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Database: UniProt
Entry: A0A0B2VLT7_TOXCA
LinkDB: A0A0B2VLT7_TOXCA
Original site: A0A0B2VLT7_TOXCA 
ID   A0A0B2VLT7_TOXCA        Unreviewed;       902 AA.
AC   A0A0B2VLT7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Histone-lysine N-methyltransferase 2C {ECO:0000313|EMBL:KHN82304.1};
GN   Name=Kmt2c {ECO:0000313|EMBL:KHN82304.1};
GN   ORFNames=Tcan_09257 {ECO:0000313|EMBL:KHN82304.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN82304.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN82304.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN82304.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHN82304.1}.
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DR   EMBL; JPKZ01001384; KHN82304.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VLT7; -.
DR   STRING; 6265.A0A0B2VLT7; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd15513; PHD5_KMT2C_like; 1.
DR   CDD; cd15514; PHD6_KMT2C_like; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45888; HL01030P-RELATED; 1.
DR   PANTHER; PTHR45888:SF6; HL01030P-RELATED; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 3.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:KHN82304.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:KHN82304.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          288..341
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          358..422
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          73..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   902 AA;  98652 MW;  95ED14B901341CC1 CRC64;
     MDEVHGSVAV SSASTSVLSP GAQRVHRIDA FATRWIHTEC DADALGGGAV EGEYVCAVCR
     NSPLVADAMM TSAGSSSLAP SPTSVSAHDE TSRNTLETGF SIQSPTNRNS PLAPLSHLDS
     TFNDIFTISH ASGHGDVSSM SSPATTTATT TASNSARASP AFFLDNTASS DTDDFRPPPR
     GGKTSSMIAL VASTAAGREA ELHTQENGDT EESKNRVEDN EYIRTVVITS AENTFFMQMP
     VCLICGSIGK DIEGTMVACA TCAQSYHTFC VGLHDKLNST IVKRGWRCLD CTVCEGCGDG
     RDESNLLLCD ECDVSYHIYC LDPPLERIPH GSWRCKWCAT CRRCSAPIPS AVDTQRMEGL
     CETCYSLRKC PKCLRLYEVG EHIIKCQHCS RWLHGKCEDI CGEDMLEAAA ENGFRCSLCR
     PQGNTPASDA LNVLICDYVP MNKCALDVLH TKHGGSLFRS TSLQEPMFDL PMHPFASRGH
     SFDDAYEEEE MEVVSVGMSG RGRGMRGGGP GRKVLKLGVG DAYEEEEMEV VSVGMSGRGR
     GMRGGGPGRK VLKLGVGGFF VKMPRHRIQA AEDDANAEEE LAPGQKPKIK RPRKPRRCQL
     EDNYPPIIQE SFFGMRPVEG RNLLEVVVDE PNLSQEINKT TLGQEKQKEV FELNEADSEA
     LREGESLLGD ITENDIFGNM EEIDFDNFDI NELLMEGEDE DDEDTLDAAT NDGGTASEDT
     SATQSQQQFA FRVPQQGRNS GGQGQGGHHQ TGAHSGGAYP LQTSIQSAGS RSNSQMGENY
     VERVNQATER WEEDEPLGER ATKAAVLYAN VNYPQWKKEY PEWCERVKHI HRMWRSLDAN
     SRQEYVNKAR ENRANRAKQP RLKRLAPTLL RASVGSPKSG SPTRGGYFAS QVCLVQLFAV
     AF
//
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