ID A0A3Q2ZT28_KRYMA Unreviewed; 1476 AA.
AC A0A3Q2ZT28;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000007038.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000007038.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR STRING; 37003.ENSKMAP00000007038; -.
DR Ensembl; ENSKMAT00000007153.1; ENSKMAP00000007038.1; ENSKMAG00000005248.1.
DR GeneTree; ENSGT00940000166425; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 1.10.720.50; PWWP, helical domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR040552; DNMT3_ADD_GATA1-like.
DR InterPro; IPR049554; DNMT3_ADD_PHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR23068; DNA CYTOSINE-5- -METHYLTRANSFERASE 3-RELATED; 1.
DR PANTHER; PTHR23068:SF52; DUF3444 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF17980; ADD_DNMT3; 1.
DR Pfam; PF21255; ADDz_Dnmt3b; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
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}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..117
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 875..930
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1045..1177
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT REGION 141..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1476 AA; 166040 MW; E2D6AF97EFDD06B2 CRC64;
MACPEVVTPD SFHDKSSRLY VVSWFNKLLK TNFKDVWEMG SGACHCQIMD CTFPGSVDLS
KVRFDAQSEE DCKHNFSLLQ DAFNKKGIAK TIPVDDLIKG DSKSNYVFLK WFKGLHTANT
QNKVYDPVTA RNSHEISPLL LSPQSRNSNL KSRTKTNHNV TPTNTFPYTE SWTDDFNWAG
PSPLGEQYTF CSSCHANLHT IKKGHVALKR HAKSDKHKKR AQTFQNRDQQ GQVSELLPCS
DAAVRFICNH CYTGSAKGEQ VAKRFVRCKL GSEYPNNIIS VCQHTPYCVY VYEGVTIGKD
DIVSVVLVGY FDIEASSHCI QFLDALQSVD GSGDQAVAAV VQTLKKFDLS TDNLAVAVCF
RSNGEASEQI CSHLRELNPN ILALGGLYTV ADAACQAGVK ELSKQTQEFM LELHAYSSRC
TKNDNLKALF GSEISENSKP FYLNASCLRF CQFVTQILGM WADLTLYFNS CHKDDEKAKL
IYSQLKDPRV KATFMFLEQA LKPLEKYQRE TQGASWATMP LILKKASTLL STYTSYFLEP
HAATRYLREH NPQILKNKKF HLSSYCLNKH RSVVEDLLKA SEAADNLSQL QEEALLFYIA
LTGCIAEKLP LSDTVLKSIA QLLNPQDKLK EAKAAAEELG TELGVCSSPE EVKQLKREIH
EYQLAEEDES EEEAKDNTAP APLEKHWSRV LKDTKPNSVF RKLVLTLLSF PCPPLDAQQV
FAQALQNGDS VIFSESESLS ESECDVTFDN SISHKDSQAH TIEIKGLSVT LKPCEVRLLK
IKNLREVLSG RNGILSKEGT CRRGFGRESS LRQKPQARTV FQAGVSSRSK PIVLDKDESK
DEVSNVALDG QSPSNTSTPR KKQRKQYQDG KGFLTGELVW GKVKGFSMWP GMVMAWKSKS
PPPGMRRVEW FGDGMFSEVG TDGLLPFSAF TRCFCKNSFT SLPSYRDAIY EIIELAGERC
GKSFAQADGN KEQELKLMVN WALEGFLPTG PQGFASPDFQ DSPSCPDSPE SSLSDYQPTP
KRKYVHKNKT AASVPTPDRN SIIKKIKEKG KTIEDFCLSC ASPEITVAHP LFEGGLCLKC
KLNFSETLYR YDDDGYQSYC TVCCSGSEVI LCSNDSCCRC FCKNCLDILV AEGTFDKLKE
VDPWNCYICS PAQCKGNLKL RPDWSVKVQD FFANDSAMQF EPHRVYPFIT ADQRRPLRVL
SLFDGIATGY LVLKELGFKI ERYIASEICD NSIAVGMIKH EGKIEYVNDV RAITRKHLVE
WGPFDLLIGG SPCNDLSMVN PQRKGLFEGT GRLFFEFYRI LTMLKPREDD NRPFFWLFEN
VVFMSASDKS DICRFLECNP VLVDAVKVSP ARRARYFWGN IPGMHRPITS SLADKVILQD
CLEIGRKAMI EKVRTITTKT SSLKKKGEVL VTMNGEEDNL WSTEMEQIFG FPKHYTDVNN
MSRTHRAKLL GKSWSVPVIR HLLAPLKDYF ECESKQ
//
