ID A0A1I8NYB7_STOCA Unreviewed; 2261 AA.
AC A0A1I8NYB7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 08-NOV-2023, entry version 36.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987, ECO:0000256|RuleBase:RU271113};
DE EC=2.1.1.360 {ECO:0000256|ARBA:ARBA00012190, ECO:0000256|RuleBase:RU271113};
DE AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|ARBA:ARBA00029821, ECO:0000256|RuleBase:RU271113};
GN Name=106090482 {ECO:0000313|EnsemblMetazoa:SCAU003150-PC};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU003150-PC, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU003150-PC}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU003150-PC};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC histone H3 to form H3K79me3. This methylation is required for telomere
CC silencing and for the pachytene checkpoint during the meiotic cell
CC cycle by allowing the recruitment of RAD9 to double strand breaks.
CC Nucleosomes are preferred as substrate compared to free histone.
CC {ECO:0000256|RuleBase:RU271113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60328, Rhea:RHEA-COMP:15549, Rhea:RHEA-
CC COMP:15552, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.360;
CC Evidence={ECO:0000256|ARBA:ARBA00001569,
CC ECO:0000256|RuleBase:RU271113};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU271113}.
CC -!- MISCELLANEOUS: In contrast to other lysine histone methyltransferases,
CC it does not contain a SET domain, suggesting the existence of another
CC mechanism for methylation of lysine residues of histones.
CC {ECO:0000256|RuleBase:RU271113}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. DOT1 family. {ECO:0000256|RuleBase:RU271113}.
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DR RefSeq; XP_013112138.1; XM_013256684.1.
DR EnsemblMetazoa; SCAU003150-RC; SCAU003150-PC; SCAU003150.
DR GeneID; 106090482; -.
DR VEuPathDB; VectorBase:SCAU003150; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR CDD; cd20902; CC_DOT1L; 1.
DR Gene3D; 1.10.260.60; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR025789; DOT1_dom.
DR InterPro; IPR030445; H3-K79_meTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21451; HISTONE H3 METHYLTRANSFERASE; 1.
DR PANTHER; PTHR21451:SF0; HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC; 1.
DR Pfam; PF08123; DOT1; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51569; DOT1; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU271113}; Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU271113};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU271113};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU271113};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU271113}.
FT DOMAIN 19..336
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 339..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1553..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1652..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1815..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..2015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2043..2152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 663..697
