ID A0A2Y9QFV3_TRIMA Unreviewed; 2576 AA.
AC A0A2Y9QFV3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific isoform X2 {ECO:0000313|RefSeq:XP_023582240.1};
GN Name=LOC101343565 {ECO:0000313|RefSeq:XP_023582240.1};
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_023582240.1};
RN [1] {ECO:0000313|RefSeq:XP_023582240.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_023582240.1; XM_023726472.1.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15648; PHD1_NSD1_2; 1.
DR CDD; cd15650; PHD2_NSD1; 1.
DR CDD; cd15653; PHD3_NSD1; 1.
DR CDD; cd15656; PHD4_NSD1; 1.
DR CDD; cd15659; PHD5_NSD1; 1.
DR CDD; cd20161; PWWP_NSD1_rpt1; 1.
DR CDD; cd20164; PWWP_NSD1_rpt2; 1.
DR CDD; cd19210; SET_NSD1; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR041306; C5HCH.
DR InterPro; IPR047426; PHD1_NSD1_2.
DR InterPro; IPR047428; PHD2_NSD1.
DR InterPro; IPR047429; PHD3_NSD1.
DR InterPro; IPR047430; PHD4_NSD1.
DR InterPro; IPR047432; PHD5_NSD1.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR047423; PWWP_NSD1_rpt2.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR047433; SET_NSD1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; PTHR22884:SF312; HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-36 SPECIFIC; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF17982; C5HCH; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00855; PWWP; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00249; PHD; 5.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00293; PWWP; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 2.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
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:PRU00146}.
FT DOMAIN 323..388
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1421..1467
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1585..1629
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1634..1696
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1768..1818
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1820..1937
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1944..1960
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 90..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1969..1989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2091..2300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2340..2405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2469..2490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2544..2576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1179
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1359
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2095..2112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2113..2146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2158..2172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2209..2225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2469..2485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2555..2570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2576 AA; 283519 MW; 4FACDFC16991302A CRC64;
