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Conserved domains on  [gi|150372936|dbj|BAF66238|]
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elongation factor G, partial [Bacillus subtilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FusA super family cl43154
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 3-137 3.81e-73

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


The actual alignment was detected with superfamily member COG0480:

Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 230.70  E-value: 3.81e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDDLGTRSDAKEIPEEYKE 82
Cdd:COG0480  125 YGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLPIGAEDDFKGVIDLVTMKAYVYDDELGAKYEEEEIPAELKE 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150372936  83 QAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:COG0480  205 EAEEAREELIEAVAETDDELMEKYLEGEELTEEEIKAGLRKATLAGKIVPVLCGS 259
 
Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 3-137 3.81e-73

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 230.70  E-value: 3.81e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDDLGTRSDAKEIPEEYKE 82
Cdd:COG0480  125 YGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLPIGAEDDFKGVIDLVTMKAYVYDDELGAKYEEEEIPAELKE 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150372936  83 QAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:COG0480  205 EAEEAREELIEAVAETDDELMEKYLEGEELTEEEIKAGLRKATLAGKIVPVLCGS 259
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
 1-137 2.15e-72

translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]


Pssm-ID: 129575 [Multi-domain]  Cd Length: 689  Bit Score: 228.54  E-value: 2.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936    1 TTYGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDDLGTRSDAKEIPEEY 80
Cdd:TIGR00484 124 NRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLPIGAEDNFIGVIDLVEMKAYFFNGDKGTKAIEKEIPSDL 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 150372936   81 KEQAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:TIGR00484 204 LEQAKELRENLVEAVAEFDEELMEKYLEGEELTIEEIKNAIRKGVLNCEFFPVLCGS 260
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 3-137 5.41e-68

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 206.19  E-value: 5.41e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDDLGTRSDAKEIPEEYKE 82
Cdd:cd01886  115 YGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDDFEGVVDLIEMKALYWDGELGEKIEETDIPEDLLE 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150372936  83 QAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:cd01886  195 EAEEAREELIETLAEVDDELMEKYLEGEEITEEEIKAAIRKGTIANKIVPVLCGS 249
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
3-137 3.18e-57

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 188.03  E-value: 3.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDdlGTRSDAKEIPEEYKE 82
Cdd:PRK12740 111 YGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDDFTGVVDLLSMKAYRYDE--GGPSEEIEIPAELLD 188

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150372936  83 QAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:PRK12740 189 RAEEAREELLEALAEFDDELMEKYLEGEELSEEEIKAGLRKATLAGEIVPVFCGS 243
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-32 1.63e-04

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 39.43  E-value: 1.63e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 150372936    2 TYGVPRIVFVNKMDKI-GADFLYSVGTLRDRL 32
Cdd:pfam00009 119 QLGVPIIVFINKMDRVdGAELEEVVEEVSREL 150
 
Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 3-137 3.81e-73

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 230.70  E-value: 3.81e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDDLGTRSDAKEIPEEYKE 82
Cdd:COG0480  125 YGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLPIGAEDDFKGVIDLVTMKAYVYDDELGAKYEEEEIPAELKE 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150372936  83 QAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:COG0480  205 EAEEAREELIEAVAETDDELMEKYLEGEELTEEEIKAGLRKATLAGKIVPVLCGS 259
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
 1-137 2.15e-72

translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]


Pssm-ID: 129575 [Multi-domain]  Cd Length: 689  Bit Score: 228.54  E-value: 2.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936    1 TTYGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDDLGTRSDAKEIPEEY 80
Cdd:TIGR00484 124 NRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLPIGAEDNFIGVIDLVEMKAYFFNGDKGTKAIEKEIPSDL 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 150372936   81 KEQAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:TIGR00484 204 LEQAKELRENLVEAVAEFDEELMEKYLEGEELTIEEIKNAIRKGVLNCEFFPVLCGS 260
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 3-137 5.41e-68

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 206.19  E-value: 5.41e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDDLGTRSDAKEIPEEYKE 82
Cdd:cd01886  115 YGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDDFEGVVDLIEMKALYWDGELGEKIEETDIPEDLLE 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150372936  83 QAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:cd01886  195 EAEEAREELIETLAEVDDELMEKYLEGEEITEEEIKAAIRKGTIANKIVPVLCGS 249
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
3-137 3.18e-57

