ID K9IVB5_DESRO Unreviewed; 1581 AA.
AC K9IVB5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
DE Flags: Fragment;
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA53513.1};
RN [1] {ECO:0000313|EMBL:JAA53513.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA53513.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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|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 EMBL; GABZ01000012; JAA53513.1; -; mRNA.
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 GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd04760; BAH_Dnmt1_I; 1.
DR CDD; cd04711; BAH_Dnmt1_II; 1.
DR Gene3D; 1.10.10.2230; -; 1.
DR Gene3D; 2.30.30.490; -; 2.
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; IPR022702; Cytosine_MeTrfase1_RFD.
DR InterPro; IPR010506; DMAP1-bd.
DR InterPro; IPR017198; DNMT1-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002857; Znf_CXXC.
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; PF06464; DMAP_binding; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF12047; DNMT1-RFD; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR PIRSF; PIRSF037404; DNMT1; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 2.
DR SMART; SM01137; DMAP_binding; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 2: Evidence at transcript level;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Initiation factor {ECO:0000313|EMBL:JAA53513.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037404-3};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein biosynthesis {ECO:0000313|EMBL:JAA53513.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037404-3};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 16..109
FT /note="DMAP1-binding"
FT /evidence="ECO:0000259|PROSITE:PS51912"
FT DOMAIN 643..689
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 752..877
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 969..1097
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 105..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1223
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-3"
FT NON_TER 1581
FT /evidence="ECO:0000313|EMBL:JAA53513.1"
SQ SEQUENCE 1581 AA; 179789 MW; C5488D608F9CAC0E CRC64;
MPARTAPARV PALASRAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLQTEIKNQ
LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGAHAFS REVNGCLENG SHSSGENRRV
RMAEENKSPK PMSKPCTPRR SKSDGETKSE VSPSPRITRQ TTRQTTITSH FTRGPAKRKP
EDDPERAKLD DSVDEEEKDQ EEKRRRVTSR ELVARPLSAE EPERVKPGTH MEEEEESDEK
EKRLRSQTKE LTPKQRSKEE SDREASPGIQ AEMDEGDEKD EKRHRSQPKD LAGKRRPEEK
EPERVKPQVS DEKDEDEREE KRRKTTSKEP TEKKMARTKT VMYSKTHFQR CIQCGQYLDD
PELKYEHHPI DAVDEPQLLT NERLSIFDAN ESGFESYEAL PQHKLTCFSV YCKRGHLCPI
DTGLIEKNVE LFFSGSAKPI YDDDPSLEGG VNGKNLGPIN EWWITGFDGG EKALIGFSTS
FAEYILMDPS PEYAPVFSVM QEKIYISKIV VEFLQNNPDS TYEDLINKIE TTVPPSVLNL
NRFTEDSLLR HAQFVVEQVE SYDAAGDSDE QPIFLTPCMR DLIKLAGVTL GKRRAERRQT
ISHSTKEKDK GPTKATTTKL VYQIFDTFFA EQIEKDDRED KENAFKRRRC GVCEVCQQPE
CGKCKACKDM VKFGGSGRSK QACQERRCPN MAMKEADDDE EVDDNIPEMP SPKKMHQGKK
KKQNKNRISW IGEAVKTEGK KTYYKKVCID SETLEVGDCV SVIPDDSSKP LYLARVTALW
EDSIQGQMFH AHWFCAGIDT VLGATSDPLE LFLVDECEDM QLSYIHSKVT VVYKAPSENW
AMEGGMDPEA LMAEDNGKTY FYQLWYDQDY ARFESPPKTQ PTEDNKYKFC ASCARLAEMR
QKEIPRVVEQ VEDIDGRLFY GSASKDGVQY RVGDGVYLLP EAFTFNIKMS SPVKRPRKEP
VDEDLYPEHY RKYSDYIKGS NLDAPEPYRI GRIKEIFCVK KNNGKPNETD IKIRLNKFYR
PENTHKSTPA SYHADINLLY WSDEEAVVDF SAVQGRCTVE YGEDLPECLQ DFSAGGPDRF
YFLEAYNAKS KSFEDPPNHA RSPGNKGKGK GKGKARVKSQ PCEPSEPKAE IQLRKLRTLD
VFSGCGGLSE GFHQAGISET LWAVEMWDPA AQAFRLNNPG STVFTEDCNV LLKLVMAGEV
TNSRGQKLPQ KGDVEMLCGG PPCQGFSGMN RFNSRTYSKF KNSLVVSFLS YCDYYRPRYF
LLENVRNFVS FKRSMVLKLT LRCLVRMGYQ CTFGVLQAGQ YGVAQTRRRA IILAAAPGEK
LPLFPEPLHV FAPRACQLSV VVDDKKFVSN ITRLSSGPFR TITVRDTMSD LPEIRNGASA
QEISYNGEPQ SWFQRQLRGS QYQPILRDHI CKDMSALVAA RMRHIPLAPG SDWRDLPNIE
VRLSDGTMAR KLRYTHHDKK NGCSSTGALR GVCSCAEGKA CDSTARQFNT LIPWCLPHTG
NRHNHWAGLY GRLEWDGFFS TTVTNPEPMG KQGRVLHPEQ HRVVSVRECA RSQGFPDTYR
LFGNILDKHR QVSAVEQSAC F
//
