ID A0A367XYT5_9ASCO Unreviewed; 738 AA.
AC A0A367XYT5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Histone demethylase JHD2 {ECO:0000313|EMBL:RCK58773.1};
GN Name=JHD2 {ECO:0000313|EMBL:RCK58773.1};
GN ORFNames=Cantr_07151 {ECO:0000313|EMBL:RCK58773.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK58773.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK58773.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK58773.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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:RCK58773.1}.
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DR EMBL; QLNQ01000027; RCK58773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367XYT5; -.
DR STRING; 5486.A0A367XYT5; -.
DR Proteomes; UP000253472; Unassembled WGS sequence.
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; cd15543; PHD_RSF1; 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; 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 Methyltransferase {ECO:0000313|EMBL:RCK58773.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000253472};
KW Transferase {ECO:0000313|EMBL:RCK58773.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 11..54
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 177..227
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 323..489
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 643..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 85638 MW; FC20D7092354A196 CRC64;
MSFNKSLLTP CPVLTPNEEE FNDPVGYLSS AAISELGATY GIVKIVPPPN WKPSFHINPD
FKFHVRKQVI SDLGITTRSR DFFRENINRF LKMRRKRQLK LFFEVEGTKV YYYDLYRDVE
EMGEPMDEPK WQALSAKFGV DLESIKREYE NSIKYYANYL HHNTSYEFPD SDSEDEYDNC
LICGQHDHPL ETLLCDNCDN PFHMKCLNPP LTVVPATNWY CDKCLIGTGE YGFDEDVDVK
YTIPEFYKMC QEFDAKFAKE YNDGKPLTVD AIEEKFWSFV DIEKSDLEVM YGADIHNSKP
GEISGFPMSD TPNLDTSNPL IQYYINHPCN LNKLPLAKGS LLNFIDTSIS GMTIPWIYVG
SLLSTFCWHV EDHYTLSANY CHFGATKKWY GIPSVYADKF EKLMKDAAPD LFKRQPDLLH
QLVSLMSPTD LVANGIPCVY ADQNPNEFVV TYPRVYHAGF NCGFNFNEAV NFATDSWLEF
GEKSVRDYRP IKKENVFNHN ELMENILVKY NKDRDVRVDL VRRSLNSFEK FVKSQSELLS
RLKGKFEVEV NHHEIVDEEC LCDYCKTHLS YQYCILLPKK PHRRIAITQL LTPESSPQDA
QLKKEMEQTK VDELANSEAS QNLSKLNREP VAELDEFQSL IEKAKQESKT KEEKEAAPAR
RRSKRLLTLK EKEEPPKKRA RMGKITKKKE PNAPNREPRL CLQCVCSLDE KLQHGKLIYR
KQIPVLEELI NETRKNLE
//
