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Entry: A0A1Z3HRK8_9CYAN
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ID   A0A1Z3HRK8_9CYAN        Unreviewed;       312 AA.
AC   A0A1Z3HRK8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Release factor glutamine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126};
DE            Short=RF MTase {ECO:0000256|HAMAP-Rule:MF_02126};
DE            EC=2.1.1.297 {ECO:0000256|HAMAP-Rule:MF_02126};
DE   AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
GN   Name=prmC {ECO:0000256|HAMAP-Rule:MF_02126,
GN   ECO:0000313|EMBL:ASC72953.1};
GN   ORFNames=XM38_039130 {ECO:0000313|EMBL:ASC72953.1};
OS   Halomicronema hongdechloris C2206.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nodosilineales; Nodosilineaceae;
OC   Halomicronema.
OX   NCBI_TaxID=1641165 {ECO:0000313|EMBL:ASC72953.1, ECO:0000313|Proteomes:UP000191901};
RN   [1] {ECO:0000313|EMBL:ASC72953.1, ECO:0000313|Proteomes:UP000191901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2206 {ECO:0000313|EMBL:ASC72953.1,
RC   ECO:0000313|Proteomes:UP000191901};
RX   PubMed=26514405; DOI=10.1016/j.bbabio.2015.10.009;
RA   Li Y., Lin Y., Garvey C.J., Birch D., Corkery R.W., Loughlin P.C.,
RA   Scheer H., Willows R.D., Chen M.;
RT   "Characterization of red-shifted phycobilisomes isolated from the
RT   chlorophyll f-containing cyanobacterium Halomicronema hongdechloris.";
RL   Biochim. Biophys. Acta 1857:107-114(2016).
CC   -!- FUNCTION: Methylates the class 1 translation termination release
CC       factors RF1/PrfA and RF2/PrfB on the glutamine residue of the
CC       universally conserved GGQ motif. {ECO:0000256|HAMAP-Rule:MF_02126}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02126};
CC   -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC       family. PrmC subfamily. {ECO:0000256|HAMAP-Rule:MF_02126}.
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DR   EMBL; CP021983; ASC72953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z3HRK8; -.
DR   STRING; 1641165.XM38_09590; -.
DR   KEGG; hhg:XM38_039130; -.
DR   Proteomes; UP000191901; Chromosome.
DR   GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR   InterPro; IPR004556; HemK-like.
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; PTHR47441; -; 1.
DR   PANTHER; PTHR47441:SF3; RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE; 1.
DR   Pfam; PF05175; MTS; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_02126}; Reference proteome {ECO:0000313|Proteomes:UP000191901};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_02126};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02126}.
FT   DOMAIN          122..211
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
FT   BINDING         138..142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         190
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         207..210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         207
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ   SEQUENCE   312 AA;  34067 MW;  29247754D64365F4 CRC64;
     MSRTEGAHTI TGSELWQWWQ MARQQALAQQ IDPAEVDWLV RAISDVDGLS LRLQSFRQRA
     AIPCRYGLPA LETLWQRRRQ EHIPVQYLVG QTQWRDFTLQ VSTAVLIPRP ETELLIELVH
     AAVAQTPALE AGTWVDLGTG SGAIALGLAK ALPRAHIIAV DCSAEALALA AANAAANGLC
     DRIELRQGHW FTPLADLRGQ LAGMVANPPY IPSAMVATLA PEVAVHEPRL ALDGGPDGLT
     AIQHLIDAAP DYLQANGLWL IEAMAGQPAT ILQQLQQHGA YCDLQRHRDL AGLERFVQAR
     CQGPQGSRRH SQ
//
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