ID A0A3Q1IU32_ANATE Unreviewed; 924 AA.
AC A0A3Q1IU32;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000021188.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000021188.2}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q1IU32; -.
DR Ensembl; ENSATET00000021546.2; ENSATEP00000021188.2; ENSATEG00000014688.2.
DR GeneTree; ENSGT00940000157166; -.
DR Proteomes; UP000265040; 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 PANTHER; PTHR24356:SF140; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 3; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00228; PDZ; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 357..601
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 602..674
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 792..891
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 85..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..915
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 104462 MW; FAED43427E7C12BE CRC64;
MKVLVNFLKC CTKRNAKEHS DVYDLGEKKT FNFMLLYSKG FSIVCYVRSF ACEMPTNAYP
AEAYVTCMSV SLRAEGRRWS LASLPSSGYG TNPPSSTVSS SSSSQERLHQ LPYQPTQDEL
HFLFKHFRST DSITDEDGRP STIIRPRSRS LSPGRSSVSF DNEIVMMNHV YRERFPKATA
QMEERLLEIV THYSPDSSLP LADGVLGFIQ HQLVELVRDC LDKSQKGLVT SRYFAELQEK
LEKLLHEAYE RSESEEVTVI IQLVRKILIV ISRPARLLEC LEFDPEEFYH LLEAAEGHAK
VGQGIKTDIP RYIISQLGLT RDPLEDMVQL EQYDACPSVS APQTLTPTRR KPLESDFETI
KLISNGAYGA VYLVRHKETR QRFAMKKINR QNLVLRNQIQ QAFVERDILT FAENPFVVSM
FCSFETRRHL CMVMEYVEGG KLFVMLMVFN VFSLNSLLIT SMGHIKLTDF GLSKIGLMNM
ATNLYEGHIE KDTREFVDKQ VCGTPEYIAP EVILRQGYGK PVDWWAMGII LYEFLVGCVP
FFGDTPEELF GQVVSDEIIW PEGDDALPVD AQDVITRLLR QSPLERLGTG GASEVKQHPF
FLGLDWNGLL RQKAEFIPQL EAEDDTSYFD TRSERYHHLA SDEDEETNDE ESSLEIRQFA
SWSHRFSKVG ARCAGKRKLW VFFQLIYLSN WSVVACSLRP RASSSSSQSE RSPSPLVMSS
THSLETMPRF ALSTDDEGRS NLICFFNVAV NKMYQCLFTV PYDSPSCLQP SPISPRSLSS
NPSSRDSSPS RDLSLSPASV GPPIVIHTSG KKYGFTVQAI RVYMGDSDVY TVHHMVSSVE
EGSPAYQAGL RTGDLITHVN GESVQGLVHP EMIELLLKSG SKVALQTIAL ENTSIKVGPA
RKTKHKGKMA RRSKKSKKRD NYDR
//