ID A0A068YK25_ECHMU Unreviewed; 1908 AA.
AC A0A068YK25;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Jumonji AT rich interactive domain 1B {ECO:0000313|EMBL:CDS42634.1};
GN ORFNames=EmuJ_001034900 {ECO:0000313|EMBL:CDS42634.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS42634.1};
RN [1] {ECO:0000313|EMBL:CDS42634.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS42634.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR EMBL; LN902842; CDS42634.1; -; Genomic_DNA.
DR STRING; 6211.A0A068YK25; -.
DR eggNOG; KOG1246; Eukaryota.
DR OMA; CEAPNGC; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR048615; KDM5_C-hel.
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; PF02373; JmjC; 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; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS51184; JMJC; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
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 129..295
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1035..1086
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 473..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1791..1874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1889..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1908 AA; 214095 MW; BF791479CBDD6710 CRC64;
MLVCDVCCCE GVYHTFCLDN PISYIPKRWL CPKCFTNEFN KKNEVNANGS RKSDTSYTLR
DFSCVADEFK TNYFKKPLTT IALAEIRDEF WRLVNDGECN VTVEYGADLC SSKGSSGFPT
TPNNLGKFDY YSSPWNLNNL AKNPLSALHY LPSNMTGIKA PSFYVGMVFS CFCWHTEDHW
SFSINYLHTG DPKTWYGVPG ARADAFEAAM QVEAGELFIH SPDVLRHVTC LVPPDRLLHR
GVPVYHLDQL AGEFVVTFPR AYHAGYSNGF NFAEAVNFCP AEWFPFGLHC VDHYALLHRP
PLFSHAELLC RLAESGLESS RVPITFLLVV TDQLAGLLAK ERSLRRHLVR LGVRRTERFV
FEALDKEARK CQLCRTTLFT SALTCSCSKS FLCLEHYQSC TCCAAEDQIL LYRYGLDELS
QFVERPQARI REYQEWKACV DDFLCSNTSF CNAKEKGEEF ALYLNSAKAE SHGKINEQRG
TGNPEGGSPT QKIPLQDLVK LRDTGHQNCY PDDLVSALNK IVETAESCAS MIGELCAQKP
EGRKRRSQAS GTSRKYDFLS AVDNKEDVVE LDLPWNPSIT KITMNEFEQY VEKVNGLPCT
MPRMEELNRF KQRLEEWHTS ACELLSLAEQ PIIGDHSGRP PPRLPEIHRI ERLVTFARGV
DVELCHLKDL KHLLECVSWL ESVERVMKLK TASNRDLPSL KELIDLDTRG QTLAYVLHPD
RLTGQSFETG KSVITTLESA LLKGGVRLQE VICEAQVVEN SIKEVLKAPN GSCELSEAEA
LVAQASCLKA TFDESEELAQ LCAKAHALLG HFACFQRLFK SPCVNTSMES RGGRDVKGKQ
EVLAEGEIGA EDAFPEEFVR RLKLYTADST PHVWLKFYEE VCSAAKKLPF VFPDTIRLRN
LLIALDRCYS RIKAAFLPSD NEHAFSPATL LEVLLPRPKS AYGLLIQRDA EVMPSSSAGG
ASGSGHDPRP FDSRAYADAC KENVSKFLRE LNDGSDFDHM YDTVYTPMIE NELQLLHYLR
RSNMRKSKER DQDAVIYCVC RQPGYTGIML QCELCKDWFH KRCVGFPSRN VDIRRVRYTC
PLCERSLRPE LSVVIAILEE LVPHVTGTVV KQGLGAKSVP SDHLSTVKSS ITSDLMAPLV
SVPFLLRLPA LAAVQMLCER AFAFVRRVRT VVLSTPELRK AFVEYEAFSG VQMQWNNFNE
AVMLHASARQ QQRSIADHQS EQELRPVGLT YSHLPPNVVR PTGMQPLVLR TTALRSLASE
RLHHLHRQHH FSNPSAPPLL FPHHLQRSTS PSRQEPSSPA FKMDDTDDRD SMRSNTEKDH
RNSNKRNEKE AAVALAIMSS ATTDLTEPLA SPREQHSPFS NPHSLPRHPR RRTLNGEGHQ
RHLQCKGSMS SAEFHCYIPP DACSWLDTLI GEACALEVSL PQIRWLWQLS LAADPDSPGA
LHPRVVYEDE MALRRREYRR RSIGEDFGVH RRARPCRSNS SERPFYFTLA HKGRESALGS
DGVESYGGRC VKRRKVSSKS SRTASLPSQR RRNKPAPRSS MGYLSYLASR RRSLFRFSRD
FKRQSETYSG EGEEEAEANV KEGENQNRGG DSDLNATADD SVKNKETPHR EPRGGVQRQP
SNSSFASISS VPSSPPTGGQ HSASSSKFQF NRGKQVSEVA QNSIDHHLAA TRRFAAAGAV
RRTSILSSTR RDRGGGGRMM KGLSRQQRQT LVPRRRSREE NKVGGVNEED KWQEFCEAPN
GCKRPRGTVA WVACDQCNYW YHQRCVGIMS TREVPEVYVC GACQFGDVGE KVGSRRPRSS
RPKSSRISSQ PWSAPKVELQ REGSTGSSTS SGSAVRAEAR DSSEDPPVQI KRSGLASPEK
NLGEVSAKKF HSDESMGAEA LLQAIAVLEA QPSTQEQPNA KHTVPPNT
//
