ID M3ILL7_CANMX Unreviewed; 1709 AA.
AC M3ILL7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=G210_2413 {ECO:0000313|EMBL:EMG47281.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47281.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG47281.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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};
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:EMG47281.1}.
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DR EMBL; AOGT01001642; EMG47281.1; -; Genomic_DNA.
DR STRING; 1245528.M3ILL7; -.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_001222_2_0_1; -.
DR OMA; EFYHRSG; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:InterPro.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR016255; Gcn2.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042:SF197; EIF-2-ALPHA KINASE GCN2; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..128
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 235..548
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 637..1022
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 711..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 80..107
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 136..192
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 723..738
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 880
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 643..651
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 666
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1709 AA; 194748 MW; A4461D9925E72F0D CRC64;
MPETSISSDL EHRQQDEISS ISSIYGDIFK DLTSKNLVWN KKPSPHFQVF LSSSTNPDRP
TVSVTLDIEF TPTYPLSPPR VKLLNAKNLL KANISKLEKK CKDLIKEYPE QEVSFTIISE
LIFMMDEIQS TTEKVLSLEE ERELRLKNER KALEEKEERQ RKEEALAKRK QNKELNAQIQ
KIQGEFDDYN DSEEIDVTSD SLLPSDDSDQ FFIFENAMEA TIPNTRKKFK FRAVSGFIKY
NQKGIFNSIG DQYLVKPYIT NDVQNKIVKH GTDLSYLLTV INLTNSHWQT EMGKREIQDL
ESELQLFMNI NHSNILKLIG FQIDKSEGWK IRLLTEFSPT SETLYDILPT AEFINWALAR
TWLIQLLPAI EYLHNAGFIH KLICPMTIVI FQERDQLYYQ NSMNDFLNSI GGEDSLTISS
KKVLKLCHPS YGHKILEMLS SHPNVGNVVD CPKVNPEAWM PPELKSSGYH HKSDIWDLGV
LFLRVMLGFD ILSTTYKTPS DFINKFSVDD FVGAEEYASL VYDVLSKMLS PKLSRRPSPL
ELNAVKFLRD GPVISKLQSE TNLSRLMKTV DADTQSRRHV QIDAAEKENA KRLNIPQNIS
RRRLSNQNTQ HPYFGENSAI LIPSGSQRNM GRYARDFEEV GKLGRGGFGE VVKARNRMEG
TFYAIKKIKH RADKLDSLLS EVLSLARLNH QYIVRYYGTW VEELEDTISA STSASQSQSA
IASDSEEDDD DTEDEFDTDE TFSSRLGRSS SMLPSYDNSF QVDYISTSFD PRIEFDELSD
DDDGGDDDPF VFANSSGTKD EAIGDEDEES TTMSRETSFK KPILAPKSIL YIQMEFCENN
TLLNLIEQGL PGNPDEYWRL FRQMLEAVSY IHREGFIHRD LKPMNIFIDR ANNIKVGDFG
LAKNSQFSSV VSTNNQVEAK DNDLSTIVGT LFYTANEVAT GNYDEKVDMY SLGIIFFEMC
YPLATGMERA RTLNDLRLKT VDFPTNFVAS KFKTEKKIIR LLLDHDPKIR PGAAQLLQSG
WLPVEHQDQV IQEALKSLAD PASPWQQQVR ETLFNQPYSL AKDLMFDSES NKQSFITSTD
YLLFDKIMNE VVKVFTNHGA VENLNTNFVL PKAPSQAREQ VYEILDKSGS VLTLPYDLTL
PTARFLSKTD LSIPKMYRHE FVYRPNARGV GMPDRYSAVH FDIVGNSEIS KPIMFAQDAE
CLKVIDEIVN LLPCFKNAVI VINHYDILDA VTSFSFGNIG IDEKRKVDIF GVLSQLGIDK
SGDEIKRYLR EDFQVPHTVT KDLVDNFNLT CEIEKSRQKL TKLMVDSPQL IKIERAYTYL
IEVFKILKQM GIKNTIVFNP LSNYNSKYYS HGIMFQAVFK SDKSKRYTRI ITGGRYDSLI
GSLANVSTKS KTPHGVGFTL TTSLLFILMK NLISRKSKID VTKWRGSRCK VIITSTQQQY
LNQCGYALLA SLWNKNISAD ITNTASKTQD EILQNGYMEG VTWIVIIRQL PSITKKVKKS
GSIFKPLKLK NIINGKEIDL EYDEAVSYLS FELSDSLDHD DDPSQTPLQL QQQSQLSSSS
ASSSQQMDDA SLEARKENLE LSGPLNSIDI DQKIIVVNND APRGRKNKRD KWESENDAKL
AGQSCLKDLS IGPVVVIDAR DEILDMISIT SIHQQDEWIR KVVFTTNNFP KSFAMNILNT
LIKEFNKGHK WVILVSSRTQ HTTIVDLRR
//
