ID G3TUY0_LOXAF Unreviewed; 1154 AA.
AC G3TUY0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Zinc finger and AT-hook domain containing {ECO:0000313|Ensembl:ENSLAFP00000019388.1};
GN Name=ZFAT {ECO:0000313|Ensembl:ENSLAFP00000019388.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000019388.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000019388.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019388.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000019388.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019388.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; G3TUY0; -.
DR Ensembl; ENSLAFT00000035695.1; ENSLAFP00000019388.1; ENSLAFG00000010205.4.
DR GeneTree; ENSGT00940000156658; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 11.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24388:SF53; COMBGAP, ISOFORM L-RELATED; 1.
DR PANTHER; PTHR24388; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR Pfam; PF13909; zf-H2C2_5; 1.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 112..142
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 268..295
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 296..323
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 351..379
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 401..428
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 429..451
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 455..483
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 739..766
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 827..850
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 906..933
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 934..961
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 963..990
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 991..1019
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 66..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 129091 MW; 176BBBBDC788A13A CRC64;
LTENTAIFMC KCCNLFSPSQ SELLSHVSEK HAEEGVNADE IIIPLRPLST PEPTNPSKTG
DEFLVVKRKR GRPKGSTKKP CAEEELAEHV MTPAENSPLA SEEGSSLAPS SLECSKCCRK
FSNTRQLRKH ICIIVLNLGE EDGDAGNESD IELEKKYKED DREKASKRPR AQKTEKVQKI
SSGKEAGQLS GVKKPIISVV LTAHEAIPGA TKIVPVEAGP PEAEAANPET TVADLAHRRG
YQEYAIQQTP YEQPMKSSRL GPTQLKIFTC EYCNKVFKFK HSLQAHLRIH TNEKPYKCPQ
CSYASAIKAN LNVHLRKHTG EKFACDACSF TCLSKGHLKV HIERVHKKIK QHCRFCKKKY
SDVKNLIRHI RDAHDPQDQK VKEALDKLCL MTREGKRQLL YDCHICERKF KNELDRDRHM
LVHGDQWPFA CELCGHGATK YQALELHIRK HPFVYVCALC LKKFVSSVRL RAHIKEAHGA
AQEAAVFNSS VNQSFCLLEP GGDIHQEALG DQLQLAEEEL VFQGVSAPKE AACPADPRPE
EGQKEPEAPV EIPAPAEHSA TPPAEGATLP PCELGATVVS SALSSPAVVS SDFLLKNDTS
STAEAHTVPE KTVDPQHGDP THTQDEGIVL LLSKDKGTNP HREARDAESP PCERQDPAAL
PPTSPDPSRY LRSGPAEASE LLPPVAGGGD VVIRQPDSCK PASEPQSDVT PFMKILNSLQ
KKQMNTGLCE RIRKVYGDLE CEYCGKLFWY QVHFDMHVRT HTREHLYYCS QCHYSSITKN
CLKRHVIQKH SNILLKCPTD GCDYSTPDKY KLQAHLKVHT ELDKRSYSCP VCEKSFSEDR
LIKSHIKTNH PEVSMSTISE VLGRRVQLKG LIGKRATKCP YCDFYFMKNG SDLQRHIWAH
EGVKPFKCSL CEYATRSKSN LKAHMNRHST EKTHLCDMCG KKFKSKGTLK SHKLLHTADG
KQFKCTVCDY TAAQKPQLLR HMEQHASFKP FRCAHCHYSC NISGSLKRHY NRKHPNEEYT
NVGTGELAAE ALVQQGGMKC PVCSFVYGTK WEFNRHLKNK HGLKLVENEG DPKWEVTDEE
PSSNHTVMIQ ETLQQASVEL AEQHHLVVSS NDVEGIETVT VYTQGGEASE FIFYVQEAVQ
PAEGQPAEPP GPEL
//
