ID A0A1S3M334_SALSA Unreviewed; 2980 AA.
AC A0A1S3M334;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=[histone H3]-lysine(4) N-methyltransferase {ECO:0000256|ARBA:ARBA00023620};
DE EC=2.1.1.364 {ECO:0000256|ARBA:ARBA00023620};
GN Name=LOC106570121 {ECO:0000313|RefSeq:XP_013997628.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013997628.1};
RN [1] {ECO:0000313|RefSeq:XP_013997628.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013997628.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000256|ARBA:ARBA00024515};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC Evidence={ECO:0000256|ARBA:ARBA00024515};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_013997628.1; XM_014142153.1.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000087266; Chromosome ssa14.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15664; ePHD_KMT2A_like; 1.
DR CDD; cd19170; SET_KMT2A_2B; 1.
DR Gene3D; 3.30.160.360; -; 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); 3.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR047219; KMT2A_2B_SET.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR002857; Znf_CXXC.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45838:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE 2B; 1.
DR PANTHER; PTHR45838; HISTONE-LYSINE-N-METHYLTRANSFERASE 2 KMT2 FAMILY MEMBER; 1.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR Pfam; PF13771; zf-HC5HC2H; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 795..853
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1054..1105
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1102..1155
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1187..1248
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1463..1570
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 2840..2956
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2964..2980
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 155..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2041..2137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2157..2216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2387..2411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2542..2564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2595..2630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2055..2071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2072..2088
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2613..2630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2980 AA; 328857 MW; F3F05268D12900C6 CRC64;
MQHQLALRCE VKGGRSLSSP LLLYRLSTGI YYKKSTFRNK SFSQLGVTLA PVACCTAAWI
PPGDLFTVCP GLSAQDEDFS GFWMEYQPTL SARNISKSSL FQSSLLKPPL APELTAKLKK
SGGKVSEEEV GEGQEENAVK PKIVAKLAAQ KKSISSGFKS TGKQATGTKA SKSKGSAKSD
GSDWKRGRKA VESSSTARKR NRQEQTTKVG RGGSGSSTAR PQSSRNKQGK LVWTLTVVKG
KGKTSKVKEA GEVTADNSET DKVKPQRSGK RRKGSQQGDK VEAQSRNGQK TTNPNTASQG
VALSPKPVNT QQRKRVSRGT EDSPEVGAEL GQEPAIPLER KKTPPYKRKS IFGFRRKPSN
