ID A0A2Y9D639_TRIMA Unreviewed; 2569 AA.
AC A0A2Y9D639;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=[histone H3]-lysine(36) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012178};
DE EC=2.1.1.359 {ECO:0000256|ARBA:ARBA00012178};
DE AltName: Full=SET domain-containing protein 2 {ECO:0000256|ARBA:ARBA00030091};
GN Name=LOC101343139 {ECO:0000313|RefSeq:XP_004368524.1};
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_004368524.1};
RN [1] {ECO:0000313|RefSeq:XP_004368524.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000256|ARBA:ARBA00000317};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_004368524.1; XM_004368467.2.
DR GeneID; 101343139; -.
DR KEGG; tmu:101343139; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd19172; SET_SETD2; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.10.1740.100; Set2, Rpb1 interacting domain; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
DR InterPro; IPR042294; SETD2_animal.
DR InterPro; IPR013257; SRI.
DR InterPro; IPR038190; SRI_sf.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR46711; HISTONE-LYSINE N-METHYLTRANSFERASE SETD2; 1.
DR PANTHER; PTHR46711:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD2; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1498..1552
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1554..1671
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1678..1694
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 2394..2427
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1836..1876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1921..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2444..2470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1836..1871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1956..1975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2023..2050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2059..2084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2094..2134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2454..2470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2569 AA; 287985 MW; 89C2C4AFEEF810EA CRC64;
MKQLPSQTPP KMGDFYDPEH PTPEEEENEA KIENVQKTGF IKGPIFKGVA SSRFLPKGTK
TKVNLEEQGR QKVSFSFSLT KKTLQNRFLT ALGNEKQNDT PNSPAIPLQA DSTPKIKVDI
GDTLSTTEES SLPKSRVELG KIHFKKHLLH VTSRPLLAAT TAVTSPPPPT VPLPAVIAES
TTVDSPPPSP PPPPPPPQAT TPSPPAPVTE PVALPHAPVT VLMTAPVPSP VDVTVRALKE
PPVSVVSESL EVDTKQDAVS NSSEEHITQN LNEQANIPSQ KGDSHIGKEE EIPDSSRSSL
GSKKTGSKKK SLQSEGTFLG SESDEDSVRT SSSQRSHDLK FSASVEKERD AKKSLAPLKS
EDLGKSSRSK TERDDKYFSY SKLERDTRYI SSRCRSDRER RRSRSRSRSD RSSRTSLSYS
RSERSHYYDS DRRYHRNSPY RERTRYSRPY TENRARESSD SEDEYKRTYS RRTSSHSSSY
RDLRTSSSYS KSDRDCKTES SYIETEKRGK YSSKLERESK RTSENEVLKR CCSPSNDVGF
RRGSSYSKHD NSASRYKVTP SKPIPKSDKF KNSFCCTELN EGIKQSHSFS LQTPCSKGSE
LRMINKIPER EKTGSPSPSN QLKDSPTFKK LDESLIFKSE FIGHDSHDSI KELDSLSKGK
YDQLRTYHPI ELNINGSPGA ESDLATFCTS KTETLLMSSD DSVTGSEVSP LIKACMLSSN
GFQNISRCKE KDLDATCMQH SKSESPFRET EPPVSPHQDK LVTLPVMVID YSKTVVREPV
DKRVSCCKTK DSDVYYTSND SNPSLCHSEA ENIEPSVTKI SSNSFMNVHL ESKTVICDNR
NLTDQNSKFG CEEYKQSVGS TSSTSVNHFD DLCQPVGSSS IASSLQSLPP EIKADSLTHL
RCAENTSPVL DAVLMSKTST EFLKHTGEET IVEVGSGLPD SRRGFSSWEN RHNNGLSEKC
LQETQEEGNS RLPDRRRRSE ISLDEGGRRH VRTSDDSEVV FSSCDLNLTM EDSDGVTYTV
KCDSSGHASE IVSTIHEDYS GSSESSSDES DSEDTDSDDS SIPRNRLQSV VVVPKNSTLP
MEETSPCSSR SSQSYRHCSD HWEDERLESR RHAYEEKFEV MANKTCPQTE KFFLHKGAEK
NPEISFTQSS RKQVDNHLPE IVHPQSDGVD STSHTDVKSD PLGHPNSEEI VKVKIASRQQ
ELPVYSSDDF EDVPSKSRQQ TTFPHRPDSR LGKMELSFSS SCEISLVDGF HSSEELRNLG
WDFSQAEKPT TTYQQPDSSY GACDGHKYQQ SAEQYGGTHS YWQGNGYWDP RSAGRPPGTG
VVYDRIQGQV PDSLTDDREE EENWDQCGGS HFSSQSNKFL LSIQQKDRGS VQAPEISSNS
IKDCLAVNEK KDLTKNLEKN DMKDRGPLKK RRQELESDSE SDGELQDRKK VRVEVAQGET
AATPGSALVG PSCVMDDFRD PQRWKECAKQ GKMPCYFDLI EENVYLTERK KNKSHRDIKR
MQCECTPLSK EERAQGEIAC GEDCLNRLLM IECSSRCPNG DYCSNRRFQR KQHADVEVIL
TEKKGWGLRA ARDLPSNTFV LEYCGEVLDH KEFKARVKEY ARNKNIHYYF MALKNDEIID
ATQKGNCSRF MNHSCEPNCE TQKWTVNGQL RVGFFTTKLV PSGSELTFDY QFQRYGKEAQ
KCFCGSANCR GYLGGENRVS IRAAGGKMKK ERSRKKDSVD GELEALMENG EGLSDKNQVL
SLSRLMVRIE TLEQKLTCLE LIQNTHSQSC LKSFLECHGL SLLWIWMAEL GDGRESNQKL
QEEIIKTLEH LPIPTKNMLE ESKVLPIIQR WSQTKTAVPQ LSEGDGYSSE NTSRAHTPLN
TPDPSTKLST EADTETPKKL MFRRLKIISE NSMDSAISDA TSELEGKDGK EDLDQLENVP
IEEEEELQPQ QLLTQQLPES RVDGEASVEV SKLPMSEPEA DSEIEPKESN GTKLEEPIAE
ETPSQDEEEG VSDVESERSQ EQPDKTVDIS DLATKLLDSW KDLKEVYRIP KKSQTEKENT
ITERGRDAVG FRDQTAAPKT PNRSRERDPD KQIQNKEKRK RRGSLSPPSS AYERGTKRPD
DRYDTPTSKK KVRIKDRNKL STEERRKLFE QEVAQREAQK QQQQMQNLGM TSPLPYDSLG
YNAPHHPFAG YPPGYPMQAY VDPSNPNAGK VLLPTPSMDP VCSPAPYDHA QPLVGHSAEP
LAAPPPVPVV THVTAPVEVS SSQYVAQSDG VVHQDSSVAV LPVPAPGPVQ GQNYGVWDSN
QQSVSSVQQQ YSPAQSQATI YYQGQTCPAV YGVTSPYSQT TPPIVQSYAQ SSLQYIQGQQ
IFTAHPQGVV VQPAATVTTI VAPGQPQPLQ PPEMVVTNNL LDLPPPSPPK PKTIVLPPNW
KTARDPEGKI YYYHVITRQT QWDPPTWESP GDDASLEHEA EMDLGTPTYD ENPMKTSKKP
KTAEADTSSE LAKKSKEVFR KEMSQFIVQC LNPYRKPDCK VGRITTTEDF KHLARKLTHG
VMNKELKYCK NPEDLECNEN VKHKTKEYIK KYMQKFGAVY KPKEDTELE
//
