ID A0A0V0XBY5_9BILA Unreviewed; 1320 AA.
AC A0A0V0XBY5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE SubName: Full=Serine/threonine-protein kinase 10 {ECO:0000313|EMBL:KRX85547.1};
DE Flags: Fragment;
GN Name=stk10 {ECO:0000313|EMBL:KRX85547.1};
GN ORFNames=T06_5049 {ECO:0000313|EMBL:KRX85547.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX85547.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX85547.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX85547.1};
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 -!- 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:KRX85547.1}.
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DR EMBL; JYDK01000001; KRX85547.1; -; Genomic_DNA.
DR STRING; 92179.A0A0V0XBY5; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46538:SF3; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:KRX85547.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 40..296
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 324..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 895..965
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1128..1158
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1194..1253
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 328..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
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:KRX85547.1"
SQ SEQUENCE 1320 AA; 150505 MW; A07FD3E20D0E5F0A CRC64;
LMPFFDKFKN LFRSNGYHAE CRQSSAYQHI RRDVDPRTVW EIVGELGDGA FGKVQRAQHV
LSKLQSAAKV IETRTEEEIE DYLIEIEILT QCRHKNVVGL YEVYFYEQCL WLMLEFCSGG
AVDSIMVELE KPLNESQIRY ICHEICEGLQ FLHNCFVIHR DLKAGNVLLT SEGGVKLADF
GVSAKNKDAM QRRDSFIGTP MAPEVMMCET FKEQPYSCKC DIWSLGITLI EFAEMDPPYH
EMSPMRVLIK IQKSEPPGLA QPKKWSGEFH NFLSRCLVKS QSERASADEL LQHSFIKNHN
DPKPVLQLLH ELKADVIAEE VEEIDTQSGH SMESVGSTPQ RSLTPDTLHI DRRALAIVEN
SGSSKIIASQ DAAKPNKPTE RGSGNLHTKT AAIEAAENSS NVQEANEILD DLYASLTNEE
LKRGSDIVFH GDNNADEQQQ QQQQQPVVPY KEKAVDVIGE EIISNDNQKL TKSASSILRV
EVRPAVNDEY VAGQSMNDDV KAETKRSQRF VKQNSEGSRH VDESSVIKSD HCRLKMDASS
AQRRCRLAHE TRSLDRVGSF DLAEPSCKEE GIFDHSTADE KRKHYFTSSP RGGSGEEEGQ
FFSCSAFAGV EQTGVVESGR TTTSGDDASP AAEKKSDRAI SADGVQNLTV GIRSTRLTSR
DTADAFCPIF EQAEATDVTL VDNKAWPRLA SAAWAACDEP PPEPPVDYDN VSPLNSGSGS
QLLSTSTSSS IEASSQSVLR LAASAPPAAT TAAANDDDHS YGSTVPGTSV HSPKFENSAS
QSGGGSGSFS DSGGAFSHHP HHHSSDHSVQ SDTLVARKSS DQLQPVAKTE VGELTAAANG
GSAVMMRRNA HRRTVTKKTR VFVVDGIQVT STTYHVMADE DANLYKVKED FRLRKVELQE
LRRLQKEEVR QFQELETRGN VAREQQARKS EQDTQTLLRQ YENDIENLTR YQKKQLEDAE
RVQEEDTKMA MKRLKLEEKK KNNRFFFILM SEIFVGKLFQ EREVKLFRES LRQEHRLLKQ
EMDILPKADR KEIYKQRKEF LELQQLEREK QFMDRIQTTN TLTLNRLEDS HRQKIALLER
QFLQQKHHLL RAREAALWDL EERQLHEKHQ LAKNQMKEVF FLQRSQMLMR HQKELEHVKK
LNQRKEDDMI RAQAAERKRL PKILRSETKT RTLMFRESLK IRMLNSPEIA AKLREFEERE
RMRMTQELKK QELKHRKRLE LLKAENETTL KELEQLQNEK RKMLLEHENL RLKHFDEEYA
NEIKNWKCNL KPRKQKLEEK FSIELAEQEQ FYQNSVPASP LLSSNYVSAS LFSGSNAMPY
//
