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Database: UniProt
Entry: A0A0E9NIV5_SAICN
LinkDB: A0A0E9NIV5_SAICN
Original site: A0A0E9NIV5_SAICN 
ID   A0A0E9NIV5_SAICN        Unreviewed;       787 AA.
AC   A0A0E9NIV5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=G7K_3886-t1 {ECO:0000313|EMBL:GAO49743.1};
OS   Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS   / NRRL Y-17804).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Taphrinomycotina incertae sedis; Saitoella.
OX   NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO49743.1, ECO:0000313|Proteomes:UP000033140};
RN   [1] {ECO:0000313|EMBL:GAO49743.1, ECO:0000313|Proteomes:UP000033140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO49743.1,
RC   ECO:0000313|Proteomes:UP000033140};
RX   PubMed=21914972; DOI=10.2323/jgam.57.243;
RA   Nishida H., Hamamoto M., Sugiyama J.;
RT   "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL   J. Gen. Appl. Microbiol. 57:243-246(2011).
RN   [2] {ECO:0000313|EMBL:GAO49743.1, ECO:0000313|Proteomes:UP000033140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO49743.1,
RC   ECO:0000313|Proteomes:UP000033140};
RX   PubMed=24646756; DOI=10.2323/jgam.60.7;
RA   Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT   "The early diverging ascomycetous budding yeast Saitoella complicata has
RT   three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT   lineages.";
RL   J. Gen. Appl. Microbiol. 60:7-12(2014).
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. STE Ser/Thr
CC       protein kinase family. COT1 subfamily. {ECO:0000256|ARBA:ARBA00038271}.
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:GAO49743.1}.
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DR   EMBL; BACD03000025; GAO49743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E9NIV5; -.
DR   STRING; 698492.A0A0E9NIV5; -.
DR   OMA; RESCSAN; -.
DR   Proteomes; UP000033140; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05573; STKc_ROCK_NDR_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356:SF400; SERINE/THREONINE-PROTEIN KINASE CBK1; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000033140};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          306..665
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          666..754
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   787 AA;  88268 MW;  141BD4722B3E7594 CRC64;
     MMNSRKKQQK PVMGPARFAA SEPLRPPKSA KNRPVLHKSF MDLLTFASLR SYAKRRTYQI
     SAPIAFEHVA HARDEEEARV LLQNWQKTSG GSKLMVSNMP LKVASRSVIS APMLLQTAPP
     QPLRAAPPIP LPADAVDKFL AELEVQQKRV SPTSLKPKSS KTPLSPPLSP ASKSTQSEPQ
     VEISTIDAVS TVVVRRVTRE TAMRVEEMFE RQLKGFRPTP TTIEKSAATK TYFELAYSKI
     LHPSASSPSP AYPYTPPALR IKALEEELLS HPSLTPQDRA EVLEKFRLEE EGYLRNMRRA
     IGPGSFVSVK NIGRGAFGVV KLVKEKDGMG APNKPKVYAM KCIKKSEMLR RGQEGHIRAE
     RDVLVKAAGS EAGKGGIVEL KWSFQDADFL YLIMEYMPGG DLLNLLIERD TFPEPFTRFY
     IAEMILCIEE THALGFIHRD VKPDNFLFDA RGHMKISDFG LATDLRWEHD GAYYEAQRRD
     LLRRTGVGVE GDTIDRRKGA EVLNKLGPDG EGAFGGGDHV LSWREKKGKR MLAYSVVGTN
     SYMAPEVIRG EGYDASCDWW SLGVILFECL YGFPPFVSKT RHATRMKILR WRESLRFPSG
     PRISPEAKDL ITRLICERQD RLGSSLSTRT AGRPNSMYAT ARGRPEERDG GIQADAGEIK
     AHPWFKGIDW ATLRDQEAPF QPEVKDIFDT RYFEELSTDE PLAAPGAAAG GAAERARDVL
     LRDRVHGALA LEMRKNLAFK GYTFKGGKKK EFLKEFRREM EQRLEEEERS RASLEVEEGQ
     GGRAMSL
//
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