ID   TAO1A_XENLA             Reviewed;        1001 AA.
AC   Q6NU21;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Serine/threonine-protein kinase TAO1-A;
DE            EC=2.7.11.1;
DE   AltName: Full=Thousand and one amino acid protein 1-A;
GN   Name=taok1-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in various processes
CC       such as p38/mapk14 stress-activated MAPK cascade, DNA damage response
CC       and regulation of cytoskeleton stability. Acts as an activator of the
CC       p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation
CC       and subsequent activation of upstream MAP kinase kinases. In response
CC       to DNA damage, involved in the G2/M transition DNA damage checkpoint by
CC       activating the p38/MAPK14 stress-activated MAPK cascade (By
CC       similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR   EMBL; BC068781; AAH68781.1; -; mRNA.
DR   RefSeq; NP_001084574.1; NM_001091105.1.
DR   AlphaFoldDB; Q6NU21; -.
DR   SMR; Q6NU21; -.
DR   DNASU; 414526; -.
DR   GeneID; 414526; -.
DR   KEGG; xla:414526; -.
DR   CTD; 414526; -.
DR   Xenbase; XB-GENE-17333323; taok1.L.
DR   OrthoDB; 617606at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 414526; Expressed in blastula and 16 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR   GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm; DNA damage;
KW   DNA repair; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1001
FT                   /note="Serine/threonine-protein kinase TAO1-A"
FT                   /id="PRO_0000086731"
FT   DOMAIN          28..281
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          324..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          458..651
FT                   /evidence="ECO:0000255"
FT   COILED          754..877
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        324..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        948..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         34..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1001 AA;  115910 MW;  42E0867F3FFFA517 CRC64;
     MPSTSRAGSL KDQDIAELFF RDDPEKLFSD LREIGHGSFG AVYFAHDAST REVVAIKKMS
     YSGKQSNEKW QDIVKEVKFL QRIKHPNSIE YKGCYLREHT AWLVMEYCLG SASDLLEVHK
     KPLQEIEIAA ITHGALQGLA YLHSHNLIHR DIKAGNILLT EPGQVKLADF GSASIASPAN
     SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN
     ESPTLQSNEW SDFFRNFVDS CLQKIPQDRP TSDELLKNMF VLLERPETVL IDLIQRTKDA
     VRELDNLQYR KMKKLLFQEA HNGPAVETHE EEEEQEHGVG RTGTVNSIGS NQSIPSMSIS
     ASSQSSSVTS LPDASDDKSE LDMMEGDHTV MSNSSVIHLK PEEENYPEEP EPRTRPSEPH
     SPPQVSRHKS HYRNREHFAT IRTASLVTRQ IQEHEQDSEL REQMSGYKRM RRQHQKQLMA
     LENKLKAEMD EHRLRLDKDL ETQRNNFSAE MEKLVKKHQA AMEKELKSIA NDEKKFQQHI
     QAQQKKELNN FLESQKREYK LRKEQLKEEL NENQSTPKKE KQEWLSKQKE NFQHFQAEEE
     ANLLRRQRQY LDLECRRFKR RMLLNRHNSE QDLVREELNK RQTQKDLEHA MLLRQHESMQ
     ELEFRHLNTI QKMRCELIKL QHQTELTNQL EYNKRREREL RRKHVMEVRQ QPKSLKSKEL
     QIKKQFQDTC KIQTRQYKAL RNHLLDTTPK NEHKAVLKRL KEEQTRKLAI LAEQYDHSIN
     EMLSTQALRL DEAQEAECQV LKMQLQQELE LLNAYQSKIK MQAEAQHERE IHELEQRVSL
     HRGLLEQKIE EEMLALQNER TERIRSLLER QAREIEAFDS ESMRLGFSNM ILSNLSPEAF
     SHSYPGASGW SHNPTGGPGP HWGHPMAGPP QAWGHPMQGG PQPWGHPSGS VQGVSRGSTM
     GVRNSPQALR RTASGGQTEQ GMSRSTSVTS QISNGSRMSY T