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Conserved domains on  [gi|307354991|gb|ACB87193|]
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elongation factor 1 alpha, partial [Isoperla sp. SS-2008]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-90 4.02e-41

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PTZ00141:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 446  Bit Score: 139.50  E-value: 4.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSEKMNWFKgwsverkegkadGKCLIEALDSILPPSRP 80
Cdd:PTZ00141 162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKRP 229

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:PTZ00141 230 VDKPLRLPLQ 239
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-90 4.02e-41

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 139.50  E-value: 4.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSEKMNWFKgwsverkegkadGKCLIEALDSILPPSRP 80
Cdd:PTZ00141 162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKRP 229

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:PTZ00141 230 VDKPLRLPLQ 239
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-90 4.83e-32

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: 115.03  E-value: 4.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSEKMNWFKgwsverkegkadGKCLIEALDSILPPSRP 80
Cdd:COG5256  153 YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEKP 220

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:COG5256  221 VDKPLRIPIQ 230
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-77 6.55e-32

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: 110.27  E-value: 6.55e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSEKMNWFKGWsverkegkadgkCLIEALDSILPP 77
Cdd:cd01883  154 WSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-90 4.02e-41

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 139.50  E-value: 4.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSEKMNWFKgwsverkegkadGKCLIEALDSILPPSRP 80
Cdd:PTZ00141 162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKRP 229

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:PTZ00141 230 VDKPLRLPLQ 239
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-90 7.70e-33

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 117.33  E-value: 7.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSEKMNWFKgwsverkegkadGKCLIEALDSILPPSRP 80
Cdd:PRK12317 154 YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GPTLLEALDNLKPPEKP 221

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:PRK12317 222 TDKPLRIPIQ 231
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-90 4.83e-32

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: 115.03  E-value: 4.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSEKMNWFKgwsverkegkadGKCLIEALDSILPPSRP 80
Cdd:COG5256  153 YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEKP 220

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:COG5256  221 VDKPLRIPIQ 230
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-77 6.55e-32

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: 110.27  E-value: 6.55e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSEKMNWFKGWsverkegkadgkCLIEALDSILPP 77
Cdd:cd01883  154 WSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-90 2.23e-28

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 105.56  E-value: 2.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAAVAFVPISGWHGDNMLEHSEKMNWFKgwsverkegkadGKCLIEALDSILPPSRP 80
Cdd:PLN00043 162 YSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYK------------GPTLLEALDQINEPKRP 229

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:PLN00043 230 SDKPLRLPLQ 239
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-90 7.54e-22

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: 87.45  E-value: 7.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPaaVAFVPISGWHGDNMLEHSEKMNWFkgwsverkegkaDGKCLIEALDSILPPSRP 80
Cdd:COG2895  163 YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDR 228

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:COG2895  229 NDAPFRFPVQ 238
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-78 2.22e-15

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: 67.59  E-value: 2.22e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPaaVAFVPISGWHGDNMLEHSEKMNWFKgwsverkegkadGKCLIEALDSILPPS 78
Cdd:cd04166  146 YDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETVEIAS 209
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-90 3.47e-14

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 65.72  E-value: 3.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYnpAAVAFVPISGWHGDNMLEHSEKMNWFKGWSverkegkadgkcLIEALDSILPPSRP 80
Cdd:PRK05506 172 YDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWYEGPS------------LLEHLETVEIASDR 237

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:PRK05506 238 NLKDFRFPVQ 247
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-90 9.25e-14

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 64.55  E-value: 9.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307354991   1 YSESRFEEIKKEVSNYIKKIGYNPAaVAFVPISGWHGDNMLEHSEKMNWFKGWSverkegkadgkcLIEALDSILPPSRP 80
Cdd:PRK05124 175 YSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPT------------LLEVLETVDIQRVV 241

                         90
                 ....*....|
gi 307354991  81 TEKPLRLPLQ 90
Cdd:PRK05124 242 DAQPFRFPVQ 251
 
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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