ID A0A1R1Y6Y8_9FUNG Unreviewed; 702 AA.
AC A0A1R1Y6Y8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AYI70_g2695 {ECO:0000313|EMBL:OMJ22721.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ22721.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ22721.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ22721.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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-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:OMJ22721.1}.
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DR EMBL; LSSN01000698; OMJ22721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1Y6Y8; -.
DR STRING; 133412.A0A1R1Y6Y8; -.
DR Proteomes; UP000187283; 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; cd05147; RIO1_euk; 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 InterPro; IPR018935; RIO_kinase_CS.
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.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OMJ22721.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000187283};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 188..556
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 67..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..642
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..702
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 80354 MW; 5EEAB8153C2A3B32 CRC64;
MENSQSATLK SQTEIDVEQD LELENDLDYY LSSDLDLDSD ELVSYEGDWA ETRGDFTKKY
NRLRDFIHSQ NNPTTPTSSK KSTVAPKPAI NSSGKAINDL EKTRSLNTMS SIDTKSQLIA
KFSNRIHLEN YQNITNSSSS NSKVSSKKSF GSNKGQVRDR ANRATTEQVL DPRTRMILFK
LLNQGVVYEI NGSINMGKEA NVYHAVTEDG QHRAIKVYKT SILIFKDRDR YFTGEYRFRN
GYSRHNPRKM VKLWAEKEMR NLKRIHQAGI LCPEPLVLRQ HVLVMNLLGD KDGWAYPRLK
DATIKKSRYP DLYFQIVTDM RIMYQVCKLV HADLSEYNIL YHNKKLYIID VSQSVEHDHP
YALDFLRSDC TNINDYFSKN GVHTLGLRQL FDFITNPKLG NTAPEFEEEL INIGKSLEKM
SEAEISKQLQ DDLVFKQSFI PRNLFEVLEY ERDVDKLNRG DTEDMLYMKM SGLALESQPD
TTPEPAAMKK DLDSSIIPQI KKSDESGRTL NPSHKNIELA STKPLELDNE NVISSSISKN
PSKKVTFDNL DSVQLIRNDL SDSQTRNSDE PDTKNESNIT LKNVESIHSD VDLSSKASTG
IDNANDDNGN NNLVNADDSG SENSNDEDGS DSDSEDDDEE GEEREWKERK TEPRGKRFLD
KDAKKEHKQN IKSEKREKRK TKIKKSVKKR KEQLTSGRKS KK
//
