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Database: UniProt
Entry: A0A131ZVC4_SARSC
LinkDB: A0A131ZVC4_SARSC
Original site: A0A131ZVC4_SARSC 
ID   A0A131ZVC4_SARSC        Unreviewed;       330 AA.
AC   A0A131ZVC4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=STE20-related kinase adaptor beta-like protein {ECO:0000313|EMBL:KPM02756.1};
GN   ORFNames=QR98_0011750 {ECO:0000313|EMBL:KPM02756.1};
OS   Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC   Sarcoptidae; Sarcoptinae; Sarcoptes.
OX   NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM02756.1, ECO:0000313|Proteomes:UP000616769};
RN   [1] {ECO:0000313|EMBL:KPM02756.1, ECO:0000313|Proteomes:UP000616769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM02756.1};
RX   PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA   Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT   "Draft genome of the scabies mite.";
RL   Parasit. Vectors 8:585-585(2015).
CC   -!- FUNCTION: Pseudokinase which, in complex with CAB39/MO25
CC       (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates
CC       STK11/LKB1. Adopts a closed conformation typical of active protein
CC       kinases and binds STK11/LKB1 as a pseudosubstrate, promoting
CC       conformational change of STK11/LKB1 in an active conformation.
CC       {ECO:0000256|ARBA:ARBA00034653}.
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:KPM02756.1}.
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DR   EMBL; JXLN01002806; KPM02756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A131ZVC4; -.
DR   VEuPathDB; VectorBase:SSCA003809; -.
DR   OMA; YDTHLQN; -.
DR   OrthoDB; 5389025at2759; -.
DR   Proteomes; UP000616769; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:InterPro.
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; IPR047173; STRAD_A/B-like.
DR   PANTHER; PTHR48014; SERINE/THREONINE-PROTEIN KINASE FRAY2; 1.
DR   PANTHER; PTHR48014:SF24; SERINE_THREONINE-PROTEIN KINASE FRAY2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KPM02756.1};
KW   Transferase {ECO:0000313|EMBL:KPM02756.1}.
SQ   SEQUENCE   330 AA;  38450 MW;  2F88F233BC2A3372 CRC64;
     MNRLLTLSKS NFTKNVEDYS IENHLNPDQT LWKAKNRSLN VQCVLRKINL IDVDLELLEN
     ESNLDEIVDH PNIINMIENF VQKDYLYTIF PFANYGSIDK LCKPYGLEEG IIALVMKDLL
     PALDYLHRNN IIHRAIKGSN ILIFGDAETS FKFTLSGLKH SFLDDSTSFL NIFDYPTTSS
     KLLNHLAPEI LEQNILGYNY KSDIHSVGIL CCELANGIIP FDNISTDELL FYKLIGDTPR
     LLDHSCDEMN IFQELIDRLE ISLKQRYRIY MKKRFSSAFH DFVQQCLHCE PINRPKAYEL
     MEHTFCSLNK SETESYDRFK EILKKKFHSQ
//
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