ID A0A383YRD2_BALAS Unreviewed; 2618 AA.
AC A0A383YRD2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=KMT2B {ECO:0000313|RefSeq:XP_007165291.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007165291.1};
RN [1] {ECO:0000313|RefSeq:XP_007165291.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007165291.1};
RG RefSeq;
RL Submitted (JAN-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_007165291.1; XM_007165229.1.
DR STRING; 310752.A0A383YRD2; -.
DR KEGG; bacu:103015601; -.
DR CTD; 9757; -.
DR InParanoid; A0A383YRD2; -.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0035097; C:histone methyltransferase complex; IEA:InterPro.
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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05493; Bromo_ALL-1; 1.
DR CDD; cd15694; ePHD_KMT2B; 1.
DR CDD; cd15589; PHD1_KMT2B; 1.
DR CDD; cd15591; PHD2_KMT2B; 1.
DR CDD; cd15593; PHD3_KMT2B; 1.
DR CDD; cd19170; SET_KMT2A_2B; 1.
DR Gene3D; 3.30.160.360; -; 2.
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; IPR041959; KMT2B_ePHD.
DR InterPro; IPR016569; MeTrfase_trithorax.
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 PIRSF; PIRSF010354; Methyltransferase_trithorax; 5.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00508; PostSET; 1.
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 ECO:0000256|PIRSR:PIRSR010354-51};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR010354-50};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR010354-51};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 860..907
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1103..1154
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1151..1205
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1237..1298
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1480..1588
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 2478..2594
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2602..2618
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1696..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1911..2065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2111..2132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2152..2316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..284
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1715..1729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1862..1876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2037..2059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2154..2169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2298..2316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2488
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2490
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2532
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2555..2556
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2558
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2607
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_007165291.1"
