ID A0A1E4S3I1_CYBJN Unreviewed; 1098 AA.
AC A0A1E4S3I1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=CYBJADRAFT_167397 {ECO:0000313|EMBL:ODV74010.1};
OS Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=983966 {ECO:0000313|EMBL:ODV74010.1, ECO:0000313|Proteomes:UP000094389};
RN [1] {ECO:0000313|EMBL:ODV74010.1, ECO:0000313|Proteomes:UP000094389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; KV453929; ODV74010.1; -; Genomic_DNA.
DR RefSeq; XP_020071049.1; XM_020214887.1.
DR AlphaFoldDB; A0A1E4S3I1; -.
DR STRING; 983966.A0A1E4S3I1; -.
DR GeneID; 30989283; -.
DR OMA; NSHESKH; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000094389; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR CDD; cd06614; STKc_PAK; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF35; SERINE_THREONINE-PROTEIN KINASE PAK; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 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:0000313|EMBL:ODV74010.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000094389};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 544..557
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 819..1070
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 848
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1098 AA; 119130 MW; FB2726B909D1320D CRC64;
MDKEESFHSV LSLQEASDVE PLKTEESEVL EHERDEPVVN QEDVPNSPGM LPRLPGTLNV
KALSNSVESE DEVEGPQSAM AAITDTVNTA GEGVLGADET ALAADEANDD NDVTIQRALA
VDGAGVRTAD DEVEDITLDP GKHEDTRVNE LVNSLDEPID FKRVSSMTSD SSHSIESFTS
SQSHVQTGRD SSESGVQDVE LEDVIDGIAQ VNSVNVATST TVSHSPKVVV SQVHSPKVAM
SNSSKELLTG GEILRDVSNG VPEGPTDETD ASQRVLKEPV LIQAKSNNQE DQVLENDDTE
ATFAEKLIGT QLQSEDPQGK EIKTTPDDIV AQDVLPNESV SNAHVSGSSY ITSSNFETKI
IDDFVGSSQS SAKDELDHLE RPIATSSNIN IPSLSSSLSD NIGNMTIREG VQEDTFEVSN
TSGSSSGLNG SGTAYNNTTA ITSSSTPKNV SSINSTDSSM IPKTETPKVP TRYSNPSVSS
TSLSQSTLPK GSTGGRRTVS SPFGNKSKRS SGNKMKGVFS NIMNSMRSSN SHESKHLSSP
SLKISSPYDA KHVHHVGVDE DGQYTGLPEE WQKLLTSSGI TKQEQQKNPQ AVMDIVAFYQ
DQTKNADEKV FRKFNQNNTH LVSTASFRTP KTTQSQFTTP QDQQLPQFPI STPRYTQPPT
PILDTDKEKT FIPSRPAPKP PGSAAASPHV VSPLLRSQSQ KSTKSTPVIR PLGTFSPQRT
APQVPKIPPP VPAHVQTPKA EPPTSLVTKD LPEQSATTGE TNDPEPPVPV AKNSQKPVRD
PEQAAIAAER KKEEKKKRNA LVYAKLATIC SEGDPSKIYR NLFKIGQGAS GGVYTAYEVG
SNKCVAIKQM NLEQQPKKEL IINEILVMKG SKHKNIVNFI DSYLLKGDLW VIMEYMEGGS
LTDVVTHSIM TEGQIGAVCR ETLQGLEFLH SKGVIHRDIK SDNILLSMAG DIKLTDFGFC
AQINDVNLKR TTMVGTPYWM APEVVSRKQY GPKVDIWSLG IMIIEMIEGE PPYLNEAPLR
ALYLIATNGT PELKEPEMLT DTLKHFLSWT LQVDPEMRAD ATELLHDPFI VGADDVSSLA
PLVKLARMKK LAEKSDDE
//
