ID A0A1S3H5J6_LINUN Unreviewed; 1359 AA.
AC A0A1S3H5J6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 2.
DT 27-MAR-2024, entry version 33.
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=LOC106152299 {ECO:0000313|RefSeq:XP_013381278.2};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013381278.2};
RN [1] {ECO:0000313|RefSeq:XP_013381278.2}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013381278.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_013381278.2; XM_013525824.2.
DR EnsemblMetazoa; XM_013525824.2; XP_013381278.2; LOC106152299.
DR KEGG; lak:106152299; -.
DR Proteomes; UP000085678; Unplaced.
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; 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; 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; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 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; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_013381278.2};
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:UP000085678};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 390..664
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 665..730
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 993..1081
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 48..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1128
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1359 AA; 152383 MW; 3E8FF46E96AEA4C6 CRC64;
MLQGVQLIIG GHSRQVMLRD ETPFYSSFFG RKDWKPITSR RRRKVFLLRT PTKGSPLDSP
RTMSPSQHGH FPFGPGKSRE GGRRWSFASL PSSGYGTNTP GSSNVSSQCS SQEKLHQLPY
QPTDRELQML TKHFDSSENI AEAEDDGRLS PVIRPRSRSL SSPAKSPGME SDIMMMNTVY
KDRFPNAKIE MEERLDRFIE DNKVLACSEE SDGTARFVHH QILELARDCL EKSQEQVISV
NYFIELSENL QTLLNDSRER SPHAAEHADP MVNRLLIIIS RPARLLECLE FDPEEFYHLL
EAAEGQARQV IQTDIPQYIV NKLGLNRDPL ADMNDIELSA KEFTAEDKDD ESEREGKDEE
RTGDDDQDGS EEYVEETEPK EAKPPCEDDF ETIKLISNGA YGAVFLVRHR ETRQRFALKK
VLKHNLVLRN QVEQAFAERD ILTFTDNPFV VSLYCTFETK KYLCMVLEYV EGGDCATLLK
NMGPLPTDMA RLYFAETVLA LEYLHSYGIV HRDLKPDNLL ITSTGHIKLT DFGLSKIGLM
NLTTNMYEGS IDKESKQFKD KQVFGTPEYI APEVILRKGY GKPVDWWSMG VILYEFLVGC
VPFFGDTTEE LFSQVINVDI EWPEEEEYSV DEDSKNLIIS LLQQNPIDRL GTGGAHEVRE
HVFFLGLDWD GLLRQKAEFI PQLDSEEDTS YFDTRVDRYN HDLEDTEDDA DDIMFHSFSS
MSPRYSKVYG KFAQMRERKR QEEKARSNSM SAVPDNTDKD VLGRKNSNIS ECSTSSVETP
SNSQRNSISD LEKEVPTLAL SIKVDEEVFS SPEVTPRSIA SNSTPESSQC ESDTLSPIMS
RKKSTPKAVK TDPIPLFSIS AEEEEEEHGK IHDTGDEPKK EGKKPIHIKP KRPEVKKKEP
TFTPPEVMAD AQEEPKPKGY LQVDLSEGPP RSTSPRLTFK PMHKSASANA LSLHIPAAEE
LVSQPISSPG SSSSRDASPS RDMLPVIGPL RPAFIIRRSP RGYGFTPKAI RVYHGDTDIY
TLHHLVVHVD DNGPAYEAGL RPGNLITHVN TECVVGMLHV QVIKLILKDP SRVSLRVTPL
DNTTIKTGGR YRAPHEGKMT RRSYKKKHQR ERSGDSHHRK RGRTSLFRRL STKRAQEQNI
NSPITPSKTF GCTLNRSLSS GDSMPNSPTR SKSPRSPPIG RVYVGAGGDS VGNTSQSSSS
GSSVPNSPAS SSQFNRPSSL HGLKHKLAAA KSPHRRKSVH NIPLSPLART PSPSPMALSP
TRSPSPLTVV HGHHQAGSSN TTQTYPTYLN SSPIATCSLS KKTLTRPKST EPGQGSPALP
RRGASPDRLH PSAAKQTKEK QSLNRKSSWH EKREYFESL
//
