ID A0A0V0X145_9BILA Unreviewed; 1239 AA.
AC A0A0V0X145;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN ORFNames=T06_223 {ECO:0000313|EMBL:KRX81673.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81673.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX81673.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX81673.1};
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 -!- 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|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:KRX81673.1}.
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DR EMBL; JYDK01000029; KRX81673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0X145; -.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000054673; 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:SF7; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA-RELATED; 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:KRX81673.1};
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:UP000054673};
KW Transferase {ECO:0000313|EMBL:KRX81673.1}.
FT DOMAIN 38..958
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 973..1169
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT REGION 731..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1236
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR608734-50"
SQ SEQUENCE 1239 AA; 140565 MW; AFD81373FA38AC4E CRC64;
MPGRVNFSAI FDDVPYAQML SKNQELFIRN MHSRTNIGVR LDYYMRLVQK TILNHTDPVT
SLFTSPLPGF TDHAWVRDNV YAVHAVWGLA LAYKKNADFD EDRAKCHELE QTCVKVMRSL
LQCFMRQSHK VEAFKKTQLP KDALHAKYSA RNWNTVVGDN EWGHLQIDAI SLYLLSLAQM
TASGMQIIFT LDEVAFVQNL VFYIEHAYRI PDYGIWERGD KTNHGVTELN ASSIGMAKAA
LQALNDLDLF GAYGSPNSVI HVMIDEIQQC QAVLKSLLPR ESYSKETDAA LLSIISYPAF
ALEDCTQIST TRATIMNKLQ GRYGCRRFLR DGYKTPREDP NRLYYEPHEL QQFENIECEW
PLFFCYFILD GFFSNNKSQV QYYRERLEEI VITSENGLKL VPELYAVPSN LVDEEIACPH
SQTRVATGSI PFLWAQSLYV LTCLIEEGFI QAAELDPLNR RLSTEKRPDT VVQVVVLAED
EEMKEKLAAQ GIEVELLKNV EPFIVQPAHV LGRLFSQLGR STKMKLSGRM STDVGLLSTS
KMYNVQDRIL VFTPQFLDWQ RFYLTHDVNI LIDTMKAELF YVKTSWNVPG RPLVVMVFSN
VMISNVSDDG KKVPLGMIGA LKKMKSGYIS GTRTILGKIS DFVTTSCIIK LHYLTDDESN
IDPKVSELLK SVLCSRKTES GGILRRSNKV KHSIGLQGEE RSRKYSFVRG ISQRHKSIML
DPSEVALMRD RRDSFVSSSS TGRKSSTNTD EEATPCSSPP VPLLSPTSPL LLRTSASGTR
LNLLDNANNK YGTKDLNEVD CKDLVEMLLD TEILEEQADI VQYLWLKQGS NWDTKLGGRA
EVTVRKLVEE LYQKACHQRL WWLVRHTAGL LNKVTESLTN AVTDLLVRQK QITVGMPSIH
EEPISCPLPP LELLKVIRAA LVEDECGIML TQEILIYLGM FIRTEPHLFT EMLRLRVGLI
IQIMITELAR GLHCSGEEAA TNVTNLSPYE LKTLLHHILS GKEFADRDEE NSEMITYTEK
TKAERTGIMQ LGKRMKDHKI VDVINSKEEM NMDNNMDWLQ WLRRRRIDGA LNRVPPEFYS
KIWLILRKCE GLLIGDQVLH QNLTQEMTTG EMKFALRVES VLNKIPDPEY RQLLVEALMV
LTILAENQTN VVLGPGLVLV DQIVHKANEF FLSDQKEANG DAVMCCAKSN KDPCGGTNGI
CRHFYDSAPS GRYGTITYMC RAVISIMPHL GEDIECAVS
//
