ID A0A0F2MK23_SPOSC Unreviewed; 1481 AA.
AC A0A0F2MK23;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839};
DE EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182};
DE AltName: Full=SET domain-containing protein 1 {ECO:0000256|ARBA:ARBA00030093};
GN ORFNames=SPSK_05816 {ECO:0000313|EMBL:KJR89190.1};
OS Sporothrix schenckii 1099-18.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR89190.1, ECO:0000313|Proteomes:UP000033710};
RN [1] {ECO:0000313|EMBL:KJR89190.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR89190.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT "Comparative genomics of the major fungal agents of human and animal
RT Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL BMC Genomics 15:943-943(2014).
RN [2] {ECO:0000313|EMBL:KJR89190.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR89190.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25480940;
RA Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA de Camargo Z.P., Felipe M.S.;
RT "Asexual propagation of a virulent clone complex in a human and feline
RT outbreak of sporotrichosis.";
RL Eukaryot. Cell 14:158-169(2015).
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|ARBA:ARBA00002789}.
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 -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC {ECO:0000256|ARBA:ARBA00011755}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJR89190.1}.
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DR EMBL; AXCR01000001; KJR89190.1; -; Genomic_DNA.
DR RefSeq; XP_016591866.1; XM_016732527.1.
DR GeneID; 27667804; -.
DR KEGG; ssck:SPSK_05816; -.
DR VEuPathDB; FungiDB:SPSK_05816; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000033710; 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: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; cd20072; SET_SET1; 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; 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; PF11767; SET_assoc; 1.
DR PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 3.
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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KJR89190.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJR89190.1}.
FT DOMAIN 1339..1456
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1465..1481
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 159826 MW; 72A9566278B7C00A CRC64;
MPPASGAGFA QFFPAAPRAA RDRATAIERE RASKQRATGS PGPRDSPSAP SARPSGDDEE
SLPGEGQSTA AATSPPMTSS SIARAGASSG SAASASASAS ASNPPSTSSS NGASYLTPLT
ADHSPSSTSI PHQQQQLQSG ASHHPNQAIN GWPSNKPLSA SSTTTSPNRQ PPPPPPPPPP
PSQLVPTPTS SSSLSDHMMA NGLNPSIGLD TLLGDRVPAR DPHRLVQGIA CVYDPQLPDD
KNTVSNFDLK RRGKHVLKEF GSEDDAPPAD PRLAKGGRLN YINVDFHLAR ARLRHTPYDL
KPYVYDPRTS LGPGPPTQVV VSGFNPLVPF SKIIAMFASF GDIAESSNKM HPETGSYLGF
GTFRYRDTKP SRSRPVPVSA IDAARRAVRQ LNGSRVEGTP VRVEYDPDGR KSSRMLETTL
RKDREKEMKA NAVRIPVAPR GLGVPANLRP PPTAPRGPAA LRMQQAPGAL APAAATAAAA
AAAVAGAGVG VGATAGPGAG PKAGMGSAVP RGPAVIAPAS AATIPDGPPG QCIEKNPIAP
RLPHTPFIFI SCDHVPVVFQ TIAHMRRRLK MQHFEEIRAD LSGYFVVFRD SATGKHDAER
CFQTANRTAF FTYELVMKLY ARGYSGGSLE DKAGTTSGLK NRRSHSPAPE KTEEQLLRDE
KAQMRKDEEA DLEEEKKQRA KNFDPVRAAV ETVRLELVEH LIRHIRADVA APLLFNYLDP
ANHDAKRRLH NIGGARLSAL LFDEQDGGER RKKPSPISTP NSRADPIERR TGRLDVAALP
RIRKAKGAKK LAAVRKQGLF DPFARQRTQD TSSRSAFRSL HYRLKDDSDD DSEDETENRF
SIGGRDTEEP ESRASEAERE AAEDDDDDDT DAEGRALKKT LAGQWTGRDE DSMTEASFSA
TPAESESTAT PATTVHTATK APVKKRKLEL QMEAALKRQK RNDEDLFGVS IGAVETKFRA
DVTAPKTEDM VIDDGVAAPR TTKSSTPAAA VSDEADKKKK PVSKKTKKTK KQILEERRAA
DEEGLRDQSN QKVPPVSEAK AVKKTDETPE PGALKGKLPA SVPASKTKGK AVKASTPAAA
PVAPLKAGRT PQEIAEFVDQ RRTMDPALYG DTLTRSLATP SDFRPSLDIL RTLSLHKADL
PDAERLAKKY STLLNSISSA KASDNKPASI SDFEMFLWKH ERVTRLNADE QSMIDAAMAE
KGNSTSAAAS AAAAAAAEAA IKDALNRPRI EGYYVPNSTG SARTEGVQKI KNSEKSKYLP
HHLKVKKARE EREARAGKAG KAAAVAAAKV ATEASASRGS SRANRVNQRR YIADLNDQKR
TLGQDSDVLR FNQLKKRKKT VKFARSAIHN WGLYAMESIP KDDMIIEYVG QEVRQSVATI
RERAYIRAGI GSSYLFRIDD ATVIDATKKG GIARFINHSC MPNCTAKIIK VEGSKRIVIY
ALRDIAQNEE LTYDYKFEPE DNPEDRVPCL CGTTACKGFL N
//
