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Database: UniProt
Entry: W5LN62_ASTMX
LinkDB: W5LN62_ASTMX
Original site: W5LN62_ASTMX 
ID   W5LN62_ASTMX            Unreviewed;      1849 AA.
AC   W5LN62;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=SET domain containing 1B, histone lysine methyltransferase {ECO:0000313|Ensembl:ENSAMXP00000021274.2};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000021274.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000021274.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   STRING; 7994.ENSAMXP00000021274; -.
DR   Ensembl; ENSAMXT00000021274.2; ENSAMXP00000021274.2; ENSAMXG00000020648.2.
DR   eggNOG; KOG1080; Eukaryota.
DR   GeneTree; ENSGT00940000154575; -.
DR   HOGENOM; CLU_001226_0_0_1; -.
DR   InParanoid; W5LN62; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000020648; Expressed in camera-type eye and 14 other cell types or tissues.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd19169; SET_SETD1; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR044570; Set1-like.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR037841; SET_SETD1A/B.
DR   PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   PANTHER; PTHR45814:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1B; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          103..191
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          1710..1827
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1833..1849
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          903..1367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1381..1519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1655..1684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..408
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..468
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        938..964
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..980
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..1007
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1025
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1026..1052
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1076
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1188..1202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1210..1228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1246..1267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1268..1291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1404..1418
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1446..1469
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1849 AA;  202748 MW;  ED1204563FBBB1D8 CRC64;
     MSRPGERDRG RVSEEHNRRT SAPMNGMENS SGERRGHHWR SYKLIIDPAL RTGSHKLYRY
     DGQHFSSPNS GIPPVDIVRD PRIGRLWTKY KETDLPVPKF KIDECYVGRI PPKEVTFARL
     NDNIREGFLT DMCKKFGEIE EVEILYNPKN KKHLGIAKVM FGSVRAAKDA VQNLHNTSVM
     GNIIHVELDP KGENRLRYVE RLVNGSYTPL TLPVGEESCE VSPRSLAEAL LACEPLRRLS
     ESSSSVVAGT VTPGSTSTPL SLDTAYSSLR QETPQSQGTP HTPRPTGTPF SQDSTYSSRQ
     GTPALQPNRT EGSGGYKSRR HETKFQNAYK RIPQRHYVHL AGGAYRANAE QSSNFKQHQP
     PEPPSPAFLN TPPLPVTPSF KPASFPTYQP PLPPVYPHAE PPAYPPQPLQ RELEYLRPQA
     PPPSTPDFMT VRDRPKTPPM PEPPPEPTTQ PTACTPPPST PDPCPSPAPE VERNSLDSRI
     EMLLKEKRTK LPFLTDRGDS DGEVRMEGSP ISSSSSQMSP IPPCPAQRPS RPSSTGLEDI
     SPTPLPDSDE DEPIAGTASL MLRPRSTSPP NAHGLNMTGG PRTPTEKPDS GMQSSGEDME
     ISDDEMPGTP ISGGDCAKGI VVNSALSPLA PQALGIPPPG FPPLPHHPQA GYALTHHHLG
     PHTTVPTPHP THLAAHLMPP LPPYPGMVPM MPVDLMSCLP QWGSVHMSFQ MQTQVLSRIA
     QSQHPYPYPH YLSGAAGAGA SAGAMQFGGP YQPLSMVGTP SGGVGHGQQW PLPSMPRYNP
     TVPPPRYDTQ KEDSHKATVD GVLMVIVKEL KAIMKRDLNR KMVEVVAFRA FDEWWEKKER
     SAKATLTPVK PGEGKEEEKE RAKPKETLSA RLLENWSKGE GLGYESIGLG IGLRGAIRLP
     SFKVKRKEPP DPASSAENKR ARPSTPVDDE LDDEERTDLP ADGTRLDADN SAAKRRHSRP
     VELDSEGEEE EEEEEETSGR EELSLSDREE EPEGETSERL STGKEPGDDE EEKDEESESE
     ASSSSDSSDE EGSSSSKSGP DSSSSSSESS SEYDSSSEEE REEEEEEEEA EVAMEVGEEE
     ETRTSSTSSS SSSSSSDEEE ESEVKALSTP PGPPLEKECE SGQQGAEEAV PPNRTAVENL
     RPPSPKGLPV EEQDVDVDIP KVEVSVEDVG TLRPLTPTGS LADSDLDVRP KSQSEEEVPR
     TPGRDGPAPS ELDTNTQMTS SGQSIHLPLP TSHALLPPPP DSCGRVRLQT DEEVPRTPGR
     DLRKGQSTET APETPGSDAP LTGNSLALSL ALSSPHVPGS PFSYPAQSPV LSAGIPRTPG
     RDLTFTPVFP DPAASSVGPL HRKASSDSLE EKPVFKEPAL KEPPLSAYLP TTTAASLTLP
     AAAAAASPQE LSAVPQTSPP ASIEGSTPLP PTDQPIPLTE IPVPLDVTPS KKKAGRAKAK
     KPPTPVTPED ALPEPPPVTP SLPPEPPVKD LFPDRPDQAF GRPDAEPQLP EPEPDTDDLD
     DLGQTVLPPS PGVHDDMLYE PVQKTRRQRR SWEELLLSMH SPAASPPRPS YVPRSEFEEM
     TILYDIWNDG IDEEDIKYLK ITYDKLLQQD NVNDWLNDTL WVHHPTTSGG SLPGLKKKRR
     EDGMRDHVTG CARSEGYYKI DKKDKLKYLI SSRPQFDEPD KDTQGKSIPA QPHASTRAGS
     ERRSEQRRLL SSFSCDSDLL KFNQLKFRKK KIRFCKSHIH DWGLFAMEPI AADEMVIEYV
     GQNIRQVIAD MREKRYEEEG IGSSYMFRVD HDTIIDATKC GNFARFINHS CNPNCYAKVI
     TVESQKKIVI YSRQPINVNE EITYDYKFPI EDEKIPCLCG AENCRGTLN
//
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