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 188.03  E-value: 3.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDdlGTRSDAKEIPEEYKE 82
Cdd:PRK12740 111 YGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDDFTGVVDLLSMKAYRYDE--GGPSEEIEIPAELLD 188

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150372936  83 QAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:PRK12740 189 RAEEAREELLEALAEFDDELMEKYLEGEELSEEEIKAGLRKATLAGEIVPVFCGS 243
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 3-137 2.55e-45

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 148.13  E-value: 2.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDdlGTRSDAKEIPEEYKE 82
Cdd:cd04170  115 AKLPRIIFINKMDRARADFDKTLAALREAFGRPVVPIQLPIGEGDEFTGVVDLLSEKAYRYDP--GEPSVEIEIPEELKE 192

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150372936  83 QAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:cd04170  193 KVAEAREELLEAVAETDEELMEKYLEEGELTEEELRAGLRRALRAGLIVPVFFGS 247
PRK13351 PRK13351
elongation factor G-like protein;
3-137 6.98e-42

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 146.64  E-value: 6.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYED-DLGTRSDAKEIPEEYK 81
Cdd:PRK13351 124 YGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQLPIGSEDGFEGVVDLITEPELHFSEgDGGSTVEEGPIPEELL 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 150372936  82 EQAEELRNSLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:PRK13351 204 EEVEEAREKLIEALAEFDDELLELYLEGEELSAEQLRAPLREGTRSGHLVPVLFGS 259
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 3-137 1.30e-12

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 62.25  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   3 YGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPigaednfegiidlvenvayfyeddlgtrsDAKEIPEEYKE 82
Cdd:cd04168  115 LNIPTIIFVNKIDRAGADLEKVYQEIKEKLSPDIVPMQKV-----------------------------GLYPNICDTNN 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 150372936  83 QAEElrnsLIEAVCELDEELMDKYLEGEEITIDELKAGIRKGTLNVEFYPVLVGS 137
Cdd:cd04168  166 IDDE----QIETVAEGNDELLEKYLSGGPLEELELDNELSARIQKASLFPVYHGS 216
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 4-110 7.41e-09

Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.


Pssm-ID: 206732 [Multi-domain]  Cd Length: 268  Bit Score: 52.21  E-value: 7.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   4 GVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDDLG----------TRSDA 73
Cdd:cd04169  123 GIPIITFINKLDREGRDPLELLDEIENELGIDCAPMTWPIGMGKDFKGVYDRYDKEIYLYERGAGgaikapeetkGLDDP 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 150372936  74 KEIPEEYKEQAEELRNS--LIEAVC-ELDEELmdkYLEGE 110
Cdd:cd04169  203 KLDELLGEDLAEQLREEleLVEGAGpEFDKEL---FLAGE 239
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 2-58 1.26e-08

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 50.45  E-value: 1.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 150372936    2 TYGVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAhAIQLPIGAEDNFEGIIDLVEN 58
Cdd:TIGR00231 107 DSGVPIILVGNKIDLKDADLKTHVASEFAKLNGEP-IIPLSAETGKNIDSAFKIVEA 162
prfC PRK00741
peptide chain release factor 3; Provisional
 4-110 1.20e-06

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 46.28  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150372936   4 GVPRIVFVNKMDKIGADFLYSVGTLRDRLQANAHAIQLPIGAEDNFEGIIDLVENVAYFYEDDLGTRSDAKEIPEEY--- 80
Cdd:PRK00741 131 DTPIFTFINKLDRDGREPLELLDEIEEVLGIACAPITWPIGMGKRFKGVYDLYNDEVELYQPGEGHTIQEVEIIKGLdnp 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 150372936  81 -------KEQAEELRNSL---IEAVCELDEElmdKYLEGE 110
Cdd:PRK00741 211 eldellgEDLAEQLREELelvQGASNEFDLE---AFLAGE 247
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-32 1.63e-04

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 39.43  E-value: 1.63e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 150372936    2 TYGVPRIVFVNKMDKI-GADFLYSVGTLRDRL 32
Cdd:pfam00009 119 QLGVPIIVFINKMDRVdGAELEEVVEEVSREL 150
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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