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Database: UniProt
Entry: Q5B0Y5
LinkDB: Q5B0Y5
Original site: Q5B0Y5 
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   16-JAN-2019, entry version 114.
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=AN5795;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community 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}.
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; AACD01000098; EAA62888.1; -; Genomic_DNA.
DR   EMBL; BN001305; CBF81174.1; -; Genomic_DNA.
DR   RefSeq; XP_663399.1; XM_658307.1.
DR   ProteinModelPortal; 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   HOGENOM; HOG000181654; -.
DR   InParanoid; Q5B0Y5; -.
DR   KO; K11422; -.
DR   OMA; PNSRADP; -.
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; 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   1220       Histone-lysine N-methyltransferase, H3
FT                                lysine-4 specific.
FT                                /FTId=PRO_0000269773.
FT   DOMAIN     1078   1195       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1204   1220       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
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
//
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