ID A0A3Q3FBF2_9LABR Unreviewed; 1062 AA.
AC A0A3Q3FBF2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Histone-lysine N-methyltransferase EHMT2-like {ECO:0000313|Ensembl:ENSLBEP00000016909.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000016909.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000016909.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q3FBF2; -.
DR Ensembl; ENSLBET00000017859.1; ENSLBEP00000016909.1; ENSLBEG00000013047.1.
DR GeneTree; ENSGT00940000159459; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0002039; F:p53 binding; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20905; EHMT_ZBD; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR043550; EHMT1/EHMT2.
DR InterPro; IPR047762; EHMT_CRR.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR46307; G9A, ISOFORM B; 1.
DR PANTHER; PTHR46307:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF21533; EHMT1-2_CRR; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00468; PreSET; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS50867; PRE_SET; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT REPEAT 676..708
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 709..741
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 742..766
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 776..808
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 809..841
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 842..874
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 964..1027
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT REGION 1..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 113783 MW; 2DECF8A5C113DCDD CRC64;
MSASETTTKE PPEGNDSETP ANSEAGPSHV KGDNAAITTA AVAKQTEPMG AMASTLLPQQ
PGKDASRAGE EGDKMSPASS PKKHAAGLAA KSFPSASASS SSSSSPSTSS ALSPGRAKMS
VSGPGSSKSI PGPALSSSSS SSATASSSPS VSPGPPKIHR ARKTMNRPPL GQMNNFELPV
APSGPSVSLS SDSETAAKRR KTDPLSDITH ETSENIPDNA QTVEETFVHK KPSTKSAAEK
SDIDVGSKSE EEEKIQTPNP SKRASGKVSE FDDGEKEGNK EIEDSVNTSD HSSESETHKA
DLSRNESEES SQEKEKNTAD VAEPVAAERS SDYTEVPLGA LDIAAADSLT LSPHHEGSDA
GDTERLEELP LCSCRMEAPR VECSSQRVSR QCMATESVNG ELRACISRTI KGETMRPSSR
VPLMVLCEVH RSHMVKHHCC PGCGYFCIAG TFLECCPDQR IAHRFHRGCV TVLSGGRSRG
NGGGGMIFCP HCGEDASEAQ EVTIPSFSSA TASATTVVTM SASSTTTPSL PPSVPTAPSL
TASTGGMKDG KMPERPVSAR MRSHGLVKPA VEQQPPQPVA SATPATAVPP VEEGVDSVGP
SLCMPNGKPI SPSALPPGPS RASLQKAILT QDTERKKKLR FHPRQLYPAA KQGEVQRVLL
MLMEGIDPTY QPDSQNRRSA LHAAAQRGLL EVCYILIQAG AQVDAQDKDL KTPLLEAIIN
NHIEVAHYLV QNGACVYHVE EDGYTGLHHA AKLGNKEIVN MLLETGQVDV NAQDSGGWTP
IIWAAEHKHV DVIRSLLNRG ADVTINDKEQ NVCLHWAAYA GNVDIAELVL NAGCSLTSVN
VHGDTPLHIA AREGYLECVT LFLSRGADID IINREGDTPL TLARADTPVW VALQINRKLR
RGITNRMLRT ERIICSDIAQ GYENVPIPSV NAVDDEGCPS DYKYVSENCE TSAMNIDRNI
THLQHCSCTD DCSSSNCLCG QLSIRCWYDK DQRLLQEFNK IEPPLIFECN MACSCYRTCK
NRVVQAGIKV RLQHYRTRRW AGEFELCRIF PREASSANMS GS
//
