ID A0A093PFL5_9PASS Unreviewed; 76 AA.
AC A0A093PFL5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=cAMP-dependent protein kinase inhibitor {ECO:0000256|PIRNR:PIRNR001667};
GN ORFNames=N305_08777 {ECO:0000313|EMBL:KFW75201.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW75201.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW75201.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW75201.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent
CC protein kinase activity, this protein interacts with the catalytic
CC subunit of the enzyme after the cAMP-induced dissociation of its
CC regulatory chains. {ECO:0000256|ARBA:ARBA00002844}.
CC -!- SIMILARITY: Belongs to the PKI family. {ECO:0000256|ARBA:ARBA00006393,
CC ECO:0000256|PIRNR:PIRNR001667}.
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DR EMBL; KL669028; KFW75201.1; -; Genomic_DNA.
DR RefSeq; XP_017934666.1; XM_018079177.1.
DR AlphaFoldDB; A0A093PFL5; -.
DR STRING; 328815.ENSMVIP00005022568; -.
DR GeneID; 103762737; -.
DR CTD; 5569; -.
DR OrthoDB; 4010609at2759; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR004171; cAMP_dep_PKI.
DR PANTHER; PTHR15416:SF2; CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA; 1.
DR PANTHER; PTHR15416; CAMP-DEPENDENT PROTEIN KINASE INHIBITOR/PKI; 1.
DR Pfam; PF02827; PKI; 1.
DR PIRSF; PIRSF001667; PKI; 1.
PE 3: Inferred from homology;
KW Protein kinase inhibitor {ECO:0000256|PIRNR:PIRNR001667};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258}.
FT REGION 49..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 16
FT /note="Important for inhibition"
FT /evidence="ECO:0000256|PIRSR:PIRSR001667-1"
FT SITE 19
FT /note="Important for inhibition"
FT /evidence="ECO:0000256|PIRSR:PIRSR001667-1"
FT SITE 20
FT /note="Important for inhibition"
FT /evidence="ECO:0000256|PIRSR:PIRSR001667-1"
SQ SEQUENCE 76 AA; 8036 MW; 5042F6B523DB8353 CRC64;
MTDVESTYAD FIASGRTGRR NALHDILVSS PGGNSSELAL KLSELDINKA EGEGDAQRNP
SEQTGEVQGE AAKQES
//
