ID H9F5I3_MACMU Unreviewed; 935 AA.
AC H9F5I3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Lysine-specific demethylase 7 {ECO:0000313|EMBL:AFE69892.1};
DE Flags: Fragment;
GN Name=JHDM1D {ECO:0000313|EMBL:AFE69892.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE69892.1};
RN [1] {ECO:0000313|EMBL:AFE69892.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE69892.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000256|ARBA:ARBA00006942}.
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DR EMBL; JU326136; AFE69892.1; -; mRNA.
DR AlphaFoldDB; H9F5I3; -.
DR HOGENOM; CLU_003540_2_1_1; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0141052; F:histone H3 demethylase activity; IEA:UniProt.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15640; PHD_KDM7; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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:SF15; LYSINE-SPECIFIC DEMETHYLASE 7A; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
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:AFE69892.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:AFE69892.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 31..82
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 224..380
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 478..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFE69892.1"
SQ SEQUENCE 935 AA; 106332 MW; AA45B5C74F7635CE CRC64;
AVAAGAAAGA AAAAVSVAAL GRASAPPPPP PVYCVCRQPY DVNRFMIECD ICKDWFHGSC
VGVEEHHAVD IDLYHCPNCA VLHGSSLMKK RRNWHRHDYT EIDDGSKPVQ AGTRTFIKEL
RSRVFPSADE IIVKMHGSQL TQRYLEKHGF DVPIMVPKLD DLGLRLPPPT FSVMDVERYV
GGDKVIDVID VARQADSKMT LHNYVKYFMN PNRPKVLNVI SLEFSDTKMS ELVEVPDIAK
KLSWVENYWP DDSVFPKPFV QKYCLMGVQD SYTDFHIDFG GTSVWYHVLW GEKIFYLIKP
ADENLARYES WSSSVTQSEV FFGDKVDKCY KCVVKQGHTL FVPTGWIHAV LTSQDCMAFG
GNFLHNLNIG MQLRCYEMEK RLKTPDLFKF PFFEAICWFV AKNLLETLKE LREDGFQPQA
YLVQGVKALH TALKLWMKKE LVSEHAFEIP DNVRPGHLIK ELSKVIRAIE EENGKPVKSQ
GIPTVCPVSR SSNEATSPYH SRRKMRKLRD HNVRTPSNLD ILELHTREVL KRLEMCPWEE
DILSSKLNGK FNKHLQPSST VPEWRAKDND LRLLLTNGRI IKDERQPFAD QSLYTADSEN
EEDKRRTKKA KMKIEERSRI EGVENEESQK PLNRFFTRVK SELRSRSSGY SDISESEDSG
PECTALKNNF TTEESESSGD EKKQEITSNF KEESNVMRNF LQKSQKPSRS EIPIKRECPT
STSTEEEAIQ GMLSMAGLHY STCLQRQIQS TDCSGERNSL QDPSSCHSSN PEVRQLYRYH
KPVECGYHVK TEDPDLRTSS WIKQFDTSRF NPQDLSRSQK CIKKEGSSEI SQRVQSRNYV
DSSGSSLQNG KYMQNSNLTS GTCQLSNGSL SPERPVSETS FSVPLHPTKR PASNPPPISN
QATKGKRPKK GMATAKQRLG KILKLNRNGH ARFFV
//
