ID A0A2Y9E6M8_TRIMA Unreviewed; 2405 AA.
AC A0A2Y9E6M8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=LOC101345928 {ECO:0000313|RefSeq:XP_004388243.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004388243.1};
RN [1] {ECO:0000313|RefSeq:XP_004388243.1}
RP IDENTIFICATION.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_004388243.1; XM_004388186.2.
DR STRING; 127582.A0A2Y9E6M8; -.
DR GeneID; 101345928; -.
DR KEGG; tmu:101345928; -.
DR InParanoid; A0A2Y9E6M8; -.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000248480; 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; 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; 7.
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:UP000248480};
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 647..694
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 890..941
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 938..992
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1024..1085
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1267..1375
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 2265..2381
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2389..2405
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1808..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1971..1992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1998..2017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1846
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2001..2016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2045..2063
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2085..2102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2319
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2342..2343
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2394
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 2395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 2400
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_004388243.1"
SQ SEQUENCE 2405 AA; 261612 MW; AB2E257A689DC2F7 CRC64;
GRGRGRGWGP SRGWVPEEES SDGESDVEEF QGFHSDEDVA PSSLRSALRS QRGRAPRGRG
RKHKTTPLLP ARLADVAPTP PKTPARKRGE EGTERMVQAL TELLRRAQAP PVPRSRACEP
STPRRSRGRP PGRPAGPCRK KPPAVVVAEA AVTIPKPEPP PPVVPVKYRT GSWKCKEGPG
PGPGTPKRGG QSGRGGRGGR GRGRGGFPLV IKFVSKAKKV KMGQLSLGSE SSQGQDQHGE
KWQESPQGRV ESGQEGDPCW KKDQKLEEEE EEEEKEEKDE EGGEEKEDRA IAEEEMVLAE
EEEAKLLSPP LTPPAPPPLP TTPSRRPLLL RAPQFTPSEA HRKIYESVLT APLLGAPEAP
EPEPPPADDS PPEPEPRALG RTNHLSLPRF APVVTTPVNA EGPPPGAPAL SNGQQPQAQL
QQPLQALQAQ LVPQAPPPQQ PQLQPPLQLQ PSPPQQPPAL EKARIAGLGS LPLSGVEEKM
FSLLKRAKVQ LFKIDQQQQQ KVASSMPLSP GGLMEAVVGT GKQIPDRGSV RSEDESMEAK
RERPSGPESP VQGPRIKHVC RHAAVALGQA RAMVPEDVPR LSALPLRDRQ DLATEDTSSA
SETESVPSRS RRGKVESAGP GGDSEPAGSG GTLAHAPRRS LPPHHGKKMR MARCGHCRGC
LRVQDCGSCV NCLDKPKFGG PNTKKQCCVY RKCDKIEARK MERLAKKGRT IVKTLLPWDS
DESPEASPGP PGLRRGAGSG GPREEVVAPP GPEEQDSLLL QRKSARRCVK QRPSYDIFED
SDDSEPGGPP APRRRTPREN ELPVPEPEEQ SRPRKPTLQP VVQLKARRRL DKDALAPGPF
ATFPNGWTGK QKSPDGVHRV RVDFKEDCDL ENVWLMGGLS VLTSVPGGPP MVCLLCASKG
LHELVFCQVC CDPFHPFCLE EAERPLPQHH DSWCCRRCKF CHVCGRRGRG AKHLLECERC
RHAYHPACLG PSYPTRATRK RRHWICSACV RCKSCGATPG KNWDVEWSGD YSLCPRCTQL
YEKGNYCPIC TRCYEDNDYE SKMMQCAQCD HWVHAKCEGL SDEDYEILSG LPDSVLYTCG
PCAGSTHPRW REALNGALRG GLRQVLQGLL SSKVAGPLLL CTQCGQDGKQ LHPGPCDLQA
VSQRFEEGHY KSVHSFMEDM VGILTRHAEE GEAPERRAGG QMKGLLLRLL ESAFGWFDAH
DPKYWRRSTR LPNGVLPNAV LPPSLDHVYA QWRQQEAETP ESGQPPGGPA AAFQGKDPAA
FSHLEDPRQC ALCLKYGDAD SKEAGRLLYI GQNEWTHVNC AIWSAEVFEE NDGSLKNVHA
AVARGRQMRC ELCLKPGATV GCCLSSCLSN FHFMCARASY CIFQDDKKVF CQKHTDLLDG
KEIVTPDGFD VLRRVYVDFE GINFKRKFLT GLEPDAINVL IGSIRIDSLG TLSDLSDCEG
RLFPVGYQCS RLYWSTVDAR RRCWYRCRIL EYRPWGPREE PAHLEAAEEN QTIVHSPPPP
SEPRDNESPP PETAALTPGA PEQHLLVQNL DPPPRSDPSS TLPLAPRSFS GARIKVPNYS
PSRRPLGGVS FGPLPSPGSP ASLTHHIPTV GDPDFPAPPR RSRRPSPLTP RLPLSRRAIS
PLRTSPQLRV PPPTSVVTAL TPTSGELAPP GPATPPPPPT EDLGPDFEDM EVVSGLSAAD
LDFAASLLGT EPFQEEIVAA GAVGSSHGGL GDSSEEEAGP NTHYIHFPVT VVSGPALAPG
GLPGTPRIEQ LDGVDDGTDS EAEAVQQTRG QGAPPSGPGV GRAGVIRAAG DRARPPEDLP
SEIVDFVLKN LGGPGEGGAG PREEPLPPPL PLANGSQPPQ GLPPSPADPA RTFAWLPGSP
GVRVLSLGPA PEPPKPATSK IILVNKLGQV FVKMAGEGEP VPSPVKQPPL PPPVPSTAPT
PWTLPPGPLL SVLPVVGVGV VRPAPPPPPL TLVLRSGPPS PPRQAIRIKR VSAFPGRSPP
APPPSKAPRL DEVGESLEGT PQAAGLSNSG SSRVRMKTPT VRGVFDLDHP GEPVGEETSG
PLQERPSLLP PPDSGPPRVP DGPPDLLLES QWHHYSGEAS SSEEEPPSPE DKENQAPKRA
GPHLRFEISS EDGFSVEAES LEGAWRTLIE KVQEARGHAR LRHLSFSGMS GARLLGIHHD
AVIFLAEQLP GAQRCQHYKF RYHQQGEGQE EPPLNPHGAA RAEVYLRKCT FDMFNFLASQ
HRVLPEGAAC DEEEDEVQLR STRRATSLEL PMAMRFRHLK KTSKEAVGVY RSAIHGRGLF
CKRNIDAGEM VIEYSGIVIR SVLTDKREKF YDGKGIGCYM FRMDDFDVVD ATMHGNAARF
INHSCEPNCF SRVIHVEGQK HIVIFALRRI LRGEELTYDY KFPIEDASNK LPCNCGAKRC
RRFLN
//
