ID W6MHV4_9ASCO Unreviewed; 759 AA.
AC W6MHV4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=JmjC domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=KUCA_T00001362001 {ECO:0000313|EMBL:CDK25393.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK25393.1};
RN [1] {ECO:0000313|EMBL:CDK25393.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK25393.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK25393.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK25393.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR EMBL; HG793126; CDK25393.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MHV4; -.
DR STRING; 1382522.W6MHV4; -.
DR HOGENOM; CLU_000991_4_0_1; -.
DR OrthoDB; 48111at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.1150; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 8..51
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 162..214
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 312..486
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 667..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 87968 MW; 037B634DEFB5B919 CRC64;
MASQVSKGFI LSPTAAQFAD PIAYLSCPEV IRAGQEYGIL KVIPPKGWNP PLSVDPERFS
FITRMQKLSE LNMRNRSREF WLQGFSNYMK MRKKKVPNEK GMVRLLNGES IHLYDIFVDD
DPRRFEEDLE DNRMVKLVLD YKAVLNNSGK KASSNSDSRK RSTACEVCHS KERQHRLLLC
DGKDCDKMYH LDCLSPQLTS VPKGLWFCED CILGGSHEYG FEEDMDSVFT LSEFQEHCKE
FEDEYVKKKW QNERYGPSIH QLEGEFWRLV ESQDDLEVRY GADIHQDDPS QISGFPIRKN
PDIDVENSKY SPYLDHPFNL CNLPFSNGSV FNYIKDEEIS GMTVPWIYVG SLFSTFCWHK
EDHYTLSANY CHAGATKKWY GVPAKHSDAF EKAFRSIAPA YFQRQPDLLH QLVTLISPDE
IIKTAREKFG EEIEITTLNQ QANEFIVTFP KVYHAGFNCG YNFNEAVNFI TSDWLKYGYD
ALQEYKTIGK ENVFNHWKLL ERILNDALHT PDDVLISKLE DKRFATLLEW TTKNFKEEYA
KINKCIFEDE KMSRVVDGIT DVKFADLLTT ETVDDSPRRI RRRMTRMAMA GSKGHSDELL
CHECKTALGF VWFEVDPSKA VKQEQLPTPK TTPVLNSESK SFEDINMDRE TEFQRIIEEA
KREDSLEAGE DRRKLRRVAR SKDDNNSVPR PVGRPRKNKD IPRLLCVNDF KKLQALKVFL
SSGDLDAAKF EQLNKSTTVY YDKFVLAMTR IQEKLGKLL
//
