ID A0A2A2LES8_9BILA Unreviewed; 1019 AA.
AC A0A2A2LES8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=WR25_02872 {ECO:0000313|EMBL:PAV84726.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV84726.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV84726.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV84726.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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 -!- 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:PAV84726.1}.
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DR EMBL; LIAE01006824; PAV84726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2LES8; -.
DR STRING; 2018661.A0A2A2LES8; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035173; F:histone kinase activity; IEA:UniProt.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR024604; GSG2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1.
DR PANTHER; PTHR24419:SF18; SERINE_THREONINE-PROTEIN KINASE HASPIN; 1.
DR Pfam; PF12330; Haspin_kinase; 1.
DR SMART; SM01331; DUF3635; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 887..912
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 513..900
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 150..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1019 AA; 115140 MW; C24A27C50D5F4433 CRC64;
MTRFRRKQPS GHVSIIVQKV GVEKSDQGTS HGQLYRTINR DKTINVKPDH GYIVEPIQLP
PEYKKAVDNY KRGAHRPNLT DISEWEDEYE EEMRRIQEEL EEYEKYELPF SDRHGNPLHK
VGRNEYISDR EAQTEEGKAK IAAWSKANEE KKANLTNRRR TVLEERQKRK TEAQVQTQTK
QTKKKSGAKK STSTDSMLEA INQSMSRMRV QEDSGDVLDA GLNEIIKNAI EKGNTTQTHV
VLPPAIDSDP TSKYDATVIT GTFHSADPTT HTAIGHDETK IINFTVFQDK SMLEKRQNRR
SSIAPLKDFA EFVKSVAATS TPRHSLATAG LFHPLDMSAI AETSSSRTLS SERSESSSSN
LEESVNEDEE DERQEVTAVE PTINETAVEP HESTLKDASV DDTLVSNKDV SEEKENVQPS
DVTKAHGITT VTETTLNKSN DVHRQTLSTT TNTTYTSFIG SMAGGKREST RIEDEPYFLK
GLPRDASMRD KLCGVCSQKD YIKWTDLPKD VLSSGLKKLG EGQFGEVFKT KYRGNDVAMK
VVPLNNETNT SEKLANGDYM TSFPAAISEI TIAKELTNLN SETAPNASST FCQLIAAHVV
EGKFPPELGR AWDRYKKEWE GKDEDKAMND DPNEYGNDAE QIWVLLAFEL CGTELEDMKL
ESASQFTSIM TQLSLALIIA ETELEFEHRD MHISNVLVSP TSEEYIEYKL DFHKYRVKTN
GLRVKIIDYS LSRINLPDAL LYRDLAADCD IFDGGEGMLQ FETYRWMREN CDNNWRKYSP
YSNILWMGYT GQTLLADKHR PPEIKGHSKA QWTKAVKKFY DLGAVSEIFK PETDEAKQAS
EVILKKNSSG FAGHKNRKDR NWTGFGICWN RLKSLSATMH LSPQTRALLV VILGLASAFF
LLLFCTLCFV FFRQKRRTTK WVTATMIPKK LDESACSNAA FDFEDEFSPR RIEERRQARQ
LALQSIDPSG SLSLNRIDPA VGRALAVEQL LSGSCLIDAK TMNPNDSYVK IIAAKRDYL
//
