ID A0A0V1A2Y7_9BILA Unreviewed; 1766 AA.
AC A0A0V1A2Y7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=CDC42BPA {ECO:0000313|EMBL:KRY18745.1};
GN ORFNames=T12_3675 {ECO:0000313|EMBL:KRY18745.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY18745.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY18745.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY18745.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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:KRY18745.1}.
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DR EMBL; JYDQ01000043; KRY18745.1; -; Genomic_DNA.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20809; C1_MRCK; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR CDD; cd05597; STKc_DMPK_like; 1.
DR Gene3D; 1.20.5.340; -; 2.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF66; SERINE_THREONINE-PROTEIN KINASE GENGHIS KHAN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRY18745.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 78..343
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 344..414
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1095..1145
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1329..1610
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1679..1692
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 511..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 440..470
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 641..675
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 712..807
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 911..973
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1007..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1766 AA; 199949 MW; 41AC46DE3CF5B496 CRC64;
MNFVPGDQRV VQLENLYLTG PLFGDSASFE TLVDVLICLF DECCNSTLRK EKNIAEFVER
LKSIVNKAKS LRLRRDDFDV LKVIGRGAFG EVAVVRMKNT DKIFAMKILN KWEMLKRAET
ACFKEERDVL VFGDRRWITN LHYAFQDEKN LYLIMDYYVG GDMLTLLSKF EDRLPEDMAK
FYICEMVLAI DSVHRLGYVH RDIKPDNVLL DINGHIKLAD FGSCLKLKSD GTVQSNVAVG
TPDYISPEIL RAMEDGKGCY GKECDWWSLG ICLYEMLFGQ TPFYAESLTE TYGKIMDHQE
ELCFPSEPAV SEEAKHLLKS LICPADQRFG KNGLSDFQNH AFFRDMDWEN IRDTNAPYIP
EISSPTDTSN FDVEESDFTP CETKPPNVSA PFTGHHLPFI GFTYTHNSKL SDSNSLAALL
TKPANLAENG VVRFTDMVTV EAYERRIERL ENEKTELDRK LKEATRLLQA QFHGSNTLER
NVHDKSQLTE VDVTTIAQLK DENQILRRRL MERESPSTSR KEANAAAASE ELEQKCRDLQ
KKHRQLLSER NQLQEQFGDA LERIKESKYQ LKEAIKHRDM ARQEFAEISV KVGELQSEKQ
KLLRMNRERD DECRTLQQKL DVIKTDVIKL EKWKREHELG AQQIQEECER ERRLREEYER
DLTALKAKME AASTTTVVNS ADQDEHISNS VKKQNDLDRS IQLTEEALEL ERTRHARQVS
MLESQLQEAK AQVQLLQAKL DDLLLQHKQE RSVLIGEHEE TLVELQAAVE RERESRLEMQ
NQLQTENDML KDRVDKLQMH VEEREKQLCL AQQECKFSLD LESRLAELSQ WVSDEKEVRD
YLQMLAAKLT DELERLKFDA EQKKHNNSGS VVGGPTTPRS KINYGLLSST LASGEKGWGS
RRSHKLAKME ILDLQRNLQS EIRAKQEVTE ELTKFRSTYF ACKQQLEAAE VRIGELTREV
HARDCQLEEA QRQLGVRVLP DYAKSLDQLV QFSSILNLFK DDEAASSGGS DSMNSNKTSN
NNNNGTNNSR DQQTDCSGAV EFCDSPQQQQ YPQQQQQQQQ QQQQPLQRRE AMTVSPPNYE
NARGINRIRA RAPPQHRFNI SVFAQPTKCH HCTSLMVGLT RQGLVCQDCQ FACHPSCLPK
AQPSCPAPQE PRRPLGIDPS RGLGTTYQGL VRVPKPGGLK KGWTSQLLVV CDLKLFLFDC
ATDRNGKPTD IAPHASLVLD MRDEDFMVSS VREPDVIHAS RKELCCIFRV SASQLHQPLA
GAGTGTGGVG GGGEPARSVL LLMAESQHEK QKWVIALNEL LRFLRKRKLA QKKAFIVREL
VDQTALPLVK GALCAAVVDK DRLLLGTDDG LYCVEVDRET VFRLGDGRRV DQIDFIADEH
LIIVMTGKER QIKLIPTAAL DGRDVKWIKV DNTKGCHTFC AGSASGSGAG GLGGGGAGPF
YFCVAVKKTV VVFEINRTPA RHKKLRELAM PGFPQFISIF QGKLCVGYPS GFRMWNLHDN
SQQALLNLED NSLQFVSLAN YDACFLVQVT DVEYLLVFHK LGFYVDQYGK RSRPLELMFP
SVPNHFAYSA PYLSVFSENH VCVFNVNTGE WVQTLNLKKA IIIAKPLLKS GVLTLCTVGD
KACLVLLSDI LADEEVMNVP SLDAIRQSKQ GQMRKRRKYT LLVLTDEDRS RKSRKSVMIS
GPSDFSHVTH MGPGEGIEFQ HLLDLNRSGQ NLVSRNSSLR SALLTPHTAD DSSVEEQNQS
RTEPDDNTSS SQLDTPSSNA HSRSAL
//
