ID F7KY36_9FUSO Unreviewed; 1211 AA.
AC F7KY36;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=HMPREF0401_00507 {ECO:0000313|EMBL:EGN63146.1};
OS Fusobacterium animalis 11_3_2.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=457403 {ECO:0000313|EMBL:EGN63146.1, ECO:0000313|Proteomes:UP000004160};
RN [1] {ECO:0000313|EMBL:EGN63146.1, ECO:0000313|Proteomes:UP000004160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11_3_2 {ECO:0000313|EMBL:EGN63146.1,
RC ECO:0000313|Proteomes:UP000004160};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., White A.P.,
RA Crowley S., Surette M., Strauss J.C., Ambrose C.E., Allen-Vercoe E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z.,
RA Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium sp. 11_3_2.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC Evidence={ECO:0000256|ARBA:ARBA00001279};
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:EGN63146.1}.
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DR EMBL; ACUO01000008; EGN63146.1; -; Genomic_DNA.
DR RefSeq; WP_008692039.1; NZ_GL945391.1.
DR AlphaFoldDB; F7KY36; -.
DR PATRIC; fig|457403.8.peg.510; -.
DR HOGENOM; CLU_007510_1_0_0; -.
DR Proteomes; UP000004160; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR047939; BREX_1_PglX.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; NF033452; BREX_1_MTaseX; 1.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 290..557
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT COILED 395..449
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1153..1187
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1211 AA; 142004 MW; 05DCABA9A317F867 CRC64;
MNKSSLKIFA IEARKELMEK MRIRLEILGI TKNGIEKAKV IGKEVEVKGT LYPKESYDSL
IRKYKQVGYE ELIEESAYTW FNRLTALAFM EANGYIDEKM IFNNGVKNEP AIIDNYYEFE
FFENLDSDLQ KELHNLRDEN TPNSIEKLYS VLMEEKCEDL SNIMPFMFKK KGTYSDILFP
TGLLMENSLL VRLREEIGAE APIELIGWLY QYYNSEKKDE VFEGLKKNKK ITKENIPAAT
QLFTPDWIVK YMVENSLGKL ALESTGINEN LKNNWKYYID SENEENLGKI KIEDIKILDP
AMGSGHILVY AFDLLFEMYE NLGWSTKETV LSILKNNLYG LEIDERAGQL ASFALMMKAR
EKFSRLFSVL KREEDFKLNT LIIEESNSLS ERIKNKIEAN NLNNLNKIIQ EFEDAKEYGS
ILKLESIDKE ILEREFNILK ESFNNNEQET LIFNEDEIII DINEELELIG NLIKQHITLT
NQYETVVTNP PYMGGKGFSP KLKTYVEKNY KDSKSDLFAV FIERCNEFTK KNCYTSMITM
QSWMFLSSFE TLRKNIIEKT EIKSLNHLGT RAFSEIGGEV VSTVAWISKK ISPKNEGTYI
RLVDYNNAEL KEQEFYNRAN YFQAKQKDFE KIPGSPIAYW ISDKIREIFE KNQKLGDIGE
AKQGLATADN NRFLRLWNEV NYNKIGYNMS NSQEALESKK KWFPCNKGGS FRKWYGNQEI
IVNWEKDGFE LKDFKNSVIR NPSYYFKEAL TWSTISSSDC SFRYSPIGNI FETKGSNYFV
KDYKNFYYLF GFLNTKIVNY LLKIISPTLD YHEGPMSNLP VTLEDSSIKL EIINNFIIEN
LNISKEEWDS RETSWDFEKL SLIDGKNLKT AYENYCSHWR ENFVQLHKNE EELNRLFIEI
YDLQDEMDEK VSFDDITILK KEANIIQIDN SIPKEFSTES EKYLYDRGIS LEFNKDELVK
QFLSYAVGCI MGRYSINKTG LIIANSDDML ELSENKFIVK GTDGEIRQEI ESKFLPDEFA
IIPITDEKDF SNDIVEKVKE FIKYVYGEEN LKDNLNFIAE ALGNKDNKPA EEIIRTYFIK
DFYSDHLQRY QKRPIYWLMN SGKKNAFSCL FYMHRYEPLT VARVRADYLI PYQEMLENKR
KFIERQLSDD DISAKEKKNI EKQLKELDTL LKELREYANE VKHIAEQKIT LDLDDGVNVN
YEKLGAILKK R
//
