ID A0A1I8IT04_9PLAT Unreviewed; 967 AA.
AC A0A1I8IT04;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0016187-snap-gene-0.2-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0016187-snap-gene-0.2-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 ---------------------------------------------------------------------------
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 AlphaFoldDB; A0A1I8IT04; -.
DR WBParaSite; maker-uti_cns_0016187-snap-gene-0.2-mRNA-1; maker-uti_cns_0016187-snap-gene-0.2-mRNA-1; maker-uti_cns_0016187-snap-gene-0.2.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000687; RIO_kinase.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF1; SERINE_THREONINE-PROTEIN KINASE RIO3; 1.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 628..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..376
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..414
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 101803 MW; C4786D15CB6FDBEA CRC64;
VRVTLSNHLR RDTTGAPASD SEEDPAATAV EPPLLPPGPA RSFNSRGVSG RGADLLTKHD
AEICGRRNAE RMAGFGHAGF RTGDTDGLQL DNRVYNSLKV HAAQEERRSA ARRQRDSQQQ
LSQQEQLEQQ RRQQLDERTR RLLQRLVTIR RLAEVGEVLK VGDQSLLIHA RCDSNSRCKG
GRPMPPDVVV KVFRRLSRSR LSSAAAAAAT SAESQLEAPC SPRGSPRARC LRELRGLRRL
RRAGVASPAP LMLRRHLLLT ELVGANGVAA PSLADCLEGG LLSEADWMKA WELTVTALRS
TLRLARLVHG NLDGRHLLWW RGSVWLTGLS RWTDRGHPRA GELLLRDCRA VCGFFERARP
GLPGLLEAAD LAELLGAGEA AGDAAAATAE AAAADEESGE EDEDDDDDAE ESGDEAGDLH
NPLTIETQSM SGADAVPWWM LDLQQEYRIA SVQVWNRLDA SDEIRFTQVS LGISSNHAVW
SSFDQSLFIR CSYWTGVPTD ATNPIPLTCS QPVSGRYLAL YKNRTGLTAS TQNYFNFCEW
VLCWRLWCWR LWLLAGLWCW RLCAGASGAS GAGASGAGAS WCCWLLAGAG ASGAGASGAG
ASGAGASGAG ASVLAPLVLA PLVLAPLVLA PLVLAPLVLA PLVLAPLVLA PLVLRASGAG
ASGAGALSGA GASVLPLAPL VLAPLVLACW PLVLAPLWPS AGASGAGASG AGASGAAGAS
GAGALVLAPL CWRWLAPLVL APLVLLRLWC WLASGYNELS AQDVKPAFSA TSASLLSVEQ
RTRSEVECLQ FCLTRPDCKL VLFRASELEC RLFNSAAVPA ESSALAGSPD AKVLAVQFRM
SGRGLARLTS NSASRRGSSG GSEQLYPASP AARPAVLGRP DGVRRRSEEN VHPSKPAVPS
ARVLFECPEH ADAAAVSPQV HAIENLLGCC QRPSSGSEGV PGALQLGEAG ACSGEEQQGG
GGCELGE
//
