ID A0A1V4JTQ5_PATFA Unreviewed; 740 AA.
AC A0A1V4JTQ5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Repressor of the inhibitor of the protein kinase {ECO:0000313|EMBL:OPJ75553.1};
GN Name=PRKRIR {ECO:0000313|EMBL:OPJ75553.1};
GN ORFNames=AV530_004061 {ECO:0000313|EMBL:OPJ75553.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ75553.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ75553.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ75553.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ75553.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ75553.1}.
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DR EMBL; LSYS01006220; OPJ75553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JTQ5; -.
DR STRING; 372326.A0A1V4JTQ5; -.
DR Proteomes; UP000190648; 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; 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 PROSITE; PS50950; ZF_THAP; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Kinase {ECO:0000313|EMBL:OPJ75553.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Transferase {ECO:0000313|EMBL:OPJ75553.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00309}.
FT DOMAIN 1..59
FT /note="THAP-type"
FT /evidence="ECO:0000259|PROSITE:PS50950"
FT REGION 99..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 85187 MW; E1E5E773B73CAB56 CRC64;
MARCQRWVEN CRRADLEDKT PDQLNKHYRL CAKHFETSMI CRSSPYRTVL RDNAVPTIFD
LTSHLNNPHS RHRKRIKELS EDEIRTLKQQ KIDEAFERQQ ATQELNESNE QNTVSEEGGE
EQEEEAVPLT LEERENKDYL KSLFEILILM GKQNIPLDGH GVDELPEGIF TSDNFQALLE
YRINSGDEVL RKRFEMTAVN LEYCSKTQQK QMLEICESCV REETLREVRD SHFFSLVTDE
VVDIAGEEHL PVLVRFVDDS HNLREEFIGF LPYEADPEIL AVKFHTTITE KWGLNMEYCR
GQAYIVSSGF ASKMKVVATR LLEKYPQAVY TLCSSCALNI WLAKSVPVVG VSIALGTIEE
VCCLFNQFPQ LLVELDNTIS VLFQNNEVKG NELKEICRSQ WTGRHDTFEV LVDLIQALVL
CLDAVCSDSS VRWNNFIAGR AFVLSSALTD FDFIVTIVIL KNALSFTRAF GKNLQGQTSD
VFFAAGSLTA VLHSLNEVME NIEVYHEFWF EEATNLATKL DVQVKLPGKF RRAQQGSLDS
EITSENYYKE ILSVPTIEHI IQELKDIFSE QHLKALKCLS LVPSVMGQLK FNTSEEHHAD
MYKNDLPNPD TLSAELHCWR IKWKHRGKDI ELPATIYEAL HLPDIKFFPN VYALLKVLCI
LPVMKVENEK YEMGRKRLKA YLKNTLTEQR SSNLALLNIN FDIKHDLDLM VDTYIKLYPE
KVEFQEDFIP SNNSEVTEDA
//
