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Database: UniProt
Entry: U9STH1_RHIID
LinkDB: U9STH1_RHIID
Original site: U9STH1_RHIID 
ID   U9STH1_RHIID            Unreviewed;        76 AA.
AC   U9STH1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
DE   Flags: Fragment;
GN   ORFNames=GLOINDRAFT_45617 {ECO:0000313|EMBL:ERZ97342.1};
OS   Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS   (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=747089 {ECO:0000313|EMBL:ERZ97342.1};
RN   [1] {ECO:0000313|EMBL:ERZ97342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DAOM 197198 {ECO:0000313|EMBL:ERZ97342.1};
RG   DOE Joint Genome Institute;
RA   Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA   Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA   Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA   Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA   Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA   San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA   Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA   Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT   "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT   evolution of the oldest plant symbiosis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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-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=2.7.12.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000972};
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   -!- 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=2.7.12.1; Evidence={ECO:0000256|ARBA:ARBA00001076};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001687};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00005843}.
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DR   EMBL; KI299703; ERZ97342.1; -; Genomic_DNA.
DR   AlphaFoldDB; U9STH1; -.
DR   eggNOG; KOG4257; Eukaryota.
DR   HOGENOM; CLU_189345_0_0_1; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00180; PKc; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR   PANTHER; PTHR46485:SF4; LIM DOMAIN KINASE 1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211}.
FT   DOMAIN          1..76
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ERZ97342.1"
FT   NON_TER         76
FT                   /evidence="ECO:0000313|EMBL:ERZ97342.1"
SQ   SEQUENCE   76 AA;  8777 MW;  ECFAFFED61151379 CRC64;
     WLVMEYANGG SLRNYLKENF NKLTWNDKYN IAYQLSCAVS CLYNEGILHN DLRSCNILVR
     DDTIKLADFG LSKRIG
//
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