ID   A9V3N8_MONBE            Unreviewed;      1048 AA.
AC   A9V3N8;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Histone-lysine N-methyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MONBRDRAFT_33094 {ECO:0000313|EMBL:EDQ87845.1};
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ87845.1, ECO:0000313|Proteomes:UP000001357};
RN   [1] {ECO:0000313|EMBL:EDQ87845.1, ECO:0000313|Proteomes:UP000001357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CH991557; EDQ87845.1; -; Genomic_DNA.
DR   RefSeq; XP_001747378.1; XM_001747326.1.
DR   AlphaFoldDB; A9V3N8; -.
DR   STRING; 81824.A9V3N8; -.
DR   EnsemblProtists; EDQ87845; EDQ87845; MONBRDRAFT_33094.
DR   GeneID; 5892713; -.
DR   KEGG; mbr:MONBRDRAFT_33094; -.
DR   eggNOG; KOG1081; Eukaryota.
DR   InParanoid; A9V3N8; -.
DR   OMA; HDNNITD; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046975; F:histone H3K36 methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd00084; HMG-box_SF; 2.
DR   CDD; cd15568; PHD5_NSD; 1.
DR   CDD; cd05838; PWWP_NSD_rpt2; 1.
DR   Gene3D; 2.30.30.140; -; 2.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 2.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22884:SF514; DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00398; HMG; 2.
DR   SMART; SM00249; PHD; 4.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR   SUPFAM; SSF47095; HMG-box; 2.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 2.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50812; PWWP; 2.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1048
FT                   /note="Histone-lysine N-methyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002742643"
FT   DOMAIN          26..66
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   DOMAIN          149..223
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DOMAIN          244..304
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DOMAIN          439..485
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          523..574
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          579..640
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   DOMAIN          714..762
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          764..881
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          889..905
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DNA_BIND        149..223
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   DNA_BIND        244..304
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          119..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  116380 MW;  CE425C5EC8503D62 CRC64;
     MGRRRRCVLV LLLARAAQEV AAVARAGVLV WVQHASFPWW PGMLTYDPHS GEFTRESANH
     RAYHIQDGGL DPTLLKVGRL SPKLANERAA ALQQAHAVAE LSLRERILRW ACDFKTERGD
     KAKPKLEESD KDQATAPGTV SAPPRKIGVP RSKTAYQFYL DHRRADVMHN LDDDGTSKFA
     RNGKVTKLIA AEWQTLTADE RLPFDKQAEK AKKQAISKAQ EMRAELEKSE PVTPERTASL
     KPAVPRTKTA YMFYLDHRRA DVMKGMDDDG TSKFARNGRV TKLIAAEWKA LSEEARAPFV
     EAAEIAKKTA IARTLELAQA DASCPDSPGD RPPPMVAAFR LFAQDFLAKA QDSGDELVHL
     DSADQGLRVH EKWMALTRTQ QRAFVRRVQP DALPNKSGAS TAAASPSASV SPDEDQASNE
     GQPAAKRSRS SRTTMTANDD TCRICGELGQ LICCDGGCRG AFHLECLSIL QPPTGEFRCD
     ECSTGNHTCY TCDKVGADLI KCQFPHCNKL YHRGCAEKQF KADNFCLVCG TGGDLVVCDG
     CPGAYHAACI KSTFAFTGKP DEQGQWFCHD CLTGTKSMIH DVVWAKYGSY RWWPAVILSA
     TEYPERCGQS PAEGNFLVKF LGSNDVAWVG HESIIPFSNG DQKNSYFTRN LKAAKKSFQE
     AVTLALDLFT ERKQEREDQL AAIRGKIIER PPRFKLIKRN VYLPPAAKPP HRKEEQEICR
     CDAALNCADM HSCLNRMMYI ECDAKCCNNG KNCRNQRFQR REYPKLIPFK TEHRGWGLRL
     GQDVEEGDLV IEYVGEVIDG AECRRRIDQY EERNTSSFYI LSLGSDTFVD AREKANMARF
     INHSCDPNCV TQKWNVLGET RVGIFAKRAL AKGTELTFDY MLDCLNSVKK TPCHCGAPNC
     SGFIGVKPNR SGTTYEDLDR TDDECFICKD GGDLLMCDKK NCDKVYHLAC LGMNKVPAGK
     FICPHHACLK CGRKATIFSE TGPEAYCSMK HIATPEVRAL CEGKRPPVTF KSPVPVLPAV
     FANGTWAKRA KRAKADPTST TQAQAASA
//