GenomeNet

Database: UniProt
Entry: A0A0V0TZ05_9BILA
LinkDB: A0A0V0TZ05_9BILA
Original site: A0A0V0TZ05_9BILA 
ID   A0A0V0TZ05_9BILA        Unreviewed;      3528 AA.
AC   A0A0V0TZ05;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Histone-lysine N-methyltransferase 2C {ECO:0000313|EMBL:KRX44236.1};
GN   Name=Kmt2c {ECO:0000313|EMBL:KRX44236.1};
GN   ORFNames=T05_934 {ECO:0000313|EMBL:KRX44236.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX44236.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX44236.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX44236.1};
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:KRX44236.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JYDJ01000101; KRX44236.1; -; Genomic_DNA.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0046983; F:protein dimerization activity; IEA:InterPro.
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; 4.10.280.10; Helix-loop-helix DNA-binding domain; 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; IPR011598; bHLH_dom.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
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; PF00010; HLH; 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; SM00353; HLH; 1.
DR   SMART; SM00249; PHD; 4.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50888; BHLH; 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   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:KRX44236.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRX44236.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   TRANSMEM        3036..3055
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3113..3137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          163..216
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          213..263
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          290..345
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          2167..2275
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          2542..2658
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          2666..2682
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          2869..2919
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          86..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          884..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1143..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1190..1220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1259..1281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1326..1377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1403..1432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1556..1599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1687..1706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2909..2936
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        90..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1200..1220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1561..1584
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3528 AA;  396009 MW;  9831E3FD9A719363 CRC64;
     MQFNILQKKT SFLNAHATMK HWGYAFKEAY LRFKFKITHL IVVYYLSDEV DLSYSHTSVE
     PISLPPQNMI TGHALPENVS RKKISTFKRN SASKGKGGST SSRSIVDKRR SQKCAKNRRN
     AVQTITEILN HHLAPNVAKH KEDDEYIHSV VVTSVKDSYV FCRDMCVVCG SFGRGQEGHM
     VACTQCGQCY HTYCANVTLN SVIVHRGWRC LDCTVCEGCG TGDDEQHLLL CDECDVSYHM
     YCLDPPLDSI PQGAWRCKWC STCQFCGATP PNGMLDSIKN LRACFKCASL YSCCFCHLQY
     KEEDMIILCD ICHRWSHANC NGLCAEDILK KGLDAGFICV YCRPGDACSS AAMHFVIEGV
     LLTKSGLSTV QWRPKPAASP VCSAVYNSTR SFESLQNATA DGFSELSTSQ IMIQDGVVSA
     SPDMEKLDFE FSSNSDMTIY ESQNGLDSFG SVDRQKRVRN RKLFKVGIGG FHTRLARSRY
