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Database: UniProt
Entry: A0A085N302_9BILA
LinkDB: A0A085N302_9BILA
Original site: A0A085N302_9BILA 
ID   A0A085N302_9BILA        Unreviewed;      1371 AA.
AC   A0A085N302;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=M514_06491 {ECO:0000313|EMBL:KFD63848.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD63848.1};
RN   [1] {ECO:0000313|EMBL:KFD63848.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD63848.1};
RX   PubMed=24929829; DOI=10.1038/ng.3012;
RA   Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA   Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA   Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT   "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL   Nat. Genet. 46:701-706(2014).
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DR   EMBL; KL367565; KFD63848.1; -; Genomic_DNA.
DR   Proteomes; UP000030758; 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-EC.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          213..470
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          851..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          922..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1008..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1064..1143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          552..606
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        16..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..949
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1009..1023
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1071..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1111..1128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1371 AA;  151419 MW;  846046C6A1EE2B46 CRC64;
     MSGSRCEEAN TGREDASISY RASNAESDGT AGAQGAVSTE TTSKIHASGG RLRCYSCFTP
     VNSASSVAWR KPDKLTSSAS PMDLSKKRKF ALKKMEAYTI SENADFFGAE EKNRIKQLED
     DWGKKLLHRR RRNLRSRQTS GDKQHVVPEI GSLPSSPGGQ RTEDLAVSTE QLSATPKIIE
     EQAEERETEE LHDDDSELLE EHPIDKSVDG RFLKFEEEIG RGSFKTVYRG LDTETGVYVA
     WCELQESKLS KLERQRFRDE AEMLKTLHHP NIVRFYDFWD INAGKRKCIV LVTELMTSGT
     LKLYIKRFKK INVKVLKSWC RQILKGLAFL HSRQPPVIHR DLKCDNIFIT GTTGSVKIGD
     LGLATLKDKS CPKSVIGTPE FMAPEMYEEN YDESVDVYAF GMCMLEMITG EYPYSECQFP
     VQIYKKGVKP QCFEKIPSSN PEIKEIIDRC TRPRREERYS AKDLLIHDFF MPEELIGLRL
     EVKDRETTVA SSSNEVQFLL RVLDEKKRKE YKQKENEAVQ FSFDLLNEKA EDVVREMVTA
     QLIQDEDYRT IVKLLQDKIG QIRKDRELYR KEQERLKENE KKAKEEAQLQ LELKQLKEKK
     ERKENVGVTE EQCVVRSDQI EQSEEGKGAI VAEEALQVPE SVQGAVDNPK KNILVIEKVV
     RRASPQSLIV ESGESKATVK DNVSVDVKSR SSEDEETDIC KKPVPYHHQK SHGMKLKVIR
     LISDRKSPPV VSCRLETQKR SITFQFAPLT DNPRFIAEAF MESSFIDGNQ AQLCSGQLEK
     VAQAVKDNPD AISGLLMGDD DGAPPLVCTS SSAVSSSSMN DRENISFDPK RLSQLSSSRL
     LSRVKIPDPG GYCTSLSNPN TADIGERSEP SFPLSASLPD FPASLKDKSS VPLSSNILSS
     EKNGRFVVNK VAASEPAEVA IPPVDFSSGN NAAGAQTPEV QEASPQDTDK ASIVQSVAAV
     PAFASQDVKA EVSSVESCTL GSDRNTKEVT SASRDGLRAV ASAKEVGLGE RAAEADVITE
     SKEELGPTTR SMPNTIHRTA EEGRPPVADI GELAMELSKL IDLKRDPSSS VSGKPVEQPA
     TQSVVKSEQP PDTDDLAKPS LTVESPFKAD LKSSEPQSKV SKAMKTTVGN LQPVKKEAPE
     LSKDTLKDLV KEAKKEEELT HAEAPKLPQK DSKEALMAIL SRQKDEMNTL ITKHKCELAA
     YFAASVKDKE TPPLTEGSIE KKKGLIAQKS VEDAVNLRKP LFCTTRDCGD NSPKLGKPTN
     TLVDVVAAPS TVNKSNALVN EFTKPSPRSA AVVTDVPAPN SRDPVTARLA SVAGISLLPN
     GSSRKCSCPT VIDCKSHIPK PLGFNKLFMN SKKKLTGNKS PCADSTSCAN N
//
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