ID A0A3Q3APX8_KRYMA Unreviewed; 1433 AA.
AC A0A3Q3APX8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000013544.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000013544.1}
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};
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DR Ensembl; ENSKMAT00000013751.1; ENSKMAP00000013544.1; ENSKMAG00000010088.1.
DR GeneTree; ENSGT00940000153424; -.
DR OMA; RSMHDFQ; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR GO; GO:0045087; P:innate immune response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08782; Death_DAPK1; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.5.460; Single helix bin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24342:SF17; DEATH-ASSOCIATED PROTEIN KINASE 1; 1.
DR PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 7.
DR PROSITE; PS50088; ANK_REPEAT; 8.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1433
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018605580"
FT DOMAIN 11..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 376..408
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 409..441
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 442..474
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 475..507
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 508..540
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 541..573
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 574..606
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 607..639
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 670..941
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1314..1397
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT REGION 1336..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1433 AA; 159876 MW; BB01C861995848FB CRC64;
CSSWRRLTLT EILWFLVGSG QFAVVRRCRH RSTSVEFAAK FIKKRRSKSS RRGVTREDIE
REVNILKEIQ HPNIIMLHEV FENKAEVILI LELVAGGELF DFLAEKESLS EEEATQFLKQ
ILDGVLYLHS KQIAHFDLKP ENIMLLNRSV PHPRIKIIDF GLAHKIDFSN DFKNIFGTPE
FVAPEVVNYE PLGLESDMWS IGVITYILLS GASPFLGDNK QETLANVSAV DYTFDEEFFS
NTSVLAKDFI SRLLVKDPKK RMTIQDTLQH PWIKPKDTQQ ALSRKESAVN MEKFKKFAAR
RKWKQSVRLI SLCNRLSRSF LSRSNISVAR SDDTLDEEDS FVMKAIIHAI NDDNVPGLQH
LLGSLNSYDV NQPNRHGTPP LLIAAGCGNI QIIEVLMRKG AEIQANDKTG ANAIYYASRH
GHVETLKFLH ESRCPLDVQD KCGETALHVA ARYGNVDVVS YLCNIRANPD LPDREQETPL
HCAAWHGYSA VARALCQAGC HVDAKNREGE TPLLTASARG FVDIVECLVE HKADLEATDK
DGHTALHLAV RRCQVDVVRC LLRHRCHLDQ QDRHGNTPLH IACKDGNLPV VMAICSAKAS
LDLPNKSGRT PLHLAANNGS LEVVRHLCLA GANIDAVTHV SQNFDPEPLQ MSVWLQDNHK
LSYIQQLRPS QTIQPRIKLK LFGHSGAGKS TLLESLKCGI LRGFFKRKRT RLTNTSRHPN
SPVNSKPAVS VSISNLYPGC ENVSVRSRSM MFEPSLTKGV LEVFSPVHGA LSAADDQATK
AIDIQHTSIH GVGDFSIWEF SGNPVYHCTY DYFAANDATA IHLVLFSLEE PYETQLGHIT
YWLNQLKALT LPQDSIMFGG RIQQPLTVVL VATHADLANI PRSFSGEFSY DKEQVLLREV
RNRFGNDLQL SDKVFVMDAG ASNSKDVKLL KNHLQELRSS VVSSCSPMTQ LSERLLSTLP
AWRKLSGPNQ LMSWQQFVSD VQDQINPLVS QDHLRTLALQ LHSMGEINLV QSETVQDVVL
LEPRWLCTNV LGKLLSVETP KAIHHYRGRY RLEEVQALAP DSDVEELLQI LDAMDVCSRD
ATNPSMVDVP ALIKTNGLHR SWTEEEDEDS LIYGGVRIVP AEHLTPFPCG LFHKLQVNLC
RWSHQQKPED DGGEDSDGDI HLWTNGAKVS QAGTEAMILL VNHGQGVEIQ VRGHDSERAK
CYTLLDTICS ITENLLGSTL PGLLTARYYL SPQQLREHHA PIMVYQPKDF FRAQVQRETS
LTNTMGGYRE SFSSILAFGC VEVYQQGIVG RDLHISDVPL LARRKLCRML DPPDAMGKDW
CLLAMNLGLT DLVAKHSSGT PNGTPDSDSQ HAELQPSPTA ALLQEWSGRA DSSVGVLMTK
LRELGRRDAA DFILRASPVF RVNMEAVGGA SGRYPPTCNG GTSYNSISSV ISR
//
