ID C1GFP2_PARBD Unreviewed; 813 AA.
AC C1GFP2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Histone-lysine N-methyltransferase ASH1L {ECO:0008006|Google:ProtNLM};
GN ORFNames=PADG_06078 {ECO:0000313|EMBL:EEH49999.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH49999.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH49999.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH49999.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KN275963; EEH49999.2; -; Genomic_DNA.
DR RefSeq; XP_010761331.1; XM_010763029.1.
DR AlphaFoldDB; C1GFP2; -.
DR STRING; 502780.C1GFP2; -.
DR GeneID; 22584881; -.
DR KEGG; pbn:PADG_06078; -.
DR VEuPathDB; FungiDB:PADG_06078; -.
DR eggNOG; KOG1083; Eukaryota.
DR HOGENOM; CLU_004379_3_0_1; -.
DR InParanoid; C1GFP2; -.
DR OMA; NCQNRYM; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000001628; 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; SM00508; PostSET; 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 Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 368..415
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 426..542
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 550..566
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 89907 MW; 5B835C03FB5E0F90 CRC64;
MARSSQSSAV APSSSSTPSS RPGSDTGLTT EISADEHLLT PPTSQSETSS RSGGAMDVEE
KDGEEVVSEE TISQRVTRSS LANEENNMVS EEMASKVDDA KEVAFHPLRS NPPEVDGGLP
TSEGARANIE MEHQLDKNEE GKNARGAKKR HKSESGSRRR SSRLALLGKI SEVVSKVSTV
LGKRAREDVM KEKDKLEIIN RRASLRSRNV AQEERVPSTT STAVATADGP VTKKRRVSKG
DAVVLNKKAS AASTTVKEQK LATVTYKRKK WLSHGLYAGQ DRYFDPRLTE EKNRIKFGKK
NEEERNKLFP LPMFAGERLI KDGRDFKLPF DIFSPLPPGQ PKPDEWRKTN KNVFVGDAAS
IWKANKLGEC STCMCTPESG CDENCQNRCM FYECDDDNCK LGAELCRNRS FEDLRQRIKA
GGKYNIGVEV IKTADRGYGV RSNRTFAPNQ IIVEYTGEII TQKECERRMR TVYKNNECYY
LMYFDQNMII DATRGSIARF VNHSCEPNCE MEKWTVAGKP RMALFAGKNG ITTGEELTYD
YNFDPYSQKN VQECRCGAET CRGVLGPKSK DSNKSRSVKQ GNTKQSSKDA KKKAVSSKSG
QALIGKKRKQ ETALDESSTS RLNKRRRVLK QTSKAFNAGI KKAVAGARLA ANSSTKAKVR
GKAKAKAKIN AATAVKAKPA PVKKTKDNSR SKTTTKSTNA RWGGRKSKIQ AETGTSVRKQ
RDRTKLNRPS KKLNSIAVSR TTSRTPAIMR RFLEAGKLAT EYEIDGTLTV DKPGSKRVVA
KRRYTNNNAS KQSKIKGTVT GVAGKVKRGR SSV
//
