ID A0A0Q3LVY3_AMAAE Unreviewed; 374 AA.
AC A0A0Q3LVY3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=cAMP-dependent protein kinase type II-beta regulatory subunit {ECO:0000313|EMBL:KQK74736.1};
GN ORFNames=AAES_169599 {ECO:0000313|EMBL:KQK74736.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK74736.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK74736.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK74736.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000256|ARBA:ARBA00005753}.
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:KQK74736.1}.
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DR EMBL; LMAW01003011; KQK74736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3LVY3; -.
DR STRING; 12930.A0A0Q3LVY3; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR PANTHER; PTHR11635:SF156; CAMP-DEPENDENT PROTEIN KINASE TYPE II-BETA REGULATORY SUBUNIT; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 3: Inferred from homology;
KW cAMP {ECO:0000256|ARBA:ARBA00023149};
KW cAMP-binding {ECO:0000256|ARBA:ARBA00022566};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022566};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..229
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 232..358
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 374 AA; 42515 MW; 6D59EFCC806E8A39 CRC64;
MWVQSLNMSQ ITYFSIVNCL DPYENENRRL YKSTSEYVAV WYATPYAILE KLKKLLYFEL
ILYIFIVIIS VCAEAYNPDE EDDDAESRII HPKTDDQRNR LQEACKDILL FKNLDPEQMS
QVLDAMFEKL VEGGEHVIDQ GDDGDNFYVI DRGTYDIYVK CDGVGRCIGT YDNRGSFGEL
ALMYNTPRAA TIIATSPGAI WGLDRVTFRR IIVKNNAKKR RMYENFIQSL PFLKSLEVSE
RLKVVDVIGT KVYKDGEQII AQGDLADSFF IVESGEVRII MSRKDKQDVE ENGAVEIARC
SRGQYFGELA LVTNKPRAAS AFALGTVKCL VMDVQAFERL LGPCMEILKR NIANYEEQLV
ALFGTNMDIA DTSA
//
