ID A0A091UUS0_NIPNI Unreviewed; 1190 AA.
AC A0A091UUS0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Zinc finger E-box-binding homeobox 2 {ECO:0000313|EMBL:KFQ94461.1};
DE Flags: Fragment;
GN ORFNames=Y956_06130 {ECO:0000313|EMBL:KFQ94461.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ94461.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFQ94461.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ94461.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC family. {ECO:0000256|ARBA:ARBA00009867}.
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DR EMBL; KL410182; KFQ94461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UUS0; -.
DR STRING; 128390.A0A091UUS0; -.
DR eggNOG; KOG3623; Eukaryota.
DR Proteomes; UP000053283; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProt.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24391; HISTONE H4 TRANSCRIPTION FACTOR-RELATED; 1.
DR PANTHER; PTHR24391:SF18; ZINC FINGER PROTEIN 1; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:KFQ94461.1};
KW Homeobox {ECO:0000313|EMBL:KFQ94461.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053283};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 187..215
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 217..239
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 258..285
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 975..1002
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1003..1030
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1031..1059
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ94461.1"
FT NON_TER 1190
FT /evidence="ECO:0000313|EMBL:KFQ94461.1"
SQ SEQUENCE 1190 AA; 133401 MW; DC0A6B53544414D5 CRC64;
VVNYENVVET GSETDEEDKL HIAEDESAIS TLDQETSPAS VPNHESSPHV SQAALPREEE
EDEMRESGVD HTWHNNEILQ ASVDGPEEMK EDYDTMGPEA TIQTTGNNGT VKNANCTSDF
EEYFAKRKLE EGDGHAVSIA EYLQRSDTAI IYPEAPEELS RLGTPEANGQ EENDLPPGTP
DAFAQLLTCP YCDRGYKRLT SLKEHIKYRH EKNEENFSCP LCNYTFAYRT QLERHMVTHK
PGTDQHQMLT QGAGNRKFKC TECGKAFKYK HHLKEHLRIH SGEKPYECPN CKKRFSHSGS
YSSHISSKKC IGLISVNGRM RNNIKTGSSP NSVSSSPTNS AITQLRNKLE NGKPLSMSEQ
TGLLKIKTEP LDFNEYKVLM ASHGFSATSP FMNGGLGATS PLGVHASAQS PMQHLGVGME
APLLGFPAVG SNLSEVQKVL QIVDNTVSRQ KMDCKAEEIS KLKVYHMKDS CSQAEEQGVT
SPNIPPVGLP VVSHNGATKS IIDYTLEKVN EAKACLQSLT TDSRRQLNNI KKEKLRTLID
LVTEDKMIEN HNVSTPFSCQ FCKESFPGPI PLHQHERYLC KMNEEIKAVL QPHENMVPNK
PGVFDKQTLL LSSVLSEKGM TSPINPYKDH MSVLKAYYAM NMEPNSDELL KISIAVGLPQ
EFVKEWFEQR KVYQYSSSRS PSLERASAKV ALAATNNTPT KDSLSARSPI KPVDSITSPS
IAELHNSVTN CDTPLRLTKP PHFTNIKPVD KLDHSRSNTP SPLNLSSTSS KNSHSSSYTP
NSFSSEELQA EPLDLSLPKQ MKEPKSIIAT KNKTKSNSVN LEHNSVSSSS ENSDEPLNLT
FIKKEFSNSN NLDKSTNPVF GMNPFSAKPL YTTLPPQSAF PPATFMPPVQ TSIPGLRPYP
GLDQMSFLPH MAYTYPTGAA TFADMQQRRK YQRKQGFQGE LLDGTPDYMS GLDDMTDSDS
CLSRKKIKKT ESGMYACDLC DKTFQKSSSL LRHKYEHTGK RPHQCQICKK AFKHKHHLIE
HSRLHSGEKP YQCDKCGKRF SHSGSYSQHM NHRYSYCKRE AEEREAAERE AREKGHLEPT
ELLMNRAYLQ SITPQGYSDS EERESMPRDG ESEKEHEKEG EDGYEKLGRQ DGDEEFEEEE
EESENKSMDT DPDTIRDEEE TGDHSMDDSS EDGKMETKSD HEEDNMEDGM
//