SET1_EMENI
ID SET1_EMENI Reviewed; 1220 AA.
AC Q5B0Y5; C8VFD2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:P38827};
DE AltName: Full=COMPASS component SET1;
DE AltName: Full=SET domain-containing protein 1;
GN Name=set1; ORFNames=AN5795;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC specifically mono-, di- and trimethylates histone H3 to form
CC H3K4me1/2/3, which subsequently plays a role in telomere length
CC maintenance and transcription elongation regulation.
CC {ECO:0000250|UniProtKB:P38827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:P38827};
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AACD01000098; EAA62888.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81174.1; -; Genomic_DNA.
DR RefSeq; XP_663399.1; XM_658307.1.
DR AlphaFoldDB; Q5B0Y5; -.
DR SMR; Q5B0Y5; -.
DR STRING; 162425.CADANIAP00003254; -.
DR PRIDE; Q5B0Y5; -.
DR EnsemblFungi; CBF81174; CBF81174; ANIA_05795.
DR EnsemblFungi; EAA62888; EAA62888; AN5795.2.
DR GeneID; 2872082; -.
DR KEGG; ani:AN5795.2; -.
DR VEuPathDB; FungiDB:AN5795; -.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_004391_1_0_1; -.
DR InParanoid; Q5B0Y5; -.
DR OMA; CHMTALF; -.
DR OrthoDB; 1017537at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR017111; Set1_fungi.
DR InterPro; IPR024636; SET_assoc.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF11767; SET_assoc; 1.
DR PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51572; SAM_MT43_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1220
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269773"
FT DOMAIN 1078..1195
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1204..1220
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1220 AA; 137240 MW; 671DE9E39E558816 CRC64;
MSRSSAGFAD FFPTAPSVIQ QKRYQATRER QRSRPHLSRE HADEEQIVTG SRTSGETVNG
NSPQNLGQEL RSDLNKSRKE VAEDGSASHG EANTPANNTS GPGTGSSNDT RLDTLTPLTN
TESSPQNNPS PSQAKAPNGD EPDGFRQARA NVSNSTMTPL HTPPTPTTHS LSQRVAIVKG
SKLVHDPDRA PSKDKRKRPC YVDIVSDEQE GRLSDPRLSI QNYTRGAGCR QKTKYRPAPY
VLRHWPYDPA STVGPGPPVQ IVVTGFDPLT PLAPISTLFS SFGEIAEINN RTDPDTGRFL
GICSVKYKDS ASFHGSGPVS ASLAAKNAFH ECKKGQRIGN NRIKVEYDRD GQTSEKLASR
AIAAQRIDSK IDMPVVGEPK SEAQVNKNEP PPTAPKGPSG RSFMRPSAVI PEGPRASFQK
PAIPSLIEET PILNQIKRDP YIFIAHCYVP VLSSTLPHLK KRLKAFNWKD IRCDRTGYYI
IFENSRRGEE ETERCYKFCH MKLLFTYIMN MESQPYGNPH YERSPSPERM KQEQRQKAET
ERLKKEAELD IEEEKKQRAL DLDPCTEVLA IVIKDLRDKL LEDVKSRIAA PALYDYLDPE
RHASRRKQLG IPDPEGIKRP MFRLDFDSRD STPDPHAKFL NKRHPSGVSG LNILSALPRI
RKAHRLDRTD VAFLDERRKQ PLRRRNVRPL YHRLQQLHDA EDSDEEQHTP LSRDTDDQDS
RPPSRIGSET ESEDADEDAA EALDNSTERL DNEDRHSEIG DLEAAVQDYS PSRKRKRTSE
SPSHRKKQKE SDDFSAVGEG TRTDDIPQVL DGVHKGTVSQ GLSDSADESS RLDHNKVLLE
ELVEDIKTTH SEEPGIKTHH VQVRQSAENM VEGAEYGEAA RHEVEWRVSN DEPRPIVDDD
DSVVMDLDGW QDVVKDEEDL QFLRNILEKQ PMSVIGNLSA WAWRQKEIKA LNRPGDVGPT
RQAASIEGYY VPNITGAART EGRKRILESE KSKYLPHRIK VQKAREEREA KAKSDPQNAA
AEAARIAAAK TISKSTSRST RVNNRRLIAD INAQKQALPS QGGDSDVLRF NQLKKRKKPV
RFARSAIHNW GLYAEVNISA NEMIIEYVGE KVRQQVADMR ERRYLKSGIG SSYLFRIDEN
TVIDATKRGG IARFINHSCT PNCTAKIIKV DGSKRIVIYA LRDIERDEEL TYDYKFEREW
DSDDRIPCLC GSAGCKGFLN
