ID S7XH19_SPRLO Unreviewed; 379 AA.
AC S7XH19;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=SLOPH_1581 {ECO:0000313|EMBL:EPR78354.1};
OS Spraguea lophii (strain 42_110) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Spraguidae;
OC Spraguea.
OX NCBI_TaxID=1358809 {ECO:0000313|EMBL:EPR78354.1, ECO:0000313|Proteomes:UP000014978};
RN [1] {ECO:0000313|Proteomes:UP000014978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=42_110 {ECO:0000313|Proteomes:UP000014978};
RX PubMed=23990793; DOI=10.1371/journal.pgen.1003676;
RA Campbell S.E., Williams T.A., Yousuf A., Soanes D.M., Paszkiewicz K.H.,
RA Williams B.A.P.;
RT "The genome of Spraguea lophii and the basis of host-microsporidian
RT interactions.";
RL PLoS Genet. 9:E1003676-E1003676(2013).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
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:EPR78354.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ATCN01000844; EPR78354.1; -; Genomic_DNA.
DR AlphaFoldDB; S7XH19; -.
DR STRING; 1358809.S7XH19; -.
DR VEuPathDB; MicrosporidiaDB:SLOPH_1581; -.
DR HOGENOM; CLU_018693_3_1_1; -.
DR InParanoid; S7XH19; -.
DR OMA; ITHENAF; -.
DR OrthoDB; 5481355at2759; -.
DR Proteomes; UP000014978; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05145; RIO1_like; 1.
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; IPR000687; RIO_kinase.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF2; SERINE_THREONINE-PROTEIN KINASE RIO1; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPR78354.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014978};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 41..367
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 343..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..379
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 44659 MW; 8F84C7FE8530592C CRC64;
MENNKVQKRI KDKKDRATVD KVLDPKTMNI LRKLENRNLL FNLGGCISSG KEANIYTGKA
STKLQSKFFK ETGEEEHIIP VVIKIYRTSK LEFKSREKYI EGERRFQSYC MSNPRKLIKL
WAEKEVRNLK RINECGILSP KPIYLKNNIL IMELIGEVGK VAPRLKDLKD QNNDDLYKDS
IRILKKLYRK AKLVHSDFSE YNLLFFNQLY LIDLGQAIET SQENSDAFLI MDIYNINNFF
MKKGVQVKNI NDLYEEITQK KIPSDLKNIE INSYSFIPQN INEVKDTKDM FMFTKNNEEE
SDVSGFITES SDSVDICNEL DKITLRKTKS KIASTKEEIK MLRKEFKDKR KEKRMSRNKM
TDKNKKLKKI SRKKKRTQH
//
