NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|338855637|gb|AEJ32097|]
View 

elongation factor Tu, partial [Synechococcus sp. RCC792]

Protein Classification

elongation factor Tu( domain architecture ID 1000100)

elongation factor Tu promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis

Gene Ontology:  GO:0005525|GO:0003746|GO:0003924
PubMed:  31708880|17446867|8073502

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00049 super family cl35051
elongation factor Tu; Reviewed
 1-122 1.24e-100

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 292.48  E-value: 1.24e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:PRK00049  14 NVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMI 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:PRK00049  94 TGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFL 135
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-122 1.24e-100

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 292.48  E-value: 1.24e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:PRK00049  14 NVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMI 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:PRK00049  94 TGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFL 135
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-122 1.86e-100

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


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 292.05  E-value: 1.86e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:COG0050   14 NIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMI 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:COG0050   94 TGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFL 135
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-122 1.31e-90

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 260.21  E-value: 1.31e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:cd01884    4 NVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:cd01884   84 TGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFL 125
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-122 2.70e-81

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 243.53  E-value: 2.70e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:TIGR00485  14 NVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMI 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 338855637   81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:TIGR00485  94 TGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFL 135
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-122 2.67e-63

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: 190.81  E-value: 2.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    1 NIGTIGHVDHGKTTLTAAI---TNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVK 77
Cdd:pfam00009   5 NIGIIGHVDHGKTTLTDRLlyyTGAISKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVK 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 338855637   78 NMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPaLVVAL 122
Cdd:pfam00009  85 EVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFI 128
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-122 1.24e-100

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 292.48  E-value: 1.24e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:PRK00049  14 NVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMI 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:PRK00049  94 TGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFL 135
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-122 1.86e-100

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


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 292.05  E-value: 1.86e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:COG0050   14 NIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMI 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:COG0050   94 TGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFL 135
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-122 5.36e-96

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 280.96  E-value: 5.36e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:PRK12735  14 NVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMI 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:PRK12735  94 TGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFL 135
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-122 1.74e-93

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 274.51  E-value: 1.74e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:PRK12736  14 NIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMI 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:PRK12736  94 TGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFL 135
tufA CHL00071
elongation factor Tu
 1-122 4.78e-91

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 268.75  E-value: 4.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:CHL00071  14 NIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMI 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:CHL00071  94 TGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFL 135
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-122 1.31e-90

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 260.21  E-value: 1.31e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:cd01884    4 NVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:cd01884   84 TGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFL 125
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-122 2.70e-81

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 243.53  E-value: 2.70e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:TIGR00485  14 NVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMI 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 338855637   81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:TIGR00485  94 TGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFL 135
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-122 5.35e-81

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 244.35  E-value: 5.35e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:PLN03127  63 NVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMI 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:PLN03127 143 TGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFL 184
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-122 8.30e-73

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 224.11  E-value: 8.30e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:PLN03126  83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:PLN03126 163 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFL 204
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-122 2.67e-63

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: 190.81  E-value: 2.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    1 NIGTIGHVDHGKTTLTAAI---TNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVK 77
Cdd:pfam00009   5 NIGIIGHVDHGKTTLTDRLlyyTGAISKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVK 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 338855637   78 NMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPaLVVAL 122
Cdd:pfam00009  85 EVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFI 128
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-120 1.44e-48

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 153.22  E-value: 1.44e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVV 120
Cdd:cd00881   81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVA 120
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-122 2.07e-45

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 151.62  E-value: 2.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAI---TNVLAKKGQAQIQNYAD------------IDGAPEERERGITINTAHVEYETDSRHYA 65
Cdd:COG5256    9 NLVVIGHVDHGKSTLVGRLlyeTGAIDEHIIEKYEEEAEkkgkesfkfawvMDRLKEERERGVTIDLAHKKFETDKYYFT 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 338855637  66 HVDCPGHADYVKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:COG5256   89 IIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAV 145
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-121 1.37e-43

