IF2A_SACS2
ID IF2A_SACS2 Reviewed; 266 AA.
AC Q97Z79;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Translation initiation factor 2 subunit alpha {ECO:0000255|HAMAP-Rule:MF_00231};
DE AltName: Full=aIF2-alpha {ECO:0000255|HAMAP-Rule:MF_00231};
DE AltName: Full=eIF-2-alpha {ECO:0000255|HAMAP-Rule:MF_00231};
GN Name=eif2a {ECO:0000255|HAMAP-Rule:MF_00231}; Synonyms=aif2a;
GN OrderedLocusNames=SSO1050;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA.
CC {ECO:0000255|HAMAP-Rule:MF_00231}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000255|HAMAP-Rule:MF_00231}.
CC -!- INTERACTION:
CC Q97Z79; Q980A5: eif2g; NbExp=2; IntAct=EBI-9010365, EBI-9010337;
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_00231}.
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DR EMBL; AE006641; AAK41314.1; -; Genomic_DNA.
DR PIR; C90257; C90257.
DR RefSeq; WP_009989173.1; NC_002754.1.
DR PDB; 2AHO; X-ray; 3.00 A; B=1-266.
DR PDB; 2QMU; X-ray; 3.20 A; B=175-266.
DR PDB; 2QN6; X-ray; 2.15 A; B=175-265.
DR PDB; 3CW2; X-ray; 2.80 A; C/D/G/H=1-266.
DR PDB; 3QSY; X-ray; 3.20 A; B=176-264.
DR PDB; 3V11; X-ray; 5.00 A; B=1-266.
DR PDB; 5JB3; EM; 5.34 A; 9=1-266.
DR PDB; 5JBH; EM; 5.34 A; 9=1-266.
DR PDB; 6SW9; EM; 4.20 A; 9=1-264.
DR PDB; 6SWC; EM; 3.30 A; 9=1-266.
DR PDBsum; 2AHO; -.
DR PDBsum; 2QMU; -.
DR PDBsum; 2QN6; -.
DR PDBsum; 3CW2; -.
DR PDBsum; 3QSY; -.
DR PDBsum; 3V11; -.
DR PDBsum; 5JB3; -.
DR PDBsum; 5JBH; -.
DR PDBsum; 6SW9; -.
DR PDBsum; 6SWC; -.
DR AlphaFoldDB; Q97Z79; -.
DR SMR; Q97Z79; -.
DR DIP; DIP-29030N; -.
DR IntAct; Q97Z79; 2.
DR STRING; 273057.SSO1050; -.
DR DNASU; 1454093; -.
DR EnsemblBacteria; AAK41314; AAK41314; SSO1050.
DR GeneID; 44129981; -.
DR KEGG; sso:SSO1050; -.
DR PATRIC; fig|273057.12.peg.1046; -.
DR eggNOG; arCOG04107; Archaea.
DR HOGENOM; CLU_033458_0_2_2; -.
DR InParanoid; Q97Z79; -.
DR OMA; DVNEHQR; -.
DR PhylomeDB; Q97Z79; -.
DR BRENDA; 3.6.5.3; 6163.
DR EvolutionaryTrace; Q97Z79; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR CDD; cd04452; S1_IF2_alpha; 1.
DR Gene3D; 1.10.150.190; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.1130; -; 1.
DR HAMAP; MF_00231; eIF_2_alpha; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR044126; S1_IF2_alpha.
DR InterPro; IPR022964; TIF2_asu_arc.
DR InterPro; IPR024055; TIF2_asu_C.
DR InterPro; IPR024054; TIF2_asu_middle_sf.
DR InterPro; IPR011488; TIF_2_asu.
DR PANTHER; PTHR10602; PTHR10602; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; SSF110993; 1.
DR SUPFAM; SSF116742; SSF116742; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT CHAIN 1..266
FT /note="Translation initiation factor 2 subunit alpha"
FT /id="PRO_0000137402"
FT DOMAIN 12..83
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00231"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3CW2"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:3CW2"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:3CW2"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:3CW2"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:2AHO"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3CW2"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:3CW2"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:3CW2"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3CW2"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3CW2"
FT HELIX 89..113
FT /evidence="ECO:0007829|PDB:3CW2"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:3CW2"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:3CW2"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6SWC"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:3CW2"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:3CW2"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3CW2"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:3CW2"
FT STRAND 177..187
FT /evidence="ECO:0007829|PDB:2QN6"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2QN6"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:2QN6"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2QN6"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:2QN6"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:2QN6"
FT HELIX 236..256
FT /evidence="ECO:0007829|PDB:2QN6"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:2QN6"
SQ SEQUENCE 266 AA; 30382 MW; A94E66BBE2931272 CRC64;
MIYSRSKLPS EGEILIATVK QVFDYGSYVS LDEYGGLQAF LPWSEVSSKW VKNIRDVLKE
NRKVIVKVIR VDRRKGTVDV SLKKVTDDER RKKNLQWKKI QRLDKILELV SQKLKLSEKD
AWEQVAWKLE AKYGDPITAI EKAVKEGEKI LIDAGVPEIW VKPLLEEASK HAEERKVKMS
GLITVRTNEP LGVEKIKEVI SKALENIEQD YESLLNIKIY TIGAPRYRVD VVGTNPKEAS
EALNQIISNL IKIGKEENVD ISVVKK
