ID Q6GVQ9_MYCAV Unreviewed; 914 AA.
AC Q6GVQ9;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
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 ECO:0000313|EMBL:AAT47738.1};
OS Mycobacterium avium.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1764 {ECO:0000313|EMBL:AAT47738.1};
RN [1] {ECO:0000313|EMBL:AAT47738.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15451099; DOI=10.1016/j.femsle.2004.08.014;
RA Danelishvili L., Poort M.J., Bermudez L.E.;
RT "Identification of Mycobacterium avium genes up-regulated in cultured
RT macrophages and in mice.";
RL FEMS Microbiol. Lett. 239:41-49(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY632749; AAT47738.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6GVQ9; -.
DR SMR; Q6GVQ9; -.
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; PR00449; RASTRNSFRMNG.
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}.
FT DOMAIN 421..581
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 52..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 430..437
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 469..473
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 523..526
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 914 AA; 95466 MW; 2FD60908F5E5A89A CRC64;
MAGKARVHEL AKELGVTSKE VLARLNEQGE FVKSASSTVE APVARRLRES FGGGKAAEGA
AKAPAKAAAK GDAKTAAKGD VKAPDKALDA ALDNAIKAGG NGEAAAPPAQ PGGTATTPAA
QATPEAPARP GPAAARPSAP APGQPKPPAP GQPPRPGATP GPRPGPAPKP AARTPRVGNN
PFSSAQPVDR PIPRPVPRPG APRPGAPRPG ASPGNMPPRP GGVGGPGRPA RPGAPRPGGG
RPGGPGGRDG GGGNYRGGGV GAPPGGGGGF RGRPGGGGGG RPGQRGGAAG AFGRPGGAPR
RGRKSKRQKR QEYDSMQAPV VGGVRLPHGN GETIRLARGA SLSDFAEKID ANPASLVQAL
FNLGEMVTAT QSVGDETLEL LGSEMNYNVQ VVSPEDEDRE LLESFDLTYG EDEGTEEDLQ
TRPPVVTVMG HVDHGKTRLL DTIRKANVRE AEQVTVEHDG VERPITFIDT PGHEAFTAMR
ARGAKATDIA ILVVAADDGV MPQTVEAINH AQAADVPIVV AVNKIDVEGA DPQKIRGQLT
EYGLVPEEFG GDTMFVDISA KQGTNIDQLL EAVLLTADAA LDLRANPDME AQGVAIEAHL
DRGRGPVATV LIQRGTLRVG DSIVAGDAYG RVRRMVDEHG DDVEEALPSR PVQVIGFTSV
PGAGDNLLVV DEDRIARQIA DKRSARKRNA LAARSRKRIS LEDLDSALKE TSQLNLILKG
DNAGTVEALE EALMGIQIDD EVALRVIDRG VGGITETNVN LASASDAVII GFNVRAEGKA
TELANREGVE IRYYSVIYQA IDEIEKALRG MLKPIYEENQ LGRAEIRAIF RSSKVGIIAG
CMITSGVVRR NAKARLLRDN VVVSENLTIN SLRREKDDVT EVREGFECGM TLGYSDIKEG
DVIESYELVQ KERT
//
