ID A0A087QMR2_APTFO Unreviewed; 2429 AA.
AC A0A087QMR2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
DE Flags: Fragment;
GN ORFNames=AS27_09434 {ECO:0000313|EMBL:KFM02516.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM02516.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM02516.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM02516.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a central role in histone code.
CC {ECO:0000256|RuleBase:RU369087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000256|RuleBase:RU369087};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU369087};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|RuleBase:RU369087};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU369087}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC association with nuclear receptors. {ECO:0000256|RuleBase:RU369087}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000256|RuleBase:RU369087}.
CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC {ECO:0000256|RuleBase:RU369087}.
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DR EMBL; KL225745; KFM02516.1; -; Genomic_DNA.
DR STRING; 9233.A0A087QMR2; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070988; P:demethylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR PANTHER; PTHR12549:SF6; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 2C-RELATED; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|RuleBase:RU369087};
KW Metal-binding {ECO:0000256|RuleBase:RU369087};
KW Nucleus {ECO:0000256|RuleBase:RU369087};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT DOMAIN 2163..2387
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 147..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1860..1953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1860..1894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1936..1953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM02516.1"
FT NON_TER 2429
FT /evidence="ECO:0000313|EMBL:KFM02516.1"
SQ SEQUENCE 2429 AA; 271053 MW; FD1D04AA874D1C97 CRC64;
TFKPLVGKSV YNSITAVEFL VDKQLDFITE DSAFQPYQDD VDSLNPVLRD NPQLHEEVKA
WVKEQKVQEI FMQGPYSLNG YRVRVYRQDS ATQWFTGIIT HHDLFTRTMV VMNDQVLEPQ
NVDPSMVQMT FLDDVVHSLL KGENIGITSR RRSRSNQNSN TVHGHYTRAQ ANSPRPAMNS
QTAAPKQNSH QHQQQRNTRP NKRKGSDSSM PDEEKMKEER YDYIGRGENP KNKNKHFLSK
RRKPEEDEKK LNMKRLRTDN ISDYSESSDS EISNKRLTDS SSEQNSENEL KSKNTSKING
EEGKSQTMEG VEQTLTDRRS PWDEIQEDKN HEETERLKSS FLDQQEKSSL HAAEQPTPYE
QNAKDPHVQE CNAEKHTAEL KNEQFVSRPP TPKCVVGITN ENNSEKESQD NAASTFGLQT
VQKTESHSSD LKQQFANANF LVARKQEADQ SWVSSVVNKV DLIQPGVVKT LSQNEHLNPE
KEKVQYGSFI SSLNVASLAE ESKLHKQSPV PDSVKSKPSA SVDHPKTKSP DVKPKFTQSS
DTVKSKVSSQ NSHATGLTRS ANKTDHDLPR SSFHPVPARV SALEATKSPL IIDKNEHFTV
YRDPTLIGQE TGTNHISPYL HQHNYPLHSS SHRTCLNPNA HHPALTGSSH LLAGSSAQAP
LSAINTHPLS TASHHSVHHP HLLPAVLPGV PAASLLGGHP RLETAHASSL SHLALAHQQQ
QQMLQHQSPH LLGQAHPSAS YNQLGLYPII WQYPNGTHAY SGLGLPSSKW VHPETPVNAE
ASLRRNTPSP WLHQPTPVTS ADSLGLLSHI PVRPSSADPL RPLKLTTHSS PPLSKSIVVE
HHKEELERKA FIEPLRSVTT APVKTELEQS RTQTTKESHM HRHFADPMLN QLPRPPQETG
ERLSKYKEEH RRILQESIEV APFTAKIKAL EGERENYSRV TSLSSSPKSH SVKYDKDAER
SVSELYKMKH SVPQSLPQSN YFTTLSNSVV NEPPRSYPSK EASSAYVDKQ TNCPSTAASP
QSLPSYISSL SKPPPLIKHQ PESEGSASKI PEQLSQSVQS HSVNSFRSDS RSPTQLSVSS
SNTLRSMPAL HRAPVFHPPV HQNLEKKESS YSSLSPPTLT PVQPVNAGGG KIQELQKPPT
LVPEPKEAQT VYKGTSEQNL SEIWKSNNAP NNEKVDWHVE RMSGKSQSAT ASVIVRPPSS
TKYDSVPVMQ SASKDRVSER SSAVTNQADC LKTAEARETG RIILPNMNSD SARTQYEKKF
PAVSQGSIPR AVTPTTTMIC STKTDVTASA ATTTSVSSWA SSEVTYSLSN AVLACAPLEC
TASRAASQAM AQAQECKVST PAPVTPAAGK TGSAAQPSSG FSTSTDFVHL KKHKAALAAA
QFKSSNTSET ESNSVKNQTF STSLSLDSAI VCNTINKANS VGSGQTSQTS QPNYHTKLKK
AWLTRHSEED KNTNKKENSG NSVSEIIKPC TVNLIASTSN DLQNNIDSKV LADKFVKEDK
HPRRKAKRTY DSGSESGDSD ESESKSEQRT KRQPKPTYKK KQNDLQKKKG DTEEEVKPNG
VLSRSAKEKS KLKLQSGCNS TGIPRSVLKD WRKVKKLKQT GESFLQDDSC SEIGPNLQKC
RECRLIRSKK GEEPTHSPVF CRFYYFRRLS FSKNGVVRID GFSSPDQYDD EALSLWTHEN
YEDDELDLET SKYILDIIGD KFCQLVTSEK TAMSWVKKDA KIAWKRAVRG VREMCDACEA
TLFNIHWVCQ KCGFVVCLDC YKAKERKSSR DKELYAWMKC VKGQPHDHKH LMPTQIIPGS
VLTDLLDAMH SIREKFEIKS HCQCTSKQST QAGKLPAMNG VSQVLQNVLN HSNKISLCMP
ESQQQNTPQK SETNGNTSPR SDVSTDSKLT PPESQSPLHW LADLAEQKAR EEKKENKECP
SGKHSKEEKD QDNLESQNCK SSPPASQNNE QGSTLRDLLT TTAGKLRLGS TDAGIAFAPV
YSTGTASGKS GRTMPNILDD IIASVVENKI PPNRAPKMNV KSEIKDEPKD DRKGIQDDCS
KLYSDIQYSW ICDKHVLWLR DHKNNNNWKL FKECWKQGRP VLVSGMHKKM NFSLWKAESI
SLDFGNQQAD ILNCKDSIIS NTNVKEFWDG FEDVSKRQKI KNGETALLKL KDWPSGEDFK
AMMPARYEDL LKSLPLPEYC SPEGKLNLAS HLPGFFVRPD LGPRLCSAYG VAATKDHDIG
TTNLHIEVSD VVNILVYVGI AKGNGVLSKS GVLKKFEEED LDDLLRKRLK DSSELPGALW
HIYAGKDADK IREFLQKIAK EQGLEVLPEH DPIRDQSWYV NKKLRQRLLE EYGVKTCTVI
QFLGDAIILP AGALHQVQNF HSCVQVTEDF VSPEHLVQSF HLTQELRLSK EEINYDDKLQ
VKNILYHAVK EMVRALKIHE GEMEDMDEN
//
