ID A0A183W274_TRIRE Unreviewed; 1700 AA.
AC A0A183W274;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Histone-lysine N-methyltransferase {ECO:0000313|WBParaSite:TRE_0000683501-mRNA-1};
GN ORFNames=TRE_LOCUS6830 {ECO:0000313|EMBL:VDQ02710.1};
OS Trichobilharzia regenti (Nasal bird schistosome).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Trichobilharzia.
OX NCBI_TaxID=157069 {ECO:0000313|WBParaSite:TRE_0000683501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TRE_0000683501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDQ02710.1, ECO:0000313|Proteomes:UP000280995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; UZAO01057456; VDQ02710.1; -; Genomic_DNA.
DR STRING; 157069.A0A183W274; -.
DR WBParaSite; TRE_0000683501-mRNA-1; TRE_0000683501-mRNA-1; TRE_0000683501.
DR Proteomes; UP000280995; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043933; P:protein-containing complex organization; IEA:UniProt.
DR CDD; cd19171; SET_KMT2C_2D; 1.
DR Gene3D; 3.30.160.360; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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; PF00856; SET; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
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.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000280995};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1173..1281
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 1560..1676
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1684..1700
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 71..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1700 AA; 188908 MW; 9803CA389EF61D95 CRC64;
MVRPNAVGFG YISHDDLSHA SHDDQVLRLV DAFHCPYNNN LRECESPQVS MVSAMCNRVV
SPDTFSDFVD KSSEFGQPES LSETEKSTVP DKDDIVSVSK YPDLNEKSYP FSDIACIPSP
CNGSLSRPGS NSDLSSHVEK SEAVKDVNGC CRPTDTPPLH DQERAKMDLD KLDETIDYVL
SFARSDEPCE GMFVLSCRAP PSPHSNNLNS PILQTCKAQT ALQSNNSCNI VSQQSMQRYI
VDQTHGIIQL SSNSPQCVSA HYSNQGVSFV QLCPDSSTNP VLQVTQHHIV SQIGQTLTTT
AAHVLFHPNV LHSFQNHTGQ PAQFTLPHST LSTAPIQRIR TPILSPVKAN IVQTKNQINK
TSLSSDANAT PYSMPNHVPE GGNPSFPNPV SINPSNICVV QTPMQSTQSL LGGALNTSVP
MGAMDDAKCS LAVSASGDKK CVQANTSVTF RHPIIPANSS ISLIPVSSVG VTSNHTLTTT
SNINTTFCQS TTGISRKRSH SSVPGSNKRR KTVGSPPFPV NSINKNPTTQ EACSTNSGAQ
EHIDKLKGVD PKLLVSAPTL QPFSSVLPPS GMCDSASTVA TEDVFLQMRG LKYLRGPMSL
KLPKCIDSTT SSKVVDSYLT QHLKLILPHS LNVYHPKIRN LPSVECNSVR ASPEPPSFEN
NMKALFSRMN QFSKQHSKDI YNEKVSYECN KLSGESLTPQ SLLHMFSHNP SNSLERTEAD
RCTPPLALYH MPNPRLLCQP IHLAPCVERS FQSVCSSISD SNVSDVKLEN NLSGISNVSN
SVTKEVSLSG DLHARSQFVD LETGETMIMP HSKPTEKLFD STLTENDKLH ITFTVNPSTV
NISKIIHRIS ELLNVEESSI DFQITRSGAQ ITLDQNQSQS EVVMRSLETH LRQQFTPLSL
HFEKDSSKDE LCQEVRSSHL MQCNVLESSP SLRHPSSNIP QSNLCKMECD TSGKTDCSLS
STQEACRYTE ETVSVNSLVA SRHRSVKSCK GCGKAVSPNV QRKWLDDLST ITGITMSLEN
SVDFVFCSND CLYSFARVLA SHHNRCLDTV PDHSAQSDLL NSNGYNFDQQ RQLIMTDFPC
SMPILLQSSL SKSKSSNLKR QHSQQSVSNK RRSANASGPQ SKLRKWQGIR WRSYSSENSH
SFDLSSRCVS ENDITSTMKA NLAVMRASHS DDKRVCVLCQ QAGDAPEDGP GRLLPLDVNN
WIHINCALWC YEVYETVGGS LNNLDVWLAK AKETNCSHCG LTGAGLPCYN PKCSCVYHVP
CAIKIRCMFF TDRGMYCPQH QTKEFHPMQL SSLVVSRRVY INRDENSQVA RVVHEDNDKH
IVRIGGVSLH SVGQLLPHQI DSGNFHNLRN IYPTGMCATR IYWSMRRPRA RAKYVCEILE
KDCHPFFRIT AVDKGMEDVS VTHETCDGAW QIILSRIESL FKEHKLVRVF PQLLKGEDLF
GLNESHIVRA IESLPGVDGL RDYVFNFGRL ELISEMPLAI NPSGCARSEP KMQTYLKRLH
DSGEFSSPSS HRTGILPGVR RLPHSGFCGL SYNNMDNTIS KQYQSNRFQQ YRKLKSEAKS
NVTLGRSRIQ GLGLFAARDL ESQTMVIEYI GELIRLEVAN RREKQYEARN KGIYMFRLDE
DTVIDATVCG GLARYINHSC QPNCYAEHLN FGDHSHIVII TNRRVKKGEE LSYDYNFDLE
DRSDKIPCLC RAPNCRKWMN
//