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 362..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1022
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1780
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1995..2015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2043..2066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2081..2095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2109..2152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2261 AA; 247727 MW; DE900A6C6502F5F1 CRC64;
MATPQVKDLV LRSPAGSSEV ITFSWPLQVG TGQDRHDNGI DIIDTIKFVC DELPSISSAF
EEINLNHIDT ACYKTMTNLV DRFNKAVDSI VALEKGTSLP AERLNKFAHP SLLRHILQLV
YNFAVLDPDK LNNYEPFSPE VYGETSYELV LQMIKHVNVT NDDTFIDLGS GVGQVVLQMA
GSFPLKTCIG IEKADTPARY AERMDVFFRQ FMAWFGKRFC EYKLIKGDFL VDEHREKITS
SSLVFVNNFA FGPNVDHQLK ERFADLRDGA RVVSSKSFCP LNFRITDRNL SDIGTIMHVS
EIPPLKGSVS WTCKPVSYYL HVIDRTILER YFQRLKTQKG AENDHVGGST RTTRDRAKRE
ANNQALGNSQ NSSLTARTSS PAANAANGIT GATATMATAS TNSTSTVTKT RQQQQQQQQQ
QQQRSNEMET STESDGDALT TNGGNSNGSG GPITRKNWSD WASSKGKSSQ SDEEENNNSI
ATTTTASSTR TVRTTTQKKR KKLTRKAAIA SKSAAAAAQR EAAAKERAEA AAAASKDNSS
KEDGGSGNTT GGAKSATTSG GRKGRLKKGA VRGRRCANIA GLEVLHKQTL LSTSVEAMSK
KLPPAPGCVD QQLTSLLTQN MAHRELDIPT SPQDTPYALQ ILLDVFRSQY MAMIEQMKSK
AFVPNIKKQI QMEQERKQRI KNRASQLDKQ IKVLIDDSVA LLKVRMNELG INVSSPNDLI
AKAKEIVGRH KELQGVAKKI QSQVTAYEME QRRLLKKQLQ HLPEYQCLYG ANGKTKLHDL
PGGELSEAAA HELVLKEIAN TLAQRKKLVA QVSCIEKEAK SLEKAAEERR ATATLLAQGT
NIIMTNPATS SNSSMSSPLN QPLQLTTHNH VNTISINHVS NTNSLNSSSS SASAAPVSSL
VPNSSAMQPS ITVTKTTGKS SRRARDHRSR SQEWPDVPDV GKIEESNPEV LAQKILETGR
KIEASKLAMA NAKQHQQQPL ALNNHHYQQQ QQAHQQHPQQ LQHHHLHQQQ QHHHHNQHAS
HSQPPPHHHP EDKPYRSKHQ RSASNEHLPG IPFSGQFSQA PPDASALMPA PKHRGEHPLN
AGLTSVANSN NNNNLNNTMR QMNGPSMASS STLPKCELPG MRKSHSATNA ASAPVVSIQE
SPKVANFEDR LKSIITSALN EDQEQRKAQQ VNQVHVEVSP ATQQSPAPKR SKHGGTVASS
SSSASNAHSS LTNIINVATH GMTHLNATTT ISPINTALPP PPSQSKYGPP TPSSKAMLQP
INNSTSSAVV NSAASSKGGS SSTSKYHPHH GPLNHQAAAA AAAGSHLNNH TYGHPSITSE
HNMLRRRSSV SAASYEQFLA QQQQHQQQQQ HLHQQQQQML LNSNSQQHLP LEFKQPPLEN
HHHLGHQQRS NSREMLQIDE PVRSSSANSD SALPYYPPTR DRLMSMERSN SRESAAMAAQ
HHGGQAQQQQ PPSRPSSNSS QPDYTQVSPA KMALRRHLSQ EKLNLHVPPV QGNGGSGNSM
PAMASKTIGD LVNGEIERTL EITHQSIINA AVNMSTVGTA SGERNPYLLD RSIYATGSEQ
QRERDRSNER ERERERERER ERERERMIIN NSAQRPERVH VKVVDEPQQL AASAGGYAEI
SSRATTASET KSAYAHNLAT LANVAYQHKS MVGSNGGPAG PSPPSAAHHG PGTSSGSTSS
SSASRHYNNR ERDATNMNTS AAYPHLPSSS GKVSSNSGNS ASSSTNRDYQ PVALPRAEMK
PCIEAYFQEE QHHPQQQQMP HHHHHTSSST HSHKSSKDKH SSRNNRLNGT NPPLEGLAAS
LMASHGRFLD GKFREEHEER QKRAAAASTS NSGNASNTSS SGHNNDHNIN SGQQQQHNRH
VEHYGTNSYG QQQQQQPTSS NHNSHHHNGS PMKVELGVKR TSPMTNHHPR AAKIPHYSHE
QNPMAHTSSG GGNNNHPLHH QQQSQHHQQT QHHASHHHHH PGQAASSTSL GNPYANTNGG
LPSNAHGHHN ASGYPPHSHS PSSSSSSSSA HRRGNNKLNM EPLLMSPEIN SIMGGDDVQR
SLQQNSAAAT KPMASSSSSA SNRTAVNNSH HHHHHKQQQQ HGHYQQQQQQ QHHLNNNNHH
HQHQNHHSQQ QQQHHSSSSN TMNNSNIHNN NSHQQHHQQQ QQHLSHNSAS NTSAAAALTN
TNSVVGGRAA DDVFKLDTST TTTSSTTTAS TTCSTTLRNF DYRRSAIQTQ LPTPQPQILP
SSQIPSSYHH HNHNTNHYHH NHQNPTKPIG IIVADSSTTK D
//
