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Database: UniProt/TrEMBL
Entry: C4R217_KOMPG
LinkDB: C4R217_KOMPG
Original site: C4R217_KOMPG 
ID   C4R217_KOMPG            Unreviewed;      1020 AA.
AC   C4R217;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839, ECO:0000256|PIRNR:PIRNR037104};
DE            EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182, ECO:0000256|PIRNR:PIRNR037104};
GN   OrderedLocusNames=PAS_chr2-2_0494 {ECO:0000313|EMBL:CAY69541.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY69541.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY69541.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(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:0000256|PIRNR:PIRNR037104}.
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:0000256|ARBA:ARBA00000944,
CC         ECO:0000256|PIRNR:PIRNR037104};
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC       {ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037104}.
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DR   EMBL; FN392320; CAY69541.1; -; Genomic_DNA.
DR   RefSeq; XP_002491821.1; XM_002491776.1.
DR   AlphaFoldDB; C4R217; -.
DR   STRING; 644223.C4R217; -.
DR   EnsemblFungi; CAY69541; CAY69541; PAS_chr2-2_0494.
DR   GeneID; 8199075; -.
DR   KEGG; ppa:PAS_chr2-2_0494; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   HOGENOM; CLU_004391_1_0_1; -.
DR   InParanoid; C4R217; -.
DR   OMA; ERLPCLC; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000000314; Chromosome 2.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd12302; RRM_scSet1p_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 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; IPR048669; SET1_RBD.
DR   InterPro; IPR024636; SET_assoc.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   PANTHER; PTHR45814:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF21569; SET1_RBD; 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; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS51572; SAM_MT43_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037104};
KW   Chromosome {ECO:0000256|PIRNR:PIRNR037104};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR037104}; Nucleus {ECO:0000256|PIRNR:PIRNR037104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000314};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR037104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037104}.
FT   DOMAIN          878..995
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1004..1020
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1020 AA;  117656 MW;  D9FB272123580A4A CRC64;
     MSYNRSYHDG YGRERTSNMR PSYNEYSDWD DFSWEKEDPH SRRYGSRPSS YIYNNPRPNA
     DRPNGSIRNH VNRTARAPRN STQGLKFQPI PEKYQNISYN VDMFPRQLHH VDEFRKFTNS
     IVSTQRNFRI VYDPEVKKDK RKGNAILIKK QEESDPKVLI DPRKELSSYP HIQRSDGTKS
     AKRMFRSLLP TKHTYDSASV GPPPTIEIII HGLSPSTAQT VLKNNYKRYG PIADCRAVVD
     PVTAVPLGLF VLSFSGKIDE AHTSCLKALN AAKDGVRVNG GVPRTTLFSE SRLNEIKHKI
     IKQNENKRQA EVSEQQRLEQ ERKLQDQRRL QYEKEQELKR QRGSLRIKKQ EEDQQRIISK
     QLLNNTELSN IFHSAMKDES HNQTLYTRNG NNGRHHRLSK VVDDAIRKRP YLFISAKFIP
     VRDVPAREIM NLLRNYPWKR VLTDAEGFYV VFDSIKEAEK CLENEDGRKF YQRRLYMDLV
     IHPDFMEDKT ELGVEQSISD QSTSIISSEL ERYLIKDIKD KIIAPTILEM LRAENFSVEI
     ESALKKKKDL EEKVSEPYTT ATTVSPVTDS FTSFKLPTLP SFRKSNISKK ESSSRKKQKL
     GTRKRYHALP MTHVLNFDSE GETDEHDSGP ETPNGVLMSM GPNRLLSERK QSFISDSSTS
     EDESEVERDS EITTPEKHLG EKSNEQELAL ETSDDKAELK NNWIMYDPKY RPTTFIRPVG
     ELYDAKTIDI PRLKKLIEDD EDLKLAQKLF SDINPDHSIP CVAYWIWNNL RAFTESSNLP
     NSLGPMYSNQ SGSFKSEGYT KIPDTEKSEY LPHRRKIHKP LNTVENDDEA ANPNPKLQSS
     RVNRANNRRF AADINAQKQM LNSETDILDL NHLTKRKKPV SFARSAIHNW GLYALEPIAA
     KEMIIEYVGE ILRQKVSEVR EKKYLKSGIG SSYLFRVDED TVIDATKKGG IARFINHCCQ
     PSCTAKIIKV EGKKRIVIYA LKDIAANEEL TYDYKFERED NNEERIPCLC GVPGCKGYLN
//
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