ID A0A091DAA6_FUKDA Unreviewed; 944 AA.
AC A0A091DAA6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN ORFNames=H920_10559 {ECO:0000313|EMBL:KFO28022.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO28022.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO28022.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO28022.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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};
CC -!- SUBCELLULAR LOCATION: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Midbody
CC {ECO:0000256|ARBA:ARBA00004214}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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; KN122825; KFO28022.1; -; Genomic_DNA.
DR RefSeq; XP_010634972.1; XM_010636670.2.
DR AlphaFoldDB; A0A091DAA6; -.
DR STRING; 885580.ENSFDAP00000005585; -.
DR GeneID; 104870886; -.
DR CTD; 5586; -.
DR eggNOG; KOG0694; Eukaryota.
DR OrthoDB; 5400441at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11631; HR1_PKN2_2; 1.
DR CDD; cd11635; HR1_PKN2_3; 1.
DR CDD; cd11622; HR1_PKN_1; 1.
DR CDD; cd05589; STKc_PKN; 1.
DR Gene3D; 2.60.40.150; C2 domain; 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; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037784; C2_PKN.
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; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF322; SERINE_THREONINE-PROTEIN KINASE N2; 1.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 3.
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; SSF46585; HR1 repeat; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 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; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO28022.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..70
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 82..164
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 165..245
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 313..433
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 617..876
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 877..944
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 74..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 944 AA; 107548 MW; 7D40E9AEFF33C75F CRC64;
MVQQKLDDIK DRIKREIRKE LKIKEGAENL RKVTTDKKSL AYVDNILKKS NKKLEELHHK
LQELNAHIVV SDPEDVTDCP RTPDTPNSDP RCSTSNNRLM ALQKQLDIEL KVKQGAENMI
QMYSNGSSKD RKLHGTAQQL LQDSKTKIEV IRMQILQAVQ TNELAFDNAK PVISPLELRM
EELRHHFRIE FAVAEGAKNV MKLLGSGKVT DRKALSEAQA RFNESSQKLD LLKYSLEQRL
NELPKNHPKS SIIIEELSLV TSPTLSPRQS VISTQNQYST LSKPAALTGT LEVRLMGCQD
ILENVPGRSK AASVALPGWS PSETRSSFMS RTSKSKSGSS RNLLKTDDLS NDVCAVLKLD
NTVVGQTSWK PISNQSWDQK FTLELDRSRE LEISVYWRDW RSLCAVKFLR LEDFLDNQRH
GMCLYLEPQG TLFAEVTFFN PVIERRPKLQ RQKKIFSKQQ GKTFLRAPQM NINIATWGRL
VRRAIPTVNH SGTFSPQAPV PTTVPVVDVR IPELVPSASD STVTKLDFDL EPEPPPAPPR
ASSLGDIDES SELRVLDTPG QDPKTVFDVE NDRNIILPKS QSEYESDTPD SGLGYSDTRE
LEDRRSQQRF QFNLQDFRCC AVLGRGHFGK VLLAEYKHTN EMFAIKALKK GDIVARDEVD
SLMCEKRIFE TVNSVRHPFL VNLFACFQTK EHVCFVMEYA AGGDLMMHIH TDVFSEPRAV
FYAACVVLGL QYLHEHKIVY RDLKLDNLLL DTEGFVKIAD FGLCKEGMGY GDRTSTFCGT
PEFLAPEVLT ETSYTRAVDW WGLGVLIYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL
STEAISIMRR LLRRNPERRL GAGEKDAEDV KKHPFFRLID WSALMDKKVK PPFVPTIRGR
EDVSNFDDEF TSEAPILTPP REPRILSEEE QEMFRDFDYI ADWC
//
