ID A0A0G2EB84_9PEZI Unreviewed; 600 AA.
AC A0A0G2EB84;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Serine/threonine-protein kinase RIO1 {ECO:0000256|ARBA:ARBA00016038, ECO:0000256|PIRNR:PIRNR038147};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|PIRNR:PIRNR038147};
GN ORFNames=UCDDS831_g05225 {ECO:0000313|EMBL:KKY19566.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY19566.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY19566.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY19566.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY19566.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY19566.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) 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 ECO:0000256|PIRNR:PIRNR038147};
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 ECO:0000256|PIRNR:PIRNR038147};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR038147-3};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196,
CC ECO:0000256|PIRNR:PIRNR038147}.
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:KKY19566.1}.
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DR EMBL; LAQI01000111; KKY19566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2EB84; -.
DR Proteomes; UP000034182; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd05147; RIO1_euk; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR017407; Ser/Thr_kinase_Rio1.
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 PIRSF; PIRSF038147; Ser/Thr_PK_RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038147};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR038147};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038147};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR038147};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038147}.
FT DOMAIN 170..424
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..538
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..600
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-1"
FT ACT_SITE 376
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-1"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-2"
FT BINDING 303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-2"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-3"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-3"
SQ SEQUENCE 600 AA; 66702 MW; 2F4D4932D54DDE01 CRC64;
MASQEISPAA AHEPTHEYAP HQGYEPEADG GVPLSTAPQP EEVQQPADGE NEFSDGDDYD
DIFEDASDEE ADDEFAADVL GSANPNDFTK SYNRQRKLND PAVSAAYKPK TNPQGAAPKP
SANTKTAIDD QIRSLSVHAS KIRLDDSRYG GGGGSGNGKG SGRNDDGGKD RADRATSEQV
LDPRTRMLLL QMINRGIVSE IHGCVSTGKE ANVYHALSLP EDEDAPPVHR AIKVYKTSIL
VFKDRDKYVT GEFRFRGGYS KSNNRAMVKV WAEKEMRNLK RLHAAGIPCP QPLHLRLHVL
VMGFVGDRKG WPAPRLRDVP ADLGLSDAEE IERRWRDLYL ELLSYMRLMY QVCRLVHADL
SEYNLLYHDG RLCVIDVSQS VEHDHPRALE FLRMDIKNVA DFFRGGQRGV DTLPDRTVFA
FITNPAGSTD MAGVRDTLEE LYRVRAEQGE VAEGEDGGIR DDEVDNEVFR KQYIPQTLEQ
VYDVERDAEL VGAGKGDSLV YQNLLAGTTK EGAAATGGHD GEDEEEDEED EDSSGEDGES
GGEKEWRDKG PPRGKRFEDK EDKKAHKLAV KEEKREKRKT KMPKHVKKSL VKSTGKGHKK
//
