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Conserved domains on  [gi|17553634|ref|NP_498737|]
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putative elongation factor 1-beta/1-delta 1 [Caenorhabditis elegans]

Protein Classification

elongation factor 1-beta( domain architecture ID 10918921)

elongation factor 1-beta stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
 124-213 3.71e-39

Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.


:

Pssm-ID: 238181  Cd Length: 88  Bit Score: 129.64  E-value: 3.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553634 124 IAKSSVILDVKPWDDETDLGEMEKLVRSIEMDGLVWGGAKLIPIGYGIKKLQIITVIEDLKVSVDDLIEKITGdfEDHVQ 203
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE--EDGVQ 78

                        90
                ....*....|
gi 17553634 204 SVDIVAFNKI 213
Cdd:cd00292  79 SVDVEAFNKL 88
GST_C_family super family cl02776
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 1-62 1.19e-16

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.


The actual alignment was detected with superfamily member cd10308:

Pssm-ID: 470672  Cd Length: 82  Bit Score: 71.69  E-value: 1.19e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17553634   1 MVADVKSPAGLAAFNTTLAEQAFATGFVLSGEDAQLFAALGSAPNASTYPNVARWYANVASY 62
Cdd:cd10308  21 SFADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATKFPHLARWYRHIASF 82
EF-1_beta_acid pfam10587
Eukaryotic elongation factor 1 beta central acidic region;
90-110 4.95e-06

Eukaryotic elongation factor 1 beta central acidic region;


:

Pssm-ID: 463158  Cd Length: 28  Bit Score: 41.74  E-value: 4.95e-06
                          10        20
                  ....*....|....*....|.
gi 17553634    90 LFGSDDEEEDAEKAKIVEERL 110
Cdd:pfam10587   1 LFGSDDEEEDEEAERLREERL 21
 
Name Accession Description Interval E-value
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
 124-213 3.71e-39

Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.


Pssm-ID: 238181  Cd Length: 88  Bit Score: 129.64  E-value: 3.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553634 124 IAKSSVILDVKPWDDETDLGEMEKLVRSIEMDGLVWGGAKLIPIGYGIKKLQIITVIEDLKVSVDDLIEKITGdfEDHVQ 203
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE--EDGVQ 78

                        90
                ....*....|
gi 17553634 204 SVDIVAFNKI 213
Cdd:cd00292  79 SVDVEAFNKL 88
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
 129-213 4.29e-39

EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.


Pssm-ID: 459919  Cd Length: 83  Bit Score: 129.47  E-value: 4.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553634   129 VILDVKPWDDETDLGEMEKLVRSIEMDGLVWGGAKLIPIGYGIKKLQIITVIEDLKVSVDDLIEKITGDfeDHVQSVDIV 208
Cdd:pfam00736   1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEI--DGVQSVDIE 78


                  ....*
gi 17553634   209 AFNKI 213
Cdd:pfam00736  79 AFNKL 83
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
 126-213 7.02e-30

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).


Pssm-ID: 214886  Cd Length: 88  Bit Score: 106.06  E-value: 7.02e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553634    126 KSSVILDVKPWDDETDLGEMEKLVRSI-EMDGLVWG-GAKLIPIGYGIKKLQIITVIEDLKVSVDDLIEKITGdFEDhVQ 203
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGaGIELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEE-VEG-VQ 78

                           90
                   ....*....|
gi 17553634    204 SVDIVAFNKI 213
Cdd:smart00888  79 SVEVEAVSRL 88
GST_C_eEF1b_like cd10308
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ...
 1-62 1.19e-16

Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.


Pssm-ID: 198341  Cd Length: 82  Bit Score: 71.69  E-value: 1.19e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17553634   1 MVADVKSPAGLAAFNTTLAEQAFATGFVLSGEDAQLFAALGSAPNASTYPNVARWYANVASY 62
Cdd:cd10308  21 SFADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATKFPHLARWYRHIASF 82
EF-1_beta_acid pfam10587
Eukaryotic elongation factor 1 beta central acidic region;
90-110 4.95e-06

Eukaryotic elongation factor 1 beta central acidic region;


Pssm-ID: 463158  Cd Length: 28  Bit Score: 41.74  E-value: 4.95e-06
                          10        20
                  ....*....|....*....|.
gi 17553634    90 LFGSDDEEEDAEKAKIVEERL 110
Cdd:pfam10587   1 LFGSDDEEEDEEAERLREERL 21
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-61 9.11e-03

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 36.03  E-value: 9.11e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17553634   9 AGLAAFNTTLAEQAFATGFVLSGEDAQLFAALGSAPNA----STYPNVARWYANVAS 61
Cdd:COG0625 133 RLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLgldlADYPNLAAWLARLAA 189
 
Name Accession Description Interval E-value
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
 124-213 3.71e-39

Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.


