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Database: UniProt
Entry: Q8X0S9
LinkDB: Q8X0S9
Original site: Q8X0S9 
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   16-JAN-2019, entry version 122.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE            EC=2.1.1.43;
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
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   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.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora 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.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   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.,
RA   Paulsen I., 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}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AL670011; CAD21415.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32336.3; -; Genomic_DNA.
DR   RefSeq; XP_961572.3; XM_956479.3.
DR   ProteinModelPortal; Q8X0S9; -.
DR   SMR; Q8X0S9; -.
DR   PRIDE; Q8X0S9; -.
DR   EnsemblFungi; EAA32336; EAA32336; NCU01206.
DR   GeneID; 3877695; -.
DR   KEGG; ncr:NCU01206; -.
DR   EuPathDB; FungiDB:NCU01206; -.
DR   HOGENOM; HOG000181654; -.
DR   InParanoid; Q8X0S9; -.
DR   KO; K11422; -.
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; IEA:InterPro.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR017111; Set1.
DR   InterPro; IPR024636; SET_assoc.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF462; PTHR22884:SF462; 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   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; Complete proteome; Methyltransferase;
KW   Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1   1313       Histone-lysine N-methyltransferase, H3
FT                                lysine-4 specific.
FT                                /FTId=PRO_0000269776.
FT   DOMAIN     1171   1288       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1297   1313       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   COMPBIAS     53    166       Ser-rich.
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
//
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