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Database: UniProt
Entry: A0A445A0Q8_ARAHY
LinkDB: A0A445A0Q8_ARAHY
Original site: A0A445A0Q8_ARAHY 
ID   A0A445A0Q8_ARAHY        Unreviewed;      1047 AA.
AC   A0A445A0Q8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Lysine-specific demethylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Ahy_B03g065102 {ECO:0000313|EMBL:RYR20023.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR20023.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR20023.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR20023.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RYR20023.1}.
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DR   EMBL; SDMP01000013; RYR20023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445A0Q8; -.
DR   STRING; 3818.A0A445A0Q8; -.
DR   Proteomes; UP000289738; Chromosome b03.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032453; F:histone H3K4 demethylase activity; IEA:UniProt.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR   GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   Gene3D; 3.30.160.360; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR004198; Znf_C5HC2.
DR   PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   PANTHER; PTHR10694:SF105; LYSINE-SPECIFIC DEMETHYLASE JMJ14-RELATED; 1.
DR   Pfam; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF02928; zf-C5HC2; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51543; FYRC; 1.
DR   PROSITE; PS51542; FYRN; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          56..97
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          267..430
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          798..856
FT                   /note="FYR N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51542"
FT   DOMAIN          858..948
FT                   /note="FYR C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51543"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..145
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1047 AA;  117155 MW;  DB73610E8780CE99 CRC64;
     MEQLILAAES DIKEDSPLRP KPKSNDAPEP SGSPRSRMVS ARWDPGEACR PIIDEAPVFY
     PTNEEFEDTL GYIAKIRPQA EPHGICRIVP PACWVPPCPL KEKDIWENAK FSTRIQQIDL
     LQNREPMKKK KRGRKRKRRN HSKMGTCRRL ANSSSGANNA SEPDEKFGFQ SGSDFTFKDF
     QLYANYFKEC YFRLKDPGEE EKFSNDSYQR RWQPSVEEIE GEYWRIIEQP TDEVEVYYGA
     DLETGSVGSG FPKSSSLTKS DSNQYALSGW NLNNFARLPG SVLSFEGSDI SGVLVPWLYV
     GMCFSSFCWH VEDHHLYSLN YLHWGDPKVW YGVPGNHASA LEDTMRKHLP DLFEEQPNLL
     NDLVTQLSPS ILKSEGVPVY RTVQHSGEFV ITFPRAYHSG FNCGFNCAEA VNVAPVDWLM
     HGQNAVELYS LQGRKTSLSH DKLLFGSAQE AVQALAELAL HGEETPKCLK WRSVCGKEGV
     LTKAIKTRIK MEEERLGCLP THLKLLKMDK DFDSYDEREC FSCFYDLHLS AVGCECSRDI
     YSCLMHSKFL CSCAMDKKFV LFRYTIDELK SLVEALEGES HAIKVWANKR LGMVSTVSSE
     VCMYEPDMEK DMYKAKNPKE EETSVIGATN NSNLNIPSRP HSHVTSEIVQ SESHDVTSGA
     SYGIIENHNH SIDKKLAADN GHKVDQEGSL DLNVEAVSDG NENNLLLKSF LTEEKLCCSG
     SGTKQGNIGL AGEHNLSQFC VLQTELSSCS RVVAYSGPFN GGKFGIDSNS GKHPNCMVKR
     EIIDSMNRSI SLSDESHLMQ VFGTTVKLIS LGSVAYGKLW CTKQAIYPRG FKSLVSFFSI
     LDPARICSYI SEVVDAGFLG PLFKVTLEGH PNEVFTDTTA DKCWESILKR LHDEIVRQRS
     LGELELPPIE LLKSINGHRM FGFHLPSVVQ AIEAQDLTHQ CAEYWNHKGA LTSQGRAIKK
     FKDGSGSSSG NGNTKGFGIN LIKQEDDDIG GSCHSLGEMQ SILQGLLKRA SADELSAMRK
     LFSSDALCSQ WRMTFLALME EINKAGR
//
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