ID A0A091NEX8_9PASS Unreviewed; 738 AA.
AC A0A091NEX8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=52 kDa repressor of the inhibitor of the protein kinase {ECO:0000313|EMBL:KFP76571.1};
DE Flags: Fragment;
GN ORFNames=N310_13336 {ECO:0000313|EMBL:KFP76571.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP76571.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP76571.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP76571.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK831055; KFP76571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NEX8; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR025398; DUF4371.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR006612; THAP_Znf.
DR PANTHER; PTHR46289:SF16; 52 KDA REPRESSOR OF THE INHIBITOR OF THE PROTEIN KINASE; 1.
DR PANTHER; PTHR46289; 52 KDA REPRESSOR OF THE INHIBITOR OF THE PROTEIN KINASE-LIKE PROTEIN-RELATED; 1.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF14291; DUF4371; 1.
DR Pfam; PF05485; THAP; 1.
DR SMART; SM00692; DM3; 1.
DR SMART; SM00980; THAP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Kinase {ECO:0000313|EMBL:KFP76571.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Transferase {ECO:0000313|EMBL:KFP76571.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00309}.
FT DOMAIN 1..58
FT /note="THAP-type"
FT /evidence="ECO:0000259|PROSITE:PS50950"
FT REGION 94..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP76571.1"
FT NON_TER 738
FT /evidence="ECO:0000313|EMBL:KFP76571.1"
SQ SEQUENCE 738 AA; 84580 MW; 0D9A9A06E3E102B2 CRC64;
VRCQRWVENC RRADLEDKTP DQLNKHYRLC AKHFETSMIC RSSPYRTVLR DNAVPTIFDL
TSHLSNPHSR HRKRIKELSE DEIRTLKQQK IDESFKQEQK SQELNKSNQQ NAVPAGGGEE
REEETAPLSL EERENKDYLK SLFEILILMG KQNIPLDGHS VDELPEGIFA SDNFQALLEY
RINGGDEVLR KRFEMTAVNL EYCSKTQQKQ MLEICENCVR EETLREVRDS HFFSIVTDEV
VDIAGEEHLP VLVRFVDDSH NLREEFIGFL PYEPDPEVLA VKFHATITEK WGLNMEYCRG
QAYVVSSGFA SKMKLVATRL LEKYPQAVYT LCSSCALNVW LAKSVPVVGV SVALGTMEEV
CCLFHQSPHL MAELENTISA LFQGNEEKGN ELKEICHTQW TGRHDTFEVL VDLIQALVLC
LDAVSSDSSV RWNNFTAGRA FVLSSALTDF DFIVTIVIMK NVLSFTRAFG KNLQGQTSDV
FFAASSLTAV LHSLNEVMEN IEVYHEFWFE EATNLAAKLD VRMKLPGKLL RARQGNLDAD
LTSENYYKEI LSVPTVEHII QELKDIFSEQ HLKALKCLSL VPSVMGQLKF NTSEEHHADM
YKNDLPNPDT LSAELHCWRI KWKHRGKDIE LPATVYEALH LPDIKFFPNV YALLKVLSIL
PVMKVENEKY GIGRKRLKAY LKNTLREQRS SNLALLNINF DIKHDLDLMV DTYIKLYPEK
VECQDCVSPN KTEVTENA
//
