ID   W0THW8_KLUMD            Unreviewed;       826 AA.
AC   W0THW8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Histone demethylase JHD2 {ECO:0000313|EMBL:BAO41724.1};
GN   Name=JHD2 {ECO:0000313|EMBL:BAO41724.1};
GN   ORFNames=KLMA_60433 {ECO:0000313|EMBL:BAO41724.1};
OS   Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS   (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1003335 {ECO:0000313|EMBL:BAO41724.1, ECO:0000313|Proteomes:UP000065495};
RN   [1] {ECO:0000313|EMBL:BAO41724.1, ECO:0000313|Proteomes:UP000065495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275
RC   {ECO:0000313|Proteomes:UP000065495};
RX   PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA   Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA   Matsutani M., Murata M., Fujimoto N., Suprayogi, Tsuchikane K., Limtong S.,
RA   Fujita N., Yamada M.;
RT   "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT   complete genome sequence and transcriptome analyses.";
RL   Biotechnol. Biofuels 8:47-47(2015).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR   EMBL; AP012218; BAO41724.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0THW8; -.
DR   VEuPathDB; FungiDB:KLMA_60433; -.
DR   OrthoDB; 48111at2759; -.
DR   Proteomes; UP000065495; Chromosome 6.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd15489; PHD_SF; 1.
DR   Gene3D; 2.60.120.650; Cupin; 2.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR011011; Znf_FYVE_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   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 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; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:BAO41724.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transferase {ECO:0000313|EMBL:BAO41724.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00146}.
FT   DOMAIN          4..47
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          289..344
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          443..611
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          128..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..290
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   826 AA;  95684 MW;  9836FE5B116B7703 CRC64;
     MQEIPTLRPS EEEFKDPIAY LSSPTVKKLG IKYGMVKMIP PAGFKPHFGI DEEHFTFKCR
     LQTLMELDIE NRSRLLFWKQ LNNLKRSRGD SKLLASAEVS IKGQSEPLYY YDIYKTVVRY
     FQTSATGGYP NHEQEDNSDG YRKSNNRSRS RRKRQRNGTP FADEGQGSFF PLVNPRDMMK
     DQKAWDAIAK QLAPSNPLEL KRVFTAHILP YYRFLYNQIL AKGEANNTHI SRLLYRYDYP
     KSLLEEENST ERSEDENEEV LPGEELDYLD SDTDVQEEED ADDDDDDEDD KCPICSRMVS
     KSSSHKTCNS CESKFHNKCV DHINNSNVKP SSVKEWICNT CIIGNGYYGF KEPSSLFTLK
     SFKEYCSQFD EKLFDGNKPT DIQSLEKMFW KHVESMDSNP LTVRYGADIH NNKPGQTSGF
     PTTEYVPSSI KNEESEEYKN YLEISAHPWN LMNLPRAKGS LLSIINRKIS GMTIPWIYVG
     STFSTFCWHL EDQYTLSANY QHAGSQKVWY SIPERDTATF DEMMKSISPD LFERQPDLLH
     QLITLISPYS KRFTDSGISC YKAIQNPGEY IITFPKCYHA GFNCGFNFNE AVNFTLDLWL
     PYGQESINDY KLAKRTAVVN IFDLMSNVLN AYLRSPESFD ASFVSTCAVE LKEWFNREFK
     NMAKVKDIVG ETLFSDGCKE TYINSRLDSS HKEIKSEKVS DFKLADNDDE EDDLDVFCSK
     CKTICPIGFV AHSKTKRLRS KRRNLTAMTP NEWNQLSAEG VIDIYCLEDY LSYVTEIDEQ
     EESEDDSENQ TSNDHFQNDI LFYFREDDEI RKLIIQVERA LEKRLR
//