VHKLSPPVSV VKRFRRKVVF DTYVPESLPT PVKQAGQEAQ WERTGTEGKP LLSPGEIQQR
GSSNISLPVV SARSSRVIKA PKRFLHDEII SLPRGSPKKK CQYKVEEDAM SLSFYDSDND
DIDNLSRTPG QNEFKPEVDG STGKKTLKTS LSSSPGSSHL EVYERLKKLT LSLAQKKKKG
LSAADGETTE EAQEYLSLTS PVRKRGRFKL KMEDLNSPGV VRKLAVLVSN AAAAASQAAS
SETLEEAAND TENVQGVEAA ADGDYEGESQ ADDGVVVEQG GTSHRSNLTS TNKRMFHLLK
RAKVQLIKID QLKRARLQLV KIDQEKPMKS SQLLSGSVKL GPRDLGGGRR RRRGSAQDQL
PGGPRIKHVC RAAAVALGQP RAVVPDDIPR LSALPLNERE GITTSPAVEG IADDPSDCTV
RHKMTRQKHK YSKQRKFKRN YNEVGPGGRA TRCGTCQGCL HEGDCSTCFN CLDKPKFGGP
NTRRQCCVLK RCVRIEARKV KRGIKPFTVL SRRRRQTSAN GLQSNNNVSA SWGEAEEMTA
PATLGDCLRP STRKQPRRNV TPRSYSSLLK SDSDTDGEGV VNSPVKNPDA PSSKDAAPSG
LLAPEDGPVP SEFVRHRRPG PPKGLLGRCR ADKNAVENMS TNILTALTNR LSQKGHLKTG
THRIRVDFKE DCAIQNVWLM GGLSILTSVP VTPQPVCLLC ASKGHHEMIY CQVCCEPFHS
FCLWPEERPQ EKNKENWCCR RCKFCHVCGR KSKNNKPVLQ CKRCQNCYHP SCLGPTYPKP
INCKMPWVCM TCIRCKSCGV TPGKTWDMAW NHEQDLCPDC STLHSKGNFC TICSKCYEEK
DHNSQMMECS RCSHWVHSKC EGLSDDLYEI MFSLPESVVY SCTRCSQSQP RFWKEELKER
LRAGLENVLT NLLSDSSAQH LITCRECEES TELNAFRDQQ QPICDLHAVG QKCTGGQYTS
LKSFHEDVVM VMRKWLKEEE SLPEDLRPTC LARSHYLKLL EETFSWFHSQ DQKMWDPISK
DFPSGMLPEA VLPPSKEHSY AQWLERTYQV TRGSGCLQQG NSIPSLYSVT THQSRALLSL
PLKSQDTHCA LTGALELDWT KDERQCALCQ QCGDATPNDA GRMLFLGQNE WAHVNCCLWS
AEVYEDNGAL LQVHSAVSRG RHMRCERCGQ AGATVGCCLS SCQSNYHFMC ARARNCVFQE
DRKVFCSRHR DLVSEKMVSG NGFEVLRRVY VDFEGISLRR KFLTGLEPES INMTIGSLQI
NRLGVLTEQS ANGARLYPVG YQCSRLYWST VDPRRRCKYT CNVTEVYSPL PEKPGEPHWW
EQEENRTIAH SFNKEMENPE ASLPIQVSPS TTSSPLKQEP GAKTPSYSQT RRPAGGTSRP
LPSPGSAMTK SLHILTLRDL DDTCQPRRLS RGRLSGDSSS PTDGLVGPMT LRSGGTLHPR
SLPFSSPSRT SENLQNSPQS VQTRAGSSSW RSSLLSPSSV TSPLSLRPGA IGSPPSNLPL
ALRHSSRIRQ SFKITTPVST EVPQDFLASS EPEEAVVVPS NEITLTANNM EEDTDIGPLM
SDQDLPFAPF DVADADVAVA SVLNAKLEFD EALLNETVAL HCGGSQTGGG DMEEALEAEP
LEEETQSQTR GGDNMDANMA PVFTKAMGPK EVLENGSSDE DMDHYLKLSR TLVVCKVSKD
SGQASLPLPP PAPTSQSISQ LDGADNGSES DSSDSTCDEE ETQEEGKSEE DQGADSQAVF
ETCDPNNDMS IEEEVLMESE QMESQKEVLL DPSSGHFVSD DDRIREYLAN NKKVVLDDSD
SSGSSTDSLI GVDDEMGDPD FEPEPKPNPK SIPVKTIMEP PRPVSMKTIP RKPTPTQRKI
IRVSLPSGPA LPLNVAFSSP PITVRTIPRT ATSTASPTPF VMNDMNSIPL QTGATTGRAI
TIRLATPRQA AQQQLTASIQ SASNSALFPQ VLLVNRQGQI LMKDPNTNTF QTVCTSSPSY
SRISQIAKII HSSGALPCAI PQMVVVPASS TLSPRTAIFH SSNLITSNRN NNTTSPTTIS
NRNNTTPAPT TNLLIRTPQS LHDGRVLVRA MPMTHGAKQV RVKCVSVPSS PMMTGNQAQA
ILDRAMATHR EPSRIRPNIL RVSTSQLSPS HFQVHPFLNK IQSPLATSDT PGQMLRHKPA
TVPESQVRVK RVSFVAERPS KKKCKTDFLP QSPSSDLDDL DGSRNCGVRT KAPTMKDVLD
LDQKKVEPKV ILPTEPEKIR PPPIPQMARQ PNRTLRPPGS STTQSSSDIH GKTHVWVSAR
HGDLSDWGPY SGFSSDEDTS PPKQNKTRFA HRNQPHLRFE ITSDDGFHVQ ADSIEVAWRA
VIDGVLEARA GFHLKALPLG GVIGARVMGL LHDAVIFLLE QLQGAASCKQ HRFRFHHSDT
PDDELPINPS GCARAEVYSR KSTFDMFNFL ASQHRQLPDI MSTPCDEEDD DVLLKSTRRA
TSTELPMAMR FRHLEKTSKE AVGVYRSEIH GRGLFCKRNI EAGEMVIEYA GNVIRAVLTD
KREKYYDSKG IGCYMFRIDD FDVVDATMHG NAARFINHSC EPNCYSRVIL VDSHKHIVIF
ALRKIYRSEE LTYDYKFPIE DDSSKLHCNC AARRCRRFLN
//
