SET1_NEUCR
ID SET1_NEUCR Reviewed; 1313 AA.
AC Q8X0S9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9Y7R4};
DE AltName: Full=COMPASS component set-1;
DE AltName: Full=SET domain-containing protein 1;
GN Name=set-1; ORFNames=18F11.100, NCU01206;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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:Q9Y7R4}.
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:Q9Y7R4};
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; AL670011; CAD21415.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA32336.3; -; Genomic_DNA.
DR RefSeq; XP_961572.3; XM_956479.3.
DR AlphaFoldDB; Q8X0S9; -.
DR SMR; Q8X0S9; -.
DR STRING; 5141.EFNCRP00000004417; -.
DR PRIDE; Q8X0S9; -.
DR EnsemblFungi; EAA32336; EAA32336; NCU01206.
DR GeneID; 3877695; -.
DR KEGG; ncr:NCU01206; -.
DR VEuPathDB; FungiDB:NCU01206; -.
DR HOGENOM; CLU_004391_0_0_1; -.
DR InParanoid; Q8X0S9; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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..1313
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269776"
FT DOMAIN 1171..1288
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1297..1313
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1313 AA; 145626 MW; 81A41BA8AD860C84 CRC64;
MSRSSGASFA QFFPAAPRAA RDRATERERA RMRAQASPPT QPLDTNGHRT PLSSFTSNRS
DDGASPGRSH ITSLNHSSSA GADATRPPLE DTESLPGDTL NTVGSASSHT STSSSIFSSS
TRQPAMASAS VRNSHTHNST TPLTTAGSPS SLYLSTSLHA KPHSVSPHHA DKQNGLTPTL
NGSATDSLVP LPDGTERVPP RDPSRSVLCT ICTYDPLLDK KLSSSEKKKA KPIYKDYGLN
DEDDAPPSDP RLAHGGKLSY INVNFHLPKA QLIDAPSNLK PYPYDPKTSC GPGPPVQILV
RGFNPLIAFT KVTTIFASFG DIAESSNKMH PETGSYLGFA TIRYKDSKPT SSRPVPVPAH
QAARRAVRGM HGRRIEANQV RVEFDPEGRK SKALMEAVLK KSRETSQTPN AAYKIPTGPK
PRAGEVIPGP PPTAPKGPAA HRALGGSEAG WTSTKPRHPN IIETEPIVNH IKSEPYIFVA
HEYVPVMPTT VAHMKKRLKQ YGFDDIRADR TGYYIIFRDS HYGRDEASKC YNSANDTAFF
TYSMVMDLHL FGTVGKSSRS SEDHRRHSYG SEKRPPPEHR QRDDQDRRRR DEEADIEEEK
KQRAKNLDPV KEAAEVIRRE MTEHLLKTIR TKITLPAVFD YLNPVNHAAK RRKLNIDDSH
SGTIPSIVFD DSEGRSSPVG TPNSRADPIE RRTARADVST LRVRKLKSRG VNARKHGFND
PFARARPTQR VDLRSLHHRL NSDSDDDSDD GVDNRYSMIR DTEEPESRPR SRVSSEEDRN
KEETGSWVAG EDDSMTEASF ALNDTSALLK KRKLDLPAET AVKRQKKAEE LFEATIARIE
TELPSQEQAV ESVTPTGVEA PLNGLPDADV KAEPAEDKET EDSRLPTPIP DNTKPKKKAK
AKKKSKKQIF EEREALKKQQ QETFEREALR AAGIEDIEGT PDAEAKSQVG EPEPVPEPEL
ETKGEALEAP ETESKPDLDP ELYPSEVVDA LVLPKDFNLD IGTLKLVPFH GEDGPDAQRL
QRKFGTAKLD CDAELWLWRR NRIRQLNSED GSVDKPVGIG GYYVPNPTGC ARTEGVKKIL
NSEKSKYLPH HIKVKKAREE REKNAKNGNT NSVAAAAEAA RLAADSLVAK GNSRANRVNN
RRYVAEINDQ RKNFGQDSDV LRFNQLKKRK KPVKFARSAI HNWGLYAMEN INKDDMIIEY
VGEEVRQQIA ELREARYLKS GIGSSYLFRI DDNTVIDATK KGGIARFINH SCMPNCTAKI
IKVEGSKRIV IYALRDIAQN EELTYDYKFE REIGSTDRIP CLCGTAACKG FLN
