E2AK2_SCHPO
ID E2AK2_SCHPO Reviewed; 639 AA.
AC Q9UTE5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Eukaryotic translation initiation factor 2-alpha kinase 2;
DE EC=2.7.11.1;
DE AltName: Full=Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase;
DE AltName: Full=Heme-regulated inhibitor 2;
GN Name=hri2; ORFNames=SPAC222.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND AUTOPHOSPHORYLATION.
RC STRAIN=SP223;
RX PubMed=12242291; DOI=10.1128/mcb.22.20.7134-7146.2002;
RA Zhan K., Vattem K.M., Bauer B.N., Dever T.E., Chen J.-J., Wek R.C.;
RT "Phosphorylation of eukaryotic initiation factor 2 by heme-regulated
RT inhibitor kinase-related protein kinases in Schizosaccharomyces pombe is
RT important for resistance to environmental stresses.";
RL Mol. Cell. Biol. 22:7134-7146(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Mediates down-regulation of protein synthesis in response to
CC stress conditions by the phosphorylation of the alpha subunit of eIF-2
CC (tif211) on 'Ser-52'. Protein synthesis is inhibited at the level of
CC initiation. Activity is inhibited in the presence of heme.
CC {ECO:0000269|PubMed:12242291}.
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 -!- 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;
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF536224; AAN04054.1; -; mRNA.
DR EMBL; CU329670; CAB60699.1; -; Genomic_DNA.
DR PIR; T50148; T50148.
DR RefSeq; NP_593146.1; NM_001018543.2.
DR AlphaFoldDB; Q9UTE5; -.
DR SMR; Q9UTE5; -.
DR BioGRID; 278430; 25.
DR STRING; 4896.SPAC222.07c.1; -.
DR iPTMnet; Q9UTE5; -.
DR MaxQB; Q9UTE5; -.
DR PaxDb; Q9UTE5; -.
DR PRIDE; Q9UTE5; -.
DR EnsemblFungi; SPAC222.07c.1; SPAC222.07c.1:pep; SPAC222.07c.
DR GeneID; 2541943; -.
DR KEGG; spo:SPAC222.07c; -.
DR PomBase; SPAC222.07c; hri2.
DR VEuPathDB; FungiDB:SPAC222.07c; -.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_000288_134_1_1; -.
DR InParanoid; Q9UTE5; -.
DR OMA; RECMWEE; -.
DR PhylomeDB; Q9UTE5; -.
DR PRO; PR:Q9UTE5; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IDA:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0070314; P:G1 to G0 transition; IMP:PomBase.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IMP:PomBase.
DR GO; GO:0023052; P:signaling; IC:PomBase.
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 Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Protein synthesis inhibitor; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..639
FT /note="Eukaryotic translation initiation factor 2-alpha
FT kinase 2"
FT /id="PRO_0000085950"
FT DOMAIN 171..588
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 298..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 177..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 639 AA; 73367 MW; 377A00AF69A938A4 CRC64;
MRFFNAHKSA EDGNYSETTN AISLKNERQS RDLSVNKHGR MLLTALLENF CQLYDNNPAK
SKRLFALICH TLQKIGILEE EYIEELAAVR SNYQDALHHL ILQAREAIRL DDAEERLLAL
PDPTNVFEKF PQETALSKFS VDGLNVRQFR FRDLTLESWL QSRNSRYIED FEEYSLLGRG
GFGSVYHVRN KIDGAEYAMK KINSTFQQMS YSKIFREIKC LAKMDHPNVI RYFSSWVEST
TEATQMPIVM SKNSSRVLGT SSYCDVNGMD SIIFEPTESS ALTDDILFAE DPGTESIIST
SRKSSYSSTT ESSNFENLES PRNLHDSNVS TFNNTTILDD DYSSSMHISK TGPTHSFIIY
IQMQLCFDDL ESYLIRRNHF LSFPLCKEQI QLHTDLFRMI INGVMYVHEG VNLIHRDIKP
SNIFLAKSLP EDRGSVPLIS YNDKNDLKEY ITPKIGDFGL VVENKKNTET ALSFLERNHL
PNLQDETQHI GTATYAAPEL LDAMSSQHNK FTKKIDTFSL GMVLFELLHP FQTNMERATK
LQDLRRGNLP EEFVEQHICE SSLILWMTAK DPTKRPSLLE VLNCGLLLPN QVSMPNISNI
VSTNHLDVET QMKLIMDENQ RLREQIAVLR SRIQHLETR
