ID A0A0V0VJE4_9BILA Unreviewed; 1621 AA.
AC A0A0V0VJE4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=T09_8581 {ECO:0000313|EMBL:KRX63591.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX63591.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX63591.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX63591.1};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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:KRX63591.1}.
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DR EMBL; JYDN01000030; KRX63591.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.10.25.160; Granulin; 3.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000118; Granulin.
DR InterPro; IPR037277; Granulin_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF414; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF00396; Granulin; 3.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00277; GRAN; 3.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57277; Granulin repeat; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00799; GRANULINS; 1.
DR PROSITE; PS50106; PDZ; 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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX63591.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 517..792
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 793..860
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1023..1101
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 135..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1266
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1621 AA; 180513 MW; A6AC27E084C5F3BA CRC64;
MFSYQFLVMR KSCASNIALS LKRFFIGELY RRCWNFHFIG ILIDHVWFWS RSGFRHVGSS
QETFLDAKAQ IFKPHLVFDL ALQSGLCNSA RLRTSLSLSC PQLSIAESSM CCSNSQSPVP
FFNALLLIDP KKRRRSGHVS GRSFNSSLSP VSNRCSSPNH HDQFRTSSVA LLSSNLQPYA
KAKWNLNPDS RRWSIASLPS SGYETPESST FSSVYSSQEK LANALTELKI NNSGSNDSCS
YCEESTLACL KSPALRWRSR SFSSFSNNVS VCEYDDLLRS SLYKSRFPKA KQNMEEKLEK
FIADNSVNPS LVLDISDNEQ PVAVIHPNIK QDPNLVKLFS DGCARFIHHQ IVELASDCLL
KSKEEIISSV YFYEMTESLK NILLQAKEKS LECYPMLNDC AKKLLMIISR PARLLECFEF
DPKEFYHLLK EMEEYAKEQQ SRLELDIPHY VISKLGLTND VNSDKGTNDQ KEQQQQQLIA
CGSNVIKAEN GKGKPQQQSS DAFDHVTNKP LLKEEDFQVM KLISNGAYGS VYLVRAKETR
KRFALKKLRK SSLILRNQLE QVFAERDIMT FSDNPFVVSF YGSFETKTHL CMLMEYVEGG
DCASLLKQIG VFPVEMARLY IAEAVLAVEY LHSYGIVHRD LKPDNLLITA MGHVKLTDFG
LSKIGLMNRT TLLCEDYFDV SETQQFRDRQ ICGTPEYIAP EVILRQGYGK PVDWWAIGII
LYEFLVGTVP FFGNTPEELF AHAIHDEIEF PEDPYCPPAE AVDLIRGLLQ VNPLDRLGTV
GSASEIKTHL FFSSLNWHSL LRQKAEFIPQ LEGDDDTSYF DSRTERYNHD VDSGDESWSE
NSSIFSSFSS CSPRYSLLAD NLMLKNNDDS NSLLLLSEDG TGQTFVSSTE ENPNAGKRRS
VGEEELCSFE REALNRTDST ISAADSSALP KLSVSLDTSD LAVQLKGNDV EQHLDTRSCE
TPVRLNVAPP KSTGGLHLII PSDVITPAVL NSPSQSSNSS HDCSPNCCSS VDIAPVVHTY
KPTVTFQRGS LAFGFSIKSI RVYLGQTDFY TIQHIVSAVE KGSAAYQNGL RVNDLITHVD
GTAVQNFTQP ELLRRLMRGG GQWVTIRATS LDQTSIRLGR PRRAAGRLAR RVGVGTVKQK
LQRRAWMEKR KVASLFRRMS GKRVSAEFGA SALTTSVLHR SVSSVEGLCS SSVPCLYSST
SCSSSSNNNN NNNSGSSSSS IEQSRHGRSA RPSSLQGLKM DVVAKTALKP TAPPPPPPPP
RRKEPQGMPL SPLARCDQAS LRTSKMLLSP AQSQSQSPLA SGLLATGASR SRSFNCPKRV
YCKPRRFLSR GTNGETHKVS LSVKRTVDCH SPCAMDAYKK VYLGFPMLII LCMLILDQKV
FLAQACIEGQ QQCPNGYTCC GFKSGYWRCC PFRNGVCCAD GINCCAHNAQ CDSEKRLCIK
ENNETYPTWR NDLLGVPDDQ QVAYAEGEDV VFGTEHINVS TLCPDKMSKC DEKSTCCETV
HGQWACCSLS KAVCCSDKLH CCPEGTQCDL KHNRCTQEND SSFDNSTTPL YGLNIDIGIP
KYFIRKSKII IGCPEKSQLC RGKHSTGCCP LKNGVCCDDN LSCCPEGYEC SKNGKCRKLE
V
//
