ID A0A0V1A374_9BILA Unreviewed; 1630 AA.
AC A0A0V1A374;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=MAST1 {ECO:0000313|EMBL:KRY19234.1};
GN ORFNames=T12_9968 {ECO:0000313|EMBL:KRY19234.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19234.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY19234.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19234.1};
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:KRY19234.1}.
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DR EMBL; JYDQ01000038; KRY19234.1; -; Genomic_DNA.
DR STRING; 990121.A0A0V1A374; -.
DR Proteomes; UP000054783; 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:KRY19234.1};
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:UP000054783};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 531..806
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 807..874
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1036..1114
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 150..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1630 AA; 181486 MW; 21BC30AC23FD0ED1 CRC64;
MFSYQFLVMR KSCASNIALS LKRFFIGELY RRCWNFHFIG ILIDHVWFWS QWFSSCWKFA
GDIVQICLQS LDAKAQIFKP HLVFVVTISA SKFDLALQSG LCNSARLRTS LSLSCPQLSI
AESSMCCSNS QSPVPFFNAL LLIDPKKRRR SGHVSGRSFN SSLSPVSNRC SSPNHHDQFR
TSSVALLSSN LQPYAKAKWN LNPDSRRWSI ASLPSSGYET PESSTFSSVY SSQEKLANAL
TELKINNSGS NDSCSYCEES TLACLKSPAL RWRSRSFSSF SNNVSVCEYD DLLRSSLYKS
RFPKAKQNME EKLEKFIADN SVNPSLVLDI SDNEQPVAVI HPNIKQDPNL VKLFSDGCAR
FIHHQIVELA SDCLLKSKEE IISSVYFYEM TESLKNILLQ AKEKSLECYP MLNDCAKKLL
MIISRPARLL ECFEFDPKEF YHLLKEMEEY AKEQQSRLEL DIPHYVISKL GLTNDVNSDK
GTNDQKEQQQ LIACGSNLIK AENGKGKPQQ QSSDAFDHVT NNKPLLKEED FQVMKLISNG
AYGSVYLVRA KETRKRFALK KLRKSSLILR NQLEQVFAER DIMTFSDNPF VVSFYGSFET
KTHLCMLMEY VEGGDCASLL KQIGVFPVEM ARLYIAEAVL AVEYLHSYGI VHRDLKPDNL
LITAMGHVKL TDFGLSKIGL MNRTTLLCED YFDVSETQQF RDRQICGTPE YIAPEVILRQ
GYGKPVDWWA IGIILYEFLV GTVPFFGSTP EELFAHAIHD EIEFPEDPYC PPAEAVDLIR
GLLQVNPLDR LGTVGSASEI KTHLFFSSLN WHSLLRQKAE FIPQLEGDDD TSYFDSRTER
YNHDVDSGDE SWSENSSIFS SFSSCSPRYS LLADNLMLKN NDDSNSLLLL SEDGTDQTFV
SSTEENPNAG KRRSVGEEEL CSFEGEALNR TDSTISADSS ALPKLSVSLD TSDLAVQLKG
NDVEQHLDTR SCETPVRLNV APPKSTGGLH LIIPSDVITP AVLNSPSQSS NSSHDCSPNC
CSSVDIAPVV HTYKPTVTFQ RGSLAFGFSI KSIRVYLGQT DFYTIQHIVS AVEKGSAAYQ
NGLRVNDLIT HVDGTAVQNF TQPELLRRLM RGGGQWVTIR ATSLDQTSIR LGRPRRAAGR
LARRVGVGTV KQKLQRRAWM EKRKAASLFR RMSGKRVSAE FGASALTTSV LHRSVSSVEG
LCSSSVPCLY SSTSCSSSSN NNNNSGSSSS SIEQSRHGRS TRPSSLQGLK MDVVAKTALK
PTAPPPPPPP PRRKEPQGMP LSPLARCDQA SLRTSKMLLS PAQSQSQSPL ASGLLATGAS
RSRSFNCPKR VYCKPRRFLS RGTNGETHKV SLSVKRTVDC HSPCAMDAYK KVYLGFPMLI
ILCMLILDQK VFLAQACIEG QQQCPNGYTC CGFKSGYWRC CPFRNGVCCA DGINCCAHNA
QCDSEKRLCI KENNETYPTW RNDLLGVPDD QQVAYAEGED VVFGTEHINV PTLCPDKMSK
CDEKSTCCET VHGQWACCSL SKAVCCSDKL HCCPEGTQCD LKHNRCTQEN DSSFDNSTTP
LYGLNIDIGI PKYFIRKSKI IIGCPEKSQL CRGKHSTGCC PLKNGVCCDD NLSCCPEGYE
CSKNGKCRKI
//
