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Database: UniProt
Entry: A6LAB6_PARD8
LinkDB: A6LAB6_PARD8
Original site: A6LAB6_PARD8 
ID   A6LAB6_PARD8            Unreviewed;       427 AA.
AC   A6LAB6;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   OrderedLocusNames=BDI_0861 {ECO:0000313|EMBL:ABR42630.1};
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR42630.1, ECO:0000313|Proteomes:UP000000566};
RN   [1] {ECO:0000313|EMBL:ABR42630.1, ECO:0000313|Proteomes:UP000000566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC   {ECO:0000313|Proteomes:UP000000566};
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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|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}.
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DR   EMBL; CP000140; ABR42630.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6LAB6; -.
DR   STRING; 435591.BDI_0861; -.
DR   REBASE; 15664; M1.Pdi8503ORF861P.
DR   PaxDb; 435591-BDI_0861; -.
DR   KEGG; pdi:BDI_0861; -.
DR   eggNOG; COG0270; Bacteria.
DR   HOGENOM; CLU_006958_5_2_10; -.
DR   BioCyc; PDIS435591:G1G5A-884-MONOMER; -.
DR   Proteomes; UP000000566; Chromosome.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
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:UP000000566};
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   REGION          188..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   427 AA;  48314 MW;  FD3C2DFC1C65F462 CRC64;
     MTHGSLFSGV GGFDLAAEWM GWENLFHCEI NEWCQKVLRF HFPKSIQYDD ITRTDFTPWR
     GKVDVLTGGF PCQPFSTAGK RRGAEDDRYL WPEMLRAIRE IRPAWVIGEN VAGITSMVQP
     GSEVTVESQA SLFEKADKET ILEQEYVIET VCRDLEREGY SVQPILIPAC GVGAPHKRDR
     VWFIAHSEGD GDRGASHEGG GTTQGSYGKE IEQSFIGSGI WTTSHPNCSR GLQFGERRDI
     RDKEQYDQDK EPERHEQPSR FGGSGEAYVI SDTDSPRFQA KGSEQQTTGI TGGGLRKDVT
     DTYGEKLQTW LKNNGREIEE ENIARLDNGV ERSCCIRAFA ESDKKRRCLM QYTSNDWPAL
     SAELWKDFPT QPPVCRRNDG LPFDVDYLAI PFTKWRQESI KAYGNAIVPQ VAFEIFKAIE
     TSTFHHS
//
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