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 146.99  E-value: 1.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTL-------TAAITNVL--------AKKGQAQIQnYADI-DGAPEERERGITINTAHVEYETDSRHY 64
Cdd:PRK12317   8 NLAVIGHVDHGKSTLvgrllyeTGAIDEHIieelreeaKEKGKESFK-FAWVmDRLKEERERGVTIDLAHKKFETDKYYF 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 338855637  65 AHVDCPGHADYVKNMITGAAQMDGAILVCAATD--GPMAQTKEHILLAKQVGVPALVVA 121
Cdd:PRK12317  87 TIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVA 145
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-121 9.46e-41

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 134.54  E-value: 9.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAaitNVLAKKG---QAQIQNYAD---------------IDGAPEERERGITINTAHVEYETDSR 62
Cdd:cd01883    1 NLVVIGHVDAGKSTLTG---HLLYKLGgvdKRTIEKYEKeakemgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKY 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338855637  63 HYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-------PMAQTKEHILLAKQVGVPALVVA 121
Cdd:cd01883   78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVA 143
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 2-122 1.70e-33

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 122.33  E-value: 1.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   2 IGTIGHVDHGKTTLTAAITNVlakkgqaqiqnyaDIDGAPEERERGITINT--AHVEYEtDSRHYAHVDCPGHADYVKNM 79
Cdd:COG3276    3 IGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLgfAYLPLP-DGRRLGFVDVPGHEKFIKNM 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 338855637  80 ITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:COG3276   69 LAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVL 111
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-122 2.00e-33

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 114.24  E-value: 2.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   2 IGTIGHVDHGKTTLTAAITNVlakkgqaqiqnyaDIDGAPEERERGITINT--AHVEYEtDSRHYAHVDCPGHADYVKNM 79
Cdd:cd04171    2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLP-DGKRLGFIDVPGHEKFVKNM 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 338855637  80 ITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:cd04171   68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVL 110
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-122 8.64e-31

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 114.59  E-value: 8.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    1 NIGTIGHVDHGKTTLTAAITNVlakkgqaqiqnyaDIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:TIGR00475   2 IIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 338855637   81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:TIGR00475  69 AGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVI 110
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-122 4.28e-29

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 108.68  E-value: 4.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYAD---------------IDGAPEERERGITINTAHVEYETDSRHYA 65
Cdd:PTZ00141   9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDIALWKFETPKYYFT 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338855637  66 HVDCPGHADYVKNMITGAAQMDGAILVCAATDGPM-------AQTKEHILLAKQVGVPALVVAL 122
Cdd:PTZ00141  89 IIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFeagiskdGQTREHALLAFTLGVKQMIVCI 152
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 2-122 3.22e-28

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 107.44  E-value: 3.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   2 IGTIGHVDHGKTTLTAAITNVlakkgqaqiqnyaDIDGAPEERERGITINTAHVEY-ETDSRHYAHVDCPGHADYVKNMI 80
Cdd:PRK10512   3 IATAGHVDHGKTTLLQAITGV-------------NADRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:PRK10512  70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVAL 111
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 4-122 5.27e-27

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 98.80  E-value: 5.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   4 TIGHVDHGKTTLT---------------AAITNVLAKKGQAQIQNYAD-IDGAPEERERGITINTAHVEYETDSRHYAHV 67
Cdd:cd04166    4 TCGSVDDGKSTLIgrllydsksifedqlAALERSKSSGTQGEKLDLALlVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 338855637  68 DCPGHADYVKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVAL 122
Cdd:cd04166   84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAV 138
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 4-121 9.03e-26

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 99.39  E-value: 9.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   4 TIGHVDHGKTTLT---------------AAITNVLAKKGQAQIqNYADI-DGAPEERERGITINTAHVEYETDSRHYAHV 67
Cdd:COG2895   22 TCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRGTQEI-DLALLtDGLQAEREQGITIDVAYRYFSTPKRKFIIA 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 338855637  68 DCPGHADYVKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVA 121
Cdd:COG2895  101 DTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVA 154
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-120 3.20e-25

