ID A0A0N5CZ90_THECL Unreviewed; 1166 AA.
AC A0A0N5CZ90;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=TCLT_LOCUS5787 {ECO:0000313|EMBL:VDN03074.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000579801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000579801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN03074.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; UYYF01004363; VDN03074.1; -; Genomic_DNA.
DR STRING; 103827.A0A0N5CZ90; -.
DR WBParaSite; TCLT_0000579801-mRNA-1; TCLT_0000579801-mRNA-1; TCLT_0000579801.
DR OMA; LEKRNGW; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd06608; STKc_myosinIII_N_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 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}; Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 8..275
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 849..1140
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 381..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1166 AA; 129742 MW; 1490DB2C00F1A1CD CRC64;
MKDPAGIFEL IEVVGNGTYG QVFKGRHVKT SQLAAIKIMN INEDEEEEIK MEINMLKKYS
HHRNIATYYG AFIKKLPSST GKLDQLWLVM EFCGSGSVTD LVKSTKGNSL KEEWIAYICR
EILRGLYHLH QNKVIHRDIK GQNVLLTDSG EVKLVDFGVS AQLDRTVGRR NTFIGTPYWM
APEVIACDEN PDATYDSRSD LWSLGITALE MAEGHPPLVD MHPMRALFLI PRNAPPRLKR
GKKWSKKFES FIETVLVKDY HQRPYTDQLL RHPFIREQPP ERQTRIAIKD HQDRHRRIIN
KKDETEYEYS GSDDDENHGQ IGKSLDVAAE LAGVVQPVQD STLRKGFQRL QENNKNMFEH
SPSQPIRQRS ALVGPVVLPS GQHHISQHQQ KHPSNSQAYH RNPTFIDEPS REHVKLRQQQ
VDPRLALNGL SHQRHGDHNR RSQRPFSHHQ AFQRGISPHH SSALMPQPNH PAAPHLADLA
NYDRKRRSEK EAARAAAEQR RDRSAASRDQ VRDMSRELKT SHIARINPSV AAAMPVRKMS
DPVLNGKTEN QNLDVLANEL TRMGRHQQNG NYSPPPPAPP PRDASIMNAD EASASHDGTL
LASEPGSGQH ENMLEEGTLR GPNKPLPPTP TDHSPISDIP GDDGTLLASR KVNGSIDVHR
PNNSDSLSKT RQSQMVKAAS MPDQTSSVAE LTGSGSSGSE GSGSSPEASP FDARKSTSRT
SASAAGGQRC GVMPDLLPRT PIERSVPFLA FTKDGNSASI ESQSVEEFPS GVNSLPKTQA
PLAARDREKS FVAYFGAGIN GGGTVNRPGR AQDTNQVQVN VNPNPGVASN GLHSDGDAPE
IRKYKKKFSG DILCAALWGV NLLIGTDSGL MLLDRSGQGK VYQLITRRRF EQMTVLEGQN
ILVTISGRKR RIRVYYLSWL KQKILRTEGV SGIELEKRNG WVNVGDLQGA VHFKIVRYER
IKFLVVGLES TIEIYAWAPK PYHKFMAFKA FSHLVHLPLI VDLTVEKNSR LKVLYGSREG
FHAIDLDSGS VDDIYTPANT ETVVTPHCIV ILPNSNGMQL LLCYNNEGVY VSTYGKATKS
VFLQWGETPS SVAYISTGQI MGWGNKAIEI RSVDTGHLDG VFMHKKAQKL KFLCERNDKV
FFSSAKGGGA CQIYFMTLNK PGLSNW
//
