ID A0A0V0Y0U0_TRIPS Unreviewed; 1659 AA.
AC A0A0V0Y0U0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=Wnk1 {ECO:0000313|EMBL:KRX93985.1};
GN ORFNames=T4E_10396 {ECO:0000313|EMBL:KRX93985.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX93985.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX93985.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX93985.1};
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:KRX93985.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDU01000079; KRX93985.1; -; Genomic_DNA.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13983; STKc_WNK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR13902:SF12; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX93985.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 321..595
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 127..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1659 AA; 182221 MW; DA58C0981FDE293D CRC64;
MFDFSAPWAT PSHLRNDTGQ SIHSMSKLLE NHLRHTFFLL LFTLPYACTW IDFASIGNIQ
ALRCNCSLFF EEIVAEGQPA LRRVSLWSCC GFNSPSNCPS ILRWVTVGNC RPSTLAAYCL
SVMQVNGGSS GKKPPDEAPK EDTKSSNDGT CQASSSSAGT GEIEPACTRA CCPSDDPANT
VETKTGDSSP ALPCRLERRQ RKFALKEMET PAIISEDFFG AEEKSRLRLL EADWGKKILQ
RRRVWQRNQR IRQASGEKSS DSPQFDASRR YHSLSGSSEL LDISHFSDEG EDVAETELSK
EEESEFLEDK AIDQSVDGRF LKFEEEIGRG SFKTVFRGLD TESGVSVAWC ELQETKLSKA
ERQRFREEAK MLKTLTHPNI VRFYDFWEIN AGKRKCIVLV TELMTSGTLK LYIKRFKKIN
VKVLKSWCRQ ILKGLAFLHS RDPPVIHRDL KCDNIFITGT TGSVKIGDLG LATLKDKSCP
KSVIGARSAS QSTGRRLTST PEFMAPEMYE ENYDESVDVY AFGMCMLEMI TGEYPYSECQ
FPAHIYKKVI QGQKPQCFEK IPTDSPDMRE IIDRCTRLRP EERYTARDLL IHNFFMPEEL
IGLRIEMKDR DAVISTTNNE IQLLLRVLDA KKRKEYKQKE NEAIQFPFNL QMDKTEDVVK
DMVKCHLVIE EDARTIGKLL QDKIVQISKA RELYQKEKER IKAQEQQQKQ TEEPKVQEEL
TKPKVEDNAK VEQQSSCIVT STVEEHKSNA EEKKIDQPKN DDEQKLQQQE RTEQDKNIPP
PILEAVTVKP QAEKQNCESG YESAKTMEKV DEDIKPLVQP TLVINEPTAS TSATNATETK
VEIAPTVEST ATSGKSTVTT TEAQTMDTLQ IAESNASSDS KSGGLHEVVD EVTKKKSQRH
KKDGLTLKVL NVTHEEAQPV RDQLSTGYAE QKHKVSVRTS RRQSSVGKSY INEKQVTICS
GQLEKVVEVL KGDPESLSGL VLSDNDRSPS ATRAGSSVNS SSTSEKEQVS YGMFKKPEMK
KKQSLSNTLA LKVIAGATGA SHSNPSTAEV TDSYPPTFPL SVSLPDFPAA IRSLTVDKAQ
PMVTGVGLSR HLSRTQVQLG KSKLTDLSVS AAVETESTKQ NLPTGAKSNE TTTSCSSSSS
ACETSSKVTS EPADDGHSRA DNGQLEKDHQ QLATNQRQAE GEACLPPPAT ESTVGVGEPV
KEQNGSASAV PKEKVQPVEA ATMAAAAASE QSKTVVEKED VTTAQANAPL KQERSLPTLS
VDLVAKVDNR TTAAGTQSTT EEQLRNAKSV PSAIHRTADE VRPPVADIGQ LAKELCKLID
LKREPSSSSN GSGTGAAGGA NNNGNGSTVV VVVVAAAAAA SAEQTSSSAS AAGKTARSEP
LATTKLVDTT TNITNPALQA SSVVATGQQE KTELEKQMLQ TTNALKQLLS RQKKEMDCLI
ADTVAKHRRE LETFCVQRGF GKSVVASKNK QQQQPVPVAT ADLTTSSEKG KIQSGPSDQN
QNQKMKIEPE PSTSAIVNVS KKAHTDPSLN NQQQQQQAPK TMREVMNRRL KNFMSDIGKV
STTVGSRSRM AAKVAQIGES RLLRDPVAAR LASVAGVELL PNGSGSRKVS CPAVADHSHR
NCYITRLSSK RLFNGSRRSR NAAQKQQQQS EKLNQNDDG
//