SQ SEQUENCE 2618 AA; 284016 MW; CF3E02B2929DEEF1 CRC64;
WGWGPSRDCL LEEESSDGES DDEEFQGFHS DEDVAPSSLR SALRSQRGRA PRGRGRKHKT
TPLPPPRLAD VAPTPPKTPA RKRGEEGTER MVQALTELLR RAQAPPAPRS RACESSTPRR
SRGRPPGRSA GPCRKKQQAV VVAEAAVTIP TPEPPPPVVP VKHRTGSWKC KEGPGPGPGT
PKRGGQSGRG GRGGRGRGRG GLPLVIKFVS KAKKVKMGQL SLGLESGQGQ DQHEESWQDA
PQGRVGSGQG EGPCWRKEQK LEEDGEEEKE EKDKEEEEEK EERAAAEEEM VLAEEKEEAK
LPSPPLTPPA PPPPPSLPPR STSPPSPLCP PPPPVSPPPP PSPPLPPAPE EEAESPPPVV
PATCSRKRGR PPLTPSQRAE REAARAGPEG TSPPTPVPST TTGGPLEDSP TVAPKSTTFL
KNIXXXXXXX XXXSSRVIKT PRRFMDEDPP KPTKVEVSPT LRPPVATSPL APQEPAPAPS
PPRAPTPPPT PAPLPEKRRS ILREPTFRWT SLTRELPPPP PAPPPAPPPL PAPVTPSRRP
LLLRAPQFTP SEAHLKIYES VLTTPPLGAP EAPEPEPPPA DDSPAEPEPR AVGRTNHLSL
PRFAPVVATP VKAEVPPPGA PAPSSGQQPQ AQLQQPVQAL HTQLLPPALP PQQSQLQPQL
QLQPPPPQQP PPLEKARTAG LGSLPLSGVE EKMFSLLKRA KVQLIKIDQQ QQQKVASLMP
SSPGGQMEEV VGAVKQIPDR GSVKSEDESM ETKRERPSGP ESPVQGPRIK HVCRHAAVAL
GQARAMVPED VPRLSALPLR DRQDLATEDT SSASETESVP SRSRRGKVEP AGPGGDSEPA
GSGGTLAHAP RRSLPSHHGK KMRMARCGHC RGCLRVQDCG SCVNCLDKPK FGGPNTKKQC
CVYRKCDKIE ARKMERLAKK GRTIVKTLLP WDSDESPEAS PGPPGPRRGA GAGGPREEVV
APPGPEEQDS LLLQRKSARR CVKQRPSYDI FEDSDDSEPG GPPAPRRRTP RENELPVPEP
EEQSRPRKPT LQPVLQLKAR RRLDKDALAP GPFVSFPNGW TGKQKSPDGV HRVRVDFKED
CDLENVWLMG GLSVLTSVPG GPPMVCLLCA SKGLHELVFC QVCCDPFHPF CLEEAERPLP
QHHDTWCCRR CKFCHVCGRK GRGSKHLLEC ERCRHAYHPA CLGPSYPTRA TRKRRHWICS
ACVRCKSCGA TPGKNWDVEW SGDYSLCPRC TQLYEKGNYC PICTRCYEDN DYESKMMQCA
QCDHWVHAKC EGLSDEDYEI LSGLPDSVLY TCGPCAGATH PRWREALSGA LQGGLRQVLQ
GLLSSKVAGP LLLCTQCGQD GKQLHPGPCD LHAVSQRFEE GHYKSVHSFM EDVVGILMRH
SEEGETPERR AGGQTKGLLL KLLESAFGWF DAHDPKYWRR STRLPNGVLP NAVLPPSLDH
VYAQWRQQEP ETPESGQPPG DPSTAFQGKD SAAFSHLEDP RQCALCLKYG DADSKEAGRL
LYIGQNEWTH VNCAIWSAEV FEENDGSLKN VHAAVARGRQ MRCELCLKPG ATVGCCLSSC
LSNFHFMCAR ASYCIFQDDK KVFCQKHTDL LDGKEMVTPD GFDVLRRVYV DFEGINFKRK
FLTGLEPDAI NVLIGSIRID SLGTLSDLSD CEGRLFPIGY QCSRLYWSTV DARRRCWYRC
RILEYRPWGP REEPVHLEAA EENQTIVHSP APSSEPPDHV DPPPDTGALI PRAPEHHSPV
ESQDTPLRPD PSSAPPPAPR SFSGARIKVP NYSPSRRPLG GVSFGPLPSP GSPSSLTHHI
PTVGDPDFPA PPRRSRRPSP LASRLPPSRR ASPPLRTSPQ LRVPPPTSVV RALTPTSGEL
APPGRAPSPP PPPEDLGPDF EDMEVVSGLS AADLDFAASL LGTEPFQEEI VAAGAVGSSH
GGPGDSSEEE ASPTPRYVHF PVTVVSGPAL APGALPGAPR IEQLDGVDDG TDSEAEAVQQ
PRGQGTPPSG PGAGRAGVIG AAGDRARPPE DLPSEIVDFV LKNLGGPGEG GAGAGEEPLP
PAPPLANGSQ PPQGLPPSPA DPTRTFAWLP GAPGVRVLSL GPAPEPPKPA TSKIILVNKL
GQVFVKMAGE GEPVSPPVKQ PPLPPPIPPT APASWTLPPG PLLGVLPVVG VVRPXXXXPP
PPLTLVLSSG PPSPPRQAIR VKRVSTFSGR SPPAPPPSKT PRLEEDGESS EDPPQGPGLC
GSGFSRVRMK TPTVRGVLDL DDPGEPTWGE SPRPLQDRSP LLPLPEGAPP RAPQGPPDLL
LESQWHHYSG EASSSEEEPP SPEDKENLAP KRAGPHLRFE ISSEDGFSVE AESLEGAWRI
LIEKVQEARG HARLRHLSFS GMSGARLLGI HHDAVIFLAE QLPGAQRCQH YKFRYHQQGE
GQEEPPLNPH GAARAEVYLR KCTFDMFNFL ASQHRVLPEG ATCDEEEDEV QLRSTRRATS
LELPMAMRFR HLKKTSKEAV GVYRSAIHGR GLFCKRNIDA GEMVIEYSGI VIRSVLTDKR
EKFYDGKGIG CYMFRMDDFD VVDATMHGNA ARFINHSCEP NCFSRVIHVE GQKHIVIFAL
RRILRGEELT YDYKFPIEDA SNKLPCNCGA KRCRRFLN
//
