ID A0A091DD56_FUKDA Unreviewed; 1072 AA.
AC A0A091DD56;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Histone lysine demethylase PHF8 {ECO:0000313|EMBL:KFO20696.1};
GN ORFNames=H920_17921 {ECO:0000313|EMBL:KFO20696.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO20696.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO20696.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO20696.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN124612; KFO20696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DD56; -.
DR STRING; 885580.ENSFDAP00000009227; -.
DR eggNOG; KOG1633; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15642; PHD_PHF8; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
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; PTHR23123:SF11; HISTONE LYSINE DEMETHYLASE PHF8; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 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; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KFO20696.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:KFO20696.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 5..56
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 195..351
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 472..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 119113 MW; 63D6FDFD3AB257E7 CRC64;
MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAAEIDLYHC PNCEVLHGPS
IMKKRRGSSK GHDAHKGKPV KTGTPMFIRE LRSRTFDSSD EVILKPTGSQ LTVEFLEENS
FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVARQADCKM KLGDFVKYYY
SGKREKVLNV ISLEFSDTRL SNLVETPKIV RKLSWVENLW PEESVFERPN VQKYCLMSVR
DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVDKC
YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFK
FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFKAWTKK EALADHEDEI
PETVRTVQLI KDLAREIRLV EDIFQQNVGK TSNIFGLQRI FPAGSIPLTR PAHSTSVSMS
RLSLPSKSGS KKKGLKPKEL FKKAERKGKE SSALGPAGQL SYNLMDPYNH QALKTGCSQK
AKFNMTGSCL NDSDDDSPDM DLDGNESPLA LLMANGSTKR MKSLSKSRRA KMAKKAEKAR
LVAEQVMEDE FDLDSDDELQ IDERLGKEKA ALILRPKFSR KLPRAKPCSD PNRVREPGEV
EFDIEEDYTT DEDMVEGVEG KLGNGSGAGG ILDLLKASRQ VGGPDYAALS EAPASPSTQE
AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG QDRSSGSSSS GLGTVSSSPA SQRTPGKRPI
KRPAYWRTES EEEEENASLD EQDSLGACFK DAEYRHVVPI QSLPSESLPL WPMFSLVHKS
EEDLSCEYLT HWALVLSPSL VGIYPSLESD DDDPALKSRP KKKKNSDDAP WSPKARVTPT
LPKQDRPVRE GTRVASIETG LAAAAAKLAQ QELQKAQKKK YIKKKPLLKE VEQPRPQDSH
LSVTVPAPGV AATLHPPTSS SPLPPPEPKQ DTLSGSLADH EYTARPNTFG MAQANRSTTP
MAPGVFLTQR RPSVGSQSNQ TGQGKRPKKG LATAKQRLGR ILKIHRNGKL LL
//
