UniProt: A0A183LVA1

Database: UniProt
Entry: A0A183LVA1_9TREM

LinkDB:  A0A183LVA1_9TREM 
Original site:  A0A183LVA1_9TREM

All links

Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
All databases (13)   

Download RDF

ID   A0A183LVA1_9TREM        Unreviewed;       472 AA.
AC   A0A183LVA1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN   ORFNames=SMRZ_LOCUS7726 {ECO:0000313|EMBL:VDO77801.1};
OS   Schistosoma margrebowiei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0000772701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMRZ_0000772701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO77801.1, ECO:0000313|Proteomes:UP000277204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zambia {ECO:0000313|EMBL:VDO77801.1,
RC   ECO:0000313|Proteomes:UP000277204};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC         L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC         COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU361271}; Single-
CC       pass type I membrane protein {ECO:0000256|RuleBase:RU361271}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|ARBA:ARBA00009605, ECO:0000256|RuleBase:RU361271}.
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   EMBL; UZAI01003182; VDO77801.1; -; Genomic_DNA.
DR   STRING; 48269.A0A183LVA1; -.
DR   WBParaSite; SMRZ_0000772701-mRNA-1; SMRZ_0000772701-mRNA-1; SMRZ_0000772701.
DR   Proteomes; UP000277204; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF98; SERINE_THREONINE-PROTEIN KINASE RECEPTOR; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361271};
KW   Kinase {ECO:0000256|RuleBase:RU361271};
KW   Magnesium {ECO:0000256|RuleBase:RU361271};
KW   Manganese {ECO:0000256|RuleBase:RU361271};
KW   Metal-binding {ECO:0000256|RuleBase:RU361271};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361271}; Receptor {ECO:0000256|RuleBase:RU361271};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277204};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU361271}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|RuleBase:RU361271}.
FT   DOMAIN          1..236
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          249..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  53422 MW;  62094A90F09EB200 CRC64;
     VIVDNSIGED KLEYWLVTEY HPLGSVYDYL HAYDIQWIDL LKICTGIAQG LAHLHMEIPN
     LSKPSIAHRD LNSRNVLLKS DLTACIADFG LAIRFEAGQC MRDAHLQLGT RRYMAPEVLD
     GAIQFSKDAF LRIDIYAMGL VFWELMMRCC CGSSKNAIIH ITSYLAPYEI ELGPQPSMEA
     LQRWVAHAKQ RPKFNPQWAS DGGLCTLWET IEECWDQDAE ARLSAGCVTK RLTTLLRLSV
     INQQYNDSYI TNSNNNDSNG INEKDNNNDN NTVMSNYLTN SQKTDCNPPP PYYYCYYSPC
     ITTSTTTIAT VTTTTLMDVP KDLCNGRYTT TSLMNYSRKE DIGVYNCSDV LSTTTTITDN
     INNGNNDKSN TILTRGNTGC PPTICLPYSM NINFSTLTDH RSNKINSEIL QCKRKNQTLC
     FNDILNRTEN QIQCDSTEYL KPIQPNQQSK TIVNEEQSTE YQKLLSSVTN MK
//

DBGET integrated database retrieval system