ID A0A1S2YT93_CICAR Unreviewed; 1093 AA.
AC A0A1S2YT93;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN Name=LOC101502069 {ECO:0000313|RefSeq:XP_004509555.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
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; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004509555.1};
RN [1] {ECO:0000313|RefSeq:XP_004509555.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004509555.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00000743,
CC ECO:0000256|RuleBase:RU000417};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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 RefSeq; XP_004509555.1; XM_004509498.3.
DR AlphaFoldDB; A0A1S2YT93; -.
DR STRING; 3827.A0A1S2YT93; -.
DR REBASE; 104485; M.CarCDCCMT2P.
DR PaxDb; 3827-XP_004509555-1; -.
DR GeneID; 101502069; -.
DR KEGG; cam:101502069; -.
DR eggNOG; ENOG502QT36; Eukaryota.
DR OrthoDB; 1215065at2759; -.
DR Proteomes; UP000087171; Chromosome Ca7.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd18635; CD_CMT3_like; 1.
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; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF34; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT2; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000087171};
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 DOMAIN 252..368
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 516..572
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 594
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1093 AA; 123474 MW; 2B86EFADA0D7DBBC CRC64;
MTDKSPKMLL LEHAAELRRS PRLKSPPTAA NRSNVGSSGK SGRKKGEIAV MNLSEENRRR
SPRFSVASEG TGSTSRDVKR QRSSRLSSSN GNENLQLVCF QEKRSPKVVH KNNKNIKLIS
TSIETFSRNY TPEVDDPECS TLSLEATISP TWVENGRKNS DYFAFALLDG NPPKKKYKTS
ASLMNGSKNE KSIPSFIGDP IPDDEARKRW GWRYELKDKK CKDQVCKINE DEEDEIIVNV
KCHYAQANIG NCIFTLGDCA FIKGEGAQKY IGKIIEFFQT TDSQNYFRVQ WFYRIQDTVV
KDEGGFHDKR RLFYSTVMND NLIDSIIEKV NVTYITPKVG LKLNSVLPSD FYYDMEYCVD
YSTFRKIPTG NAVDNTNELS QPAVPENLSM EASTITKDLP CPESHKTELA LLDLYSGCGG
MSTGLCLGAK TSPVNLITRW AVDSDRSASK SLKLNHPDTH VRNESAEDFL QLLKEWEKLC
KRYSSDTERT IPLRSKSSGG KKNVNSQAQD IPDDELEVSR LVDICYGDPS KTGNRSLYLK
VHWKGYSESE DTWEPIENLR NCKQSIQDFV REGIQSKLLP LPGEADVVCG GPPCQGISGY
NRYRNTASPL DDERNRQIVV FMDIVRFLKP KYVLMENVVD ILRFDNGSLG RYALSRLVHM
NYQARLGIVA AGCYGVPQFR LRVFLWGAHP DEVLPQFPFP THDVVVKYWP PPEFERNTVA
YDEDQQREVE KAIVIQDAIS DLPPITNFET RDEMSYQNPP ETEFQRYIRS TKYEMTGSTL
NGTTEERHLL YDHRPCFLFE DDYLRVCQIP KRKGANFRDL PGVVVGADNV VRTHPTEKIP
LLPSGKPLVP DYCFTFEQGK SKRPFGRLWW DETVPTALTF PSCHNQVVLH PEQDRVLTIR
EFARLQGFHD YYRFCGTVKE RYCQIGNAVA IPVSRALGYA LGTAYRKLSG NEPLMTLPPK
FSLSNYVQLS SNRVGNTHGH NIQLSSNHVG VTDEHNVQLS SNRVGDTDEH NVQLSSNHAG
DSDEHNLQLS SNHAGDTVEH NVQLSSNCVG NGNTDEHNVQ LSSNHVGDTN EHNVKLSSNH
VGDTDGHNVH PIL
//