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Database: UniProt
Entry: A0A076MNS4_AMYME
LinkDB: A0A076MNS4_AMYME
Original site: A0A076MNS4_AMYME 
ID   A0A076MNS4_AMYME        Unreviewed;       974 AA.
AC   A0A076MNS4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=AMETH_2446 {ECO:0000313|EMBL:AIJ22538.1};
OS   Amycolatopsis methanolica 239.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX   NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ22538.1, ECO:0000313|Proteomes:UP000062973};
RN   [1] {ECO:0000313|EMBL:AIJ22538.1, ECO:0000313|Proteomes:UP000062973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=239 {ECO:0000313|EMBL:AIJ22538.1,
RC   ECO:0000313|Proteomes:UP000062973};
RA   Tang B.;
RT   "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       complex. {ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR   EMBL; CP009110; AIJ22538.1; -; Genomic_DNA.
DR   RefSeq; WP_026153043.1; NZ_CP009110.1.
DR   AlphaFoldDB; A0A076MNS4; -.
DR   STRING; 1068978.AMETH_2446; -.
DR   KEGG; amq:AMETH_2446; -.
DR   PATRIC; fig|1068978.7.peg.2613; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_9_3_11; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000062973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000062973}.
FT   DOMAIN          469..641
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          49..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..132
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..191
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..253
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         478..485
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         528..532
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         582..585
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   974 AA;  101771 MW;  F0AB0DF6A8EF59A0 CRC64;
     MAGKARVHEL AKELGVTSKE VLAKLKEQGE FVKSASSTVE APVARRLRDA FVTKDSKPAG
     RSGGARPGPP AGNGNGAAPK PAAPRQQQPQ ARPVPGAKPG PRPGPQQQAP APQASAPQAP
     APQAPAPQQQ RPAQQPAPQQ QAPAAKAQPQ APKPPVPRPG AGGSGQSGSV VPPKPQGPKP
     GPKPGPRAPR PGNNPFGVGQ GAPAPRPPAR PGGQGGERPA ERSGGGDRPA PRPGGGARPN
     PGNMPPRPNP GMMPGRVQRP GGGPGGAGRG GPGGGRGGAG AGRGGPGGPR GGGAPRGGPG
     GGGGGFRPGG GGGAPAGGGF RGGGGRGGGG GRGGTAGAFG RPGGPSRKGR KSKRQKRQEY
     MENMQAPSVG GIRLPKGSGE TIRLPRGASL TDFAEKIDAN PASLVQVLFH LGEMVTATQS
     VSDEVLELLG SEMNYNVQVV SPEEEDRELL ETFDITYGED EGGEEDLQVR PPVVTVMGHV
     DHGKTRLLDT IRKTRVHERE AGGITQHIGA YQVETELDGN PRLITFIDTP GHEAFTAMRA
     RGANSTDIAV IVVAADDGVM PQTVEAINHA QAAKAPIVVA VNKIDKEGAN PQKIRQQLTE
     YNLVAEEYGG DTMFVDISAR ENINIDGLLE AILLTADATL DLRANPDMPA QGVAIEAHLD
     RGRGPVATVL VQRGTLRVGD SVVAGDAYGR VRRMVDEYNE DVTEALPSRP VQVIGFTSVP
     GAGDTFLVVE EDRVARQIAE RRQARIRNAQ NAAKRKRVSL EDLDSALKET NSLNLIIKGD
     NSGTVEALEA SLMQLDVGDE VELNVVHRGV GGVTESDIDL ATASDAIVLG FNVRAEGKAT
     ERANREGVDV RYYTVIYQAI DEIEQALKGM LKPEYEEVEL GRAEVREVFK SSKFGTIAGC
     LVQSGEIRRN AKARLLRDNV VVAENLPVSS LRRFKDDVVE VREGYECGLT LGSYSDIKVD
     DVIETYEQRE KPRV
//
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