ID A0A2T7NRE8_POMCA Unreviewed; 2001 AA.
AC A0A2T7NRE8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=[Histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=C0Q70_17028 {ECO:0000313|EMBL:PVD23755.1};
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:PVD23755.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD23755.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD23755.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD23755.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:PVD23755.1}.
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DR EMBL; PZQS01000010; PVD23755.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7NRE8; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg10.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd20391; Tudor_JMJD2_rpt1; 1.
DR CDD; cd20392; Tudor_JMJD2_rpt2; 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); 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 1.
DR Pfam; PF02373; JmjC; 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; 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.
PE 4: Predicted;
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:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 110..276
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1714..1829
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 301..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2001 AA; 218143 MW; D4077869E70EAF86 CRC64;
MESSSGGNST PRIMVIPPAE WCPRKAGYDD LDIIIPAPIE QVVQGCQGLY TQYNIQRKAL
HVSDFKKMAN SDKYLTPKHF DYEELERKYW KNATFGNAIY GADISGTLTD PDQDCWNINR
LGTILDYVAG DYGIKIEGVN TAYLYFGMWK TSFAWHTEDM DLYSINYLHF GAPKSWYAVP
PEHGQRLERL AQGFFQGSFQ ACPAFLRHKM TLISPSILKK FSIPVNKITQ EAGEFMITFP
YGYHSGYNHG FNCAESTNFA TERWIEYGKR CLQCECRNDG VKISMDTFVR RFQPERFEAW
KEGRDIAPHP EGHTVIRRPA RNDAKKKEAD GSGTVSKRHP PSKQFSKRSK VKAEKKTKAE
KSAVSDDDSE VDGTGKDEVN EAEKKPNKKT KSGNPQRAKS GDKAAKPKGN KKAAEDGEQK
SAGETKRKKK QVAKTSGSAP KNKKVTPKTA EKLSAEIPSS QPTRVEMSIQ TEETVAPGEP
LSSPGAKLDF YYNDTKVKAQ PVVFQQSKHT YEDEFRKKIA EIEAMRHFTA QDYELKRKKN
GTKPSPENRK YVLETDGPSS KKPKVEESEG TNSPPLDYLK GTEPEGTFKP IPLERISTMG
IKGVGIFKLA SLLGNTTGLQ AFGISPHLPG GQGGVSVVQN AAVVKQNGYD TNGGTKNANQ
GCQANTWTED MTQTPTWLQE SDVKSDQSGS SAACQNMTQT LRLAPFPPQN KTRSPVHAQQ
PLINFSSMGT KPISAILQAS QEKRALMKVT DTPVQSSVIP LATISQSCQA KNILPWKITQ
EQQHLMFANG SQHGSVEVLS TSDIFENPSF YINSYGTTGE MTSQVHQSPN LQSDHGYATS
PMSDIKRDGS PQPPVLSPIP SPQHKILDQS PPHLISSSLS LSHLSELPHL EPSVATTEIS
QSLHNLQTMD SKNMQQPQSR LVGPKRSKRS STSVNVRNSN VMPTGSIDTS SDHSSTSCSA
SSSRATGATC LDLSDLTPPG NIRSTEHRIM EILAQAQRLK VAQEKQREQQ RELEAQVRQS
LESNEGGPNA GNTSKKSSKP RAPRTSRKTS SKTSKGQATG QSANIANNLQ ATITTQPVTL
VTNNMASTMN QPQQLNATVS PQRITPLTQS SGISFSPTTN TGPVVTVVTQ NRPAGHVQLQ
GYPPAVATNQ SHFILKGVTR VLPGNAATYT TSVVPPLISL QNVPVTIVDS AGKASLVSTL
PSVSSVDTRQ DSENVTSADC VTVTTCRENA THGNNAINVN SQENTQGYVI NAAGDADTMG
LEIGKAATSG SIIITSFPCQ QQLINTQGTM AGAELAGRTM ASFGFGRPLQ MAAAHRMVTT
ASGGKLDVSP QLLPHPPPIL AGTLLGRATQ LGGKTCAEND GASEPPTLSR ITIDTSVTHS
PSSLDSSGPP VLTPSSHLHN YSLPSPLDPL SSLPLGDLGL GLAPSPSPDA WPRVDPSTSE
LPISKGNKGC KQLKSAASSR SATKHQKGKK ETRTSSSSSD ADENKSVKKD SRVKKNSGSE
SDHSSNFDDS ISEPPDNHDG NSSSTKPMIT KPRKKYGPSA VPVSCTLKNT HSVSTIRTSF
SDEDGPISEV EPANSHHSPL WAQHLTQLWQ GQPVNMAAER AYNRAMSHRP PNCCICAFFK
RFDVESEQGI FDESGLQMVV PQRSLPMIPE TLFAISKTNQ KPFCDYSLLE QDGLSPLLIC
STCNICVHAS CYGAGHVGNP DSWKCSRCAA FSTHAECCLC VLRGGALKPT TDGNWAHVVC
ALAVFEVSFV DVRERNLIDV SQLSPARQKL RCSLCGPVTS SSSQPSTCIQ CSHGRCTLAF
HPTCAYAAGV QFETSDWPFP IYCTCHRHQT SHREKVKDRQ LNDLYEGGRV IAKHKNGRYY
HATIMEVQRN RLYEVDFDDG SVSDDLLPED IVGHNCISEG PPSVGKHIQV RWTDGDLYGA
VFRGVNNQDE YTVEFENGSQ LILRRAELWT EDEELPKHVK SRLSMATERK YSLFYPEQER
GGPRPKKKID YVAMLAPGSG S
//
