ID   A5DVI3_LODEL            Unreviewed;      1156 AA.
AC   A5DVI3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 107.
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=LELG_01369 {ECO:0000313|EMBL:EDK43191.1};
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43191.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK43191.1, ECO:0000313|Proteomes:UP000001996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC   NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(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; CH981525; EDK43191.1; -; Genomic_DNA.
DR   RefSeq; XP_001526541.1; XM_001526491.1.
DR   AlphaFoldDB; A5DVI3; -.
DR   STRING; 379508.A5DVI3; -.
DR   GeneID; 5234168; -.
DR   KEGG; lel:LELG_01369; -.
DR   VEuPathDB; FungiDB:LELG_01369; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   HOGENOM; CLU_004391_1_0_1; -.
DR   InParanoid; A5DVI3; -.
DR   OMA; ERLPCLC; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000001996; 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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd22249; UDM1_RNF168_RNF169-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; IPR000504; RRM_dom.
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; 2.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50102; RRM; 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   Reference proteome {ECO:0000313|Proteomes:UP000001996};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
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          262..347
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          1014..1131
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1140..1156
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          365..417
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        27..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..675
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..769
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..983
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1156 AA;  131572 MW;  51B9D9B9DFE0543A CRC64;
     MAYGESYRSR GYRGDRGAGY YGDSSYRKPH SQRDDHGSSR SRLDDTRRNY SPSSGSGGFP
     SDGFNRRYAN KGRGSTYEKE DWSYRDKRRW HHSGAGVGAS GALANTSGKA TPLTNTSDRN
     SLDAVYSGTD TKTGVNRTDL EFTKLAHHTD FTNAITILNT DSSTPNNSSS SSSSSSNSKN
     YKVLYDPELD TSLSKAERKM KSKKLRFNGE GVPTDQLVDP RIANLSHYLL KPNKKSSKFP
     FKQLPQARFI YDSDSLGPAP LTTLVIWDLP ISVNMQYLKN YLGTYGLIEN IEIINDPNTA
     VPLGVATFRF KGTPEKSSDL ATKFVERVKI ELIKINGIAL KIGLNDSEDT LLNQKVNIAR
     GKIINQRLKR EQEEEKRRLK LQEEQKKQEE IAKKEAEIKK QQEIEEAKRR AAELKYKPNT
     TLLSSRHDHK VEEGVFLPNE LTKYIKNRPY LLIRDKYVPT KKVSSQEIKR TLKKYDWTRV
     LSDKTGYYVV FNSLKECIKC FEQEDCRKLF EFRLVMELAV PEGFEESQRG NDEADNDIIE
     EASNVLIKEF ESFLVKDIRE RIIAPHILKL LDHSHYPALV EELKAKEQQE AKAKIAATSN
     ASLKLNALSL LEKQKQNLKP KTKYFKQVED RFGSRKHGKK GAIIPMQHAL NDDDDDDDDH
     EDEDDDNDGE GASSDEDEIT SGSTTPMVRE PLKRVHSSSA TSIVDEFEVG EPERKKHKKL
     RKEMSTESDD EMESISGKNE EDTEDVKRDK KEEEEEEEAE KKEKSTEEQE PMDAEMDDVD
     QMSLDSKYRP TEKRPRTVYP ETTIPDTVDL RCLQEFIKDA EDLKFAQSIL GDVDVMESDV
     PVLKNIEYWA WKQGKNTNES EEIVERDEGF IDDEQEAEEI EEEPEEELPA HLESASGCFK
     SEGYKKIPDE DKNHYLPHRK RADKFIKTVQ YEEDDDEKAT EGSHSNNNSN SNNSNSINNG
     SSSTTTNNSN SNTNAAQSSR VNRANNRRFA ADITAQIGTE SDVLSLNALT KRKKPVTFAR
     SSIHNWGLYA MEPIAAKEMI IEYVGERIRQ QVAEHREKSY LRTGIGSSYL FRIDENTVID
     ATKKGGIARF INHCCSPSCT AKIIKVDGKK RIVIYALRDI EANEELTYDY KFERETNDDE
     RIRCLCGAPG CKGFLN
//