ID A0A3Q1ELD1_9TELE Unreviewed; 2973 AA.
AC A0A3Q1ELD1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Histone-lysine N-methyltransferase ASH1L-like {ECO:0000313|Ensembl:ENSAPOP00000004167.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000004167.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000004167.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR STRING; 80966.ENSAPOP00000023729; -.
DR Ensembl; ENSAPOT00000010507.1; ENSAPOP00000004167.1; ENSAPOG00000005745.1.
DR Ensembl; ENSAPOT00000010539.1; ENSAPOP00000023729.1; ENSAPOG00000005745.1.
DR GeneTree; ENSGT00940000156698; -.
DR OrthoDB; 2882778at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProt.
DR CDD; cd04717; BAH_polybromo; 1.
DR CDD; cd05525; Bromo_ASH1; 1.
DR CDD; cd15548; PHD_ASH1L; 1.
DR CDD; cd19174; SET_ASH1L; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR043320; Bromo_ASH1L.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR043319; PHD_ASH1L.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46147; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR PANTHER; PTHR46147:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF20826; PHD_5; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00384; AT_hook; 6.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
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 2043..2094
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 2097..2213
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2221..2237
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 2404..2474
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 2611..2748
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1759..1878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2260..2286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2503..2529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2775..2914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1031
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1847..1864
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2507..2529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2788..2820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2821..2835
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2836..2851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2852..2877
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2973 AA; 328666 MW; 7DC4963F1EC10512 CRC64;
MDQKIQGRTA TPPPLLAGAP TGEREKEGGG GKKDEEDEKK RDREKEGAAA VTAGAGGAGG
PGGAGGDQSH FSIKESSLSE GNVKLKIGLQ AKRMKKPPKI LENYVCRPAF RATVRHTSRG
GGGARGNRAA AAGDGQGAQN QSPSQAREKE REKSPSVNKP PATSSSSASS AKAPTPPPPA
PPPAASTTTI TPSQVNGSTP AKRGPPKMDC KSDSKSDTKA ASTTSERPLN LHRPPSDSKS
HSSGKKTPTP QPNPRTSSPS PPLPASKESS FEGVKPPQYT YSTESQRDKD KGVQSWGAPT
VTEKLAQLIA TCPPSKNPKP AKPAKIDPTP SLQSSGFMAP TAKQRDRAMA NRNTYSRMVH
LSPPPPVSRP PGRPYGSRNK DSVLENLPSL TPLRKEDLDG AGKASSSSGN NSISLSGSNS
SSRSNSPAFT YGNNRLSAMS KDSNNDNSNS SISKPQSRPA HCLPHTTSSP SCPISSSSST
SAEQRTVSAV SHLGSPVPSQ GHHARESPAL AEESSAGEQE QNRDSPRDLT KCPPSTGTGK
SEGKDKGASN QSLRVERAKS SSPSKRSPNR DCSRPGRTSS PSESVRQRAP SPLEPDDDES
PHTPLRDDSP DSSLDSPTEQ DSKPLKKRRG RKPRWTRVMN KTQSQRAGQD SPFNENKTTM
PLSSSLETPS PPGKRPVGRP PNPNKVKPNP VPQRPVSQLF TSQTKKRGRP KSKMPRLDAP
APGNPPNKLA PSKVFSSLLK SKEEQDPPVL HPEVDLNPPK PMPRKRGRPK RLPPTLPQEG
QPPTLAPEAG DMGDKRFRSK GNGQLIMKTI IGKINKMKSV KRKRILSQIL LGPRPEEAPK
GTTSGVAGSV EAATQSLSSL AASFGGKLGP QINVSKKGTI YMGKRRGRKP KATCNVTATS
SPEPFLSPNT TSPLHHHQSQ SQQQHQLSSS EVFPSPSLSQ SSGGHSPISD ASFVEPGSVH
FASHSHYSNA HHSHNTFSFP PPTFSAPNPR NTGLGSTSSS SAAAASQKKS SYRGYHHHHH
YRQHYHYHKL SPPRPLHPTS PAPLSELKEA TPSPVSESHS EETVPSDSGI GTDNNSTSDR
GEKAGGAGGL GAIGMPPGMG SGLLMPGVIG SAMGPGMGLN SRGRRRHSAV LMEHPSPSPS
PHGTRSSPDP RRPHPTAPAS SLIGHKEKHK HKCKRRSHGC PGYDKLKRQK RKRKKKYLQL
RSRRLDPDFL AELDEIVVRL SEIRIAHRTT GHRLSSGIGI AAGSSRVPGV GSRASGGIGG
TGGPPPHHYV HRDLLPTIFR VNFGSFYSHP AYSCDPLHYV RKPDMKKKRG RPPKLRESMS
EVPFVPGLGF PLSSGGFYHP SYSVPYSSGP LGLGYYRGYP PASALYPHPH HQSPHTAPSH
HSHHSPSFPP PPPTSYMHHH HPSHLLLNPS KFHKKKHKLL RQEYLGGGRS PVLYPPMSSE
LSFNWHHKHK HRHKHRERCG EEDREEAARG GSANRTSAGI SDSGASGKGE RVGGLGMAES
LQRCRFGRDA SSTSSSKQAA ATSANSPSSS SSSSAERYKR KEGSMSCLGP SRLALGSSSK
GHHPVESWFR MGSSEADYSK LSRSQVAAGQ GSFSDGRAED PAGCSDSEDE EPLSPTEDVE
AHESPNLTNL FASALTRTSL KGGRNRKTDV VTESSSFSHV DRPLRKDRSM SAERRELASS
GIQSRGVALP TNEGPEGSLH HRQQHHHQPS LFHSHASVSS SCLSSSQDCC LDASLPHHSH
RAQPSKHSLH HVNKILRAKK LQRQARTGNN VVKKRGPGRP RKHPLPSPPP SPPPVVELNQ
TRHRDRGGER LAGGRGWEGD TVTDAIESVV QGQRRKGQKR KQWERDGDEE EEEDEVEEER
EVEEPEQQLP EREENLGNLV ARSRAATGRS WLSQDELQHF HGSVESKPDG HCSPERPGTV
SREQAPPMPI TSQREKRAAR PPKKKFQKAG LYSDVYKTED PRSQLQQLKK EKLEYIPGEH
EYGLFPAPIH VGKYLRQKLI DFQLPYDILW LWKHDQLYKR PDVPLYKKIR SNVYVDVKPL
SGYETTTCNC RPPEGSTEKG CLDDCLNRMS FAECSPSTCP CGDQCDNQHI QRHEWVQCLE
RFRAEGKGWG IRTKESLRSG QFIIEYLGEV VSEQEFRSRM MEQYFSHSGH YCLNLDSGMV
IDSYRMGNEA RFINHSCEPN CEMQKWSVNG VYRIGLFALK EISSGTELTY DYNFHSFNTE
EQQVCKCGSE SCRGIIGGKS QRINGLPGKT GGTRRLGRLK EKRKSKHQLK KREEESSDSN
KFYPHLMKPM SNRERNFVLK HRVFLLRNWE KMREKQELLK REGERERDAS SLSIYTRWGG
VIRDDGNIKS DVFLTQFSAL QTSRSVRTRR LAAAEENTEV TRTARLAHIF KEICDMITSY
KDSAGQTLAA PLVNLPSRKR NSQYYEKVSD PLDLSTIEKQ ILTGHYKTVE AFDTDMLKVF
RNAEKYYGRK SSVGRDVCRL RKAYYSARHE AAVQIDEIVG ETASEADSSD SLERDHGHHH
HGGGGPGSHD KDDDVIRCIC GMYKDEGLMI QCEKCMVWQH FDCMRLETEV EHYLCEQCDP
RPIDREVPMI PQPSYAQAGS IYYICLLRDD LLLHQGDCVY LMRDSRRTPE GQPVRQSYRL
LSHINRDKLD IFRIEKLWKN EKGERFAFGH HYFRPHETHH SPSRRFYQNE LFRMPLYEII
PLEAVVGTCC VLDLYTYCKG RPKGVKEQDV YICDYRLDKS AHLFYKIHRN RYPVCTKPYA
FNHFPKRLTP KRDFSPHYVP DNYKRNGGRS AWKSERPKEA GGCEDDGSSC DRGEDFPPEA
EDGRGVEDDM DMAPEDPELL PAKPRRAEQD REGDEDEDEE EEEEEEEEEE EGQEAEERKE
LEDVTTERIG EMLELPSSSA SSPLHHPALG RREAQRERLN KILLDLLHRT PSKNGEGPGT
KQGAIDVTYL LEEGAGRRLR RRTLGFGDFV GRK
//
