ID A0A0V1CXT8_TRIBR Unreviewed; 1586 AA.
AC A0A0V1CXT8;
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};
DE Flags: Fragment;
GN Name=Wnk1 {ECO:0000313|EMBL:KRY53999.1};
GN ORFNames=T03_12718 {ECO:0000313|EMBL:KRY53999.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY53999.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY53999.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY53999.1};
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:KRY53999.1}.
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; JYDI01000076; KRY53999.1; -; Genomic_DNA.
DR Proteomes; UP000054653; 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:KRY53999.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 237..497
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 45..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1386..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY53999.1"
SQ SEQUENCE 1586 AA; 173923 MW; B5C57502A2DBE284 CRC64;
LWSSCGFTSP SNCPPILRWV TVVGNSRPSI LLAYCCLSIM QVNGDSSGKK PPDEAPKEDK
KSSNDGTRAS LSSAGTGEME PACTRACCPS NDSANTVETK TGDSSPALPC RLERRQRKFA
LKEMEAPAII SEDFFGAEEK SRLRLLEADW GKKILQRRRV WQRNQRIRQA SGEKSSDSPQ
FDASRRYHSL SGSSELLDIS HFSDEGEDAA ETELSKEEES ELLEDKAIDQ SVDGRFLKFE
EEIGRGSFKT VFRGLDTESG VSVAWCELQE TKLSKAERQR FREEAKMLKT LTHPNIVRFY
DFWEINAGKR KCIVLVTELM TSGTLKLYIK RFKKINVKVL KSWCRQILKG LAFLHSRDPP
VIHRDLKCDN IFITGTTGSV KIGDLGLATL KDKSCPKSVI GTPEFMAPEM YEENYDESVD
VYAFGMCMLE MITGEYPYSE CQFPAHIYKK VIQGQKPQCF EKIPTDSPDM REIIDRCTRL
RPEERYTARD LLIHNFFMPE ELIGLRIEIK DRDAVISTTN NEIQLLLRVL DAKKRKEYKQ
KENEAIQFPF NLQMDKTEDV VKDMVKCHLV IEEDARTIGK LLQDKIVQIT KARELYQKEK
ERIKAQEQQQ KQTEEPKVQE ELTKPKVEDN GKVEQQSSCM VTSTVEEHKS NAEEKKIDQP
KNDDEQKLQQ RERTEQVKNL PPPPPPPILE AVTVVKPQAE KQSCESGYES AKTMERADED
IKPPVQPTVA VNEPTTSTSA TNATETKAEL APNTNHESTT TTTATTSGKT TTAEPQTMEI
SKIAESNASS DSKSGGLQEV VDELTKKKSQ RHKKDGLTLK VLNVTHEEAQ PVISCQLDTQ
NKSIKFQFAP VGDNPQYIAE AFVGKSYINE KQATICSGQL EKVVEVLKGD PESLSGLVLS
DNDRSPSATR AGSSVNSSST SEKEQVSYGM FKKPEMKKKQ SLSNTLALKV IAGAAGASHS
NPSTAEVTDS YPPTFPLSVS LPDFPEAIRC SSTITGANLS RQSSRTQKSK LLVDNVVETE
STKQNPLTGA KSNETASAAT CCSSSTSACG TSSKMTSEPS DDGHSQVDND QLSTNKRQVE
SSEACLPPRA TVELAAGVGE PVKEQNGSAS AVPKDKAQPV EVATMAAAAG VASGELSKTV
SEKEDVTAAQ GNAPLKQERS LPTLSTDFVA KADNRTVVTA GTQSAAGATE EQLRNAKSVP
TAIHRSADEV RPPVADIGQL AKELCKLIDL KREPSNGSGG GGANNNNNAN TVAVTVEQTP
SSSASAPVVV VAAAAAGRTT TARSEPPVAT KLVDAAATNT TNPALQASSV VARGQQQQQQ
QVGNCVIQIS EKIELERQML HTTNALKQLL SRQKKEMDRL IADTVAKHRR ELEAFCVQRG
FGESVVSRTK QQQQQRPLSL RNDGPVAELT TSSATGKIQG GPTDQKMNLE PEPSTSATVN
VSKKAYTDPA INNQQQQQPT VQQQQQAPKT MREVMNRRLK NFMNDIGKVS TTVGSRSRMA
AKVAQIGESR LLRDPVAARL ASAAGVELLP NGSSRKVSCP AVADHSQRNC YIPRLSSKRL
FNGSRRSRNA AQKQHESEKL NQNDDA
//
