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Database: UniProt
Entry: Q4WNH8
LinkDB: Q4WNH8
Original site: Q4WNH8 
ID   SET1_ASPFU              Reviewed;        1241 AA.
AC   Q4WNH8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   10-APR-2019, entry version 119.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=COMPASS component set1;
DE   AltName: Full=SET domain-containing protein 1;
GN   Name=set1; ORFNames=AFUA_6G06335;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000006; EAL88486.1; -; Genomic_DNA.
DR   RefSeq; XP_750524.1; XM_745431.1.
DR   ProteinModelPortal; Q4WNH8; -.
DR   SMR; Q4WNH8; -.
DR   STRING; 746128.CADAFUBP00007032; -.
DR   PRIDE; Q4WNH8; -.
DR   EnsemblFungi; EAL88486; EAL88486; AFUA_6G06335.
DR   GeneID; 3508771; -.
DR   KEGG; afm:AFUA_6G06335; -.
DR   EuPathDB; FungiDB:Afu6g06335; -.
DR   HOGENOM; HOG000181654; -.
DR   InParanoid; Q4WNH8; -.
DR   KO; K11422; -.
DR   OMA; PNSRADP; -.
DR   OrthoDB; 1017537at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
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   1241       Histone-lysine N-methyltransferase, H3
FT                                lysine-4 specific.
FT                                /FTId=PRO_0000269765.
FT   DOMAIN     1099   1216       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1225   1241       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
SQ   SEQUENCE   1241 AA;  139368 MW;  084B0B9578429E63 CRC64;
     MSRTSAGFAD FFPTAPSVLQ QKRVRAPRDR PCPKDRPEDQ LHVQDDNGQS SCSPGTSAAN
     VSTNGSPPSV SVSETGTGVE NSGCKLVGET NTDITGTDTS ILSASLAQCR ATQVNEARFD
     NLTPVTNAES SPPRKLSPHQ SKSVEVAEYE SNKFATDESK LAATPLHTPP TPRSQTSRSG
     VIKGCKLVYD PDLEKRSSKE KRRKPQYVDF VVNEQDGCSP DPRLSILNYT RGAGCKQKTK
     YRPAPYRLKQ WPYDTATTIG PGPPVQIVVT GFDPLTPVAP INALFSSFGE ISEINNRTDP
     ITGRFLGVCS VKYKDSTSFR GAGPVPAATA ARRAYVECKK EQRIGTRRIR VELDRDGAVS
     DRIVARAIES QRMGHKKNIV GEEAKVEPQA KKNEPPPTAP KGPSRSSTRP VAAVPEGPRA
     SFLKPAIPSL IEETPILAQI KRDPYIFIAH CYVPVLSTTI PHLKKRLKLF DWKDIRCDKT
     GYYIIFENSR RGEEETERCF KVCHMKPLFT YIMNMESQPY GNPNYERSPS PERLQAERRE
     RAERERLKKE ADLDLEEEKK QRAIDLDPCR EVLALIVRDL KDKLLEDVKS RIAAPTLYDY
     LDPDRHAARR RALGIPDPEG IRRHTFRLDA DNFGSNNPRS FLPGDRSFSP YGLNILALPR
     IRKARRLNRA NAAFLDERRK QPVRRKEVRP LYHRLQQLHD VDDSDEDQRT PFSRDIDEQD
     SRPPSRMSSR SSISDDGEES EPLDGLAPQG KRHESRLLGL EYEDSGNTLN EAVDGYSRHD
     SPGLSSTRKR KRVAEGIDVR KRPKEESERS QLNRSVEAGD TFYEESQHSE AAELGTVKPE
     NLAGIGGKFL GRVEDRSINE DGEKENMERL HIESAIQGAN LGIQQPLPDE STTTKSHEDP
     ITEIEWGVSN DEPRPTVVDD ETIILDLDGW QNLVKDEEDL CFLRHVLDGQ SRSKVGNLSA
     WAWRQKEIKA LNRAGESGPV HQETRIPDYY VCNPTGAART EGRKRILESE KSKYLPHRIK
     VQKAREEREA NAKSDPHASS AAEAARISAA KTISKSTSRS TRVNNRRLVA DINAQKQALP
     MQGGDGDVLR FNQLKKRKKP VRFARSAIHN WGLYAEENIS ANDMIIEYVG EKVRQQVADM
     RERQYLKSGI GSSYLFRIDE NTVIDATKRG GIARFINHSC TPNCTAKIIK VDGSKRIVIY
     ALRDIGRDEE LTYDYKFERE WDSDDRIPCL CGSTGCKGFL N
//
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