ID Q41700_VICSA Unreviewed; 1641 AA.
AC Q41700;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=ENBP1 protein {ECO:0000313|EMBL:CAA65242.1};
GN Name=ENBP1 {ECO:0000313|EMBL:CAA65242.1};
OS Vicia sativa (Spring vetch) (Tare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX NCBI_TaxID=3908 {ECO:0000313|EMBL:CAA65242.1};
RN [1] {ECO:0000313|EMBL:CAA65242.1}
RP NUCLEOTIDE SEQUENCE.
RA Christiansen H.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAA65242.1}
RP NUCLEOTIDE SEQUENCE.
RA Christiansen A., Hansen A.C., Vijn I., Pallisgard N., Larsen K., Yang W.C.,
RA Bisseling T., Marcker K.A., Jensen E.O.;
RT "A novel type of DNA binding protein interacts with a conserved sequence in
RT an early nodulin ENOD12 promoter.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01002}.
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DR EMBL; X95995; CAA65242.1; -; mRNA.
DR PIR; T10955; T10955.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:InterPro.
DR CDD; cd02208; cupin_RmlC-like; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR014977; WRC_dom.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12549:SF66; ENBP1 PROTEIN; 1.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
DR SMART; SM00384; AT_hook; 4.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51667; WRC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 7..51
FT /note="WRC"
FT /evidence="ECO:0000259|PROSITE:PS51667"
FT DOMAIN 815..861
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1224..1604
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1641 AA; 181242 MW; 2560E38158736AE0 CRC64;
MDVGGGDEEF RRCNRNGSGR RCKDGALPGN LQCEKHQLCA VERKKNRKET SSGRKRKAEE
SLLDEDDGGN GLFAGGAGGA GGAGGGVFVE GGVNVGIGSE SFNLWQEGEG QQVEVFGEGS
GNLGKFLGDG VEFLGGFVED RNVVGLGQPW SSVGVFGNAG GVAGVGKEDH GSRVDGVCGN
DSLAFHSQGI EGLIGEEEGG FGNLYDRSFQ ALLCQGKVCD EDVNLIGGAT GFQGLVGESA
FNFSGQDGEG VGNLSQHDGK FDGEKNVGNI LEAPSSSNKM KAIGVEEGVE LLPSAGVSAN
EEARGEVLKP LTSRGGRPKG SKNKKKKGVS LVLDGEAVCG SDNAGTIGMG TVEVLENEKS
VFCGKSDGEG VDTGEIARTR ECSPPENQKS TTEIFLAHGY EVAGVGEISR PLNKEKNVEE
VSSEVAVEIS RSKKRGRPKG STKKKVTCSA SRKGAGDIAT QGSEEKMLIV PYQKDADEFA
SLTSKLGPAL STRNKLRSTE FEGCKHPGMS SNVRLEENDG TASGLEITTL APLREAEKGM
PFESAKHIEN LTTPPIVKRG RPKGSKNKKK TLADQEHIGH GGDIIKLIGM ESSEAAVSVG
DQELVVQPLV KVRFRMLNPK MGRPKGSKNK KKNVDGEAEN GLHKEGKKRG RPKGSVNNPK
ETGNEKIAKG LVSESSNVHK IERRGRPKGS APNPKENASR LDAEIEREKN THVYGILSTT
MPHKHIHEES ILLLEDHVNK KDDADFVLEC SKESGIEKIA KGLVSESDNV HKTHDVEVGD
IFYEKEVKET IDHRLEPSDM LGDCETKKEP RNSRCHQCWK KSRTGLVVCS KCKKKKYCYE
CVAKWYQDKT REEIETACPF CLDYCNCRMC LKKAISSMNG NDEADRDVKL RKLFYLLKKT
LPLLQDIQRE QRYELEVEAT MHGSQLVEEE DIRKAEVDDD DRVYCDNCNT SIVNFHRSCS
NPNCEYDLCL TCCTELRLGV HCKDIPTSGN EEMVDAPPES IAWRAETNGS IPCPPEARGG
CGTAILSLRR LFEANWIDKL TRGVEELTVK YQPPIMDLAL GCSECRSFEE DVAQNSARKA
ASRETGYDNF LYCPDAVETG ETTFEHFQRH WIRGEPVIVR NAYKKASGLS WDPMVMWRAF
MGARKILKED AVNFKAIDCL DWCEVEINAF QFFKGYLEGR RYRNGWPAML KLKDWPPSNF
FEECLPRHGA EFIAMLPFSD YTHPKSGILN LATKLPAASK PDLGPKTYIA YGTSDELSRG
DSVTKLHCDI SDAVNILTHT AEVKPPPWQS RIIRKLQKKY EDEDMRELYS QDKKEVGLPR
KRGRKRRVGF SVDPKTSEKE DTSGRDSTLQ GSQGKEEKLD DQESSEPTKI EFDLNASEQE
ISDSPRFQQF DLNSHDSSLL VPGNDCESMH YDNVQERCSS QGDGSYKGIS SVIDDQPCSG
TKETKNVNKL NSSDDNCSDI ETNNIDSVEK DILSNSLCQN DVHLGTQNGS AVWDIFRRHD
VPKLTEYLKK HHREFRHIVN LPVNSVIHPI HDQILYLNEK HKKQLKIEYG VEPWTFEQHL
GEAVFIPAGC PHQVRNRKSC IKVAMDFVSP ENVRECVQLT EEFRLLPKNH RSKEDKLEIK
KMALYAADVA VAEANKLLGA K
//