     DKLQEECVAT ASPEMMGNSL GGNAQLDNNA VAAGDSIVEE GHDKPKRRKR NRRKVVLEDY
     YPSYIQEAFF GISAEESSYT NGGNVNGPAP FPMSPFDLQE QDIAFAIPRS PDTEINSEVI
     KNAESSSQVY KLRNANVLPE VCLNEAIDMN ENEEIFPHEL QNHDFTNLLD MLMQADMDPI
     VSNTDISAID SVEMDTLMDN VFDAELKRAS ELTETQLLAN SAAAAAEMHQ PNGRCLKDLT
     AMCGDNAPTP FVSLPVEIGT AASQQMAPKN FNEQQTDLIG NMAGNIFPNS NNSSNSNNVN
     SDNMIGGGMV ESTAVRPRMC ESPPVEAKNY LDRWLQDEPL GDRSSIAAVL YANLNAPDLK
     TRYPCWPDRA KCIAKIWRSL NQDHRQQYVQ MARENRSLMR QECKARRQQQ QQQQQQQQPC
     LLASSPAVRR SSSSGGQLMK LIESSSPPSM VNCAATSDTA SNPMSGATPA PMPLNISVAD
     ETSHRADIPM KPHFPVIRDF FPFQQRLHNQ HHPNQQHFPT HLIHHNHQPQ EDQQRQLKNF
     TMNFSQREFF QNHDGTAGTV AHHQHQQQRK FSLPEDGLAF AVQKNDVIKQ PVDHQYGMMV
     NSGESFRLGK AEPLDALGRR ASCPSSAEAL VGMAACCNNS LSSALAPAPV LSPSQAQILT
     REMRSPPVSW SQANRIDHHH QQQQQQPQQP QQQGQFGCAA QAKLLPRTPV VGDGHELMTG
     MRNQQGQNHS NKQQQDNKLA QVAQSVETTM HEEWLMQTVG SLEHQQKSLE SELNQLRRTK
     KNTASKQRQM RKNGVEPPQA DQAALASLTQ TIGERQKLLE RIRKQLKTHN SLVQDYQQQD
     KRVDGALSIA GGGSGQSSSY PAPAQSPVPS PAYQPAVSPM DCGFAAEPGH TAPPRSEQAF
     MAPTAGRQRH FNFVQPMLVD HHQHLPQQQQ QQQQQQQPPH YPQQQQRHYE QQHPNLHPQS
     ALTAANFGVL AMNGASGLVA GQTVAPEPSP SAVGAEMMKP TMMNITAPPY YQRMVPVRVP
     LDSTVAVAPG LAPPPPLPDP PLPPEFAAAY VNEGIIHYSM PGRRFAPHPL GDVAVGAAAP
     PPSLPVQPPP AQAAPPPPPP YHHHHQQQQP EVKKRKRIRR KKSEIKEQIL TCCKAYDGIP
     DDETVLSRTK CLNLCSMSRC YGSEVVATVK DLLDRVSDDE YGEATEAVLH MFSKIYPTDQ
     CYDFDGSRRK GKGQLSRKRS RRSNKAKSFC GNEDAVDEMG ELTDHQWFYY LQQLPPLTIV
     EPESRFDTAI THFYGVTPLT DCKGLVEGTL GKVTLSFAED YYRRSCGGDG ARNNSLVRMA
     ESTTRGQIEK SFSNVKVEND FLFENRSSNS PDELIYSDGS GDEENLPCYP YLKPEMSADG
     RLSPNFRLVA PVPVRAVPGD PPAGALNKTI NEYVQSQQSR VVTLTLDSAA ASNVSNVLRN
     LACLLNVDVP ELFDLQIDTP PHTPDRVLSR EYAETQRRFC CYCATALQQA MVKKNLAELG
     FTPKNDDSDE VVFCSDACFV QFAVSRKMPI SPGNPSKVLP NKTVITSGFE NALERSNSSS
     MSICTANQLR IAESENSRHR LVNNVKLDEI IRSVVGTSKV YTGTSKESVV HVRDLPRLKD
     TVEVESENQD ASHYESKIEK KLKGARWQLY NNCQKSLLKV LACNTPEALW KEMLSIFWLP
     QSLPQDTRIC ELCSRMGDGE TEVCGRLLNM DAGRWVHVNC VLWSAEVYET MDGGLVNVEQ
     AVRRASVTRC VLCDLPGATI PCYKMKCGSN FHLHCAVDSR CTFMMDKTMF CFEHPPLCRD
     KILYNLAVFR KVYIERDDEQ LLSKLYQQSE SGEYAMRIGS LLFHHVGQLL PEQLNRFHTK
     DCIFPVDYTV SRIYWSTFHP RRRQIYQCHI GEFEGAPLFS VTAKYPGTPE VRYQSKSINE
     VWQNNILTPL QGLRNCNDIL KLFPSYISGE SFFGLFEPSI QKMLESLPGI DSLVTYEFKY
     GRSLWMEPPL VLNPSGSARC EPCFRTYIKR SRKLNAMSAH SIQSLLAFSG MPSDGYFYSF
     GNKQSLVAKC YQYRKLKQEW KSNVYLARSK IQGLGLFANR DVEMNAMVIE YVGEVIRNEV
     AERREKSYQK RNRGVYMFRL DSDHVIDATV AGGPARYINH SCDPNCIAER IDFDRESRIV
     IMSCRPICKG EELTYDYQFD FEDELNKLPC LCRAPNCRNK EAVYMKMQTG CASCVRFTTF
     AEGTILALRM VSSQSFGYYT GGQHVENFAP NNACMASSPN EEFYFAVPDE QQQFVSSGPQ
     ATTYWDNSCN LNVVNPVEFQ WTTDHYYPLT NWNSAPTAAA AYTHGVGNVV DEGAVPARTF
     IFNGQSCWNL MAEDSAIAVV KNNQIEEADE EELASADTGT VSKNRNPCRR RCAHSVIERR
     YRSSINERIA ELKTLVIGPS ARASKSTVLR AAIDKLKQLK QLNDSLRAEN EQLKACCTCS
     PFSLSMHSLD FGQNNFDISV SSTEELNNNS NNSSVSTNSK FTLFLLFACV VIVNPFHMVS
     QISTVGVAPL GKLWNAPLLK SVDISRIRAE IIENNILRIL LLSVINGLVV ALVIVKLRFC
     RRLILKDPTC PKVKSRSLTV LGDDRGREDS PPPVPAPMVM RCSQFKRTFA EQLLQILLTF
     FHFILLPVNL FCLLSNVDDE EQKSADMGKF HYSNPTTLLQ HFTDDKPHLS RFADKKRYSS
     IELALNSVKL AAKVDNKLEK PILVNVYCMA ALQIRLLPWI GNSLAKLLYN RANQEYRKVE
     SDLNVCWLFT SIGKKFFFNL NLNDKQFWLL KRALLLNSKE TEEYLNFVKH SRDEFKKKRL
     FGVTMSNQET DYFWYVSFIL FGFGQDHRAS LMDERNLLKD IQELATSAVQ EACCKAAIAC
     HLGTSSENKE NIVCEILQLC MDVHQSMMSS SVADYPLENI TLVLAVDWCL KALIVSSEMN
     VHLLVNKNCT NADVNGKHMF RLLLKQKRRF ISNLQPFLSR ETIRYEAIGC LLDGMNPTFV
     QKLLMKYAKV DQFDRPWTCT NNSGGIEKWL FSLGPQQWLT SLLLSEEN
//
DBGET integrated database retrieval system