ID B3RM32_TRIAD Unreviewed; 428 AA.
AC B3RM32;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=TRIADDRAFT_52215 {ECO:0000313|EMBL:EDV28891.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV28891.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV28891.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV28891.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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DR EMBL; DS985241; EDV28891.1; -; Genomic_DNA.
DR RefSeq; XP_002108093.1; XM_002108057.1.
DR AlphaFoldDB; B3RM32; -.
DR STRING; 10228.B3RM32; -.
DR EnsemblMetazoa; TriadT52215; TriadP52215; TriadG52215.
DR GeneID; 6750045; -.
DR KEGG; tad:TRIADDRAFT_52215; -.
DR CTD; 6750045; -.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_000288_26_6_1; -.
DR InParanoid; B3RM32; -.
DR OMA; IASICHE; -.
DR OrthoDB; 460351at2759; -.
DR PhylomeDB; B3RM32; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
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 PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF35; SERINE_THREONINE-PROTEIN KINASE PAK; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|RuleBase:RU000304};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|RuleBase:RU000304}.
FT DOMAIN 178..428
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 39..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 428 AA; 47758 MW; 000145A3642E9EB7 CRC64;
MPSKWSSLLK TANISKAEQE KNPQAVIDAL EFFDAKEVKN DSSKTHIESK VKAVVDADEG
VESAGPDDDE ELSTSLPYKS ERSLNETPAE NEVCVDLILA LIKAIDKYTR DKIIKQLPVE
VKPSPLAKAP APRAVEQATP EAATPPARVR EKKKKMSDEQ VMVELRKIVS VGDPKQRYKE
YKEIGRGASG VVYTAVEIVT ENQVAIKQMN ITQQPKKELI INEIKVMKDN KNSNIVNYLD
SYLVDNQLWV VMEYLAGGSL TDVVTETCMD EGQIAAVCRE CLQALEFLHK QNVIHRDIKS
DNVLLGENGN VKLTDFGFCA QITPEQSKRS TMVGTPYWMA PEVVTRKAYG PKVDIWSLGI
MAIEMLEGEP PYLNENPIRA LYLIATNGTP KIANPERLSE SFRDFLNKCL EADVDERASA
MELLKVNN
//
