ID A0A093UZ12_TALMA Unreviewed; 1169 AA.
AC A0A093UZ12;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=GQ26_0240410 {ECO:0000313|EMBL:KFX45185.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX45185.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX45185.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX45185.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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, 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|ARBA:ARBA00011755, ECO:0000256|PIRNR:PIRNR037104}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037104}.
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:KFX45185.1}.
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DR EMBL; JPOX01000024; KFX45185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093UZ12; -.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_004391_1_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
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 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; 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; 2.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF82199; SET domain; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR037104}; Nucleus {ECO:0000256|PIRNR:PIRNR037104};
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 1046..1164
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 19..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 529..556
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 103..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 131181 MW; 7B98A3CA19B68038 CRC64;
MSRLSAGFAD FFPTAPSVLQ SRKSRISENR TRSRSQSETS NGLAQPVAVA TKNALLTHGK
DEDDMRALLL QNDASAKNIN RSTTLISVDS DLSAHAIATE LPTMNGNGSL QQTSVTQSPS
QSLSRNANSL HEDQPSSSRS AIDIKHNEPV GNSPAPGRSD VTAETSSSGI RASLPCELKG
RKVTYDPELD RKLGTKDKRK KLEYSDFVQT DRFQVPADPR LSIANYTRGS ANAQKVRLRS
TPYSVRHWPF DAATSIGRAA TSQLVVTGFD PLTPIAPITA LFSSFGEVAH IDNRTDPVTG
RPLGICLVKF KDATSFQNQG PLSASAAARR AYYECKKEQR IGTRRIRADL DRDGLLCQRL
VDKAVESWRK SNPPSLDSGH RDTPPKNNEP PPTAPKGPSG RSSVRPAFNP PEGPKAASKP
VVSPAIEETP ILQQIKRDPY IFIAHCYVPV LGSTLPHLQK RLRTFDWKAV RCDKTGYYII
FENSRRGEEE TMRCYKMCHM TPLFTYIMNM ESQPYGNPNY ERSPSPERLQ AELKARAEEK
RVLREAELEI EEEKQQRASS LDPSKEVLSI VIHELKTKLL EDVKFRIAAP FLYEYLDPER
HSERRKVLGI QDPETRKSNP FQLGLPSNSL HSRPLDLLAL PRIRKSYHDQ VNGTNYLDER
RGHIRRRRDV RPLHHRLRHL HAAGDSDDDM RTPMSRDTDE LGSRSPSQMS FDTSVSDTED
EAYNIYASRS PSEDPEATDY VNTADVDSEP HDELMFQQVD PNLSKKRKRT FEDGLDSRKR
HKDDYDITGI DAITLDVDVP PGSFDTVCTD DDLILRSAEI SLGMCTLKIP TFQEYCSSLA
EAETNIYSKP EVNFEVSFDQ PRPSVLDDDA LVLDLDGWQT LIKDDEDLDF LRDIMSDTLP
SKVGDITIWA WKQREAKLLN RFGETGPVFT PTTIPGYFVP NSTGSARTEG KKRIFEAEKS
KYLPHRIKVQ KAREEREALA QSDPQSVLVD SAKAGPTKPV NNSTSRSTRV QNRRLAADIN
AQKQVLPPQG GDGDALRFNQ LKKRKKPVRF ARSAIHNWGL YAEENITAND MIIEYVGEKV
RQQVADMRER RYLKSGIGSS YLFRIDENAV IDATKRGGIA RFINHSCTPN CTAKIIRVDG
SKRIVIYALR DISKGWSFGS STWNSKPPC
//
