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Database: UniProt/TrEMBL
Entry: V4AHI0_LOTGI
LinkDB: V4AHI0_LOTGI
Original site: V4AHI0_LOTGI 
ID   V4AHI0_LOTGI            Unreviewed;       740 AA.
AC   V4AHI0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Histone-lysine N-methyltransferase ASH1L {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LOTGIDRAFT_143999 {ECO:0000313|EMBL:ESO96362.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO96362.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESO96362.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KB201470; ESO96362.1; -; Genomic_DNA.
DR   RefSeq; XP_009052947.1; XM_009054699.1.
DR   AlphaFoldDB; V4AHI0; -.
DR   STRING; 225164.V4AHI0; -.
DR   EnsemblMetazoa; LotgiT143999; LotgiP143999; LotgiG143999.
DR   GeneID; 20234774; -.
DR   KEGG; lgi:LOTGIDRAFT_143999; -.
DR   CTD; 20234774; -.
DR   HOGENOM; CLU_352882_0_0_1; -.
DR   OMA; TCEQEEH; -.
DR   OrthoDB; 2882778at2759; -.
DR   Proteomes; UP000030746; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin 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; 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; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
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; PF01426; BAH; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF20826; PHD_5; 1.
DR   Pfam; PF00856; SET; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
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; 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:UP000030746};
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          1..119
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          127..143
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          309..379
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          517..654
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          149..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..724
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  86208 MW;  86206BC7DE37F84A CRC64;
     MYNTIIIHSC ISQIVSTKFY VVIISGDFIL EYLGEVVSEQ EFRRRMTEDY SKDCHHYCLS
     LDSGMVIDGY RMANIGRFVN HSCEPNCEMQ KWTVNGLYRM VLFALRDIDP MEELTYDYNF
     DSFNMETQQV CKCGSENCRG VIGGKTQKNN QIKEKLSSTR PVGRPPKDKR KSKYKLKKFK
     DKVKPTSANN KLLNHSVIKP MSNRERTYCI KHGVFLIRNV ERTKHKQLKQ DGVEVKETCN
     ISTTVNNTDN NNITTVIKPG YQLTQREDRS VKTRLVSRVE DNPELQKRCQ LIKLFNKVYD
     TVANYKDEDD NILATPLMNL PNKKKCPDYY KIIDEPVDLT TIRNQIQTGE YETLDSLDKD
     VLQLFRNVER YCGRKSDMGR LVLKLRKVYC SAKNEVIPLI DDILSDGQIV SNTPPIAPPE
     IDTESIENRA IRDPPDEEEE IIRCLCNVFR DEGLMIQCEK CFIWQHCDCV GATGNEEYYV
     CEKCDGRTYD KEIKLVPQPT DGDSENDYYM TLLRDDLQVA IGECVYILRD YKRNSDGTPD
     IRPLSDYTNI TPDKLDIFRI ERLWKNKAGE RFADGHPFVR PHETFHEPTR KFFPNELFRL
     PTLEIVPVEV MVGTCCVMDL YTYCKGRPKL VKEKDIYICE YRVDKTAHLF YKVVKNWYPI
     NTKSYCFNTF KEKLNAKRTY SPHQVPEEYL RRTDKQSSTS KSSTDNSSKN TDKNKTEDKN
     SKKSNKTTKI KKRLSVSFSL
//
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