ID A0A1E4RQR8_9ASCO Unreviewed; 812 AA.
AC A0A1E4RQR8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=JmjC-domain-containing protein {ECO:0000313|EMBL:ODV69578.1};
GN ORFNames=HYPBUDRAFT_102980 {ECO:0000313|EMBL:ODV69578.1};
OS Hyphopichia burtonii NRRL Y-1933.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Hyphopichia.
OX NCBI_TaxID=984485 {ECO:0000313|EMBL:ODV69578.1, ECO:0000313|Proteomes:UP000095085};
RN [1] {ECO:0000313|Proteomes:UP000095085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1933 {ECO:0000313|Proteomes:UP000095085};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) 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; KV454538; ODV69578.1; -; Genomic_DNA.
DR RefSeq; XP_020078645.1; XM_020218236.1.
DR AlphaFoldDB; A0A1E4RQR8; -.
DR STRING; 984485.A0A1E4RQR8; -.
DR GeneID; 30992786; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000095085; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16100; ARID; 1.
DR CDD; cd15543; PHD_RSF1; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
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; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51011; ARID; 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 Reference proteome {ECO:0000313|Proteomes:UP000095085};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 13..56
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 79..167
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 185..235
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 330..496
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 704..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 94450 MW; ECCF271E1F266044 CRC64;
MPLSFDKSLL TACPIFRPSA EEFSSPIEYL SRPDIAAVGS KYGLVKVIPP DGWKPPFLLS
SDFKFHTRHQ KLSDLGLTTR SRKFFINNIN RFLKMRRKKQ INSYFKVDDK KIYYYDLYSS
VESHGGPDRL NDDIWSRINL KFGLPTDFKD LNIQYELNIK SYAQFLSTNS NKSYEFPESD
LEDDSANCLV CGKNNLPTTT LLCDNCNNPF HMRCLSPPLT SIPSGTWYCD KCLIGTGEYG
FEEPVEIKYT LPQFYQMCLD FESSFKQIYN NNQPLTIDLI EKKFWEFIDI EKNDLEVKYG
ADIHNLRPGQ ISGFPMSNTP NIKIDSNFES YIKHPCNLTK LPFAPGSLLN YINTSISGMT
IPWIYIGSLL STFCWHVEDH YTLSANYCHF GATKKWYGIP SSYANSFEKL MKDSAPDLFK
RQPDLLHQLV TLLSPMTLVK NGIPVMYADQ QPNEFIVTYP RVYHAGFNSG FNFNEAVNFA
MPQWLEFGEQ SIHDYKLIKK ENVFDHYQLV ENILHDFQRK KVKGIQLTKE EINLVERCIK
SYESFYQAQT NKLDQFNKIK KNFIIKFQPK FFKERKFEDE QLGYFPQDNN DQDEDYEDDL
CDICRTKISY QYCIIDNKRH RFHTIASSDA MDSKLKSIEP ITPTIKQEAT FESFNKIPIS
QLLTPESSPY EEITNRPKKE LLAEHDLGPN ESKSEADEWN KLIEDAKNDD NDNNRKRRRS
RRVSKEEEPL HKNRKPNHPT IQPKGKMTVV QNTCSLNQLN DQEEIRLCLQ CCLNLCGEHG
ERAPINSTLV YEMYPDTMAH LISSTRSLLH DL
//