Pssm-ID: 238181  Cd Length: 88  Bit Score: 129.64  E-value: 3.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553634 124 IAKSSVILDVKPWDDETDLGEMEKLVRSIEMDGLVWGGAKLIPIGYGIKKLQIITVIEDLKVSVDDLIEKITGdfEDHVQ 203
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE--EDGVQ 78

                        90
                ....*....|
gi 17553634 204 SVDIVAFNKI 213
Cdd:cd00292  79 SVDVEAFNKL 88
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
 129-213 4.29e-39

EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.


Pssm-ID: 459919  Cd Length: 83  Bit Score: 129.47  E-value: 4.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553634   129 VILDVKPWDDETDLGEMEKLVRSIEMDGLVWGGAKLIPIGYGIKKLQIITVIEDLKVSVDDLIEKITGDfeDHVQSVDIV 208
Cdd:pfam00736   1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEI--DGVQSVDIE 78


                  ....*
gi 17553634   209 AFNKI 213
Cdd:pfam00736  79 AFNKL 83
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
 126-213 7.02e-30

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).


Pssm-ID: 214886  Cd Length: 88  Bit Score: 106.06  E-value: 7.02e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553634    126 KSSVILDVKPWDDETDLGEMEKLVRSI-EMDGLVWG-GAKLIPIGYGIKKLQIITVIEDLKVSVDDLIEKITGdFEDhVQ 203
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGaGIELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEE-VEG-VQ 78

                           90
                   ....*....|
gi 17553634    204 SVDIVAFNKI 213
Cdd:smart00888  79 SVEVEAVSRL 88
GST_C_eEF1b_like cd10308
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ...
 1-62 1.19e-16

Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.


Pssm-ID: 198341  Cd Length: 82  Bit Score: 71.69  E-value: 1.19e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17553634   1 MVADVKSPAGLAAFNTTLAEQAFATGFVLSGEDAQLFAALGSAPNASTYPNVARWYANVASY 62
Cdd:cd10308  21 SFADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATKFPHLARWYRHIASF 82
EF-1_beta_acid pfam10587
Eukaryotic elongation factor 1 beta central acidic region;
90-110 4.95e-06

Eukaryotic elongation factor 1 beta central acidic region;


Pssm-ID: 463158  Cd Length: 28  Bit Score: 41.74  E-value: 4.95e-06
                          10        20
                  ....*....|....*....|.
gi 17553634    90 LFGSDDEEEDAEKAKIVEERL 110
Cdd:pfam10587   1 LFGSDDEEEDEEAERLREERL 21
GST_C_CysRS_N cd10310
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase ...
 9-61 1.36e-04

Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Cysteinyl-tRNA synthetase (CysRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of CysRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of CysRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. CysRSs from prokaryotes and lower eukaryotes do not appear to contain this GST_C-like domain.


Pssm-ID: 198343  Cd Length: 73  Bit Score: 39.11  E-value: 1.36e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17553634   9 AGLAAFNTTLAEQAFATGFVLSGEDAQLFAALgSAPNASTYPNVARWYANVAS 61
Cdd:cd10310  21 ARAEALNEYLSTRSYLQGFGPSQADVEVFRLL-SRPPADRLVHVLRWYRHIEA 72
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
 6-62 2.76e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198322 [Multi-domain]  Cd Length: 82  Bit Score: 35.75  E-value: 2.76e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17553634   6 KSPAGLAAFNTTLAEQAFATGFVLSGEDAQLFAALGSAPNAS------TYPNVARWYANVASY 62
Cdd:cd10289  20 ELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLsdkekkKFPHVTRWFNHIQNL 82
Csf3_U cd09707
CRISPR/Cas system-associated RAMP superfamily protein Csf3; CRISPR (Clustered Regularly ...
 132-170 6.44e-03

CRISPR/Cas system-associated RAMP superfamily protein Csf3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein


Pssm-ID: 187838  Cd Length: 214  Bit Score: 36.48  E-value: 6.44e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 17553634 132 DVKPWDDETDLGEMEKLVRSIEMDGLVWGGAKLIPIGYG 170
Cdd:cd09707  38 SADPWGDARDLSEDLPLGKEEEGDSWVWKASRLEVLAFL 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-61 9.11e-03

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 36.03  E-value: 9.11e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17553634   9 AGLAAFNTTLAEQAFATGFVLSGEDAQLFAALGSAPNA----STYPNVARWYANVAS 61
Cdd:COG0625 133 RLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLgldlADYPNLAAWLARLAA 189
 
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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