ID A0A2T7NUC5_POMCA Unreviewed; 1754 AA.
AC A0A2T7NUC5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN ORFNames=C0Q70_15241 {ECO:0000313|EMBL:PVD24755.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD24755.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD24755.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD24755.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD24755.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000604};
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 JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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:PVD24755.1}.
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DR EMBL; PZQS01000009; PVD24755.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7NUC5; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg9.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16864; ARID_JARID; 1.
DR CDD; cd15606; PHD2_KDM5A; 1.
DR CDD; cd15610; PHD3_KDM5A_like; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 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; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR047970; KDM5A_PHD2.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 18..59
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 83..173
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 295..461
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1008..1070
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 943..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1713..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1454..1481
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 943..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1364
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1671
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1754 AA; 196293 MW; D6D032EDCA4A8810 CRC64;
MNLDLSDPYN NFVPPPEAPV FSPTEEEFAD PLAYIAKIRP IAMQSGICKI NPPRDWQPPF
AVDVETFRFV PRIQRLNELE AHSRIKLNFL DQLFKFWELQ GHTLRIPHVG RKLLDLHDLY
KMVEEEGGME YVSKERKWSR IATKLGLPTA KGQGSIVKMH YERVLYPYFL FKKGDTLVTE
ESMIDYSANS ELKKLQFFGA GPKAAVPPLN PKDEKLSIEL KEEKGSMKTR IKKVSPGVYT
TERVTTGMVE KEFWRLVHSL EEDVCVLYGA DIHAVEMGSG FPTKGTPNLL PEDEEYINSG
WNLNNLPVLE QSVLCHINAD ISGMKIPWCY VGMCFSSFCW HIEDHWSYSI NYLHWGEPKT
WYGCPGTAAD QFEAVMRESA PELFEQAPDL LHQLTTIMNP NLLMAKSVPI FRTDQHAGQF
VVTFPRAYHA GFNTGYNFAE AVNFCPSDWL SLGRQCIEHY RMLHRQCVFS HEELICKMAA
DPDSLELGLA AATHFDMLHI VETEKKLRKK LLDRGTVDAE REAFELLPDD ERQCDICKTT
CFLSSVTCPC SPSRLVCLYH VDDLCHCPAS RHCLRYRYTL DELPAMLHRL KIRAESFDNW
NMKVTAALEA SGTDKLDLGD FKELLQEADE KKFPDSELKN TLATAISEAE KCASVANQLV
SKKVRTRNRQ SLDGKYVAKL TLDELNCFYE QVMALPCSIR EAVLIKELLD KVVAFQEEAQ
EALSAEVPDS RQLEKLIDIG ITLDVDLPEI PRLKQVLQQA RWLDEMYSTL KDPQSVTLDV
MRKLIESGVG LAPHPALETA MAHLQELLTV SERWEEKARI CLQARPRHLK STLEAIISET
RNIPAFLPNV CALREAVRKA NEWTGKTSDS YPYLEVLEGL VNKGRPIPVR LDQLSQVELQ
VSAAKSWRER TARTFLKKNS TYTLLEVLSP RLDIGVYNSG KNRKKKTKEL EKSSHDGENS
QPEVKSEDTY DPATIVASFK LSEVREVDLM RDLRARNMEK SNGGDGDARF CVCRKGAFGF
MLQCELCKDW FHGTCVPLPK SAGMKAKPGQ PAVLQTSREM KFLCPVCLRS RRPRLETILS
LLVSLQKLPV RLAEGEALQC LTERAMAWQD RARQMLTTPE LAAALATLSV LTQRRQEQVA
REKTQKIISA ELRKAASNPE LQGHLASVTQ SAFGRQLDAG GTMAKEGGSP NSEEQAASPL
GPGAESASPR GAGDSMADDI GAEVDIPVVA SLGMSSEHAY SSVSKTGTNG SPRKHPRKTP
LVARQCEWPV LEISETVRAQ LEELMMEGDL LEVTLDETQH IWRLLQACHP HADPRFLDFQ
DTENQVGGGI KERPEKKVLK VKRRKEKEQI KTKNKLKSLK EKKLKRKKPM GDGSAINNGV
NGASTGEKGV EGSDHPSPIK KIKVEEGFRE KALKKIKAKR KDKVRLKLNK GPVKTEDTGV
KTGEDCITQR TVTGEKIKKK KKFLKVKIEA LENKEIEKKK KVLKKMRPDM KVKVKKERKP
KNGDKDSDDD NDEDCSATKC LRPVGEEVNW VQCDGCELWF HLLCVGLGKE QVTEEEDYVC
HTCSHTSGKS PDTSDIKQEP DGDADMPVVT AATSFLDASS ISSDLEALSK AAKASSDGEK
HEGGVQTSPP SEPVSDQVQQ RKENAEEEDE AGNSEEVVLV EEDDEEMEEA VNMGSQGEVE
EAELVEGVKQ AEESAVVVVV QSDGSDSALI KTSKPCVQQD VSLESPSQPS GTVVSDEGCS
SGQEQQHSAD VIES
//
