ID A0A0V0YNK2_TRIPS Unreviewed; 2399 AA.
AC A0A0V0YNK2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Histone-lysine N-methyltransferase 2C {ECO:0000313|EMBL:KRY01874.1};
GN Name=Kmt2c {ECO:0000313|EMBL:KRY01874.1};
GN ORFNames=T4E_10159 {ECO:0000313|EMBL:KRY01874.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRY01874.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRY01874.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRY01874.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRY01874.1}.
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DR EMBL; JYDU01000001; KRY01874.1; -; Genomic_DNA.
DR Proteomes; UP000054815; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15512; PHD4_KMT2C_like; 1.
DR CDD; cd15513; PHD5_KMT2C_like; 1.
DR CDD; cd19171; SET_KMT2C_2D; 1.
DR Gene3D; 3.30.160.360; -; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_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; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KRY01874.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRY01874.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 123..176
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 173..223
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 250..305
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1884..1992
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 2259..2375
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2383..2399
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 45..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2399 AA; 270765 MW; C8ADFDFA6F95E6B0 CRC64;
MKICLGSEMM DLSYSHTSVE PVSLPPQNMI TGHALAENVS RKKISNFKRN SASKGKGGSS
SSRSMVDKRR SQKCAKNRRN AVQTITEILN HHLAPNVAKH KEDDEYIHSV VVTSVKDSYV
FCRDMCVVCG SFGRGQEGHM VACTQCGQCY HTYCANVTLN SVIVHRGWRC LDCTVCEGCG
TGDDEQHLLL CDECDVSYHM YCLDPPLDSI PQGAWRCKWC STCQFCGATP PNGMLDSIKN
LRACFKCASL YSCCFCHLQY KEEDMIILCD ICHRWSHASC NGFCAEDILK KGLDAGFICV
YCRPGDACSS GGDTFYNSKS AMHFVIEGVL LTKSGLSTVQ WRPKPAASPV CSAVYNSTPS
FESLPNATTD GFSELSTSQL MIQDGVVSAS PDLERLDFEF SSNNDVMIYE SQNGLDSFGS
MDRQKRVRNR KLFKVGIGGF HTRLARSRYD KLQEECVATA SPEMMGNSLG GNQLDNNAVA
SADSIVEDGH DKPKRRKRNR RKVVLEDYYP SYIQEAFFGI SAEENSYTNG CGAGSSSSEA
NGPAPFPLSP FDLQEQDIAF AIPRSPDTEI NSEVIKNAEN SPQVYNKLRN ANVLPEVCLN
EAIDMNDNEE IFPHELQNHD FTNLLDMLMQ ADMDPIVSNT DISAIDSVEM DTLMDNVFDA
ELKRTSELTE TQLLANSAEM HQANGRCLKD STALCGDNAP TPFVPLPVEI GTTTASQMVP
KSFNEQTDLV GNMAGNIFPN SSSSNNNNNN GNNDNINMIG GAMVESTAVR PRMCESPPVE
AKNYLDRWLQ DEPLGDRSSI AAVLYANLNA PDLKTRYPCW PDRAKCIAKI WRSLNQDHRQ
QYVQMARENR SLMRQECKAR RQQQQQQQQQ QQQQQQQPCM LASSPTVRRS SASGGGHLMK
LIESRSPPSV VNCAATSGSS SNPMPGATPS PMPLNVNVAD DASHHADIPM KPPFPVIRDF
FPFQQRLFHH HHYHQHFLHH NHHSQEDQQR QLKNFMMNFS QREFFQNHDG TAAIAQHQHP
QQRKFSLPED GLAFAMQKND VIKQPGDHQY GMMVNTGESF RLGKAEPLDA LARRASCPTS
AEALVGLAAC CNNSMSSSPL APAPVLSPSQ TQISARDIRS PPVSWSQVNR VDHYHHHHQQ
QQQQQHRHHQ LVTSTRNQQG PNYNNNNSKP QQQQHEKNKL VAQSAESMHE EWLMQTVGSL
EHQQKSLETE LNQLRRTKKN TASKQRQMRK NGVEPPQADQ AALASLTQTI GERQKLLERI
RKQLKTHNSL VQRCQQQRHY HQQHQNPHPQ NDKNVCRYFL FFFGNLEMKK RKRIRRKKSE
IISKEQIFTR KAYDGLPDDE TILSRTKCLN LCSMSRCYGS EVVATVKDLL DRVSDDDYGE
ATEAVLHMFS KIYPTDQCYD FDGPRKKGKG QLSRKRSRRS NKTKSFCGNE DSLDEMGELT
DHQWFYYLQQ LPPLTIVEPE SRFDTAITHF YGVTPLTDCK GLVEGTLGKV TLSFAEDYYR
RSCGGDGARN NSLVRMAESS TKGQTEKSFS NVKVENDLLF ENRSSNSPDE LIYSDGSADE
ENLPCYPYLK PELSADGRLS PNFRLVAPVP VRAVPGDPPA GALSKTINEF VQSQQSRVVT
LTLDSAAASN VSNVLRNLAC LLNVDVPELF DLQIDTPPHT PDRVLSREYA ETQRRFCCYC
ATALQQAMVK KNLAELGFTP KNDDSDEVVF CSDACFVQFA VSRKMPISPG NSTKVLPNKT
VITSGFENAL ERSSSSMPIC TANQQLRIAE SENNRHRLVS NIKLDEIIRS VVGTSKVYTG
TSKESVVHVR DLPRLKDTVE VESENQDGAH YESKIEKKLK GARWQLYNNC QKSLLKVLAC
NTPEALWKEM LSIFWLPQSL PQDTRICELC SRMGDGETEV CGRLLNMDAG RWVHVNCVLW
SAEVYETMDG GLVNVEQAVR RASVTRCVLC DLPGATIPCY KMKCGSNFHL HCAVDSRCTF
MMDKTMFCFE HPPLCRDKIL YNLAVFRKVY IERDDEQLLS KLYQQSESGE YAMRIGSLLF
HHVGQLLPEQ LNQFHTKDCI FPVDYTVSRI YWSTFHPRRR QIYQCHIGEF EGAPLFSVTA
KYPGTAEVRY QSKSINELWQ NNILAPLQGL RNCNDILKLF PSYISGESFF GLFEPSIQKM
LESLPGIDSL VTYEFKYGRS LWMEPPLVLN PSGSARCEPC FRTYIKRSRK LNAMSAHSIQ
SLLAFSGMPS DGYFYSFGNK QSLVAKCYQY RKLKQEWKSN VYLARSKIQG LGLFANRDVE
MNAMVIEYVG EVIRNEVAER REKSYQKRNR GVYMFRLDSD HVIDATVAGG PARYINHSCD
PNCIAERIDF DRESRIVIMS CRPICKGEEL TYDYQFDFED ELNKLPCLCR APNCRKWMN
//
