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Database: UniProt
Entry: G8PFN6_PSEUV
LinkDB: G8PFN6_PSEUV
Original site: G8PFN6_PSEUV 
ID   G8PFN6_PSEUV            Unreviewed;       252 AA.
AC   G8PFN6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Protein containing Methyltransferase type 11 domain {ECO:0000313|EMBL:AEV35773.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:AEV35773.1};
GN   OrderedLocusNames=PSE_1261 {ECO:0000313|EMBL:AEV35773.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV35773.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV35773.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV35773.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008361}.
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DR   EMBL; CP003147; AEV35773.1; -; Genomic_DNA.
DR   RefSeq; WP_014284061.1; NC_016642.1.
DR   AlphaFoldDB; G8PFN6; -.
DR   STRING; 911045.PSE_1261; -.
DR   KEGG; psf:PSE_1261; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_049344_5_1_5; -.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR44942; METHYLTRANSF_11 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR44942:SF4; METHYLTRANSF_11 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AEV35773.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEV35773.1}.
FT   DOMAIN          44..131
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
SQ   SEQUENCE   252 AA;  28338 MW;  FEB6EA0BAACDED9B CRC64;
     MTQNDLAASH FQSAGENYAK YRPTYPPELV EFLAAQCKHH NLAVDVGCGT GQFSALIAQY
     FQQVLATDVS TSQIENAAPV PKVRFAVEPA EQCSAKEDSV DLIVAAQAAH WFDLPSFYKE
     ARRIAVPGCV IALVSYGVLS MDNAKCNDRF RQFYYDEIGP YWPPERQHVD NGYASFDFPF
     EELSYPAMSI ERDWTLEQFL GYVRTWSSVK AAGKEGKASL MDRFAEELAG LWGDPQELRK
     ISWPVAMRLG RI
//
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