ID A0A0L9VI80_PHAAN Unreviewed; 1666 AA.
AC A0A0L9VI80;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 36.
DE RecName: Full=DNA (cytosine-5)-methyltransferase {ECO:0000256|PIRNR:PIRNR037404};
DE EC=2.1.1.37 {ECO:0000256|PIRNR:PIRNR037404};
GN ORFNames=LR48_Vigan10g058500 {ECO:0000313|EMBL:KOM54693.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM54693.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
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|PIRNR:PIRNR037404,
CC ECO:0000256|RuleBase:RU000417};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037404}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family.
CC {ECO:0000256|PIRNR:PIRNR037404, ECO:0000256|PROSITE-ProRule:PRU01016,
CC ECO:0000256|RuleBase:RU000416}.
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DR EMBL; CM003380; KOM54693.1; -; Genomic_DNA.
DR STRING; 3914.A0A0L9VI80; -.
DR EnsemblPlants; KOM54693; KOM54693; LR48_Vigan10g058500.
DR Gramene; KOM54693; KOM54693; LR48_Vigan10g058500.
DR OMA; KINDAEC; -.
DR Proteomes; UP000053144; Chromosome 10.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd04712; BAH_DCM_I; 1.
DR CDD; cd04708; BAH_plantDCM_II; 1.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR InterPro; IPR017198; DNMT1-like.
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; PF01426; BAH; 2.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF12047; DNMT1-RFD; 2.
DR PIRSF; PIRSF037404; DNMT1; 5.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 2.
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 DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037404};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR037404};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037404};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR037404};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037404};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1578..1599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 758..892
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 932..1071
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 31..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..708
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1221
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1666 AA; 187874 MW; EC26DBA159FBF4D4 CRC64;
MVLWGDLTFG HVVVKNTKSK EDFALSNGEG EVMSTNKQNK RSLAESPEQA PASRKMPKRA
AACKDLKEKS FSISDKSCLI ETEKDQIVDE EIVAVRLTAG QDDGRPNRRI TEFILHDENG
KGQHLEMLEV TDLYITGVIL PLEPSTGKKK EKGIKCEGFG RIESWDISGY EDGSPVIWIS
TDVADYDCQK PAASYKKFYD QFFEKARACV EVYKKLAKSS GGDPSISLDE LLAGMARSMS
GSKSFSGTAS LKDFVISQGE FIYKQLIGLD MTSKSNDMMF ADIAALIALR DEAKKQANHA
LMQVVPSNGT LRIGSGAEEE ENKNQMDFVD SPNDEDEDVK LARLLQEEEY FKSMKQKKNN
RSGSASNKFY IKINEDEIAN DYPLPAFYRT SLQETDEFIV FDNDYDVYDT EDLPRSMLHN
WSLYNSDARL VSLELLPMKS CSDIDVAIFG SGVMTADDGS GFHLESDAGQ SSSSSPEAQA
ADGMPIYLSA IKEWMIEFGS SMIFISIRTD LAWYRLGKPA KQYAPWYETV LKTARLAIAI
ITLLKDQTRV SRLSFGDIIK KVSEFNQKNV SYISSDPLAV ERYVVVHGQI ILQLFAEFPD
VKIRKSPFVT GLSNKMEERH HTKWLVKKKK VLPRSEPNLN PRAAVGPIVS KRKAMEATTT
KLINRIWGDY YSNHLPEDSK EGPVSELKEE DELEEQEENE EDDNEEEPIL LEGTSKKNSH
SKQTNKFSGD AEIMWEGKPE GKTTSGYPVY KQAIINGEVI SVGKFVLVEV DETDEFPDIY
CVEYMFESKN GRKMFHGRMM QHGCHTVIGN AANEREVFLT NDCRDLGLQD VKRTVAVNIQ
KRPWGHQHRK DNIITDRVDR ARAEERKKKG LPTEYYCKSL YWPERGAFFS LPFDTLGQGS
GICSSCKIHD YEKAKNIFSV NSFKSGFLFK GTEYSLDDFV YVSPFEFEEK IEQGTHKSGR
NVGLKAYVVC QVLEIVVKME IKHPEIKSTQ VKVRRFFRPE DVSNEKAYCS DIQEVYYSDE
THIISVDSIE GKCEVRKKSD IPEQSAPGMF QNVFFCELLY DPATGSLKKL PAHIKVKYST
GQTSDAAARK RKGKCKEGDD DSESSKEGKT LNEKRLATLD IFAGCGGLSE GLEQSGVSST
KWAIEYEEPA GDAFKANHPD ALVFINNCNV ILRAVMEKCG DIDDCISTTE AAELAAKLDE
SESSSLPMPG QVDFINGGPP CQGFSGMNRF NQSSWSKVQC EMILAFLSFA DYFRPRYFLL
ENVRNFVSFN KGQTFRLTLA SLLEMGYQVR FGILEAGAFG VSQSRKRAFI WAACPDDVLP
EWPEPMHVFS APELKIPLSE NVHYAAVRST ANGAPLRAIT VKDTIGDLPA VGNGASKGNM
EYQNDPVSWF QKRIRGEMIV LTDHISKEMN ELNLIRCQKI PKRPGADWRD LPEEKVTLSN
GQVVDLIPWC LPNTAKRHNQ WKGLFGRLDW QGNFPTSITD PQPMGKVGMC FHPDQDRILT
VRECARSQGF PDNYKFSGNI IHKHRQIGNA VPPPLAFALG RKLKEAVNRI EWIMLRRDHF
DNLDFLDEYM FLLFMKKMAW NFMAVIPFSP PSLYILFIFS EKTLTLSLLR SSFRHCRSDS
GVKSFQINRS VCEAELVSPS LHPIVRLPRH ANPVLFIGVD HHSSNE
//
