ID A0A091MWF1_9PASS Unreviewed; 1198 AA.
AC A0A091MWF1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
DE Flags: Fragment;
GN ORFNames=N310_01280 {ECO:0000313|EMBL:KFP81017.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP81017.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP81017.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP81017.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC serine in certain substrates, including troponin I. The alpha chain may
CC bind calmodulin. {ECO:0000256|ARBA:ARBA00002837}.
CC -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC {ECO:0000256|ARBA:ARBA00005131, ECO:0000256|RuleBase:RU364123}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342,
CC ECO:0000256|RuleBase:RU364123}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342,
CC ECO:0000256|RuleBase:RU364123}. Membrane
CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
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}.
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DR EMBL; KK837834; KFP81017.1; -; Genomic_DNA.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000053537; 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:SF5; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA, LIVER ISOFORM; 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:KFP81017.1};
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:UP000053537};
KW Transferase {ECO:0000313|EMBL:KFP81017.1}.
FT DOMAIN 3..891
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 1024..1133
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT REGION 998..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1195
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR608734-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP81017.1"
FT NON_TER 1198
FT /evidence="ECO:0000313|EMBL:KFP81017.1"
SQ SEQUENCE 1198 AA; 134529 MW; 17F9EA6B7FC57ED9 CRC64;
CGQNPVTGLL SAGTDHKDAW VRDNIYSILA VWGLGMAYRK NADRDEDKAK AYELEQNVVK
LMRGLLQCMM RQVDKVEKFK RTQSTKDCLH AKYNSATCAT VVGDDQWGHL QVDATSLYLL
FLAQMTASGL RIIFTLDEVT FIQNLVFYIE AAYKVADYGI WERGDKTNQG IPELNASSVG
MAKAALEAID ELDLFGAHGG HKSVIHVLPD EVEHCQSILY SMLPRASTSK EIDAGLLSII
SYPAFAVEDL NLVNVTKSEI ISKLQGRYGC CRFLRDGYKT PREDPSRLHY DPAELKLFEN
IECEWPVFWT YFLIDGIFNE DKIQVQEYRE ALEGILIREK NGLVLMPELY AVPPEKVDEE
YENPHSVDRI PVGKLPHLWG QSLYVLSCLL AEGFLAAGEI DPLNRRFSTG FKPDVVVQVT
VLAESNHIKN LLQDRGINVQ SIADIQPLRV QPARILSNLY TMLGRNKNMK LSGRPHRHIG
VLGTSKLYVI RNQIFAFTPQ FTDQHHFYLA LDNQMIVEML KIELAYLTSC WRMTGRPTLT
FPITHTMLVD DGTDIHPAVL ATIRKLEDGY FGGARVKIGK LSEFLTTSFH TYLSFLDPDC
DLKVFDDHNE GCSSPDSEYG DYPADFYEKD SQDELDQYIN DVLQSTALKS YLPPTSKTAN
QPPVFSANHS TEEILSIMAK TKGLEVPAVS MSLPTKVLNT HRKSLNLVDN PHFFETKDFV
LHLPKDAHGD LDCKKLVDQL KECPTLHDQA DILYILHILK GADWDTELDG QYGVTVHCLL
NELYRKAGLN QEWGLIRYIS GILKKRVEVL AEACTDLLSH HKQLTVGLPP EPREKIITAP
LPPEELTDLI YEASGQDISI AVLTQEIIMY LAMYVRSQPS LFVEMLRLRI GLIIQVMATE
LARSLKCSGE EASESLMNLS PFDXXXXXXX XEFGVERSLR PVDSSSSSPA ISIHEMGHSG
ATKTERSGIT KLKSCPVKLW MPYPWGYLRK QLTKALMSLQ RSSTPSSPTS TSPTGSSGDM
SWGDRKGQWL RRRRLDGAIN RVPVGFYEKV WKILQKCHGL SIDGYVLPSS TTREMTPCEI
KFAVHVESVL NHVPQPEYRQ LLVEAILVLT FLSDIEVSSI GGIIHVDRIV HMANDLFLQE
LKSFGATGSI LEKDVATGIC HFFYDSAPSG AYGTMTYLTK AIIIYLHDFL PSTGCAMQ
//
