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Database: UniProt
Entry: A0A0F2J4L7_9BACT
LinkDB: A0A0F2J4L7_9BACT
Original site: A0A0F2J4L7_9BACT 
ID   A0A0F2J4L7_9BACT        Unreviewed;       480 AA.
AC   A0A0F2J4L7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN   ORFNames=MCHI_000200 {ECO:0000313|EMBL:KJR43902.1};
OS   Candidatus Magnetoovum chiemensis.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Candidatus Magnetoovum.
OX   NCBI_TaxID=1609970 {ECO:0000313|EMBL:KJR43902.1, ECO:0000313|Proteomes:UP000033718};
RN   [1] {ECO:0000313|EMBL:KJR43902.1, ECO:0000313|Proteomes:UP000033718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS-04 {ECO:0000313|EMBL:KJR43902.1,
RC   ECO:0000313|Proteomes:UP000033718};
RA   Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT   "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT   conserved set of magnetosome genes.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU362026}.
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:KJR43902.1}.
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DR   EMBL; JZJI01000069; KJR43902.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2J4L7; -.
DR   PATRIC; fig|1609970.3.peg.224; -.
DR   Proteomes; UP000033718; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR007560; Restrct_endonuc_IV_Mrr.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   PANTHER; PTHR13370:SF24; TYPE III RESTRICTION-MODIFICATION SYSTEM HINDVIP ENZYME MOD-RELATED; 1.
DR   Pfam; PF04471; Mrr_cat; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KJR43902.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033718};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJR43902.1}.
FT   DOMAIN          23..301
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
FT   DOMAIN          354..421
FT                   /note="Restriction endonuclease type IV Mrr"
FT                   /evidence="ECO:0000259|Pfam:PF04471"
SQ   SEQUENCE   480 AA;  55276 MW;  F24FF47BD33DC9E6 CRC64;
     MENILYYGDN LNILRNSIAD KSIDLIYLDP PFNSKADYNI LFKEATGEQS QAQITAFGDT
     WHWTEETGMA FNDIVNTSPV EVVEMMRAFK QFVGLNDLMA YLTMMCVRLV ELKRILKDSG
     SIYLHCDPTA SHYLKILMDT IFDKKNFRNE ICWCYRGAGY PKKDFGRRHD IILRYSLTSE
     HIFYLDDVRE QYADTTKERF KHYIGNIRKG KDFGVQSLHP LGKQPDDWWQ IQPIAPSANE
     RLGYPTQKPE ALLERIIKAS SNEGDIILDP FCGCGTTIAV AQKLKRNWIG IDITHLAINL
     IKWRLKDMFS LEPKKDYNVI GEPEDLSGAR ELALHNRYQF QWWALSLIDG RPYRDKKKGA
     DTGIDGYIYF TDEKDKTKSA IVQVKSGKVG VKDIRDLGYV IDREKSDIGI FITLEIPTQP
     MIKEALSKGY YKSIGFSKDY PRIQILTIDE LLSGKLPQIP ITIPAYKKAQ WADTEEQLDI
//
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