ID A0A0V0YM65_TRIPS Unreviewed; 648 AA.
AC A0A0V0YM65;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
DE Flags: Fragment;
GN ORFNames=T4E_8498 {ECO:0000313|EMBL:KRY01243.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRY01243.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRY01243.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRY01243.1};
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 -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC serine in certain substrates, including troponin I.
CC {ECO:0000256|RuleBase:RU364123}.
CC -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC {ECO:0000256|RuleBase:RU364123}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU364123};
CC Lipid-anchor {ECO:0000256|RuleBase:RU364123}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU364123}.
CC -!- PTM: Although the final Cys may be farnesylated, the terminal
CC tripeptide is probably not removed, and the C-terminus is not
CC methylated. {ECO:0000256|PIRSR:PIRSR608734-50}.
CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC family. {ECO:0000256|RuleBase:RU364123}.
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:KRY01243.1}.
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DR EMBL; JYDU01000004; KRY01243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0YM65; -.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR045583; KPBA/B_C.
DR InterPro; IPR008734; PHK_A/B_su.
DR PANTHER; PTHR10749; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10749:SF7; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA-RELATED; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR Pfam; PF19292; KPBB_C; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|RuleBase:RU364123};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU364123};
KW Cell membrane {ECO:0000256|RuleBase:RU364123};
KW Glycogen metabolism {ECO:0000256|RuleBase:RU364123};
KW Kinase {ECO:0000313|EMBL:KRY01243.1};
KW Lipoprotein {ECO:0000256|PIRSR:PIRSR608734-50,
KW ECO:0000256|RuleBase:RU364123}; Membrane {ECO:0000256|RuleBase:RU364123};
KW Prenylation {ECO:0000256|PIRSR:PIRSR608734-50,
KW ECO:0000256|RuleBase:RU364123};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Transferase {ECO:0000313|EMBL:KRY01243.1}.
FT DOMAIN 234..367
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 382..579
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT REGION 143..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 645
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR608734-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY01243.1"
FT NON_TER 648
FT /evidence="ECO:0000313|EMBL:KRY01243.1"
SQ SEQUENCE 648 AA; 72791 MW; 92BEECB4D9FB76DB CRC64;
LECAWTSIGS DDVAGDSKKV PLGMIGALKK MKSGYISGTR TILGKISDFV TTSCIIKLHY
LADDESNIDP KVSELLKSVL CSRMTESGGI LRRSNTVKHS TALQSEERNR KYSFVRGISQ
RHKSIMLDPN EVALITMRDR RDSFVSSGST GRKSSINTDE EATPCSSPPV TLSSPTSPLL
LRTSASGNRL NLLDNANNKY GTKDLNEVDC EDLVEMLLDT EILEEQADIV QYLWLKQGSN
WDTNLGGRAE VTVRKLVEEL YQKACHQRLW WLVRHTAGLL NKVTESLTNA VTDLLVRQKQ
ITVGMPSIRE EPISCPLPPL ELLKVIRAAL VEDECGIMLT QEILIYLGMF IRTEPHLFTE
MLRLRVGLII QIMITELARG LHCSGEEAAT NVTNLSPYEL KTLLHHILSG KEFADRDEEN
SEMITYTEKT KAERTGIMQL GKRIKDHKMV DVIKSKEEMN MDNNMDWLQW LRRRRIDGAL
NRVPPEFYSK IWLILRKCEG LLIGDRVLHQ NLTQEMTTGE MKFALRVESV LNKIPDPEYR
QLLVEALMVL TILAENQTNV VLGPGLVLVD QIVHKANEFF LSDQKEANGD AVMCCAKSNK
DPCGGTNGVC RHFYDSAPSG RYGTITYMCR AVISIMPHLG EDIECTVS
//
