ID A0A1G4MFQ8_LACFM Unreviewed; 1693 AA.
AC A0A1G4MFQ8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=LAFE_0F12244G {ECO:0000313|EMBL:SCW02695.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW02695.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) 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; LT598490; SCW02695.1; -; Genomic_DNA.
DR STRING; 4955.A0A1G4MFQ8; -.
DR OMA; EFYHRSG; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000190831; Chromosome f.
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; cd14012; PK_eIF2AK_GCN2_rpt1; 1.
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; 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; PF00069; Pkinase; 3.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000190831};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..128
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 218..526
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 599..1014
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 548..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 868
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 605..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 629
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1693 AA; 192584 MW; 065E26857D169F5B CRC64;
MSLSNLTLDQ YYEIQKNELE ALRSIYMDDF ADKTVQKSAW DKHPLLEFEI SLRSADKEPA
ESSVTIHFIL TPTYPHSKPQ VIFKNVCNVL ESQLVSLQAH FQEIYERSKG QEIIYEMTSL
VQEKLDEVQT LASTQSLEDQ RLQRIKEEKQ KLELEEIERT KSIEAERLKE QKLIDEIVKK
EIEKRQEDDD FTFKHENIID LMPPSDWVAS GEAFVFPRTI RAKLPNNSFY KFRAVVNPKS
IKLDNDILNF SSQKLVKPYI PPDSPLANTL TSSDMLDNFY YLLTEVLLDN AYFNTSNGKR
DISNLEKELE TMLKVNQNNV SKLYAYTVER TGKSSSTFVW KIRLLTEYSP PYFIGEVIES
VGFVNLATAR GWVLRLLEGL ESLHKHGVVH KNISLQTVNL AKDADFGTII PKLLHPSYGF
TILTLLSRHP NKSGLKVDVN RSTWIAPELV KFNNSKPQRK TDIWQLGVLF VQIINGVDTV
LNFPSPQDFL DSVSMNDSLF DFLEKMLDPE PKKRFGPLEL LPMKFLRTNI DPSINKLQIL
QDSVPNSTNN STLHMSASQL QRSHRSSRTS QGGGRRSFNV GSRFSSVNSG SRSRYATDFE
EIAILGKGAF GQVVKARNAL DSRYYAIKKI RHTEEKLSTI LSEVMLLASL NHQYVVRYYA
AWLEEDTLDD NAVTSTDEES ETSDDEATKS LTGSSIINSR TAQSLNNNNW DFISNSFQES
GYPDIVFANS SDEIVDENVS SSDEESLGTN IESNTKKTTL ETSEEEESSY GFSNYDSLGA
KTMGRHQKNG INEGKHRRFI EAGKSLTVSN TKTKSTLFIQ MEYCENRTLY DLIHTENLSS
QKDEYWRLFR EILEALSYIH SQGIIHRDLK PMNIFIDESR NIKIGDFGLA KNVHRPVDIL
RMDSYMNAGS TDDLTSAIGT ALYVATEVLT GNGNYNEKID MYSLGIIFFE MIYPFSTGME
RVNVIKKLRA PDVEFPSDFD NSRLKTERKI VRLLLDHDPN KRPGASMLLK SGWLPVKHQD
EVTKEALKNL ADPSSPWQQQ VRESLFTQPY SVTADILFDN SKTFSSAFNQ LLRSQMMEEV
VKIFRTHGGI ENNEPSIIFP KAPIYSTQSV YEVLDKGGSV LQLQYDLTYP MARYISRNSS
CVSKQYRMQY VYRPPEQSQS SMEPRKFIEI DFDIITTSSS DMAFYDAESM KVIDEIITQF
PVFEKTNTLF VINHADILDS VFNFCSIDKA QRSFVSHVLS QVGFKKSLKD VKSELKSLLN
ISSTSLNDLE LFDFKLDFDT AKKRLQKIMV DSPYLSKVEE SLMYISKVLN YFKPFGVTRN
VVISPLSNYN WGFYKGNIMF QAVYDDERTR NLIAAGGRYD SLISYIAKPP GHRNNHSQKA
VGFNLAWETI MIVAQNYFKL AAGRNIKKRS KFLKEGTIDW KPKRCDVLVS SFSNSILNSY
GVEILSRLWK AGISADFVRN CFTVDDVVSA AQVDGVDWII LIKQQTYSVP SHKRKYKPLK
VKKIGSEMDV DLDIDEFLTL YQQESAPGLS SNELLAINDM SAANDDKRWE DVVSTDGSQE
GGSDVSFTGG HHQKVVYIPN MATRAKKSNK KEKWIYEDSA RIASKSIINS LSSAPIFAVD
AIRDETLEII SITSLAQKDE WLRKVFGSGN NSAPRSFATS IYNNLSKEAS KGNKWAIIHC
NKTGKSCVVD LQR
//
