ID A0A1I8AQT1_9BILA Unreviewed; 2328 AA.
AC A0A1I8AQT1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Histone-lysine N-methyltransferase {ECO:0000313|WBParaSite:L893_g8502.t1};
OS Steinernema glaseri.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g8502.t1};
RN [1] {ECO:0000313|WBParaSite:L893_g8502.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR WBParaSite; L893_g8502.t1; L893_g8502.t1; L893_g8502.
DR Proteomes; UP000095287; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd15512; PHD4_KMT2C_like; 1.
DR CDD; cd15513; PHD5_KMT2C_like; 1.
DR CDD; cd15514; PHD6_KMT2C_like; 1.
DR CDD; cd15489; PHD_SF; 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; IPR009071; HMG_box_dom.
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; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 5.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00267}; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 398..451
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 477..532
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 860..926
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1754..1864
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 2190..2306
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2312..2328
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DNA_BIND 860..926
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 175..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2090..2112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1040..1120
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 175..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2328 AA; 258169 MW; 45A7ABBD972B6440 CRC64;
MVFGSDAPAN GAGSVESKAL RGRRVDNVAS KLARAVAAQQ NVGQQPTSSS RSCCQKCGIV
QGPEDRWPAP GFCTACVQKL CGVCKNPITK QQSSIRCLSC HCFIHVHCDS SASLQTQYTC
PPCQRTRIAM AQQQQQQQQL NPQQLAQLVR SVDPTSFATA FPPQQLLQHL MHFNKPSASP
QSSSDFDDSS QNVSRSAMSS PTTITTTASG SASPALANGD SLDGEEFRMT PRRGEGASRG
ARAGKKKPGV GRPAKNRSGG KPASTIAYLA EKGPPGKGPA GKGGKARGRS QKGKGKAPKA
RKYRAEPRAA LRADEGAENE DPKIRTVDEN DYVRTAIVTS ALDTYVKEAP LCLVCGSIGK
DVEGTMLACS SCAQSYHTYC VGMHDKMSTT ILKRGWRCLD CTICEGCGDG KDESKLLLCD
ECDMAFHTYC LDPPLTAIPQ GSWRCKWCTT CTRCQSRVPS AFDLQHNEGF CGPCYSQRKC
PKCKKLYENG DLMIRCQHCS RWLHGRCEDL TTEEMLENAA ENAYRCSLCR PKSQDPSTTM
LIDNVLLTKA ALEEMSQRHG NHFLRSTSSM SLGAVIDPFH RVPQPGFDND GFVDDGALED
RCDSDFVVAR GRGRGGMRGT RMPRLGVGGF IVKQPRHRML ATMSLEEEEA EGELQANGKP
KVKRPRKPRR PPLEECYPPQ VQESFFGMQP VDSRTLEAVD EPMLDIYLKT GLDAQMEKTG
CVLRGEVAEQ LANEDMMIDD AELAGLDMDM DVEDFNLLMD DDDEALNQML GDNDDLADAL
DIAQSDPLFE AARQPQPLID QHHQVTAGMP VSFHNAHVPP HMQQMQRPQP PPQRPPQKAK
PDIEKGNQAT ERWQDDEPLG DKATKAAVLY ANITRPNLRQ EFPEWSERQK QITRMWRALD
QAERIKYVAK ARENRTNNTK KARLMKKATE CPSTSAVPRP VAPVSMAPQL QMAAMRQQQI
KMEHPAQMTL PPKQAFKVPT VPQTPIDHGP ATSFPVPPQM RPMQPQFVPQ SPVPQHPPQM
LLPPQVIEQY ELMRKRTLDL ERQQMSIENE LLRMRKAKKN LTAKRRQLQK SADGAAELNE
ADLQQLGSLA EAIPERQRAL EECRKDLRAH QATVLEFEAK YGIQGVMRPT STAPSPHRQS
PAVKMELLEF SEPPTPSSGR PGSSASFDFQ NQPAKRGRKR KVKTEEPASQ PMPTLGGYSL
EMMRSDEEIG AYFVLLDVVN RATRMVDGSE HEDGIRQILQ QATQGRPPPP QAFPQNQLQM
PMLGEPPKAK KKRAQPLKKP LVEADDYTLF VQRVDTQLQM CLPIAHYLQN PSSTRWKGDQ
YMLRDMGLST LPEKGPQTAV IGNEFGEVRL NFVRDYFDDL EHRRHRDAPG PVAYSNPSTQ
PPPMATICQE VNLANLSHYP GSHQAPAVYF DAAGPADPFS EAGFELLGLR LWSGAGRLSP
VVRARHRFVD RPYAMASIRE PGRQAMLDSE REKEEETLSV GITFANGVDV SKVVGCLREI
LGADVVPDIV PFESPPMSPS ARTNSVVPEQ PAMNGIVEEM RSLICRQCSS AMRDAAIQQS
LNQMGIIPSE SPSDDKENTV SFCSMQCYYT FVADRKIALT PEQVQDAEQY VDKPTLVKLQ
QVAAENFARC LNQGKLRVSD LPMGPRIVCP PSALSSSGVN SPTTSEGPPL LGGVANAREM
TIRVADIPTL LGDVRHTPEA APEPRKVWRG RGWTVCDMQL LESFTKAREQ AKCLCIVDQI
RANERNKIKV EADLRQCVLC GDVGDGELDV CGRLLNFDAD KWVHVNCALW SPEVAEVNGA
LRNVEDAVRR GQTVACRLCG RLGATLMCAK QDCHLLRGGF HLKCAKQARG CFVRDKTFQC
DLHVVREDQQ VFQLRALRRI YVDKDENQLI SKLFHSNAAS NSSTGALLMR VGSLIFTKIG
QLQPDQLKNF HTSTNIFPSG CERRHGSPPA GYTVSRLFWS PDSLDYRVRY DCTIVDSGNQ
PQFQVSFGGK VNRDVSATKA WMPVLMAVKR IRDEHGEVLK MFPTQMSGET LFGLNEPAIS
KLTESLPGAE QLPSYNFKHV DPLNGPLMDL PLALNPSGCA RCEPLTRNFQ KQKKTRWQIT
PQKSRPSQHF ASSTASSSSA CVDLLSSRET RARHASSVGA ILRSCDPGMV RKLRANGLSD
ESIAMAMGGG PSTTSATFSQ YKKMTKEWRN NVYLARSKIQ GLGLYAKRDI EMSTMIIEYI
GEQIRSEVGE IREKRYLAQN RGVYMFRIDE SSLIDATMTG GLARYINHSC DPNCSTKVVT
VCDEKHIIIY ANRPIKADEE LTYDYLFEEE DEKIACLCGA PNCTKFMN
//
