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IF2_SYNR3
ID   IF2_SYNR3               Reviewed;        1106 AA.
AC   A5GVG4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=SynRCC307_1970;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) 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:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR   EMBL; CT978603; CAK28873.1; -; Genomic_DNA.
DR   RefSeq; WP_011936385.1; NC_009482.1.
DR   AlphaFoldDB; A5GVG4; -.
DR   SMR; A5GVG4; -.
DR   STRING; 316278.SynRCC307_1970; -.
DR   PRIDE; A5GVG4; -.
DR   EnsemblBacteria; CAK28873; CAK28873; SynRCC307_1970.
DR   KEGG; syr:SynRCC307_1970; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_3; -.
DR   OMA; QVRPEMI; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001115; 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; cd03702; IF2_mtIF2_II; 1.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   PANTHER; PTHR43381; PTHR43381; 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; SSF50447; SSF50447; 2.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00487; IF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1106
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008362"
FT   DOMAIN          598..771
FT                   /note="tr-type G"
FT   REGION          57..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..614
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          632..636
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          657..660
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          711..714
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          747..749
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        77..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..125
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..150
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..234
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..277
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..371
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..396
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         607..614
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         657..661
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         711..714
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1106 AA;  116652 MW;  DC7C2971774FF948 CRC64;
     MTSGGKVRIY ELSRDLGLDN RDVLNAAEKL SIAAKSHSSS ISDGEAAKIK ALLNSNGKAA
     GGAKAPAKPD AGNQILSLKK APSTPSQSAG APASAPPSRK PEIVAKPAAP ASPAKPAPSA
     PPSRKPEIVA KPAAPASPAK PAPSAPPSRK PEVVAKPAAP ASPAKPAPKP VAKPVAKPAS
     APAPARPAQP LRPQASNRPP QQPSNRPPAR PAAKPPVVMS KPTAPPPRPA RPGAPAPRRD
     QNRPAVPMRP PNQQQRPSPQ RSGPPRSGAP IRPGAPQRPG MPGRGGAPQQ RRGPGGPGGR
     PPSSLELVGK PIRREPNAPQ GRQGGAPSRP GGPGGMRKPV SPGELMQLQK PGSRPTPGDG
     PRRPPARPGS EAPRRPGEAP NRPNAPTAPP RRPGYRPAAA PGMAGRPRRP DWDDSARLDA
     LRSRSPQKQR QKVHIIGEND DSLAAQTGGF AGGQEALVLQ ASLARPSKPK NLPGNKGARP
     VALRRRKKET TRQRQRRRAM ELRQAREAKQ IRPEMLVVPE GNLTVQELAD KLSVESSEII
     KSLFFKGIIA TVTQTLDLES IEKVSQEFGV PVLQDDIEEA AKKTVEMIEE SDLDHLIRRP
     PVVTVMGHVD HGKTSLLDAI RKTRVAAGEA GGITQHIGAY QVDVDHAGAS KKVTFLDTPG
     HEAFTAMRAR GTKVTDVAIL VVAADDGVRP QTLEAISHAR AAEVPIVVAI NKVDKEGAQI
     DRVKQELSDQ SLLAEDWGGD TVMVPVSALK GEGLDKLLEM ILLVTEVEDL KANPERMAKG
     TVVEAHLDKA KGPVATLLVQ NGTLRPGDVV AAGPVLGKVR AMVNDSGRRV KEAAPSSAVE
     VLGFSEVPAA GDEFEVYPDE KAARSVVGDR ASEARATRLA QQMASRRVSL TSMSGQASEG
     ELKELNLILK ADVQGSVEAI LGMLEQLPQG EVQVRVLLSA PGEVTETDVD LAAASGAVIV
     GFNTTLASGA RRAAELAGVD VRDYNVIYKL LEDIQAAMEG LLEPELVESP LGEAEVRAVF
     SIGKSAVAGC YVTSGSIQRN CKIRVHRGKQ LVFSGDLDSL KRMKNDVKEV NTGFECGFGC
     DRFADWQEGD RVEAFAMVTQ RRTLAT
 
 
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