ID A0A0B2VJC7_TOXCA Unreviewed; 1409 AA.
AC A0A0B2VJC7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN ORFNames=Tcan_18784 {ECO:0000313|EMBL:KHN83596.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN83596.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN83596.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN83596.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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:KHN83596.1}.
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DR EMBL; JPKZ01001178; KHN83596.1; -; Genomic_DNA.
DR STRING; 6265.A0A0B2VJC7; -.
DR OMA; QIWPSWK; -.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000031036; 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 CDD; cd00024; CD_CSD; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
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; PF00385; Chromo; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR Pfam; PF19292; KPBB_C; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS50013; CHROMO_2; 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:KHN83596.1};
KW Lipoprotein {ECO:0000256|RuleBase:RU364123};
KW Membrane {ECO:0000256|RuleBase:RU364123};
KW Prenylation {ECO:0000256|RuleBase:RU364123};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Transferase {ECO:0000313|EMBL:KHN83596.1}.
FT DOMAIN 1239..1291
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
SQ SEQUENCE 1409 AA; 160818 MW; A783CC6A680E4ADF CRC64;
MTASDQRRHQ RGSTSSRLRR FTQPYLISAH HLQPKVVKNV LEQVDNVYHM VQKVILDHQS
VTSGLFPRYS KDRNIGYVKD SIYCALACWA SSIAYKRLDD DRGRQTELRQ SAVKAMRGIM
FAWMQQLDNL NNFKDKNAPE YALHARFDLH TGMALKSPND KAGRLSVYGH LQMDLIALFL
LALVQMTAGG VQVVFTHDEV CFVQNLVFYI ERTYRTPDFG MWERGTRYNI GEPELHASSL
GMVKAALEAI NGFNLYGASG TSASVIYVDI DGHNRNRTTF ETILPRESNS KNTDAALLVA
VGWPAFGTHD PQLFEKTVNK CVRRLEGKYG MKRFFRDGYH TELEDASRQH YNIHETCRFQ
DIECQFPMFF AFMVITSELR GNQESAKKYW DKLTELLVST ENGVHLVMPE CYIIEEEFMA
EERDKPNSQD FYAASPNEFG HHLWSNAVYI IALLLHRQLI HASDIDPIYR HLPASQRPSN
PNRHSAFQVS LTEVFIMALM DYMIQRETDS SDMSFGSMEG NPVVQVALIA ESSRLQMMLS
TYGISAQTPH ELEPVQIWPS WKMVKGSMEG NPVVQVALIA ESSRLQMMLS TYGISAQTPH
ELEPVQIWPS WKMVKVFESL GKNNKLGLRG RPPRPFGPLN TSKIFKLFGD TILCYPLLFE
VKDFYINADP AVLIDDIKLD LEFISKRWKL AGRPTFCLVL REENVSGEYF SHMLDLLVSM
KNGFVNGVRV RIGRVHQLLN TGCTEHVDFA TSEDASVAED AFEELGGKTS QMISRISLRD
VVEEDVTSRE QDFLSRPDQE LYELVKKHDV DNLRVVAFAN AVLCRRYGSE FQVDGETLAV
RMERVYRQAC AWRLWWLVRF CAGKLRKTMN SLAPSITNML VRGKQVTLGV RGCREVTVSS
PMTPGEIMDI LFNSCPDNDP QAAVLQQELI IACSDLICKK PYAFDGVLTI RLSWLSDAIA
LMLDYVQNTK CGDRSPHSRR TAPTTPTRVR FPPKFEQETH VYDLSPTEIK DVVAALLTRK
NWHLLTPLQS RRLNGSLNRV PTNLYDSVWK ILERTEGGLV IAGHYLPQQP TLSDMTQFEL
TFAYKIESMM SVIAHPEYRQ VLVELLCIVA VILERNRELM FTGKLDCDHL VRRAFRRYCE
EQGIQDQDDM TPFYQLDDSD LTARSTANYL ARTVIDVLLS GATTGRRKLS TFMPCDKLST
SDRPDEQINS CIFELADRME SGDTSHSVKA GCASDCDTYE VEKIVGYRRN VQMNRDEYLV
KWQQYPVNES TFEPIHHLVH CRNNLSAFHS RLLKSAGVTA NTEVQSDDSD DSDIVLPLEA
INEENMLKRM YPNEQESGIA KGWAVKRIVG AQLNNQPYTY LVEYEDQKQL EHIGIDFLRE
KCPKIVDDFH LSIDKPYPCE SESGLSEHN
//
