ID A0A167Q5E3_PHYB8 Unreviewed; 585 AA.
AC A0A167Q5E3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=PHYBLDRAFT_120971 {ECO:0000313|EMBL:OAD79098.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD79098.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-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}.
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DR EMBL; KV440972; OAD79098.1; -; Genomic_DNA.
DR RefSeq; XP_018297138.1; XM_018428772.1.
DR AlphaFoldDB; A0A167Q5E3; -.
DR STRING; 763407.A0A167Q5E3; -.
DR GeneID; 28989678; -.
DR VEuPathDB; FungiDB:PHYBL_120971; -.
DR InParanoid; A0A167Q5E3; -.
DR OrthoDB; 5481355at2759; -.
DR Proteomes; UP000077315; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000077315};
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 180..417
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..47
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..585
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-1"
FT ACT_SITE 371
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-1"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-2"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-2"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-3"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR038147-3"
SQ SEQUENCE 585 AA; 66849 MW; 8AA8B71E2B77064F CRC64;
MSSEITTKPT TESHADAFAD AEEIDESELA YQEDSDDDDY DDYLDDELND TDLWDSASGD
FTKQYNRLRQ QVAPVARAGP AAPSFSGAST TTTITTTTTT TTAIAPAANK KTKTATNAST
AKEDVAAKKQ LLESQIESLS KFTSRIQVRA YEPPRMSSSV ASDIKLSSKK ASGERNTQKD
KSDRATVEQV LDPRTRIILF KMLNRGVFYE INGCISTGKE ANVYHAATED GLHRAIKVYK
TSVLTFKDRD RYVTGEYRFR HGYSKSNPRK MVKVWAEKEM RNLRRIKAAG IPSPEALVLR
MHVLVMEFLG DKNGWAYPRL KDAQIEQSKY ASLYYQLIKN VRTMYQVCRL VHADLSEYNL
LYHKGLLYII DVSQSVEHDH PHASEFLRKD LSNVTDYFSK RGVRVMGLMD LFSFVTDPSF
SNEDAVVDDV LEKIQTKMNS EPEKERNTLE EEIFMRSYIP QTLEEVIDVE RDTLLIAEGE
GKDVSIILYF RLSWLSIKKS KKDVEESEDN DDDDSEDDDS EDDSEDDSED DGGRKKPLRG
KKNEDKDDKK DRKKKAKEEA REKRKHKLPK AEKKRKIKIS RNRKK
//
