ID A0A445CV06_ARAHY Unreviewed; 1429 AA.
AC A0A445CV06;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Lysine-specific demethylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Ahy_A06g030041 {ECO:0000313|EMBL:RYR54762.1};
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:RYR54762.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR54762.1, 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:RYR54762.1};
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:RYR54762.1}.
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DR EMBL; SDMP01000006; RYR54762.1; -; Genomic_DNA.
DR Proteomes; UP000289738; Chromosome a06.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:InterPro.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR024752; Myb/SANT-like_dom.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12549:SF11; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLASE 2, ISOFORM A; 1.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF12776; Myb_DNA-bind_3; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 147..193
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 571..802
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1348
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1429 AA; 162900 MW; 44FBC14E4AAC5596 CRC64;
MLPARKRRGR RPRTTQVINF GTPENEVPSD NNVDLDKDAK DDDGATNSSL VQNSKGMRQD
RKRKMAKISS NIGTSSRSRA ESEEEENGYS TATESELPSD NVELGLDKDS QKDDANGRRF
LLRKHQQETP KVIRRGPKFI QEESLMCHQC QRNDKGEVVR CKNCKRKRFC IPCLATWYPE
LKPEDAVLCP VCRGNCNCRA CLRSTALIKA MRHHVPRNEQ ERFEHSKYLL KRLLPYLRQL
DKEQMIEKDI EAKRKGLSLP KLNIEKSEYR QDERTSIFDY HRFCRKCSFH LCLICCYELR
NGELLGGADP DELGFVNWGI DYQHGCDISR DKSNSAHEDA KPDSKKNLAH SDAKPDVRGW
SRSGWHAKSD GRIPCPKNTC RNRFLELRSV LGPNFISELV HKAEEAEAHK LHTAVENPVS
WCSCLRLSRN TDCRSNNNTL KSASRENSID NFLYHPRAIS QKPEELKHFQ CHWSRGEPVI
VSNVLEHSSG LSWEPRVMWR AFRSFKANGN QHLDMKAFDC LDWAQGDINI HQFFCGYEIG
RWDRCGWPQM LRLNDWPPDF TERAPRHYAE FMSLLPFGEY THPFGGVLNL ASKVHGTGST
PNMEPKEYIA YGFPQELGRG DSVVKLHYDI SDTVNILTHT AGKVRLTSDQ LRTIEHLKRK
HHDQDKRELL VTYQEESNIL AGGDASDGVL WDVFRRQDIP VLKEYLKKHF KEFRHNYCCP
LDKVIHPIHD QTIYLTVGHK RKLKEEYGIE PWTFIQKLGD AVFIPAGCPY QVRNLKTCIN
VALSFVSPES VGECFRLAEE IRTLPINHRS SEDKLEVKKM TIFAINNVLE NLSRSSLNEN
LKPERNIQEK QPTGEKDKWD EYTTGVFLDV CVEEIASGNR ADADFNEEGW INVIAKFNGK
TGRNYDCRQL KDKWDILKGD FNLWEKLLEI GVGWDPVKKT IKASQEFWVA RRKENPEFLK
FRFQCPSHLD KLEACFKDMK AIGDVALKTH ADPSSAEVRV CGKENEDNHE LRAFGEGVRD
SDSVAYEEPH TSYSVGHTTS NDNPNKRQIQ LNDKKQFGKV NKLQHSVSVP LEEEEHSIPP
EENPAFLKFE HQGPPHLDKL EACFEDAKGT SYVAIYADPS PNGVGFYGEE NEDNLELRAS
NEDDGDSGDD VAIEETHHTQ NVQHREYNEN NPELRASEEG FSDVVDVAIE ETHHHMHNVE
PRKENENNPE LRASDEGVSS ADVPIREENE INPELRAFDE GVSGSDVAID KTHDTHNVEL
SEENEDNPEL RASHEGDGDV VGIANVEPLG ENEDNLELRA SDEGVGDGDG VANKETYHSH
NAEPGPSNSV PKKRKRLRKA KKHSGKAVKA KANNTATGFE CNLDLDSCLT LLGSVPGLEK
GSTLYFIACR VLTKIVNRQT FVHLMRDDPK LAFGWLNTFT LEDLKNLTG
//