ID J6EBI7_SACK1 Unreviewed; 737 AA.
AC J6EBI7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=YGL021W {ECO:0000313|EMBL:EJT41759.1};
GN Synonyms=SKDI07G2330 {ECO:0000313|EMBL:CAI4061965.1};
GN ORFNames=SKDI_07G2330 {ECO:0000313|EMBL:CAI4061965.1}, SKUD_187502
GN {ECO:0000313|EMBL:EJT41759.1};
OS Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS NBRC 1802 / NCYC 2889) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT41759.1, ECO:0000313|Proteomes:UP000002753};
RN [1] {ECO:0000313|EMBL:EJT41759.1, ECO:0000313|Proteomes:UP000002753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753}, and IFO 1802
RC {ECO:0000313|EMBL:EJT41759.1};
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [2] {ECO:0000313|EMBL:EJT41759.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT41759.1};
RA Cliften P.F., Johnston M.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000002753}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753};
RX PubMed=22384314; DOI=10.1534/g3.111.000273;
RA Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA Rine J., Johnston M., Hittinger C.T.;
RT "The awesome power of yeast evolutionary genetics: New genome sequences and
RT strain resources for the Saccharomyces sensu stricto genus.";
RL G3 (Bethesda) 1:11-25(2011).
RN [4] {ECO:0000313|EMBL:EJT41759.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT41759.1};
RA Cliften P., Hittinger C.T., Wang B., Sudarsanam P., Desikan A., Fulton L.,
RA Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:CAI4061965.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO1802 {ECO:0000313|EMBL:CAI4061965.1};
RA Byrne P K.;
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; OX365902; CAI4061965.1; -; Genomic_DNA.
DR EMBL; AACI03001952; EJT41759.1; -; Genomic_DNA.
DR AlphaFoldDB; J6EBI7; -.
DR HOGENOM; CLU_022568_0_0_1; -.
DR Proteomes; UP000002753; Unassembled WGS sequence.
DR Proteomes; UP001162087; Chromosome 7.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR024604; GSG2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1.
DR PANTHER; PTHR24419:SF18; SERINE_THREONINE-PROTEIN KINASE HASPIN; 1.
DR Pfam; PF12330; Haspin_kinase; 1.
DR SMART; SM01331; DUF3635; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000002753};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 625..734
FT /note="Serine/threonine-protein kinase haspin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01331"
FT REGION 51..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..359
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 83171 MW; 10B996586B672B8E CRC64;
MDFETSFEEF VEDKRFIALE VSDNDDDYDT DLTADTTDEL ESSVALNIKN CKAPLNGTTG
HNTPRKTNSN SKKRWSLLSN HSTVSSSKSK KRWSVLSSSF TSESHKDREP RGSLQQKRKS
LQSYSSLDTV ASSSSMSASS SLKQSSTGLS LRQLFTKIGI NDEVPQPGVG IAEGKENLPP
ILDKKTSPIA PIGSENRIRT PLKPLVNQPR RSTLQHQQQH QQQQQPLYNA SLASRRSSIS
STASSASSSK WKFWKRDKNM LPPTSQADHH SFAAMNRRGS MTLVEPRIKV KHKSSFSEFH
KAIFNSNTYS ESSDTVSSME TTMKNKASSS SLSLNVLKKR SSQSSLKHKS SHASLQKFKR
NKGKPSIMAS STVTSSSNDD SCSYSSKSST LSHRISLPIP DQVSRDKIKN KLRNSNSLLS
LNSKTSPPIN KNDQDESFLR QILQNCDIKR ILNPAKGDML PLINDVNHLS SIQLTSHVWQ
IGELICKKVA LGSIDDVTSD RKSLSLQELQ KFKIMNRKFN GIPQLLKSFV VKEANNTLFL
YFLFKDHGTP VSLISLKNWK QIMKIFWSCV GIIHGLETNL KFEHRNLSLD NILIDGNGNI
TIIDFKCSRL QTPEDDVLCL RLDHPLFFPD GNDKNKINEY QYQFEFEVYQ SMRILLNMDS
KAFEPITNLY WLYYLSRVLL KLGDRKLGKN DINRDKLAKV VSHLEVNLAV YKRGGQLSNR
LETADIKNTG DLLRLYE
//