MDQTCELPRR NCMLSFSNPV NLDAPEDKDS PFGNGQSNFS EPLNGCTMQL PTASGTSQNA
YGQGSPSCYI PLRRLQDLAS MINVEYLNGS ADGSESFQDP EKSDSRAQSP VVCTSLSPGG
PTALPMKQEP SCNNSPELQV KVTKTIKNGF LHFENFTCVD DADIDSEMDP EQPVTEDESI
EEIFEETQTN ATCNYEPKSE NGVEVAMGNE QDSTPGSRHG AVKSPFLPLA PQTETQKNKQ
RNEVDGSSEK AALLPAPFSL GDTNVSVEEQ LNSINLSFQD DPDSSTSTLG NMLELPGTSS
SSTSQELPFC QPKKKSTPLK YEVGDLIWAK FKRRPWWPCK ICSDPLINTH SKMKVSNRRP
YRQYYVEAFG DPSERAWVAG KAIVMFEGRH QFEELPVLRR RGKQKEKGYR HKVPQKILSK
WEASVGLAEQ YDVPKGSKNR KCVRSSIKLD SEEDMPFEDC TNDPESEHDL LLNGCLNSLA
FDSEHSADEK EKPCAKSRVR KSSDNPKRTS VKKSHMQFEA HKEERRGKIS ENLGLNFISG
DVSDKQASNE LSRIANSLTG SNTAPRSFLF SSCGKNTAKN EFETSNCDSL LGLPEGALIS
KCSGEKKKPQ RGLVCSSKVQ LCYIGAGDEE KRSDSISICT TSDDGSSDLD PVDHSSESDN
SVLEITDAFD RTENILSMQK NEKIKYSRFS ATNTRVKAKQ KSLITNSHTD HLMDCTKTAE
PGTETSQVNL SDLKVSTLVC KPPSDFRNDS LPPKFNTSSS ISSENSLIKG GTTNQSLLHS
KSKQPKIRSI KCCKHKENPV VVEPPITNED CNLKCCSSDT KGSPLASISK SGKVDGLKLL
SNMHEKTRDS SDIETAVVKH VLSELKELSY RSLNEDVSDS GTSKPSKPLL FTSASGQNHI
PIEPDYKFST LLMMLKDMHD SKTKEQRLMT AQNLVSYRSP GLADCSANSP AGASKVLVSG
ASTHNSEKNG DDTQDSAHPS PSGGDSALSG ELSTSLPGLV SDRRDLPASG KSRSNCITRR
NCGRSKLSSK LQDGFSAQLG KNTVNQKALK TERKRKLNRL PGVTLEAALP GDRESGGSAS
VSSRGGREDP GKEEPLQLKG HLTSEDCSHF SDIHFDNKVR QSDPDKIPEK APSFENRKDP
ELDSEMNSKN DEHNGVHQVV PKKRWQRLNQ RRTKPRKRTN RFREKENSKG AFGVLLPGDP
VQKGSDFPEH RPPTSTNVLE DAVTDPNCAG HLDSAGPRLN VCDKTNASIE EMEKEPGIPS
LTPQSELPEP AVRSEKKRLR KPSKWLLEYT EEYDQIFAPK KKQKKVQEQI HKCYETGHLG
NGITESCAAT HSKEFGEGAT KMFDKPRKRK RQRHATAKMQ CKKVKNDDPS KETAGSEGEL
MTHRTAASPK EAIEEGVEHD HGMPVSKRMQ GERGGGAALK ENVCQNCEKL GELLLCEAQC
CGAFHLECLG LTEMPRGKFI CNECRTGIHT CFVCKQSGED VKRCLLPLCG KFYHEECVQK
YPPTVMQNKG FRCSLHICIT CHAANPASVT ASKGRLMRCV RCPVAYHAND FCLAAGSKIL
ASNSIICPNH FTPRRGCRNH EHVNVSWCFV CSEGGSLLCC DSCPAAFHRE CLNIDIPEGN
WYCNDCKAGK KPHYREIVWV KVGRYRWWPA EICHPRAVPS NIDKMRHDVG EFPVLFFGSN
DYLWTHQARV FPYMEGDVSS KDKMGKGVDG TYKKALQEAA ARFEELKAQK ELRQLQEDRK
NDKKPPPYKH IKVNRPIGRV QIFTADLSEI PRCNCKATDE NPCGIDSECI NRMLLYECHP
TVCPAGGRCQ NQCFTKRQYP EVEIFRTLQR GWGLRTKTDI KKGEFVNEYV GELIDEEECR
ARIRYAQEHD ITNFYMLTLD KDRIIDAGPK GNYARFMNHC CQPNCETQKW SVNGDTRVGL
FALSDIKAGT ELTFNYNLEC LGNGKTVCKC GAPNCSGFLG VRPKNQPIAT EEKSKKFKKK
QQGKRRTQGE VTKEREDECF SCGDAGQLVS CKKPGCPKVY HADCLNLTKR PAGKWECPWH
QCDICGKEAA SFCEMCPSSF CKQHREGMLF ISKLDGRLSC TEHDPCGPNP LEPGEIREYV
PPPVPLPPGP SSHPAEQSSG MATQGPKMSE KPPADTNQTL SLSKKALAGT CQRPPLPERP
LERTDCRPQP LDRVRDLAGP GTKPQSLGSS QRPLDRPPAT AGPRPQLSDK PSPVTSPSSP
SLIRSQPLER PLGMAGSRLD KSIGAASPRH QPLEKAPVPT GLRLPPPERL LITSGPKPQA
SDRPPDKSHA SLSQRLPPPE KVLSAVVQTL VAKEKALRPV DQNTQSKNRA ALVMDLIDLT
PRQKERAPSP HEGTPQADEK MPVLESSSWP PSKGLGQMPR AGERGSVSDP VILPPGKAAA
PSEHPWQAVK SLTQTRLLSQ PPAKAFLYEP ATQASGRPPA EAEQTLGLPS QAPGLVKQMA
GGQQLPGLAA KGTTLSGQSF RPLGNAPASL PTEKKTLATT EQSPWVLGKA SLGPGLWPMV
AGQTLTPPCW SSGSTQTLAQ TCWSLGRGQD PKPEQNTVPA LNQAPSSHKC AESEQK
//
