ID A0A2B4SEX9_STYPI Unreviewed; 504 AA.
AC A0A2B4SEX9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Serine/threonine-protein kinase 1 {ECO:0000256|ARBA:ARBA00016885};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=Pim2 {ECO:0000313|EMBL:PFX27117.1};
GN ORFNames=AWC38_SpisGene8190 {ECO:0000313|EMBL:PFX27117.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX27117.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 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 -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
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:PFX27117.1}.
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DR EMBL; LSMT01000110; PFX27117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4SEX9; -.
DR STRING; 50429.A0A2B4SEX9; -.
DR EnsemblMetazoa; XM_022932403.1; XP_022788138.1; LOC111328054.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR22984:SF25; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22984; SERINE/THREONINE-PROTEIN KINASE PIM; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Kinase {ECO:0000313|EMBL:PFX27117.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:PFX27117.1}.
FT DOMAIN 246..500
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 504 AA; 57904 MW; 22048C0E1F66EC70 CRC64;
MPKRNSRFSK KARSGQDKDR NENPKSNQNS RKRKAGTDVL PESKRKQTEK EIENFLKIQR
SVCSPRLPRE KSNCSGIVPQ TSYLKESKDC KVSSEKVLNQ ASLPEEKHAN IKPITSKSEQ
PSRKRKAKSN LLAATKRTEN ESRASFGKRQ QESHDSGYKL SRKRSSCAEA RLQGNSPQEN
NISKELLDYE DYEDPEEPDW LKDCHSPLWS PSYEPNYGSY VEAVKNTEPP DYIKELASSN
ADLAKYEIGK LLGSGSFGQV VAATRKSDNK PVALKFVNRS SVQEFKKLRG REIPAEAYLM
SRVRHPNVIQ IYQLIFTEEH YCFVMERPES CKDFFDVIQD RNSTGNPLSE KEVRRYFSQI
LEANIRCEEK GVIHRDIKPE NILLDLTNDE VKLIDFGLAS EIQEEPFDSF RGTNQYMPPE
FMKTSKYDGC EATVWAMGIL LVDMLSPVIS AFEKPQHCLS MEPRIPQHFS SEVKHVVRML
LNPEADQRPT LKQVLQHPWF SMKD
//
