ID A0A0V0UQN7_9BILA Unreviewed; 1570 AA.
AC A0A0V0UQN7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=T09_13432 {ECO:0000313|EMBL:KRX53512.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX53512.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX53512.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX53512.1};
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 -!- 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:KRX53512.1}.
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DR EMBL; JYDN01000200; KRX53511.1; -; Genomic_DNA.
DR EMBL; JYDN01000200; KRX53512.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042:SF197; EIF-2-ALPHA KINASE GCN2; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Initiation factor {ECO:0000313|EMBL:KRX53512.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX53512.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Protein biosynthesis {ECO:0000313|EMBL:KRX53512.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..134
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 242..491
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 537..930
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1419..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 155..201
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX53512.1"
SQ SEQUENCE 1570 AA; 179734 MW; 3B02DD4272E5E6DD CRC64;
LYFTMPKRKK KFYLQKQLDE ILVLRAIYGK DFKVDEDGLN DLIHPKGFSV KLHPLVDMSG
IEKPEIYVSV QMNVKYPKNY PAKLPMIEFS NLEGIGNEAM GKIKSIIYEM AEKKKGEVMI
YELCIEVQEQ LIHLNRPAEF HSFYDGMIHN NLLKKQKEQG EHQLMKKKLQ EQEERENKEI
LEKLDKRRAE ARQALRSKKH EQRLFADNTE QVAISKHLGD TSIAIVRKFN LGWVKNISPP
KFVKLQEISC NNNLSIYSCM LKNELATVTE WRLDFEKCSV EKSCQISLEL ERVLCDFDSL
KNVKHSNILQ YLYAGCYFQG SCLLVGIWKK HDHVLPVSRY VRNNNPGRCP LSVIKLMAKD
ILQALRFLHD RNITHDAITL DCLWEGGHQF FLSDFSTAHQ LNRIQWSLAE NGPMKNVSNR
VEDVEHAKSD DVSALGFCIV ELAVGVEADH IYLRDRIASI IRPLKNLINL MVAKRRSERW
TCELLLSHAL LTSDVNIDEE QNDQTNSQFS HADLLQSIHD VSSIDCYEQS KRIESEFQVL
KVLGRGGFGD VLKVKNKLDR CQYALKRVPL STGDISQSRK ILREVKLLSH LNHDNVVRYY
NSWIETVHLK QNIPPNDCTK SYSTGSGEQQ LSLELLNLDV KTQTSANSSS FIVFEDEHND
DNEIVLENND SGEMSSIGDL SNEISMENDD DDDSLLIAFE NGDEEQQQSI DENSELDSTV
VRHPEMIQIL YIQMEICEKS TLRLAIDNGE LFVKPDRAWR FFREILEGLT YIHSKGCIHR
DLKPSNIFIS LNDQAKIGDF GLAISGQSER FGMDDSQSFT LNESDMKDTT ISNVGTALYM
SPEMSDSHRC SAKVDIYSLG IILFEMLYPM KTSMQRADVL VELRKPEIII PDDFLLMSKG
DEVKKLLKLM LDHRSDQRPS SAALLNSELL PISEMEPFEF HYNLSKVLAN CCSSNMKQLF
SMIFSKSPSA IEEYLYDDQL TCYFKGHFQD QLAMCRTKCE TKLAALFHLF GGVHVNAPLL
VPRTRILSES YPNRMELMNT DGMVLNLPYD LRYNFARFAA RQKIMRLKRY EIGTVFRQRE
NPMNPQELLE CAFDILAPQP DFTHAIVELF SLISAVVDEF SFVKYSDLQI KINHLGLLKA
FMENCSVTES SMQQKFLVTL SSLKSKFQRE CAICDLLKEW KITAPKLVEL VSKERCLSDA
LQWFAQDAQQ YELYLSELKR IISMAEMVCG QLAICVDFGY VVYPNIYTDV VFCVTECKKF
SKLREDCVAV GGCYSNLMRN LLGPGFKNQP VPLTAVGLSF WFNRLFFTLA QDTAACEQNL
DSSSRVLIIS IGQDSKIEQK FRLMKMLRAN KIPTDCWYES SESLDQAICW ARRMYIGCVI
LLKAGDPDLR VKMIEKDRVV DRRVSMAELV PFLLERNSSA GDSSTAAHDN SPSTSGRGSS
HQHQHHQSSL TNLNWHFVTA APLTAKLRRG CEDRVSLMLF PFLNAVNFQH SVPVIVTDMP
GLIVRDFGSM NMETEATFNA SIVQLIEIRQ HYKKQILSVG SIIIDELFKS CHAFVLFAST
ADNIYQILHR
//
