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Database: UniProt
Entry: A0A0D0Q5W6_9RHOB
LinkDB: A0A0D0Q5W6_9RHOB
Original site: A0A0D0Q5W6_9RHOB 
ID   A0A0D0Q5W6_9RHOB        Unreviewed;       354 AA.
AC   A0A0D0Q5W6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=peptide chain release factor N(5)-glutamine methyltransferase {ECO:0000256|ARBA:ARBA00012771};
DE            EC=2.1.1.297 {ECO:0000256|ARBA:ARBA00012771};
GN   ORFNames=Wenmar_03612 {ECO:0000313|EMBL:KIQ67882.1};
OS   Wenxinia marina DSM 24838.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Wenxinia.
OX   NCBI_TaxID=1123501 {ECO:0000313|EMBL:KIQ67882.1, ECO:0000313|Proteomes:UP000035100};
RN   [1] {ECO:0000313|EMBL:KIQ67882.1, ECO:0000313|Proteomes:UP000035100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24838 {ECO:0000313|EMBL:KIQ67882.1,
RC   ECO:0000313|Proteomes:UP000035100};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC         methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC         factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC         COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61891; EC=2.1.1.297;
CC         Evidence={ECO:0000256|ARBA:ARBA00000932};
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:KIQ67882.1}.
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DR   EMBL; AONG01000019; KIQ67882.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0Q5W6; -.
DR   STRING; 1123501.Wenmar_03612; -.
DR   PATRIC; fig|1123501.6.peg.3739; -.
DR   eggNOG; COG2890; Bacteria.
DR   Proteomes; UP000035100; Unassembled WGS sequence.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:UniProt.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004556; HemK-like.
DR   InterPro; IPR040758; PrmC_N.
DR   InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   NCBIfam; TIGR00536; hemK_fam; 1.
DR   NCBIfam; TIGR03534; RF_mod_PrmC; 1.
DR   PANTHER; PTHR18895; HEMK METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR18895:SF74; MTRF1L RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE; 1.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF17827; PrmC_N; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035100};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..75
FT                   /note="Release factor glutamine methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17827"
FT   DOMAIN          97..189
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
FT   REGION          222..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  37498 MW;  0BFFC6C418A74A3D CRC64;
     MTGSALLVAA VRRLGEAGVP DAALDARRLL AHALGIAPDR LTLHLPEAVP DAVAAAYEAL
     ISRRAAREPV AQITGRRMFY GREFLVTADV LDPRPETEVL IEAALAAPFE TVLDLGTGSG
     CILLTLLAEM EGSRGVGTDV SGPACDVAEE NARRLGMGDR ARIVHTDWWA GVTGSFDLIV
     SNPPYIAAAE MAGLEPEVRE WEPRGALTDE ADGLGAYRTI LSGAPQRLVP GGRADPRDRG
     GAGGGRRRPG PPRRFHRGAA DPRSRRPGPR HRGRSRAGRA VLGTDPRGRA VFSGVASCHR
     APRMFSRTCT TGEDAAAPSP RGRSPDHPAV PPARHDHGAA DPDKTNLQAE RRAT
//
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