ID I3J7V8_ORENI Unreviewed; 1721 AA.
AC I3J7V8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=PR/SET domain 2 {ECO:0000313|Ensembl:ENSONIP00000004948.2};
GN Name=prdm2 {ECO:0000313|Ensembl:ENSONIP00000004948.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000004948.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000004948.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR RefSeq; XP_005453521.1; XM_005453464.3.
DR STRING; 8128.ENSONIP00000004948; -.
DR Ensembl; ENSONIT00000004951.2; ENSONIP00000004948.2; ENSONIG00000003925.2.
DR GeneID; 100697429; -.
DR KEGG; onl:100697429; -.
DR CTD; 797296; -.
DR GeneTree; ENSGT00940000159410; -.
DR InParanoid; I3J7V8; -.
DR OMA; TSPTSHY; -.
DR OrthoDB; 5399106at2759; -.
DR Proteomes; UP000005207; Linkage group LG5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd19188; PR-SET_PRDM2; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR044414; PRDM2_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR16515:SF37; PR DOMAIN ZINC FINGER PROTEIN 2; 1.
DR Pfam; PF21549; PRDM2_PR; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR Pfam; PF13912; zf-C2H2_6; 3.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 6..137
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 336..363
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 368..395
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 466..489
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1148..1175
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1205..1233
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1489..1516
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 180..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..942
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1721 AA; 187045 MW; C6197B2D20EF6672 CRC64;
MAITGGTVES LNEIPAHVWK GLPDYLNLGP SAVNQSRIGV WATRVIPKGK KFGPFVGEKK
KRSQVTSNVY MWEVYFPTRG WMCIDATDPM KGNWLRYVNW ARSSEEQNLF PLEINRAIYY
KVLRPIGPGE ELLVWYTVED NPEITAALEE ERASSLSRKN SARARRARRK LLEKARQAGL
GGFKKTSGTK PTVKEMWDGE GGVKGTEKDG TPLSVQEIKT AHSLGSTDHK DVQDMSTALT
DRGDLEEAEE DEEDDEVEEE GEEEEEEDGD DVEDSEAALH LTVTDSMLNK LACPEESHGD
AQVKSESSSL AGREPEVDPD LDPDGDLEGD PQGEPYPCQH CERHFATRQG LERHIHIHAM
SNQQAQLFKC RYCNKSFGSQ VGRRRHERRH ESGSKKRPGY LAGPASPVVQ TDSSPDCTSP
TTHYIATGSQ FTGGQLHNSD MQRKELGPQV DRPFMLDENG ESKELHPCKY CNKAFGTHTN
MRRHQRRIHE RHLLPKGVRR KAMLQQEAAR QPDGSPSMSP PTVYVPSADT EDEADRDDYA
VDISKNISEN LSFYIDGKIV STSAVSTCEV IEVDSRSAAL FGLDTVILNP TQISQALKVE
TRTTNTKQTS NTGQPAAKRR TSTPPLIPNL KVETETSASS SSSSSTSSSS NLLVGGLYQQ
ATDSSAFQRE KNVYLSPKLK QLLQAQDIQK STVTLITDSH KLASQLSVMP LQGSSGKFKR
RTASPPSSSP QLSPASKKES GKVEVASSYA LKVPKLESQT ASPSESLMDK DDRETLSPSG
NATQNQPSSS SGGNSCNQQP LDLSSSVSKK SENLNKMLGD SALDLSFHRK TTAEPESKGN
ATPQPLTKKR KPNTSMLAKV LMNEYAGLNL PGDEGPSTLA NLSSFPSHSP NVASDSANPS
PPSLTPMTMT PSSPGTSSVT SPTPPPPVLP TIPSPPAMPS SPLSQPSDSS LLRPLPVLSP
KMSPRSVEEK SHLEEESFLA EENKDEEEKH ISELLDSPDI SLKGPSNGSS TPSPPEPESV
DMPTTEDDVS QTETSNSLPN GNQNHDTVSE TEKPDFAAIS SQPESSSSSK SPSESRDSSS
SQASQSPHPI TIKEEPEHCI DELLGTSHAS PCGVDSSPQP AAALPAAPEP TDKTAEPEEI
DMTYCKTFVC NVCEEPFGSI KELSGHIVEH AADWPFKCEF CVQLFGDAPA LLAHRTTLHG
VGQIFVCSIC SKEFAFLCNL QQHQKDLHPN EACSHTTVES GKLRPQNYTD PSRAKEESSP
STPAPEMADE NAPPSDSHLL KEEPDVNGNH AEEGAEDPNE ELYTTIKIMA SEGGKPKGPD
VRLGINQHYP SYKPPPFPYH SRSHAGSVAS ATNFTTHNIP QTFSTAIRCT KCGNSFDNMP
ELHQHILVCA SASDKKRYTP KKNPIPLKQI VKSPNGVASA TAATAGQSAF RRMGQPKRLN
FNQDPGKTKM SALSKKKNQL VQKAISQKNK TATNAKKAAI KVEEEHTSNV CPHCSRVFTY
TASLTKHMAV SCPMKPVVVK KGKRGLAEVK KEPGSVADKN TSLRKKASDG EAHAETESKP
LGKTRARSSG GADPERLQAR KGKTPAAVGR PKRPASFPAP VPASKRTKKG QIQYLPPTPT
AVDTPSEASQ RPAMRMQRMG KEAAPKRLTE AKSSSSSPPS TMQQQQQQVK KEERFSLRTR
ERVGGPVTRS LQMASTAPAA EVKTDEPPVQ EPKDTQEVAT K
//