ID A0A445BB57_ARAHY Unreviewed; 1017 AA.
AC A0A445BB57;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Lysine-specific demethylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Ahy_A10g051006 {ECO:0000313|EMBL:RYR35912.1};
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:RYR35912.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR35912.1, 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:RYR35912.1};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01002}.
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:RYR35912.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SDMP01000010; RYR35912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445BB57; -.
DR STRING; 3818.A0A445BB57; -.
DR OrthoDB; 3473445at2759; -.
DR Proteomes; UP000289738; Chromosome a10.
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; IPR014977; WRC_dom.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR PANTHER; PTHR12549:SF42; PROTEIN B160; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF08879; WRC; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51667; WRC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 12..58
FT /note="WRC"
FT /evidence="ECO:0000259|PROSITE:PS51667"
FT DOMAIN 249..295
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 676..980
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 50..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 117144 MW; 86C3B5578D1B340E CRC64;
MGKKRNKVEE ALPDNLRCSR TDGRQWRCRR RVMDNLKLCE LHYLQGRHRQ YKQKVPESLK
LQRTTSTKTE GQNSTTSQND PVLKSTEIRA RISKLMMLRR KKRKLSGGSE GGPIKRKSKK
KKKKEKRDAH LELLRMVLQR EVEKSKGKKK DQSENGNVEE DLELHHYYDE GELRRELPNG
VMEIAPAAST PHDYTNVGSH FDVKVGIFDH GRALTPRYFR SKNVERDPVG KLQVVPYGVN
LKKGKRKKCH WCQRSDSWNL IKCSRCQKEF FCMNCIKERY FDTQNEVKMA CPVCRGTCTC
KDCLAIQRKD RESKEYLAGR SRVDRILHFH YSICMLLPVL KQISEDQHIE LETEAKIKGK
TITDILVKQV EFGRNEKNYC NHCKTPILDL HRSCLSCSYS LCLSCCQELR QGRTSEEVSS
YLSKLPDEIH SCTAGENHLL DDKAILHENS TGSSTLPESS GFDGTYGVSC PSTELGGCGD
SHLDLRCLFP LSWIKEMEVM ADEIVCSYEF PEILDKSSSC LLCIDRDQQL QKAAQREDSN
DNCLFYPTIL DITSDHFEHF QKHWGKGHPV IVQDALKSTS NLSWDPLILF CAYLERSITR
YENNKDLLEA CLDWCEVEIN IRQYFTGSLK SQPQRNAWHE MLKIKGWLSS QLFKEEFPAH
FAAIIDAIPI QEYMNPMSGF LNMAVNLPQG TTKHDMGPYI YISYGCADEE TDSVTKLCYD
SYDLVNIMAH TTDVPLSAEH LTKIRRLLKK HKALCRRESS KITAEHAEDT EQNGHQGVVR
EGMDFFRRVN RISSIPTEAR TKTNHSLDTD TSGSGECDLV SDAGKAQSSS PIHKTVKSTE
MSPDHDNTRR TLENPNGDKS KFTEDSGAQW DVFRREDVPK LLEYLKRHHD EFSYSHEYQE
EMVHPILDQS FYLNNFHKMR LKEEFEIEPW TFEQHVGEAV IIPTGCPYQI RNPKCSVHVV
LEFVSPENVS ESIQLIDEVR LLPKDHIAKV DKLEVKKMAL YSMNTAIKEI RDFTSKA
//
