ID   A0A0V0YDI8_TRIPS        Unreviewed;       952 AA.
AC   A0A0V0YDI8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN   ORFNames=T4E_7987 {ECO:0000313|EMBL:KRX98381.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX98381.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX98381.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX98381.1};
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|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}.
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:KRX98381.1}.
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DR   EMBL; JYDU01000022; KRX98381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0YDI8; -.
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   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
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:SF8; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT BETA; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   Pfam; PF19292; KPBB_C; 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}; Kinase {ECO:0000313|EMBL:KRX98381.1};
KW   Lipoprotein {ECO:0000256|RuleBase:RU364123};
KW   Membrane {ECO:0000256|RuleBase:RU364123};
KW   Prenylation {ECO:0000256|RuleBase:RU364123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Transferase {ECO:0000313|EMBL:KRX98381.1}.
FT   DOMAIN          42..803
FT                   /note="GH15-like"
FT                   /evidence="ECO:0000259|Pfam:PF00723"
FT   DOMAIN          806..886
FT                   /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT                   C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19292"
SQ   SEQUENCE   952 AA;  108412 MW;  373EE6FBB6B07789 CRC64;
     MYRKNSMLEE RPISPDSIQL LHAGMNHSVR LSASEKIASQ QQLDYYYAVV KKQILQFQSY
     TTGLFPRYST ENNVGYVRDS LYCAMTCWAL SRGYLRLNDD QGRYYELGQA AVKTMRGILL
     CWMRQSDKVE NFKRVHSAVF ALHSKFNLLT GEAVEGTENY GHLQIDVVAL FILTLVQMIT
     SGLEIIYTTD EVSFVQNIVF YIERAYRTPD FGMWEMGTRY NDGTPELHAS SIGMVKAALE
     AINGCNLYGS KGTVGSVIYV DIDAHNRNRT TFETLLPRES NSKNVDASLI PTISFPCFAA
     HDESLHHRTF AKCIRKLKGK YGFKRFLRDG QFCVLENPNR QFYQSGETKL FQGVECQWPM
     FFVYMIIDGV YMGNQHQKQS YRIIIIFKLK VFITSVLILD LRSCCQAWAR DFSYGAKREN
     LIHVSDIDPS YRHLPANQRP KVDNRHSVFQ GSLTNPVLQI AFITESQKLQ TMLSTYGITT
     QTLHQVEPVQ IWSPGQMVKV FENLGKNVRL QLSGRPNRPL GALGTSKVYR VFGETVLCYP
     LLFDVQDFYL SSDAEVLIDD IKRDLKFIEC RWQLAGRPTI CLLLTEDLVC GEHFSKVLNL
     LVDLKSGLCN GIRVRVGRLQ NLLSAGCLEH LDFAPQGYSV DFIPEPMREV KSMSDYSSLS
     DLSHCLMEAV TDKDFDVEPF KTQPTEEIIA TLKNLPKAAL YTQCRRVVRY CAALLRKVVD
     SLAPSITSIL VRGKRLTVGV FGGEEVIIDS PVTPNVIEEE LYRVCFPHDI LACVLQQELI
     IVLGHFISVE PELFIGILKV RIGTAMQQRQ LNGSLNRVPP DFFEHMWRTL ERTSDGIVVA
     THHLPQQPTL SDMTEYELNF ALTIDELLSR IQIPEYRQIM VELISKAFGY YADDKKLTDR
     QDMTPFYELY PHLFGGSSTY LAKAVINDLL SIPTDSVDSK KQLSCDTNCR LS
//