ID   MTA1_ANAVA              Reviewed;         482 AA.
AC   P0A462; P70802;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Type II methyltransferase M.AvaI {ECO:0000303|PubMed:12654995};
DE            Short=M.AvaI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.113 {ECO:0000250|UniProtKB:Q04845};
DE   AltName: Full=Modification methylase AvaI;
DE   AltName: Full=N(4)- cytosine-specific methyltransferase AvaI;
GN   Name=avaIM {ECO:0000303|PubMed:8917312};
OS   Anabaena variabilis.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=264691;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=PCC 7118 / ATCC 27892;
RX   PubMed=8917312; DOI=10.1007/bf02173975;
RA   Ruan H., Lunnen K.D., Scott M.E., Moran L.S., Slatko B.E., Pelletier J.J.,
RA   Hess E.J., Benner J. II, Wilson G.G., Xu S.-Y.;
RT   "Cloning and sequence comparison of AvaI and BsoBI restriction-modification
RT   systems.";
RL   Mol. Gen. Genet. 252:695-699(1996).
RN   [2]
RP   NOMENCLATURE, AND SUBTYPE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: An alpha subtype methylase that recognizes the double-
CC       stranded sequence 5'-CYCGRG-3', methylates C-1 on both strands, and
CC       protects the DNA from cleavage by the AvaI endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8917312}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC         Evidence={ECO:0000250|UniProtKB:Q04845};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X98339; CAA66984.1; -; Genomic_DNA.
DR   PIR; S72471; S72471.
DR   AlphaFoldDB; P0A462; -.
DR   SMR; P0A462; -.
DR   BRENDA; 2.1.1.113; 322.
DR   PRO; PR:P0A462; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 2.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..482
FT                   /note="Type II methyltransferase M.AvaI"
FT                   /id="PRO_0000087919"
SQ   SEQUENCE   482 AA;  56579 MW;  795ED0B445EA9E0C CRC64;
     MTSFELESPI EIKTDPTDLD QESDSFVQEI SRFNKALEQR FRDKMRLHES LSRKIVSFQA
     NKSKPQYRWF KYKEAFSVDL VNQLIFEYEK KSFERILDPF AGAGTMLFAC SDAGIQADGI
     EVLPIGQEII EVRKIIQRQF RREDFLRLIE WYKQKPWNQH NNRKYLNRLR ITDGAYPPET
     EASIERFLFS IEKENILVKQ VLRFALLCIL ESISYTRKDG QYLRWDKRAF RKSGSDKFDK
     GKILDFDEAI TEQIKLILND SFDLISNTLF CYGTQRSGIN LFNASCLKIL PEFEQDFYDC
     IITSPPYCNR YDYTRTYALE LALLGVGERD IVQLRQDMLS CTVENKEKSL IHNWQEALRI
     LDKQELLQSI LRFLERELER KKLNNNGIPR MIKGYFYEMA CVIIECFRVL KNGSPLFMVN
     DNVRYAGIDI SVDLILSNIA EEIGFNVEKI LVLPTGKGNS SQQMGTHGRK TLRKCVYVWR
     KP