ID A0A0V0VQU0_9BILA Unreviewed; 1761 AA.
AC A0A0V0VQU0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=T09_3554 {ECO:0000313|EMBL:KRX65860.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX65860.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX65860.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX65860.1};
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:KRX65860.1}.
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DR EMBL; JYDN01000014; KRX65860.1; -; Genomic_DNA.
DR Proteomes; UP000054681; 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:KRX65860.1};
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:UP000054681};
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 1096..1146
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1328..1609
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1674..1687
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 512..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1716..1761
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..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1761
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 1761 AA; 199524 MW; EE38404686128FD2 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 AASTATVVNS ADQDEHMSNS VKKQNDLDRS IQLTEEALEL ERTRHARQVS
MLESQLQEAK AQVQLLQAKL DDLLLQHKQE RSVLIGEHEE TLVELQAAVE RERESRLEMQ
NQLQTENDML KDRVDKLQMH VEEREKQLCL AQQECKFSLD LESRLAELSQ WVSDEKEVRD
YLQMLAAKLT DELERLKFDA EQKKHNNSGS VVAGPTTPRS KINYGLLSST LASGEKGWGS
RRSHKLAKME ILDLQRNLQS EIRAKQEVTE ELTKFRSTYF ACKQQLEAAE VRIGELTREV
HARDCQLEEA QRQLGVRVLP DYAKSLDQLV QFSSILNLFK DDEAASSGGS DSMNSNKTSN
NNNNGTNNSR DQQTDCSGAV EFCDSPQQQL YPQQQQQQQQ QQQQQPLQRR EAMTVSPPNY
ENARGMNRIR ARAPPQHRFN ISVFAQPTKC HHCTSLMVGL TRQGLVCQDC QFACHPSCLP
KAQPSCPAPQ EPRRPLGIDP SRGLGTTYQG LVRVPKPGGL KKGWTSQLLV VCDLKLFLFD
CATDRNGKPT DIAPHASLVL DMRDEDFMVS SVREPDVIHA SRKELCCIFR VSASQLHQPL
AGAGTGGVGG GGEPARSVLL LMAESQHEKQ KWVIALNELL RFLRKRKLAQ KKAFIVRELV
DQTALPLVKG ALCAAVVDKD RLLLGTDDGL YCVEVDRETV FRLGDGRRVD QIDFIADEHL
IIVMTGKERQ IKLIPTAALD GRDVKWIKVD NTKGCHTFCA GSASGSGAGG LGGGGAGPFY
FCVAVKKTVV VFEINRTPAR HKKLRELAMP GFPQFISIFQ GKLCVGYPSG FRMWNLHDNS
QQALLNLEDN SLQFVSLANY DACFLVQVTD VEYLLVFHKL GFYVDQYGKR SRPLELMFPS
VPNHFAYSAP YLSVFSENHV CVFNVNTGEW VQTLNLKKAK PLLKSGVLTL CTVGDKACLV
LLSDILADEE VMNVPSLDAI RQSKQGQIRK RRKYTLLVLT DEDRSRKSRK SVMISGPSDF
SHVTHMGPGE GIEFQHLLDL NRSGQNLVSR NSSLRSALLT PHTTDDSSVE EQNQSRTEPD
DNTSSSHLDT SSSNAHSRSA L
//
