ID A0A1S3HXS6_LINUN Unreviewed; 2669 AA.
AC A0A1S3HXS6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Histone-lysine N-methyltransferase ASH1L isoform X6 {ECO:0000313|RefSeq:XP_013389874.1};
GN Name=LOC106158443 {ECO:0000313|RefSeq:XP_013389874.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013389874.1};
RN [1] {ECO:0000313|RefSeq:XP_013389874.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013389874.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_013389874.1; XM_013534420.1.
DR EnsemblMetazoa; XM_013534420.1; XP_013389874.1; LOC106158443.
DR GeneID; 106158443; -.
DR OrthoDB; 2882778at2759; -.
DR Proteomes; UP000085678; Unplaced.
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; 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 PRINTS; PR00929; ATHOOK.
DR SMART; SM00384; AT_hook; 8.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 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; 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|PROSITE-ProRule:PRU00035};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
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 1827..1876
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1879..1995
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2003..2019
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 2178..2253
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 2396..2534
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 42..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2024..2072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2279..2315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2561..2614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1807
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2043..2061
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2561..2603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2669 AA; 304047 MW; B4908A9C16CC6784 CRC64;
MCARHCAFLC GKKCIDTITG VNSLIPGNKE VHSQKCFLEY RHKKEKERSR DRKKSKMRSK
SLPSPRTSDT YNSASEARHP QIHRSLSMLQ DHDVPDLTES LTKTLVNGSA GREESGSLQE
INEEDLAAIL PDVNNTANGG DHCQVPFPVD LAESGSEEEV DDDALREQIV NELARAVENG
SLPISEVEYT SYGSETCYQP DSRHGGEKHE KTSETRDNSV EETQKTVLAV SHSENKAKTR
DDESDKDISC KASQDSLVHN SRHFTDALVP NLNEEQHSQQ QSHVQQKPEE PVKRKRGRPP
KAKPIPEPPR VAEVAVPRYE PPEPIHLRID TEYNVSPDSG IQSIAGSPEG QESPSPTAAA
EPVSAQTDQH RARASDEPPP GGGDSEHLPK QQESVTVENT LERNVEDSFV KNETKGNCDI
STGHINTENS TSVGHGLISS TNKPPFEQPK VKRPKGRPPS KHKLLQRTVT AETLSSITSD
SAECTKISNR KTKNKRIGAR KVKNISDSSI QNLSEIPLKR RPGRPKGSGK KKKTLSLVHT
LSGYQKPFKQ NSQTVPGKRK PGRPRKHPLP QTVGDQESIS KGTLDELPVL ERAPCLEHSL
SSRRRLRKSL HDDDELPVLV KAPGMECQKR RRKSEDFDTL IKSVNASIST QFKDVASSED
EGENVNSRLD SVDLDPVKVT SQLKDSRNPK PKIKKPKLHV MMRKHKKRGR KKKAQILSKQ
RQQESDEVVD FFKDLPSTST DVFFQEGENV SERDDVRPRR RDTMTSMSSD ISDNVSHILQ
SSKLNFLSCS QHKPPSDGKK RKKKKLIYFK SKHKNIVDPV FLADLDDITE DLENLALSAK
YPLTVSCLPG QTLLPSIFQI NKNMCRRKNT NLPLEIKEKK AKLKIAKERK MLMSLEQMHA
LQKLKKKLPE HHITSSSPPP LLDHKQNCLP LKKRHKVLSM LPSTSVPNSL SPQFPVASLP
PQGVPVKRRV GRPRKYPRPE DLQLQLVQQW HQVQVQNNTQ QHTRPSVTSV QSTSTPSSSH
KVQKKRGRPR KSPQEKLETV RRRKLAEMKK KLQMGKSLDN VPLALLAKAK NFQLNYRKKE
KTRTVTASKA SVRDEIASVS ADRNIAIVPK RRGRPPKKKP LGNKSQNLNI PRQPHNFQHS
PNRQISKPYD CVTTGISTES QDFEGTLPRA RSQSLNIDMI GKGRQRNCSS SRTRKSSLSS
PVRESDSLKP LTLIGEKRKG RKNRESSLSP NCDSAWKRPV RTRSVSMSSS SERRRINSGS
SDAVASCDGH RSPSMSRSGE PLQGNRSRSV SGSRKTICNQ QEIPKYTSDT RLSRWDLPWK
RQQSPDTGSR SGESSTTSPL RKDDHVDHDD FPDGKGEPTS PRAKMRKLSK DEGSLSPKGM
SSSETKLIKT RSISGSRLSS AHVPVWHKYT SGVSSPPRQG HHRTQETITL EGEGPNSSPS
KNLEKIKNKA SAMSVIESYH RDQNDQVAIH SPSLSVSKTE SNHKHQKNRT HSPQNHSKMT
LMEFQSEFEQ FIKTPAHGIT SMYKEGNSLS QKIFHEEGGS LDLNNISKSL SYDNTGDNRL
ISQEPVVILE HLQGNNYRKQ PREHKPGNYR TPQSDSDSDN EVLTILREKV KSNKKSKDLE
QAKAIKNRQS DIKPLPTSMK RKSTQDGRLE HKKFKKSKVA DPISSPREGC SDPQRVLKPP
KKKYQKAGLF SNYYKTDEPR KPQEIKKDKL YYNPSEHEHG LMPPPIHIGK HLRQKKQEFK
LSYDLWWLYK HKMVKTQAGP AEKLVHSGPA SKSSVLSPSL STHHKLSRCN TTDSKKHKKK
LRKGTSSPKY KKIRHNVYVD AKPMCDYEPH PCNCERPADR RGCGEECLNR MVYTECAPGS
CPCADFCQNQ RIQRREWLDC LEKYQTGDRG YGVRTKAHIK TGSFILEYVG EVVSEHEFRR
RMMETYSHDF HHYCLNLDSG TVIDGYRMGN IGRFVNHSCQ PNCEMQKWNV NGVYRIGLFA
LKDIPADTEL TYDYNFHAFN MDSQQICKCG STKCRGIMGG KTQRLNGQIR DKTNTSRPVG
RPPKDKRKSK SKLKKYKDKK HDNNHKNTPI KPMSHRERTF AQKHRIFLLR NIEKVKQLRH
RQNHQDVTSR QKQNYITHTP FSKTDVFMTQ FTALNTARSV KTRRLTLAEE NSEVTRAARL
AQVFKDICTA VTSCKDEDGN ILATPLMSLP SKKNLWFCRY PEYYEMIEDR IDLSTIQNNI
FTGRYETVDA FDADFLKLFR NVEKYCGRKS EMGRLVLRLR KVYCAAKADA QTLFEEILGE
NIPHTTSETE STDMGEGGSE KSPEEEEKEE DAPEEEEEEI IRCICNIYRD EGLMIQCEKC
MIWQHCDCVG IDGNVENYLC ERCDPRVINP EVYQIPQPHD GLQGCKYYMT LMRDDLQIRV
GDCVYITREN PQRRSDGLPV RMSYRLLSNT NPDDMEIFRI ERLWISEKGE KFAYGHYYCR
PHETFHEPTR KFFQNEVFRL PLYDIIPLEC IVGQCWVLDL NVYCKGRPFG CREQDVYICE
YRLDKTAHLF YKISRTKFPV NTKSYCFKTF EKKLQPKRTF SPHDVPDVYK RRSPAEHHSS
DLNTRMRQET DELNGKPDLD PCNTEDESDS ESVPLAKVKQ DEINKKKTRL NAYLIKLLGS
IPGKQKIDIT YLLDEGCGKR ARKKSLHAF
//
