ID H9GNH0_ANOCA Unreviewed; 2826 AA.
AC H9GNH0;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 71.
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|Ensembl:ENSACAP00000016400.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000016400.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000016400.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000016400.3};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000016400.3}
RP IDENTIFICATION.
RG Ensembl;
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_008115314.1; XM_008117107.1.
DR STRING; 28377.ENSACAP00000016400; -.
DR Ensembl; ENSACAT00000016725.4; ENSACAP00000016400.3; ENSACAG00000016679.4.
DR GeneID; 100556600; -.
DR KEGG; acs:100556600; -.
DR CTD; 9757; -.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00940000161496; -.
DR HOGENOM; CLU_000208_1_0_1; -.
DR InParanoid; H9GNH0; -.
DR TreeFam; TF319820; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000016679; Expressed in embryonic post-anal tail and 13 other cell types or tissues.
DR GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042800; F:histone H3K4 methyltransferase activity; IBA:GO_Central.
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:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd15694; ePHD_KMT2B; 1.
DR CDD; cd15589; PHD1_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; IPR017956; AT_hook_DNA-bd_motif.
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; 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; SM00384; AT_hook; 2.
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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
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 1000..1048
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1233..1284
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1281..1335
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1367..1428
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1612..1720
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 2686..2802
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2810..2826
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 83..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..2020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2046..2152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2169..2205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2256..2276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..328
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1847..1861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1945..1977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1988..2005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2006..2020
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2181..2205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2256..2270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2826 AA; 311103 MW; 95C4594EF5C824A7 CRC64;
MQRGLLLGLG CHGNISGKTW RVARAGRRGR EPRAGLSAGA AAAAVGGGRG GRAGRGCGGD
