ID   C5PIP9_COCP7            Unreviewed;       742 AA.
AC   C5PIP9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=SET domain containing protein {ECO:0000313|EMBL:EER24402.1};
GN   ORFNames=CPC735_057720 {ECO:0000313|EMBL:EER24402.1};
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929 {ECO:0000313|EMBL:EER24402.1, ECO:0000313|Proteomes:UP000009084};
RN   [1] {ECO:0000313|EMBL:EER24402.1, ECO:0000313|Proteomes:UP000009084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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:EER24402.1}.
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DR   EMBL; ACFW01000049; EER24402.1; -; Genomic_DNA.
DR   RefSeq; XP_003066547.1; XM_003066501.1.
DR   AlphaFoldDB; C5PIP9; -.
DR   GeneID; 9692017; -.
DR   KEGG; cpw:CPC735_057720; -.
DR   VEuPathDB; FungiDB:CPC735_057720; -.
DR   HOGENOM; CLU_004379_3_0_1; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000009084; 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; SM00570; AWS; 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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          341..388
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          399..515
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          523..539
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..148
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..637
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  81822 MW;  68B23FA93A627716 CRC64;
     MARDPMLSPS STPTSSALDS DATAIDATVP VLTPATSISE QSTPVDTEKD GEHRAKKAKP
     SRRVTRSSLK NGELEANGGG EAMLTRPNDG SLDNTNTQED EDCTSLLNGA EDASGSVDKQ
     SGKNAKAAGK KPNKKAGNKS PKRRSTRLSL LAKTKDLAQS APSVLGKRTL DAISKSKDKV
     KTIDRKASLR PRVENERKEA STPAPQEPSP KKRRVSGDNK STCQVPRQEQ TATRENSLIR
     QKRKPWLKHG LYAGQEYIDS SVPKSKRGTR DAKNNGQQSQ VFPFPMYAGA RLLENGRAYK
     LPFDIFSPLP HGQPKPNEWR KANKNVFVGD AASIWKAAKI KEHSTCTCTP ETGCDENCQN
     RYMFYECDDT NCKLGSELCR NRPFSALRRR AKAGGKFNIG VEVIKTEDRG YGVRSNRSFD
     PNQIIVEYTG EILTQEECER RMRTVYKKNE CYYLMYFDQN MVIDATRGSI ARFINHSCEP
     NCRMEKWTVA GKPRMALFAG EDGIMTGEEL TYDYNFDPYS QKNVQECRCG APTCRGVLGP
     RPKESWKNKD KEKKSAPAAK RKVDSALDES ASRLNKKPKP SRASSLKTGV KKAVSKARTA
     LKSTQAKGKV KRVGRPAKKA ASIKPIPVKK RRSTLTRAKM PVKSASKSAE GDEKPPRNKG
     RKLKMPSKPR LGNSIAAARA SNKTPALMRK FLEAGDTKGG AKVVSDTIKP GRKIRAARTA
     DVRSSPDNVP VSRKRGRAKK TL
//