ID A0A183LUR7_9TREM Unreviewed; 217 AA.
AC A0A183LUR7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN ORFNames=SMRZ_LOCUS7542 {ECO:0000313|EMBL:VDO76873.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|Proteomes:UP000050790, ECO:0000313|WBParaSite:SMRZ_0000754301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0000754301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO76873.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDO76873.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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|ARBA:ARBA00005131, 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 -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC family. {ECO:0000256|ARBA:ARBA00007128, ECO:0000256|RuleBase:RU364123}.
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DR EMBL; UZAI01003062; VDO76873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183LUR7; -.
DR STRING; 48269.A0A183LUR7; -.
DR WBParaSite; SMRZ_0000754301-mRNA-1; SMRZ_0000754301-mRNA-1; SMRZ_0000754301.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000050790; Unplaced.
DR Proteomes; UP000277204; 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:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR011613; GH15-like.
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 SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860,
KW 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|ARBA:ARBA00022600,
KW ECO:0000256|RuleBase:RU364123};
KW Lipoprotein {ECO:0000256|RuleBase:RU364123};
KW Membrane {ECO:0000256|RuleBase:RU364123};
KW Prenylation {ECO:0000256|RuleBase:RU364123};
KW Reference proteome {ECO:0000313|Proteomes:UP000277204}.
FT DOMAIN 4..201
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
SQ SEQUENCE 217 AA; 24831 MW; 644D2BEB93EDC7D7 CRC64;
MDKKKLDFYF TLLESSILCY QHSITGLIPS SSKSSHAWVR DNTYASLSIW GLSLVYRKLP
DVDEDRCRSY ELEKCVVKLM RGILICYMKQ SDKVELLKKT QNPIHSLHAK FDSTSYKTVV
GDLEWGHLQI DAISVFLLIL AQMTAAGLRI IWTLEEVAFV QNLVFCIEHA YRIPDYGIWE
RGDKTNHGLP ELNTTSVGMA KVSNVCFSLN FCVYMIC
//