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 93.97  E-value: 3.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKkgqaqiqnyADIDGAPEERERGITINTAHVEYETDSRHYAH-------------- 66
Cdd:cd01889    2 NVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLDLGFSSFEVDKPKHLEdnenpqienyqitl 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 338855637  67 VDCPGHADYVKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVV 120
Cdd:cd01889   73 VDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV 126
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-121 1.13e-24

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 96.46  E-value: 1.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAkkgqaqiqnyadiDGAPEERERGITINTAHVE--------------YETD------ 60
Cdd:PRK04000  11 NIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatirkcpdceepeaYTTEpkcpnc 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338855637  61 ------SRHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMAQTKEHILLAKQVGVPALVVA 121
Cdd:PRK04000  78 gsetelLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIV 145
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
 1-121 5.12e-24

Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444075 [Multi-domain]  Cd Length: 408  Bit Score: 94.52  E-value: 5.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAkkgqaqiqnyadiDGAPEERERGITINTAHVE--------------YETD------ 60
Cdd:COG5257    7 NIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTEpkcpnc 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338855637  61 ------SRHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMAQTKEHILLAKQVGVPALVVA 121
Cdd:COG5257   74 gsetelLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIV 141
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
 1-121 5.60e-24

translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.


Pssm-ID: 274720 [Multi-domain]  Cd Length: 406  Bit Score: 94.35  E-value: 5.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    1 NIGTIGHVDHGKTTLTAAITNVLakkgqaqiqnyadIDGAPEERERGITINTAHVE--------------YETDS----- 61
Cdd:TIGR03680   6 NIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvcpnc 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338855637   62 -------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMAQTKEHILLAKQVGVPALVVA 121
Cdd:TIGR03680  73 gsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIV 140
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 1-122 1.51e-23

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 89.63  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQaqiqnyadidgapEERERGITI-------------------NTAHVEYETDS 61
Cdd:cd01888    2 NIGTIGHVAHGKTTLVKALSGVWTVRHK-------------EELKRNITIklgyanakiykcpncgcprPYDTPECECPG 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637  62 --------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMAQTKEHILLAKQVGVPALVVAL 122
Cdd:cd01888   69 cggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQ 138
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-119 1.20e-19

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 82.83  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYAD---------------IDGAPEERERGITINTAHVEYETDSRHYA 65
Cdd:PLN00043   9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDIALWKFETTKYYCT 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338855637  66 HVDCPGHADYVKNMITGAAQMDGAILVCAATDGPM-------AQTKEHILLAKQVGVPALV 119
Cdd:PLN00043  89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFeagiskdGQTREHALLAFTLGVKQMI 149
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 4-121 1.76e-19

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 82.28  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   4 TIGHVDHGKTTLT---------------AAITNVLAKKG-QAQIQNYA-DIDGAPEERERGITINTAHVEYETDSRHYAH 66
Cdd:PRK05506  29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVGtQGDEIDLAlLVDGLAAEREQGITIDVAYRYFATPKRKFIV 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 338855637  67 VDCPGHADYVKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVA 121
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLA 163
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 4-121 2.50e-19

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 81.65  E-value: 2.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    4 TIGHVDHGKTTLT---------------AAITNVLAKKG-QAQIQNYA-DIDGAPEERERGITINTAHVEYETDSRHYAH 66
Cdd:TIGR02034   5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKHGtQGGEIDLAlLVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 338855637   67 VDCPGHADYVKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVA 121
Cdd:TIGR02034  85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLA 139
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 1-103 1.45e-18

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 79.91  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTaaiTNVLAKKGQ-----AQIQNYADIDgaPEERERGITINTAHV----EYETDSRHYAHVDCPG 71
Cdd:PRK07560  22 NIGIIAHIDHGKTTLS---DNLLAGAGMiseelAGEQLALDFD--EEEQARGITIKAANVsmvhEYEGKEYLINLIDTPG 96

                         90       100       110
                 ....*....|....*....|....*....|..
gi 338855637  72 HADYVKNMITGAAQMDGAILVCAATDGPMAQT 103
Cdd:PRK07560  97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT 128
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 1-104 1.69e-18

Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 79.68  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAI---TNVLAKKGQAQ--IQNYADIdgapeERERGITI---NTAhVEYETdsrhyaH----VD 68
Cdd:COG1217    8 NIAIIAHVDHGKTTLVDALlkqSGTFRENQEVAerVMDSNDL-----ERERGITIlakNTA-VRYKG------VkiniVD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  69 CPGHADY------VKNMItgaaqmDGAILVCAATDGPMAQTK 104
Cdd:COG1217   76 TPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR 111
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-107 2.33e-18

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 79.28  E-value: 2.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQaqiqnyadidgapEERERGITIN--------------------TAHVEYETD 60
Cdd:PTZ00327  36 NIGTIGHVAHGKSTVVKALSGVKTVRFK-------------REKVRNITIKlgyanakiykcpkcprptcyQSYGSSKPD 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338855637  61 S-------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVCAATDG-PMAQTKEHI 107
Cdd:PTZ00327 103 NppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHL 163
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
 1-120 3.51e-18

GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]


Pssm-ID: 273597 [Multi-domain]  Cd Length: 594  Bit Score: 78.88  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    1 NIGTIGHVDHGKTTLtaaITNVLAKKG----QAQIQNYAdIDGAPEERERGITI---NTAhVEYetDSRHYAHVDCPGHA 73
Cdd:TIGR01394   3 NIAIIAHVDHGKTTL---VDALLKQSGtfraNEAVAERV-MDSNDLERERGITIlakNTA-IRY--NGTKINIVDTPGHA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 338855637   74 DY------VKNMItgaaqmDGAILVCAATDGPMAQTKehILLAK--QVGVPALVV 120
Cdd:TIGR01394  76 DFggeverVLGMV------DGVLLLVDASEGPMPQTR--FVLKKalELGLKPIVV 122
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 1-119 3.97e-18

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: 76.51  E-value: 3.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAI---TNVLAKKGQAQIQN-YADIDGApeERERGITINTAHVEYETDSRHYAHVDCPGHADYV 76
Cdd:cd04168    1 NIGILAHVDAGKTTLTESLlytSGAIRELGSVDKGTtRTDSMEL--ERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 338855637  77 KNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALV 119
Cdd:cd04168   79 AEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTII 121
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 1-120 4.03e-18

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 75.71  E-value: 4.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLtaaITNVLAKKGQ-AQIQNYAD--IDGAPEERERGITI---NTAhVEYetDSRHYAHVDCPGHAD 74
Cdd:cd01891    4 NIAIIAHVDHGKTTL---VDALLKQSGTfRENEEVGErvMDSNDLERERGITIlakNTA-ITY--KDTKINIIDTPGHAD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 338855637  75 Y------VKNMItgaaqmDGAILVCAATDGPMAQTKehILLAK--QVGVPALVV 120
Cdd:cd01891   78 FggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLKPIVV 123
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 1-120 4.55e-18

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: 78.55  E-value: 4.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAI---TNVLAKKGQAQiqnyadiDGA------PEERERGITINTA--HVEYEtDSRHYAhVDC 69
Cdd:COG0480   11 NIGIVAHIDAGKTTLTERIlfyTGAIHRIGEVH-------DGNtvmdwmPEEQERGITITSAatTCEWK-GHKINI-IDT 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 338855637  70 PGHADYVKNMITGAAQMDGAILVCAATDGPMAQTkEHIL-LAKQVGVPALVV 120
Cdd:COG0480   82 PGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT-ETVWrQADKYGVPRIVF 132
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 4-121 6.54e-18

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 78.03  E-value: 6.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   4 TIGHVDHGKTTLT---------------AAITNVLAKKG-QAQIQNYAD-IDGAPEERERGITINTAHVEYETDSRHYAH 66
Cdd:PRK05124  32 TCGSVDDGKSTLIgrllhdtkqiyedqlASLHNDSKRHGtQGEKLDLALlVDGLQAEREQGITIDVAYRYFSTEKRKFII 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 338855637  67 VDCPGHADYVKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVA 121
Cdd:PRK05124 112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVA 166
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 1-104 2.12e-17

