ID A0A0V0SG99_9BILA Unreviewed; 454 AA.
AC A0A0V0SG99;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=cAMP-dependent protein kinase regulatory subunit {ECO:0000313|EMBL:KRX25752.1};
GN ORFNames=T07_1986 {ECO:0000313|EMBL:KRX25752.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX25752.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX25752.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX25752.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX25752.1}.
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DR EMBL; JYDL01000010; KRX25752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0SG99; -.
DR STRING; 6336.A0A0V0SG99; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd12097; DD_RI_PKA; 1.
DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
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:SF126; CAMP-DEPENDENT PROTEIN KINASE TYPE I-BETA REGULATORY SUBUNIT; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000313|EMBL:KRX25752.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022566};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KRX25752.1}.
FT DOMAIN 213..328
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 331..452
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 86..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 50244 MW; 716C11D546FF7069 CRC64;
MLPFSIMSSI FGKGNDDGLV MSHRSAWARL CEDYLERHNI SDLIKRAVVR LCIAQPDDPV
AFLSHYFQLL EKGEVVGTVI VGKRQSDGAG PLPTEQAPSN KPPPTVVIQE SSGDVSALPQ
QGTTATTTTA TTRAESNKVS TLNQPSPSES HDEEDLGAVD SAGAADSKAR SRRGAVSAEV
YSEEDIANYV KKVVPKDEET KKALEKAMCQ NVLFAHLDEN EKKDIFNAMF PVEANAGEVI
IQQGDEGDNF YVIDSGEVEV FVNNKSVTTI KESGSFGELA LIYGTPRAAT VLAKTRVKLW
ALDRDTYRRI LMGSTIRKRK QYEEFLSKVK ILEDLDKWER LTVADALEPV AFEKGTHIVE
QGQPGDNFFI ILEGEAEVYQ KRSEDSKPEL VGHLNPSEYF GEIALLLDRP RAATVVAKTP
LKCAKLDRAR FERVMGPCSE ILKRNILNYN SYRV
//
