ID A0A151MUF9_ALLMI Unreviewed; 1196 AA.
AC A0A151MUF9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Lysine-specific demethylase 2A isoform A {ECO:0000313|EMBL:KYO28099.1};
GN Name=KDM2A {ECO:0000313|EMBL:KYO28099.1};
GN ORFNames=Y1Q_0005094 {ECO:0000313|EMBL:KYO28099.1};
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:KYO28099.1};
RN [1] {ECO:0000313|EMBL:KYO28099.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO28099.1};
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 -!- 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:KYO28099.1}.
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; AKHW03005047; KYO28099.1; -; Genomic_DNA.
DR RefSeq; XP_006260152.1; XM_006260090.3.
DR AlphaFoldDB; A0A151MUF9; -.
DR GeneID; 102565389; -.
DR KEGG; amj:102565389; -.
DR CTD; 22992; -.
DR eggNOG; KOG1633; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd21784; CTD_KDM2A; 1.
DR CDD; cd22181; F-box_FBXL11; 1.
DR CDD; cd15643; PHD_KDM2A; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR002857; Znf_CXXC.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23123:SF3; LYSINE-SPECIFIC DEMETHYLASE 2A; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF16866; PHD_4; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00367; LRR_CC; 5.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KYO28099.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:KYO28099.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 185..353
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 602..648
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 655..716
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..906
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1196 AA; 136729 MW; 38D90AD7A3CF144D CRC64;
MAAAAPVRGQ RKRRDLEEEE EDSSPGVSFS LSSEESEMEP EEERIRYSQR LRGTMRRRYE
DDGISDDEIE GKRTFDLEEK LSTNKFNSTF VVFMEGKDFT VEYIQRGGLR DPLIFKNSEG
LGIKMPDPDF SVNDVRLYVG SRRMVDVMDV NTQRDIEMSM AQWARYYETP EEEREKLYNV
ISLEFSHTRL ENLVQRPATV DLIDWVDNMW PRHLKESQTE STNAILEMQY PKVQKYCLMS
VKGCYTDFHV DFGGTSVWYH IHRGGKIFWL IPPTPQNLEL YENWLLSGKQ GDIFLGDRVS
ECQRIELKQG YTFVIPSGWI HAVYTPTDTL VFGGNFLHSF NIPMQLRIYS IEDRTRVPNK
FRYPFYYEMC WYVLERYVYC ITNRSHLTKD FQKESLSMDM ELSSSESGNV DEEEDAPDKE
PRRPVTRRSV LTSPVANGAN LDYDELSKGC RSLPGLKKTP STDSSDSSRA PQNGQAWDPL
ASSPHKSNKV HLTQFELEGL RCLMDKLESL PLHKKCVPTG IEDEDALIAD VKLLLEEYAN
SDPKLALTGI PIVQWPKRDK LKFQARPKLR LPTIPITKPH TMKPAPRPAP VRPTVSPIVS
GARRRRVRCR KCKACMQGEC GMCHYCRDMK KFGGPGRMKQ SCVLRQCLAP RLPHSVTCAL
CGEVDQNEDS QDFEKKLMEC CICNEIVHPG CLQMDGEGLL NDELPNCWEC PKCYQGDDSE
KGQKRKMEES DEDTVQAKVL RPLRSCEEPL TPPPNSPTPM LQLIHDPASP RGMVTRSSPG
AGPSDHHSAS RDERFKRRQL LRLQATERTM VREKENNPSG KKELSEVEKA KLHGSYLTVT
LQRPTKDMHG TSIVPKLQAI TASSTNLRHS PRVVMRHSPA RTPQRGGDEE AEDEEEEEEE
EDESAEEGGA ARLNGKGRLQ DGEESWMQRE VWMSVFRYLT RRELCECMRV CKTWYKWCCD
KRLWTKIDLS RCKSITPQAL SGIIKRQPVS LDLSWTNISK KQLTWLVNRL PGLKDLILAG
CSWSAVCALS TSSCPLLRTL DLRWAVGIKD PQIRDLLTPP TDKPSQDNRS KLRNMIDFRL
AGLDITDATL RLIIRHMPLL SRLDLSHCNH LTDQSANLLT AVGSSTRNSL TELNMAGCNK
LTDQALLYLR RISNVTLIDL RGCKQITRKA CEHFISDLSI NSLYCLSDEK LIQKIS
//
