ID A0A498S8E0_ACAVI Unreviewed; 1109 AA.
AC A0A498S8E0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein kinase C {ECO:0008006|Google:ProtNLM};
GN ORFNames=NAV_LOCUS4528 {ECO:0000313|EMBL:VBB29736.1};
OS Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB29736.1, ECO:0000313|Proteomes:UP000276991};
RN [1] {ECO:0000313|EMBL:VBB29736.1, ECO:0000313|Proteomes:UP000276991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000946};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};
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DR EMBL; UPTC01000683; VBB29736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498S8E0; -.
DR STRING; 6277.A0A498S8E0; -.
DR Proteomes; UP000276991; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd11623; HR1_PKN_2; 1.
DR CDD; cd05589; STKc_PKN; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF242; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF02185; HR1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00742; Hr1; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; HR1 repeat; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000276991};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 152..227
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 230..309
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 788..1040
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1043..1109
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..110
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 817
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1109 AA; 124738 MW; AA1159535FBD6BA9 CRC64;
MADVARPDPI SWQHIVESSE GDPCSSNDTA VPEELALLAD KYTFSFGEQK SLQKDVIELK
KKIRTSCNKQ MRIKQGYVQM QKVTKERKQS DFLKKEIRDL SDQISDMKDD LQTLDMYDSG
AFDDGDDING MPNSPSEDAL TADGSSDGAG LELSAENSET VTNSRLTSLQ KELDKEMKVK
DGLERFLAIG QTNRKLQEES KSMLFDSKAK IALLRMQIEK MQRQEQVDAG LSGKTIPTKT
EMIVDDLLFR LRKEAAIAEG ARNMIRILSS QRKSDGKSLS QAFDNQMQSE EKLDLIRLAL
AKYSARLPND SPKKNEIRDA ILESERLPLT GHYHHHRDGT FSPPSSAPGS PSQDDSKSAS
LPRLALSLKR LYALPSLAVS GRLEVRLIGC QNLMVDIPRR LPRTDISSVV TTAGDSLSGF
TQKTRNTRGN GPRTSRISMG QQVNDSIVTV ALCAANDSDI STLRQDRHQC GVLRPAQQQI
HCMFFSLLFT GTAKLSPNDE VTATVLLDSR EVASTDSRPV SQQAWDQHFS IDLDRSKELE
IEIRYRDWRS ICAFTVVKLG DIVEPSERAG MVLNLEPQGD LFAEFKYLNP VVSRKPKLER
QKRLFRVKER KEIASAKKQL GVAAWSRLMK QFGGSQSNES IEPVLSPTYG GLYTAANTTA
TAPLPPVAKS AHTLPSRLTV DRPLTSSTSG LFAPESSHMR PVLPSLLPSS IRFGDSSEMS
KTKQNQRFYE QPKIPPVIPS RPSPKTQVVA SRIESPPPLP TSKPPPLTHR RTSRITSPAI
SSLTIDKFHL ISVLGRGHFG KVILAKYKGN GEYYALKVLK KGDVLGRDEV ESLMIATSRR
HPFLVNLFAC MQSKEHVFFV MEYSMGGDLM RHIHDDIFTE ERSCFYAACV LLGLEFLHAN
NIIYRDLKLD NLLLDREGYV KLADFGLCKE GMGPTDRTST FCGTPEFLAP EVLTENSYTR
AIDWWGLGVL IFEMLVGEPP FSGEDEEEIF DSIVNDDVRY PRFLSIESIS IMRRLMRKNP
EKRLGSGQND ALDVKQQRFF KHVNWDWDKL LNKEIRPKFV PQIKNLEDVS NFDEEFTKET
PRFSSAKDKR LITDADQMLF KDFDFSLIH
//
