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Database: UniProt
Entry: A0A151P0J0_ALLMI
LinkDB: A0A151P0J0_ALLMI
Original site: A0A151P0J0_ALLMI 
ID   A0A151P0J0_ALLMI        Unreviewed;      1023 AA.
AC   A0A151P0J0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE            EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN   ORFNames=Y1Q_0000238 {ECO:0000313|EMBL:KYO42554.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO42554.1};
RN   [1] {ECO:0000313|EMBL:KYO42554.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO42554.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC         [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC         lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC         COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC         EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC       {ECO:0000256|ARBA:ARBA00009711}.
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:KYO42554.1}.
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DR   EMBL; AKHW03001382; KYO42554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151P0J0; -.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15714; ePHD_JMJD2B; 1.
DR   CDD; cd15576; PHD_JMJD2B; 1.
DR   CDD; cd20464; Tudor_JMJD2B_rpt1; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.10.330.70; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR040477; KDM4-like_Tudor.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR047483; Tudor_KDM4B_rpt1.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10694:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR   PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF18104; Tudor_2; 2.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00333; TUDOR; 2.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..42
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          128..294
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          718..831
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          358..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1023 AA;  115662 MW;  713DDC97874BA9C7 CRC64;
     MTFRPTLEQF RDFAKYVAYI ESQGAHRAGL AKVIPPKEWK PRRSYDDIDD MVIPAPIQQV
     VTGQSGLFTQ YNIQKKPTTV GEYRRLANSE KYCTPRHQDF EDLERKYWKN LTFVSPIYGA
     DISGSLYDAD VEEWNIGNLN TLLDMVEHEC GIIIEGVNTP YLYFGMWKTT FAWHTEDMDL
     YSINYLHFGE PKSWYAIPPE HGKRLERLAK GFFPGSSQGC DAFLRHKMTL ISPSILKKYG
     IPFDRITQEA GEFMITFPYG YHAGFNHGFN CAESTNFATL RWIDYGKMAT QCTCRKDMVK
     ISMDVFVRVL QPERYDLWKQ GKDIAVLDHM KPTALTSPEL DAWNETKSEL KSKLLRRIGE
     EEEDSKHNYR SHRKRSQPRR HKTEDQKSLG EVMAIETVLD EVKVKEELKR GPDLDEEEKS
     KATEGGEGDC KQPAEEETPP ARPLVPVAAA ATAEKSLPPV PLNIIQPSEV PNEQAFEQFA
     TQKGLGWREQ AVPGELPVKE EESAEAENAE VATEASDLQT AAAFSKMKME IKKSRRHPLG
     KPPTRSPLSV VKQEASSDEE TFPFSGEEDV SDPEALKSLL SLQWKNKVHN FPAERKFNAA
     AALSEPYCAV CTLFYPYNQS LQVDKEAVQV SVAESPSLLQ LSKCGQKTKP LIPEMCFTSS
     GENTEPLPSN SYIGEDGTSL LISCAKCCLQ VHASCYGIRP DLVNESWSCS RCSANAWAAD
     CCLCNLRGGA LQMTTDGRWV HIICAIAVPE AHFLNVIERH PVDISAIPEQ RWKLKCIYCR
     ERMKKVSGAC IQCSYEHCST SFHVTCAHAA GVPMEPDDWP YVVSITCFKH KAANHNIQFR
     REISLGQTVI TKNRNGLYYR CKVIGMTTQT FYEVNFDDGS YSDNVYPESI TSRDCVQMGP
     PPEGEMVQLQ WTDGIVCKAK FIAAQISQIY QVEFEDGSQL MVKRGDIYTL EEELPKRVKS
     RLSLSTGAPQ EEMFSGDEVK AAKRPRVVNS RNPEDYGQNP DYLAFMETLL QTQYQPGTQS
     NMF
//
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