ID   D4D4K2_TRIVH            Unreviewed;       709 AA.
AC   D4D4K2;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Histone-lysine N-methyltransferase (Ash1), putative {ECO:0000313|EMBL:EFE43204.1};
GN   ORFNames=TRV_02019 {ECO:0000313|EMBL:EFE43204.1};
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE43204.1, ECO:0000313|Proteomes:UP000008383};
RN   [1] {ECO:0000313|Proteomes:UP000008383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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:EFE43204.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ACYE01000105; EFE43204.1; -; Genomic_DNA.
DR   RefSeq; XP_003023822.1; XM_003023776.1.
DR   AlphaFoldDB; D4D4K2; -.
DR   GeneID; 9582397; -.
DR   KEGG; tve:TRV_02019; -.
DR   HOGENOM; CLU_004379_3_0_1; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR22884:SF512; N-METHYLTRANSFERASE (ASH1), PUTATIVE (AFU_ORTHOLOGUE AFUA_3G06480)-RELATED; 1.
DR   PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EFE43204.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFE43204.1}.
FT   DOMAIN          366..413
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          424..540
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          548..564
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   709 AA;  79062 MW;  0D9262ECE27E54E0 CRC64;
     MSRVARESTT STSITPDSDS TLLDSTGHTL TPATSVSETS SNVDVPVTEP VSQTKPPQTR
     RVTRAASTRG GIDNDTEHNG NKHGDALRGD ISASVSEGRT VVKREPARRP ERRSLRGRRG
     LPAGALEPCE EETTAEIQLE NTESNTGDEP IKEETGSRPQ SSTKVDPAQP RRRSGRLTLL
     EKTKTVLNQV SSILGKRQRD DKEYSKSKSK VEDRRSSLRS RAVVRKETQE ESATKKRRVS
     EDVSTPKKEK KVDQPPLSAP VQTVPKRKKW LTHGLYAGPN AFAKLELPGP QSKRKGTRQA
     PRERVLFPMP KYSGALLLEK GRPFRLPYDI FSPLPRGQPK PDEWRKINKN IFIGDAAGIW
     KATMPTEQST CLCTPEMGCE ENCQNRHMFY ECDENNCKLG EDLCRNRNFS ELRKRIKTGG
     KYNIGVEVIK TESRGYGVRS NRTFEPNQII VEYTGEILTQ IEAQRRMKTI YKKNECFYLM
     DFDQDMIIDA TRGSIARFVN HSCEPNCKME KWIVAGKPRI ALFAGDNGIM TGEELTYDYN
     FDPYSNKNVQ ECRCGTPSCR GVLGPRPKGK DSKEKSTVKP ASTRTKRKSQ GVTNSQASKK
     QKTTKQSSVK SGLKRVASKA SQGIKSQAKS IRVPKKRVGV QFNKSAKART TAAADVSFKS
     VSRSSRTSRQ AASSTKLRMP SRSRVRLAKT AVQTVLNGRG GRRTSARSR
//