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 74.19  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTaaiTNVLAKKGQAQIQNYADI---DGAPEERERGITINTAHV--EYETDSRHYAH-------VD 68
Cdd:cd01885    2 NICIIAHVDHGKTTLS---DSLLASAGIISEKLAGKArylDTREDEQERGITIKSSAIslYFEYEEEKMDGndylinlID 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 338855637  69 CPGHADYVKNMITGAAQMDGAILVCAATDGPMAQTK 104
Cdd:cd01885   79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTE 114
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
5-120 3.84e-17

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 75.55  E-value: 3.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   5 IGHVDHGKTTLTAAI---TNVLAKKGQAQIQNyADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMIT 81
Cdd:PRK12740   1 VGHSGAGKTTLTEAIlfyTGAIHRIGEVEDGT-TTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVER 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 338855637  82 GAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVV 120
Cdd:PRK12740  80 ALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIF 118
PRK13351 PRK13351
elongation factor G-like protein;
1-119 5.04e-16

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 72.68  E-value: 5.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAI---TNVLAKKGQAQIQNyADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVK 77
Cdd:PRK13351  10 NIGILAHIDAGKTTLTERIlfyTGKIHKMGEVEDGT-TVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTG 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  78 NMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALV 119
Cdd:PRK13351  89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLI 130
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 1-120 1.19e-15

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: 70.31  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAI---TNVLAKKGQAQIQNyADIDGAPEERERGITINT--AHVEYEtDSRHYAhVDCPGHADY 75
Cdd:cd04170    1 NIALVGHSGSGKTTLAEALlyaTGAIDRLGRVEDGN-TVSDYDPEEKKRKMSIETsvAPLEWN-GHKINL-IDTPGYADF 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 338855637  76 VKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVV 120
Cdd:cd04170   78 VGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIF 122
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
 4-122 4.01e-15

translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]


Pssm-ID: 273102 [Multi-domain]  Cd Length: 587  Bit Score: 70.18  E-value: 4.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    4 TI-GHVDHGKTTLTAAITNVLAKKGQAQiqnyadidgapeererGIT--INTAHVEYEtDSRHYAHVDCPGHADYVKNMI 80
Cdd:TIGR00487  91 TImGHVDHGKTSLLDSIRKTKVAQGEAG----------------GITqhIGAYHVENE-DGKMITFLDTPGHEAFTSMRA 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 338855637   81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPaLVVAL 122
Cdd:TIGR00487 154 RGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAI 194
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 6-122 1.06e-14

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 65.96  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   6 GHVDHGKTTLTAAI--TNVlakkgqaqiqnyadidgapEERE-RGIT--INTAHVEYETDSRHYAHVDCPGHADYvKNMI 80
Cdd:cd01887    7 GHVDHGKTTLLDKIrkTNV-------------------AAGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMR 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 338855637  81 TGAAQM-DGAILVCAATDGPMAQTKEHILLAKQVGVPaLVVAL 122
Cdd:cd01887   67 ARGASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAI 108
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 1-112 1.01e-13

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 63.71  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAI---TNVLAKKG-QAQIQNYADIdgapeERERGITI--NTAHVEYE-TDSRHYAH--VDCPG 71
Cdd:cd01890    2 NFSIIAHIDHGKSTLADRLlelTGTVSEREmKEQVLDSMDL-----ERERGITIkaQAVRLFYKaKDGEEYLLnlIDTPG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 338855637  72 HADYVKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQ 112
Cdd:cd01890   77 HVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALE 117
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 4-121 2.76e-13

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 64.65  E-value: 2.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   4 TI-GHVDHGKTTLTAAI--TNVLAkkGQAqiqnyadidGapeererGIT--INTAHVEyeTDSRHYAHVDCPGHADYVKN 78
Cdd:COG0532    8 TVmGHVDHGKTSLLDAIrkTNVAA--GEA---------G-------GITqhIGAYQVE--TNGGKITFLDTPGHEAFTAM 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 338855637  79 MITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPaLVVA 121
Cdd:COG0532   68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVA 109
PRK10218 PRK10218
translational GTPase TypA;
1-104 3.65e-13

