ID A0A3B4V431_SERDU Unreviewed; 2962 AA.
AC A0A3B4V431;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Histone-lysine N-methyltransferase ASH1L-like {ECO:0000313|Ensembl:ENSSDUP00000025533.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000025533.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000025533.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR STRING; 41447.ENSSDUP00000025533; -.
DR Ensembl; ENSSDUT00000026001.1; ENSSDUP00000025533.1; ENSSDUG00000018480.1.
DR GeneTree; ENSGT00940000156698; -.
DR OMA; DKDNGHE; -.
DR Proteomes; UP000261420; 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:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1L; 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; SM00297; BROMO; 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 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 2048..2099
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 2102..2218
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2226..2242
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 2409..2479
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 2615..2752
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1765..1949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2265..2291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2508..2534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2779..2908
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 171..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..335
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1159
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1204
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1788..1803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1873
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1885..1904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2512..2534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2792..2824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2825..2839
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2840..2854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2855..2875
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2962 AA; 327818 MW; 176F085C20499B79 CRC64;
MDQKIQGGTA TPPPLLSGAP TGEREKEGGG GKKEDEEEKK RDREKEGAVT VSAGTGGASA
GGPGGASGDQ SHFSIKESSL SEGNVKLKIG LQAKRMKKPP KILENYVCRP AFRATVRHTG
RGGGSARGNR AGATGDGPGG QSQSPSHGRE KEREKSPSVN RPAPSSSSTP SAKAPTPPPP
APPPASTTGL SPSQVNGSAP AKRGPPKLDC KSDTKPDMKA ATTTSERPLN LHRPPPDSKT
HPSVKKTQTP QLNPRTSSPS PPLSASKEPS FEGVKPPQYT YSTESQRDKD KGVQNWGAPT
VTEKLAQLIA TCPPSKTPKP AKPTKIDPAP PLPSSGFMAP TAKQRDRALA NRNTYSRMVH
LSPPPPVSRP PGRPYGSRNK DSVMENSPSL APLRKEDMDG TGKASSSGNN ISNSMSMSSS
NSSSRSSSPA LTYGNNRLSA MSKDSNNDNN NSSISKPQSR SAHCQPHTTS LPSCPISSSS
TTSVEQRTVS AVSHLGSPAP SQGHHARESP ALAEESSASE REQDRDSPRD LTKCPPTTGT
GKPEGKDKGI NNQSLRVERG KSSSPSKRSP NRDSSRPGRT ISPPEPVRQR ASSPPEPDGD
ESPQTPLRDD SPDSSIDSPA EQDCKPFKKR RGRKPRWTRI MNKTQSQRTG QDSPFDQSKT
TMPLSSSLET PLPPVKRPVG RPPNPNKVKP NPVPQSSVSQ LFPPQPKKRG RPKSKMPRLD
ALAHGHPPNK LAPSKVFSSL LKSKEEQDPP VLHPEVDLNP PKPMPRKRGR PKRLPPTLPQ
EGQPPTLAPE AGDMGDKRFR SKGNGQLIMK TIIGKINKMK SVKRKRILSQ ILLGPRPEET
PKGTTSGVVG SVEAATQSLS SLAASFGGKL GPQINVSKKG TIYMGKRRGR KPKAVANATA
TTPPPEPFLS PNTTSPLHHH QSQSQQQHQL SGPEVFPSPS LSQSSGGHSP ISDASFVEPG
SVHFAGHAHY SNSHHSHSTF SFPPPTFSAP NPRNPGLGST SSSMATAASQ KKSSCRGYHR
HHPHYRQHYH YHKLSPPRPL HPTSPAPLSE LKEATPSPVS ESHSEETVPS DSGIGTDNNS
TSDRGEKAGG AGGLGAIGMP PGMGGGLLMP GVISSAMGPG VGLNSRGRRR HSTLLMEHPS
PSPSPHGARS SPDPRRPHPA APASSLMGHK EKHKHKCKRR SHGCPGYDKL KRQKRKRKKK
YLQLRSRRHD PDFLAELDEI VVRLSEIRIA HRTTGHRLGS GIGIAAGTSR VPGVGNRASG
GIGGTGGPPP HHYVHRDLLP TIFRVNFGSF YSHPAYSCDP LHYVRKPDMK KKRGRPPKLR
ESMSEVPFVP GLGFPLSSGG FYHPSYSVPY SSGPLGLGYY RGYPTASALY PHPHHQSPHT
APAHHSHHSP SFPPPPPTSY MHHHHPSHLL LNPSKFHKKK HKLLRQEFLG GGRSPVLYPP
MSSELSFNWH HKHKHRHKHR ERCAEEDREE AARSGSGSRA NAGISDSGAS GKGERVGSLG
MAESLQRCRF GRDTSSASAS KQAAATSANS PSSSSSSSAE RYKRKDSSMS CLGPSRLALG
SSSKGHHPVE SWFRMGSSEA DYSKLLRSHV APGQGPFSDG RAEDPAGCSD SEDEEPLTPT
EDVEPGAHDS PNLTNLFASA LTRTTLKGGR SRKTEVVPES SSFSRMDRPM RKDRSTSSER
RELGSSSIQT RVVALPTPEG PEGSLHHRQQ HHHQPSLFHS HGSASSSCLS PSQDCCLDAS
LPHHSHRAQP SKHSLHHVNK ILRAKKLQRQ ARTGNNVVKK RGPGRPRKHP LPSPPPSPPP
PVVELNQARH RDRGGERPAG VRGWEGDTVT DAIESVVQGQ RRKGQKRKHW EREGDEEEEE
EEEDGEVEET EERLPDREEN LGNLVARSRT GTGRSWLTQE ELQHFRGSME SKPDGHCSPE
RPGTVSREQA PPMPITSQRE KRAARPPKKK FQKAGLYSDV YKTEDPRSQL LQLKKEKLEY
IPGEHEYGLF PAPIHVGKYL RQKRIDFQLP YDILWLWKHD QLYKRPDVPL YKKIRSNVYV
DVKPLSGYET TTCNCRSPEG STEKGCLDDC LNRMSFAECS PSTCPCGDHC DNQHIQRHEW
VQCLERFRAE GKGWGIRTKE TLRSGQFIIE YLGEVVSEQE FRSRMMEQYF SHSGHYCLNL
DSGMVIDSYR MGNEARFINH SCEPNCEMQK WSVNGVYRIG LFALKDITSG TELTYDYNFH
SFNTEEQQVC KCGSESCRGI IGGKSQRING LPGKTGGTRR LGRLKEKRKS KHQLKKREEE
SSDSNKFYPH LMKPMSNRER NFVLKHRVFL LRNWEKMREK QELLKREGER ERDASSLSIY
TRWGGVIRDD GNIKSDVFLT QFSALQTSRS VRTRRLAAAE ENTEVTRTAR LAHIFKEICD
MITSYKDSAG QTLAAPLVNL PSRKRNSQYY EKVSDPLDLS TIEKQILTGH YKTVEAFDTD
MLKVFRNAEK YYGRKSSVGR DVCRLRKAYY SARHEAAVQI DEIVGETASE ADSSDSLERD
HGHHHHGGGP GSHDKDDDVI RCICGMYKDE GLMIQCEKCM VWQHFDCMRL ETEVEHYLCE
QCEPRPIDRE VPMIPQPSYA QAGSVYYICL LRDDLLLHQG DCVYLMRDSR RTPEGQPVRQ
SYRLLSHINR DKLDIFRIEK LWKNEKGERF AFGHHYFRPH ETHHSPSRRF YQNELFRMPL
YEIIPLEAVV GTCCVLDLYT YCKGRPKGVK EQDVYICDYR LDKSAHLFYK IHRNRYPVCT
KPYAFNHFPK RLTPKRDFSP HYVPDNYKRN GGRSAWKSER PKGAGGCEDD GSSCDRGDDF
PPEAEDGRGV EDDMDMAPED PELLSAKPRR TEQEGEGDED EEEEEEEEEG QEAEERKDLE
EGSTERIGEM LELPSSSASS PLHHPALGRR EAQRDRLNKI LLDLLHRTPS KNAIDVTYLL
EEGAGRRLRR RTLGFGDFVG RK
//
