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Database: UniProt
Entry: A0A1S2YT93_CICAR
LinkDB: A0A1S2YT93_CICAR
Original site: A0A1S2YT93_CICAR 
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
//
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