV PGITSYQACA SRLNTPLVEG EESLLITSGV KGGDRLRNTS PRPENIVFLK
     AYRNAADISL ALEESNMVDN SVGISCCSLP QEEIIRDIRA FKDRKPGYWT IIIAKQNP
//
DBGET integrated database retrieval system