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 64.34  E-value: 3.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLtaaITNVLAKKG----QAQIQNYAdIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYV 76
Cdd:PRK10218   7 NIAIIAHVDHGKTTL---VDKLLQQSGtfdsRAETQERV-MDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFG 82

                         90       100
                 ....*....|....*....|....*...
gi 338855637  77 KNMITGAAQMDGAILVCAATDGPMAQTK 104
Cdd:PRK10218  83 GEVERVMSMVDSVLLVVDAFDGPMPQTR 110
PTZ00416 PTZ00416
elongation factor 2; Provisional
 1-103 4.59e-12

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 61.22  E-value: 4.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAItnvLAKKGQAQIQNYAD---IDGAPEERERGITINTAHVeyetdSRHYAH----------- 66
Cdd:PTZ00416  21 NMSVIAHVDHGKSTLTDSL---VCKAGIISSKNAGDarfTDTRADEQERGITIKSTGI-----SLYYEHdledgddkqpf 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  67 ----VDCPGHADYvKNMITGAAQM-DGAILVCAATDGPMAQT 103
Cdd:PTZ00416  93 linlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT 133
infB CHL00189
translation initiation factor 2; Provisional
 5-122 8.05e-12

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 60.62  E-value: 8.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   5 IGHVDHGKTTLTAAITNVLAKKGQAQiqnyadidgapeererGITINTA----HVEYETDSRHYAHVDCPGHADYVKNMI 80
Cdd:CHL00189 250 LGHVDHGKTTLLDKIRKTQIAQKEAG----------------GITQKIGayevEFEYKDENQKIVFLDTPGHEAFSSMRS 313

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338855637  81 TGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPaLVVAL 122
Cdd:CHL00189 314 RGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAI 354
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 1-103 1.16e-11

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: 59.43  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAI---TNVLAKKGQAQIQNyADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVK 77
Cdd:cd01886    1 NIGIIAHIDAGKTTTTERIlyyTGRIHKIGEVHGGG-ATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTI 79

                         90       100
                 ....*....|....*....|....*.
gi 338855637  78 NMITGAAQMDGAILVCAATDGPMAQT 103
Cdd:cd01886   80 EVERSLRVLDGAVAVFDAVAGVQPQT 105
GTPBP1 COG5258
GTPase [General function prediction only];
1-110 4.90e-11

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 58.41  E-value: 4.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAITNVLAKKGQAQIQNYadIDGAPEERERGIT---------------INT---------AHVe 56
Cdd:COG5258  124 VVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSadlsyavygfdddgpVRMknplrktdrARV- 200

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 338855637  57 YETDSRHYAHVDCPGHADYVKNMITG--AAQMDGAILVCAATDGPMAQTKEH--ILLA 110
Cdd:COG5258  201 VEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA 258
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 1-120 6.18e-11

Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 56.89  E-value: 6.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLT-----AAITNVLAKKGQAQIQNYADIdgAPEERERGITINTAHV-EYETDSRHYAHV----DCP 70
Cdd:cd04167    2 NVCIAGHLHHGKTSLLdmlieQTHKRTPSVKLGWKPLRYTDT--RKDEQERGISIKSNPIsLVLEDSKGKSYLiniiDTP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 338855637  71 GHADYVKNMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVV 120
Cdd:cd04167   80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV 129
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 5-103 2.70e-10

Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 56.18  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   5 IGHVDHGKTTLtaA-----ITNVLAK-KGQAQIQNYADIdgapeERERGITI--NTAHVEYET-DSRHYA--HVDCPGHA 73
Cdd:COG0481   12 IAHIDHGKSTL--AdrlleLTGTLSErEMKEQVLDSMDL-----ERERGITIkaQAVRLNYKAkDGETYQlnLIDTPGHV 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 338855637  74 DY---VKNMItgAAqMDGAILVCAATDGPMAQT 103
Cdd:COG0481   85 DFsyeVSRSL--AA-CEGALLVVDASQGVEAQT 114
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 1-120 3.02e-10

