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Database: UniProt
Entry: A0A238FNU4_9BASI
LinkDB: A0A238FNU4_9BASI
Original site: A0A238FNU4_9BASI 
ID   A0A238FNU4_9BASI        Unreviewed;      1802 AA.
AC   A0A238FNU4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE            EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN   ORFNames=BQ2448_6281 {ECO:0000313|EMBL:SCV73851.1};
OS   Microbotryum intermedium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV73851.1, ECO:0000313|Proteomes:UP000198372};
RN   [1] {ECO:0000313|Proteomes:UP000198372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; FMSP01000019; SCV73851.1; -; Genomic_DNA.
DR   STRING; 269621.A0A238FNU4; -.
DR   OrthoDB; 317994at2759; -.
DR   Proteomes; UP000198372; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.490; -; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000198372};
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          1..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1335
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   1802 AA;  204318 MW;  201B60225C15E50B CRC64;
     MKRRRRKATS SELGEVVDAT MPDGLGVRGK APLSSEPQRV DDDEQQDEVE PLLGLPPLPS
     LAPSEASSPT ETRPQPRPPT RSVSFSLGVA SSVASTSTST STESGSGRSP PPTPPESPSA
     DSDGVSDFGI DSRRRPASAT QPGRGHHPKY YTDEELDQEY RAFERDCQVW LKAHYNYPQY
     RLFESIKVRL SDLIKNRWRW WKGVSNYERL SYFEDRKWPN QDQVIALRHR VGPKAIDLTI
     EDSDDESNHE DHQLLDLEWR DPDEESAPTE LNEFGQIYSG DAFLNDPQRF LALPKPPPTV
     EERFARYQRE TARVETVRKR EKKRRRVDQE KEPTPDTWDA RIPPILEPNS SQEVPELMNL
     EEDIKGKSTA RTRARDQDAA QEKPLVARQA APPGQSRTTN RRKWIENPRP RRLFGMARKR
     KLLQGRRSQL LPDRKPLPPQ ADPTMNEFHE YHLFELFEMP LPTTNKTKGA FAMRDFALYS
     KRGQGRSMAD LLLLDGSNKG QFERLEFEGW VLPEMETLPE SERASGDEGW VDFDGTDVEW
     ETCGDRIPHK FDGVRKVIIA ASDIVGLVPR LERSSGRPCL YLVTKLGSYR LETPNDSYRK
     GHFFDRARIY INLFVFGRET HVLGQNNRPI RDLVADLMAK LYDYKLVKTT MQTLRRLPPD
     YQLPKPLPSY ADYARDLEIA RLLHRHLVNT PFVTPIIYNL VAPFLEPKSL RTDERAAILG
     RAEADSAAAV EVQEQMEQAI LDWWEDKSDP ETALEGAGLL KEHPDRANGR DGDRLFGSGI
     TVYDCMRVET NVFKTGDTVL VAGTPTDVQN EAEDASAIER ARMEAQREDQ EGDWYDDGPP
     PSFPTKALPA KLWYAKIVYF FTLNDDTDPD RDIKAHVSWL IPLCDTPLGS LAPKRALYYN
     DHCSTISANT IAQKINIVEL DHHSGVPPST GLYYSLHWDR HTNNYVDSHP VEYLSGPKTF
     ERCDTASIVR CSSCERRIEE SETSFFDPKT ELSTDRASWI ESSPIPAFKV GQNTYHLGDY
     CYLLPLGSDD STNGPAKREP YLLGQLIGVG SVKLGDRPRR LPPFDSETYL QVRALLRYDD
     VSDKNLVFGK RDFDERRLVL TDIEYGGFYW SNLEGTFRLE TWKEVMDQAA EMFPNRLNGN
     DKAEREAIAL AGLQKRQDVF YTGRGLSFLE VDEDTDWSLA RNWVSSTCND IELGEKNVLR
     SLRQDEIDDI ARCSECHRVY ELERLQRAQI TEAMSREPDK YSLDALSAYS GVDLLSIGLE
     RGCSAIKTKA AIEQNPYAAA ALKANGQKVF NCPTSDYVEA FYYSQSVPVQ DADHRPRPTA
     LKRGEVHLIQ SGPPCQGFSA QNQYKTQDDV RCLEPFVWLS AVEQYRPLFA VFENVSDIQR
     FILPRGSEKE APEKGGLLRL LMSALIQLGY QVRLDIHQAA AFGTPQARRR VILMCARRGL
     SLPAAPQPTH AFTDKGLKTF AAPYETGTKI HTTCSSLRRG GHAPHHAVTI EEAINDLPSF
     GFADPFDLTP AGDADFAWEP YLPIGFRSRQ HVLEQDHKAK SFYASKYPKS SFQSCLRVRT
     IKSGHTILTP ETSEHVVPAV PEIHASYFAN IAKRSTMRNS RVPGKSHNYH DIPLEVTIEY
     EDGVEQSFAL RPELPSAMQD EDKRGSRDAE HFWARLEWTQ VISTLLTQLQ PAGYWHGPRI
     HPVDNRQLSV RETARLFGCP DHINLEALGR ADDEDERFDE MYKLVGNAVP VPLAEAIGRE
     LHRVVEIMIY DARDAQSEPL ALYDDGGETN LFSTMWTKLE ASDARQRLDN DATKCSGSRS
     LS
//
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