GenomeNet

Database: UniProt
Entry: N8ZUS7_9GAMM
LinkDB: N8ZUS7_9GAMM
Original site: N8ZUS7_9GAMM 
ID   N8ZUS7_9GAMM            Unreviewed;       458 AA.
AC   N8ZUS7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=F960_00270 {ECO:0000313|EMBL:ENV35498.1};
OS   Acinetobacter gerneri DSM 14967 = CIP 107464 = MTCC 9824.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1120926 {ECO:0000313|EMBL:ENV35498.1, ECO:0000313|Proteomes:UP000013117};
RN   [1] {ECO:0000313|EMBL:ENV35498.1, ECO:0000313|Proteomes:UP000013117}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 107464 {ECO:0000313|EMBL:ENV35498.1,
RC   ECO:0000313|Proteomes:UP000013117};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter gerneri CIP 107464.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000256|ARBA:ARBA00000743,
CC         ECO:0000256|RuleBase:RU000417};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01016, ECO:0000256|RuleBase:RU000416}.
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:ENV35498.1}.
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; APPN01000020; ENV35498.1; -; Genomic_DNA.
DR   RefSeq; WP_004871898.1; NZ_KB849555.1.
DR   AlphaFoldDB; N8ZUS7; -.
DR   GeneID; 84211793; -.
DR   PATRIC; fig|1120926.3.peg.253; -.
DR   eggNOG; COG0270; Bacteria.
DR   HOGENOM; CLU_006958_2_2_6; -.
DR   OrthoDB; 9813719at2; -.
DR   Proteomes; UP000013117; Unassembled WGS sequence.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}; Reference proteome {ECO:0000313|Proteomes:UP000013117};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01016};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}.
FT   ACT_SITE        199
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   458 AA;  51396 MW;  BAF6354444268170 CRC64;
     MLDSNFSGQE LRLFRESQKV SQAKLAKETS IVQAKISSFE LDKGVLSDED KAKIFQFFSN
     SSKVEKVVKA KKKITKQSNF SISSLDVDER KKKYALSPKN KKYVQDLDTL YDRHLNSNKD
     FKAISLFSGC GGLCLGFSAA GVRIAGFIEK DKDISQIYRD NFSSTPQLAN DITSLSHKDI
     EEYKESIGDV DIVIGGPPCQ GFSLSGKRDK SDARNKLFEN YLDIVSVFKP KIALLENVQL
     LTSMKDESGK YIKDLIINKF QDLGYKITYF EVNTKDYGVP QSRARVFFLA IKNDIALDLG
     FPTIEKENLT FGDACSDLEY LESGESSNVD ELHFAVNHPP HVLEWLWNVP EGSSAHDNED
     ESLRPPSGYN TTYKRQVWNE EGSTVQTTFG MISGCRNVHP VATRSLTVRE AARIQSFPDR
     FIFNGKVGTI RTAIGNAVPP LLAYKIASYL VDELKKTK
//
DBGET integrated database retrieval system