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 56.27  E-value: 3.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAItnvLAKKGQAQIQNYADI---DGAPEERERGITINTA--------------HVEYETDSRH 63
Cdd:PLN00116  21 NMSVIAHVDHGKSTLTDSL---VAAAGIIAQEVAGDVrmtDTRADEAERGITIKSTgislyyemtdeslkDFKGERDGNE 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338855637  64 YA--HVDCPGHADYvKNMITGAAQM-DGAILVCAATDGPMAQTkEHIL---LAKQVgVPALVV 120
Cdd:PLN00116  98 YLinLIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI-RPVLTV 157
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 1-121 2.67e-09

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: 51.99  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    1 NIGTIGHVDHGKTTLtaaiTNVLAKKgqaqiqnyadiDGAPEERERGITINTAHVEYETDSRHY--AHVDCPGHADYVK- 77
Cdd:TIGR00231   3 KIVIVGHPNVGKSTL----LNSLLGN-----------KGSITEYYPGTTRNYVTTVIEEDGKTYkfNLLDTAGQEDYDAi 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 338855637   78 -----NMITGAAQM-DGAILVCAATDGPMAQTKEHILLAKQvGVPALVVA 121
Cdd:TIGR00231  68 rrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVG 116
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 5-104 1.59e-07

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: 47.98  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   5 IGHVDHGKTTLT-------AAIT---NVLAKKGQaqiqNYADIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHAD 74
Cdd:cd04169    8 ISHPDAGKTTLTeklllfgGAIQeagAVKARKSR----KHATSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHED 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 338855637  75 YVKN---MITGAaqmDGAILVCAATDGPMAQTK 104
Cdd:cd04169   84 FSEDtyrTLTAV---DSAVMVIDAAKGVEPQTR 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-121 1.95e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 41.29  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   5 IGHVDHGKTTLtaaiTNVLAKKgqaqiqnyaDIDGAPEERERGITINTAHVEYETDSRHYAHVDCPGHADYVKNMITGAA 84
Cdd:cd00882    3 VGRGGVGKSSL----LNALLGG---------EVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 338855637  85 QM-----DGAILVCAATDGPMA--QTKEHILLAKQVGVPALVVA 121
Cdd:cd00882   70 RLllrgaDLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVG 113
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 1-120 1.06e-04

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 39.97  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   1 NIGTIGHVDHGKTTLTAAIT--------------------------------NVLAKKGQAQIQNYADIDGAPEERErgi 48
Cdd:cd04165    1 RVAVVGNVDAGKSTLLGVLTqgeldngrgkarlnlfrhkhevesgrtssvsnDILGFDSDGEVVNYPDNHLGELDVE--- 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338855637  49 tintahvEYETDSRHYAHVDCPGHADYVKNMITG--AAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVV 120
Cdd:cd04165   78 -------ICEKSSKVVTFIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV 144
PRK04004 PRK04004
translation initiation factor IF-2; Validated
 6-121 1.48e-04

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 39.78  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637   6 GHVDHGKTTLTAAI--TNVLAKKGQAQIQNyadIdGAPE------ERERGITINTAHVEYETDSRHYahVDCPGHADYVK 77
Cdd:PRK04004  13 GHVDHGKTTLLDKIrgTAVAAKEAGGITQH---I-GATEvpidviEKIAGPLKKPLPIKLKIPGLLF--IDTPGHEAFTN 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 338855637  78 NMITGAAQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVA 121
Cdd:PRK04004  87 LRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAA 130
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 1-121 4.97e-03

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 34.13  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338855637    1 NIGTIGHVDHGKTTLTAAITNVLAKkgqaqIQNYAdidgapeererGITINTAHVEYETDSRHYAHVDCPG--HADYVKN 78
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAI-----VSDYP-----------GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 338855637   79 MITGA----AQMDGAILVCAATDGPMAQTKEHILLAKQVGVPALVVA 121
Cdd:pfam01926  65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVL 111
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH