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
//