GGGRHLPWAA CWASAAGGDG SQRLLGSVGG GSGSSSSEDE PEEFLGFHLE DEVTQSSRRA
ALRSKRGTAL PVRKKERKKR AATEDTPPKR LVKQKAVESQ RERMVKALAE LLQKSKRSPA
RIGRPPISGP KVGRKLPKQT KQGPEPDDSI KSTISPTLSS QIEKTINSIV SPRPRGRPPG
SSRKRLVTEA ESPCESTKAP SSIPEPSISP QSSSPSSQPP EDLKKPPLIL KFFSKARRHK
SGQLVVTHVR LKTPGHRRGR KRKWSVVPRK KMSPLPSQSV SESETPLSES EASAPEPEQK
EESSASQTQP QEVLAPDPEP QPECVVPKPE PQPEVITQEP EQPPEVSLEP VAFEVEQQTP
AQGADVPALL DEVSWKGESQ EPCPEHDGTE GLSEEGSSSI AHSTRAQCLK RGRGRPPLTP
TQRAQRMAIQ QLPTKAKEEG LGAVQQSGNA CQEEASTHKT NFLKNIRQFI MPVVSARSSR
LIRTPRRFMD EIPQKTPKPT ESPVTDGICL DKQESSQLPL QGVSPRVAHP EPVSPDEEIS
RVLSSPPSPS VPQITSPAAP ALPEKRRSIL REPTFRWTSL SPTSSPKDVG KTLFQLPCED
SSPLPSTPAP LPSPPAKRSP LLRAPQFTPS EAHLKIYESL TVSPEDSESV PASPEVRRDP
PAPQHESPTL PYEPVVTRSG KKLLARVNHL ALPLFTEVSS PPKTEGKELI TMEDVNSPGV
VHKVAIRRVL PPPIQVEQER TSDKPENKVE PASLIQKEQK SSDAPKPIIT QLSSMDKVYS
LLTRAKVQLY KIDQQKQFKF IPGCQSVRAG AFEIPKVPAE KTVTSDVKAE EEEEEEEEKE
DRKDARNQGQ ESPVQGPRIK HVCRHASVAL GQSRAMVPED VPRLSALPLR EREEITVSPT
VEETSSASES ESGLQKQVKV ETSIKTVPPP VRRHVSHHHG KKNRMTRCGR CKGCLKLQDC
GECNNCLDKP KFGGPNTKKQ CCVYRKCDKI EARRVERLSK KGRTVVKAIV PWDSEDSQEA
FPAPLEVILG ATETAEQDSL LQRKSARRCV KQRPSYDIFE TSDSDTEAVS GSATHRRKSS
RDSDLLPMDS EEQSRPRRTP LQPVVQLKAR KKPEKDLTNS GTFRSFSNGW NGKQKSTDGI
HRLRVDFKED CDLENVWLMG GLSILASVPV TTQLVCLLCA SKGFHQLVFC QVCCDPFHVF
CLEDDEQPLP EQEESWCCRR CKFCHVCGRK NKASKQLLEC ERCRNCYHLA CLGPNYPTKP
FRKRKNWVCS ACIRCKSCGT APGKNWDTEW SNDYSLCSAC SVLHDKGNYC PICLHCYEDN
DYESKMMQCA KCDHWVHAKC EGLSDEGYEI LSNLPESVVY ACRPCCGSDK AKWREVLSVE
LRKGLRQVLQ GLMSSKCATP LLQCAQCCPD DGVRVHLRPC DLCTVNKLFE QGHYSSVHSF
NEDMVGVLLG QTEDQQNSLL AKALYIELMG KFFSWFDAQD EKHWIRNTTL PNGMLPNAVL
PPSSDHIYAQ WRQPEETNPV TKSHLTLSGP EKIAPKDADA SPQEPLADSE DKRQCALCLQ
YGDAPSKDAG RLLYIGQNEW THVNCAIWSA EVFEENDGSL KNVHAAVARG RQMRCEHCQR
TGATVGCCLS ACLSNYHFMC ARLRQCTFQD DKKVFCQKHV DLLDGTEIVA DDGFDVLRRV
YVDFEGISFK RKFMVGLEPD IINMMIGSMK IDSLGMLTDL SECEGRLFPV GYQCSRMYWS
TVDAHRRCWY KCRVLEYRPK QSQEEPDASG VQEENHTIVH SPTVPADSSI EEKHLKDVST
SMPPPEHHSP IQNPGSLPHP EAAVTKPKSL TGARIKVPNY SPTRRPISGV SSRPLPSPGS
ASSMSHHILT VGDPDFPPPR RTQRLSPLSP SSAHRTHRSS FPPQTMANRT SPASTSLRAM
PLLPDNPTTG NGFRQNSTSD GQRPSLTSPP PSPPPVPPEL AFELNVSDLE FDDSLLDEPF
QEEELGVTRM CPSSPGLGLP QLDGLGDAES EEEGEESRYF RFPRTVVTRE SPLPPYPLDL
PLPHINQLDG IDDGTDSEAD SAGGHPSAKG KQAEPRVERE LAGPAPAPED LPSDIVDFVL
KNMDTPESKA PLPSCLNQMP MPPAPATSTS FNGTESAHPT PAPDLTPTLT LSCAQVPGAP
EVRMLGPEGQ KPGSRIILVN KLGQVCVKVQ SEEDILNSQD GEQASSCDAK PNSIPAPLPA
PTPAPSLGTV ILRAPLGLNP NPLPTWTIRG PVISMVPMVN VVGTTPQALG GGQLALSAPA
LVTPSLGLQQ TCLLQPVTMN SGVLSIPGLV SLPGPRPAIR VKRVSTFVGN VPVKKVKMDG
VNEEEPLPMS PTATPDHLTN NCISGSTVAS GIGRVRMKTP TTKGVLDLDA LKEEADVSGS
DHSPMEHCPS LVPLHSHPGS PEQNQELLLE PAWHRYAGEL SSSDEDNQHL EDKENEIPRK
TQPHLCFEIT NEDGLNVQAA TIDGAWKAVI EKVQEARTNA RLKHLSFAGM NGVRMLGMHH
DAVIFLVEQL YGAKACHKYK FRYHQHEGEE EELPLNPHGC ARAEVYSRKC TFDMFNFLAS
QHRVLPEGGP YDEEEDEVQL KSTRRATSLE LPMAMRFRHL KKTSKEAVGV YRSAIHGRGL
FCKRNIDAGE MVIEYSGIVI RSVLTDKREK YYDSKGIGCY MFRIDDFDVV DATMHGNAAR
FINHSCEPNC YSRVIHVEGQ KHIVIFALRR IFRGEELTYD YKFPIEDAGS KLPCNCGAKR
CRRFLN
//
