ID A0A182QFD5_9DIPT Unreviewed; 1781 AA.
AC A0A182QFD5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF009061-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF009061-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF009061-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR EMBL; AXCN02000595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 69004.A0A182QFD5; -.
DR EnsemblMetazoa; AFAF009061-RA; AFAF009061-PA; AFAF009061.
DR VEuPathDB; VectorBase:AFAF009061; -.
DR OrthoDB; 5400441at2759; -.
DR Proteomes; UP000075886; 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 CDD; cd05589; STKc_PKN; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_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; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1454..1713
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1714..1781
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1781 AA; 194632 MW; 317AB531E67256F8 CRC64;
LLPYSLVLRH HAPGMSAPGL QPPSEITAEW TVHAQLTLSS TNRSSDASSS ATGITTNEGC
NERFGEQVPG HTTNISEGAV GGGECYDLNP PQPSTPLTTS SSSAVGNPVK VVYKFSTTDR
PLQQKQSPTA PTSPVASAGG VGGKSNVIFT TDPSPTTSTT PVTLAQTPTT GEGPPPPDAD
NAVPLSFPKC TSTCSIVLTA CTDLLPTSSE TLPIIVNKCE SINNIVVDKS TNFPEKLIRK
SISPHLNPLV SPSNTIRSQQ SNSVRDTSAA KKKPRTVHID VYCTGSDAES GSECGSCCSF
HDEAKSLPSS GTSSASSSHS SVSSGSRFDT SHMMELKAAT HPINDPTHPT VYESEEMRVR
HKRAGKHEVP RRLMQQTNDQ NTLSTIGSLK RTGSARHGRI RRNTTTDEIT ESKKLLFSKH
LGEAPKPEEQ IQEAFSKYFR RDVSDDAISS NYALSADRST RRDITGSSLS SAFACGGFYE
NDEDRETPSR LNRSGTTATQ SDSFEYDNSE DRYRIHEMER VWKQQHWKSP SVERRLLQLH
NPQVSQSACQ SPDSDHNLTE SDHSFVYDEA PHAQASNPSL NEYSDSSPST VKSASQRVTG
APTSRAVFLQ QQAVLAATLH QKHREFSPVE GYTDEYLAIA RRFGSLITGR RKPGTHMGPV
RNPECPCEHC RRWVLERDGN GISGSVLRER ALSVDAATVT PNGIVDMRRQ FHLRNTNAQG
RLSESSRKLD LLRKALELRR LELPPDCPTA QQLKAELQNV QASSPGPVQY TMRNSFRGSA
HGRPAQSQQS FSRCAAVTGK LEVRLMGCQD LLEDVPGRSR RDKDAGSSSP GDLKSFVKGV
TSRSSSKSYS VKDETSSEIM AVIKLDNITV GQTSWRPCSQ QAWDQRFSID LDRSRELEIG
VYWRDWRSLC AVKFLRLEEF IDDIRHGMAL QLEPQGVLFA EIKFLNPMIS RKPKLQRQRM
IFNKQQVKNI PRAKQMNINV ATWGRLLKRN TTSSSTTAAA TGPGALATTP SSGTAPVASG
MLANQTSGST VTTPSTPGSI GLSYDPLQDD PAETLGESAD HNIVGLGGGR PLGIHGVSVL
PESPSSHSLL NQGTPTSALT GGRPLPPPQS ISTPSSFRQK KQPMPSPRQA TPPKIDPELE
YALSKFDFLH QHDSLSGVGL YDKQLQQQEK LLTAVSSTGA AETDREQINN CDSTPLADTE
EDDSDVPPLP STPPPMLRSN GSHPSSTITP PAAVLQKSLS EDLLRPVLSM PPPILYGGCV
YSNRDSYYST VSSTGSPIVE EPPSPAPNQH LQYDAPFPED SLTYDSIIEI LPFDQFTIGG
NVVPPPLPPP HHHHHHPSTA LVAQQASLAA AAAVQAQQQQ QFYQQQQQLL LHQAPVGPQH
VAGGSQTSSA VVAGMADVGG SAAAAGSGVG IGPPVNRRAA GPTAARTLQY RDSAYESRRQ
SQAQAGAGMS LDSFRLLSVL GRGHFGKVIL AQYKNTGEYF AIKALKKGDI IARDEVESLL
SEKRIFEVAN TMRHPFLVNL FSCFQTDQHV CFVMEYAAGG DLMMHIHTDV FSEPRAVFYA
ACVVLGLQYL HESKIIYRDL KLDNLLLDTE GYVKIADFGL CKEGMGFGDR TGTFCGTPEF
LAPEVLTETS YTRAVDWWGL GVLIFEMLVG ESPFPGDDEE EVFDSIVNDE VRYPRFLSLE
AIAIMRRLLR KNPERRLGSS ERDAEDVKRQ AFFRNIVWDD LLLRKVKPPF VPTIRSQEDV
SNFDEEFTSE KPALTPPKDP RVLTETEQTY FKDFTYMADW C
//
