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Database: UniProt
Entry: A0A1C1CVA6_9EURO
LinkDB: A0A1C1CVA6_9EURO
Original site: A0A1C1CVA6_9EURO 
ID   A0A1C1CVA6_9EURO        Unreviewed;      1406 AA.
AC   A0A1C1CVA6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   02-APR-2025, entry version 27.
DE   SubName: Full=JmjC domain containing protein {ECO:0000313|EMBL:OCT52422.1};
GN   ORFNames=CLCR_09447 {ECO:0000313|EMBL:OCT52422.1};
OS   Cladophialophora carrionii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT52422.1, ECO:0000313|Proteomes:UP000094526};
RN   [1] {ECO:0000313|Proteomes:UP000094526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA   Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA   Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:OCT52422.1}.
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DR   EMBL; LGRB01000008; OCT52422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C1CVA6; -.
DR   STRING; 86049.A0A1C1CVA6; -.
DR   VEuPathDB; FungiDB:CLCR_09447; -.
DR   VEuPathDB; FungiDB:G647_03823; -.
DR   eggNOG; KOG0955; Eukaryota.
DR   eggNOG; KOG0958; Eukaryota.
DR   OrthoDB; 9547406at2759; -.
DR   Proteomes; UP000094526; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:TreeGrafter.
DR   GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR   CDD; cd15571; ePHD; 1.
DR   FunFam; 2.60.120.650:FF:000024; Putative jumonji family transcription factor; 1.
DR   Gene3D; 2.60.120.650; Cupin; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR055500; DUF7072.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10694:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR   PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   Pfam; PF23258; DUF7072; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094526};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          246..409
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          490..612
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          44..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          942..993
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1013..1078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1109..1215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..448
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..856
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..881
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1015..1031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1047
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1064..1078
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1127..1163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1174..1188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1406 AA;  156375 MW;  6B09983B8EE0DC09 CRC64;
     MVKTIKIKNP ITQEFHGAQG IYTQRNMEKM RSYNLPQWKA LCEQTENQPP AKRGEKRLNA
     DKLLGRGSVR GKKKEASATP EASQRRGSRA PTVTVKEEPA DQDSTLLAPP TPTSPEVKPA
     ALENEDKDDE ATSHAAAIPT PAKRPRGRPP GSGKPRGRPP KNAGAKKEAS GHAKGSETTV
     AARRLRNAQA ANDEIDEEAF QDFDYRVYDN DQWTAERCDE LEDKYWKSLN FSNPMYAADM
     PGSLFDNDTK EWNVAKLPNL LDLLGAPIPG VNTAYLYLGM WRATFAWHLE DVDLYSINYI
     HFGAPKQWYS ISQKDAPKFE AAMKSIWSTD AKACDQFLRH KTYLVSPSIL KSKFGVTVNR
     VVHREGQFVI TFPIGYHSGY NLGYNCAESV NFAIENWLQY GKTARKCQCE ADSVFIDVDW
     FVRKMNGEPS PEFEEVEVTD DEEDDEPTDL PTPPSDKIKI KIGMKRKRGQ KEPGPNKKLK
     KIKIRKISKN QPCCLCPNDF SWEELLPTSH GQRAHRTCAM YTPETYIATK DGKEMVYNVE
     NISKDRLELK CHECRQKKGS CFQCSSAKCT KAYHATCAMQ AGVQVDKGPI AVWHEGVEYR
     DIGFDWRCRL HRTVKRTRIT SEMSACNHAN SCWKNTEFRH FLFNLKEGEL IQFQATNSDD
     IEAGLVIASY DPGQDSVLVK VLPDLKQVKE VEPTAILFVD SATSCLQRPS VNALDLPEDL
     QGKTASLPES TEKKPSPGDL FTETPRTEWE EFVAAAPPLN SAQKPVNLAK EKQLWLYLGD
     KSTDTKASYT ADADKPVHDP ASNFLDLVMP PKPIMAPPPQ PKRQALSASY PSANVAAKNA
     APANTRQTIQ QKQGQQIPKY PTLPGTFSGT THNLTGSSQA KPIQMKPAQY KDITTAQEAR
     INEQARILQR QQAKAQQLAS AEHRPNSMGH SSIGVDHDAV QRQRQFQQTA SQHAKHMKEW
     SNDPSLPPLN QYEPFPSFDA LDNGGRYGPS TMTSNMRTQQ YQYSTDWMNP AAAGRSSSVD
     YPPNTGLNSV LPQYGQPQSP AASPFPSYVQ QSHLQFPYQG HADPTPQTSS GPSTPYQQPR
     LESIRAAASQ PPLPPPSAEV ERQRRISNPA YPFKSPDQIK AQKEAHQNSP PGSRPGSSYM
     LSSPAMQQQQ SFNVHSGSSS ASPAIQPLDP QNPPQFINPN ATQISPPGSS AGRRSTRNSF
     STVLGLGSGT SASTHMGLRR THSMDMMDLD MIHDMAPFPA ANLNSMQMQV SNYIAKRSIF
     DPLNPVNTTG PIGQLHKSAQ IMPQLIPQAQ LAPSLPPMAA PSPLLLQSLE KRPLAPSGLL
     DNDRPIPPQL AEWQARGGFW GKVSAYYIQK HQGMASVYTS PFRKMDEKQS AWDGKEKGLA
     ERYFEGLDWE LKAKVDEIRG QMGRRP
//
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