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Database: UniProt
Entry: A0A1V9XJS4_9ACAR
LinkDB: A0A1V9XJS4_9ACAR
Original site: A0A1V9XJS4_9ACAR 
ID   A0A1V9XJS4_9ACAR        Unreviewed;      1055 AA.
AC   A0A1V9XJS4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Histone-lysine N-methyltransferase trr-like {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=BIW11_01079 {ECO:0000313|EMBL:OQR73767.1};
OS   Tropilaelaps mercedesae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC   Tropilaelaps.
OX   NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR73767.1, ECO:0000313|Proteomes:UP000192247};
RN   [1] {ECO:0000313|EMBL:OQR73767.1, ECO:0000313|Proteomes:UP000192247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR73767.1};
RX   PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA   Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT   "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT   is shaped by the parasitic life history.";
RL   Gigascience 6:1-17(2017).
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:OQR73767.1}.
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DR   EMBL; MNPL01009352; OQR73767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9XJS4; -.
DR   STRING; 418985.A0A1V9XJS4; -.
DR   InParanoid; A0A1V9XJS4; -.
DR   OrthoDB; 5490909at2759; -.
DR   Proteomes; UP000192247; 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   CDD; cd19171; SET_KMT2C_2D; 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; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR001965; Znf_PHD.
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; PF00856; SET; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00249; PHD; 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; 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:UP000192247};
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          606..714
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          915..1031
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1039..1055
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OQR73767.1"
SQ   SEQUENCE   1055 AA;  114486 MW;  DA813DF8C02898F4 CRC64;
     AVSCLPVSHT SFDSQPLHSQ TAGSLHNPQS LPHTTIGPGS MYVKSELVSS AAGSGHFSPG
     PMGPPLHPNN QPLSTTASQQ LQRPPISPMG GTGPGGPQRV SPFGPSATQM ASGKPPQANS
     NNQDTSGSVG GILTSQQQSQ THQQQTSNPR KRPHKQQSGG LASAVGGVHG GAGGVGASTS
     PTKKRAKKSG AGTPSGIRGE EGPGLPLTVE STSMGEPVSC SLTGSDLGTP ASAKMWSLPA
     VRIVEPSIHA NYSACPIFGR DRGTPIQPQL AGSFGSGELK KVSKYGGDFY KHLGSNMRSS
     RARRNRLALN GRGFYNQEFS HRFSSNSDRA LSPETVCYCS SPEGDVREKL LEMKGLRLIS
     QETPAGSGQL KGSSDHNSNL MPSTLKTNDK ERAPSPALPL YAPVPLRPSF NGHQLVTILD
     HKSSHVNAAT NGLLLVTLTM NSSHDIKTVL SSLSKILELE AKEPYADADG QLLYEVIERI
     ETPPSERKQY GDEYLWPDGK KKFCKHCEVV VHRRRGLTKL LDILAELVKR VSEQTPSKPV
     QPRKPFLAQR SDPNRKSAKG TKWMIWEAGT RQKLLSKKNT TVGVEEANTR LDASPIGIRL
     AGVTDARACL LCLAVGDGAS EGPGRLLNLD TDQWVHLNCA LWSSEVYETV NGSLMNVEEA
     CRRARRVRCA RCGLTGASVR CFKMRCMQTF HFGCARTHAC MFFKDKTMLC PAHQPKLPQA
     DLLLPSASVL RRVYISRDEV KQVLEPIEKM RLEDKAIKVF SKYVTGHDLF GLTEPLLLRL
     IESIPGIDTL LDYTFRYGPS IDLPLAVNPT GCARSEPKLR THFKRSHALL HSSNAVGAAG
     GWAGAGNVSG ASSALSASAG TPASLAMPHH SLLLCSDSPG GQGLSPSPEM GSPYSKQFVH
     SKASQYRRMK TEWRSNVYLA RSKIQGLGLY AARDIEKHTM VIEYIGQVIR NEVANAREKQ
     YESQNRGIYM FRLDENRVID ATLTGGLARY VNHSCNPNCV TEVVDVDKDQ KILIIAKRRI
     ARGEELSYDY KFDFEDDQHK IACLCGAPNC KKWMN
//
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