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Conserved domains on  [gi|634743310|ref|NP_001278903|]
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eukaryotic peptide chain release factor subunit 1 isoform 2 [Homo sapiens]

Protein Classification

eukaryotic release factor 1 family protein( domain architecture ID 1903216)

eukaryotic release factor 1 (eRF1) family protein such as eRF1 that directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
aRF1/eRF1 super family cl42864
peptide chain release factor 1, archaeal and eukaryotic forms; Directs the termination of ...
1-384 4.93e-155

peptide chain release factor 1, archaeal and eukaryotic forms; Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. This model identifies both archaeal (aRF1) and eukaryotic (eRF1) of the protein. Also known as translation termination factor 1. [Protein synthesis, Translation factors]


The actual alignment was detected with superfamily member TIGR03676:

Pssm-ID: 456209 [Multi-domain]  Cd Length: 403  Bit Score: 443.27  E-value: 4.93e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310    1 MISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNID 80
Cdd:TIGR03676  22 LISLYIPPDKQISDVVKQLRDEYSQAANIKSKQTRKNVQSAIESIMQRLKLYKKPPENGLVLFCGMVPTGGGKEKMETYV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310   81 FEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARL 160
Cdd:TIGR03676 102 IEPPEPINTYLYRCDSKFYLEPLEEMLEEKDVYGLIVLDRREATIGLLKGKRIEVLKELTSGVPGKHRAGGQSARRFERL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  161 RMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTE 240
Cdd:TIGR03676 182 IEIAAHEFYKRVGEAANEAFLPLKDKKLKGIIIGGPGPTKEEFAEGDYLHYELKKKIIGLVDVSYTGESGLRELVEKAED 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  241 VLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQ--GTEEEKilylTPEQE 318
Cdd:TIGR03676 262 ALKDLEYMKEKKLMERFFKELAKDTGLAAYGEDEVRKALEMGAVDTLLISEDLRKIRVTFKCPncGYEEEK----TVKPE 337
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634743310  319 KDKSHFTDKETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRV 384
Cdd:TIGR03676 338 EGDKSGTCPKCGSQLEIVEEEDIIEELSELAEESGAKVEIISTDTEEGEQLLKAFGGIAAILRYRV 403
 
Name Accession Description Interval E-value
aRF1/eRF1 TIGR03676
peptide chain release factor 1, archaeal and eukaryotic forms; Directs the termination of ...
1-384 4.93e-155

peptide chain release factor 1, archaeal and eukaryotic forms; Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. This model identifies both archaeal (aRF1) and eukaryotic (eRF1) of the protein. Also known as translation termination factor 1. [Protein synthesis, Translation factors]


Pssm-ID: 274719 [Multi-domain]  Cd Length: 403  Bit Score: 443.27  E-value: 4.93e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310    1 MISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNID 80
Cdd:TIGR03676  22 LISLYIPPDKQISDVVKQLRDEYSQAANIKSKQTRKNVQSAIESIMQRLKLYKKPPENGLVLFCGMVPTGGGKEKMETYV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310   81 FEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARL 160
Cdd:TIGR03676 102 IEPPEPINTYLYRCDSKFYLEPLEEMLEEKDVYGLIVLDRREATIGLLKGKRIEVLKELTSGVPGKHRAGGQSARRFERL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  161 RMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTE 240
Cdd:TIGR03676 182 IEIAAHEFYKRVGEAANEAFLPLKDKKLKGIIIGGPGPTKEEFAEGDYLHYELKKKIIGLVDVSYTGESGLRELVEKAED 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  241 VLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQ--GTEEEKilylTPEQE 318
Cdd:TIGR03676 262 ALKDLEYMKEKKLMERFFKELAKDTGLAAYGEDEVRKALEMGAVDTLLISEDLRKIRVTFKCPncGYEEEK----TVKPE 337
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634743310  319 KDKSHFTDKETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRV 384
Cdd:TIGR03676 338 EGDKSGTCPKCGSQLEIVEEEDIIEELSELAEESGAKVEIISTDTEEGEQLLKAFGGIAAILRYRV 403
eRF1 COG1503
Peptide chain release factor 1 (eRF1) [Translation, ribosomal structure and biogenesis]; ...
2-384 1.02e-101

Peptide chain release factor 1 (eRF1) [Translation, ribosomal structure and biogenesis]; Peptide chain release factor 1 (eRF1) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 441112 [Multi-domain]  Cd Length: 384  Bit Score: 306.82  E-value: 1.02e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310   2 ISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTeegkeKKVNIDF 81
Cdd:COG1503   26 LSLYIPPDPPISDVVNQLREELSQAKNIKSKQTRKNVQDALERIIERLKLYKKPPENGLAIFAGAVPT-----DMLTYVI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  82 EPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLR 161
Cdd:COG1503  101 EPPEPVRTFRYRCDSRFYLEPLEDMLEEKERYGLLVIDRREARIGLLRGGRIEELDELESEVPGKHRKGGQSQRRFERLI 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310 162 MEKRHNYVRKVAETAVQLFISGDkvnVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEV 241
Cdd:COG1503  181 EEAAHEFFKEVAEAANELFLRDK---LKGLIIGGPGPTKEEFLEGDYLHHRLRKKVLGLFDVSYTGEAGLRELVEKAEDL 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310 242 LSNVKFIQEKKLIGRYFDEISQDtGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQGTEEekilyltpEQEKDK 321
Cdd:COG1503  258 LKEQEREEEKELVEEFFEELAKG-GLAVYGLEEVLEALEMGAVDTLLISEDLRKPGVRCPCCGCLG--------EEECPC 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 634743310 322 SHFTDKETGQEhELIESMPLLewfANNYkkfGATLEIVTDKSQEGSQFVKGFGGIGGILRYRV 384
Cdd:COG1503  329 CGCGGEVEEEE-DLVDELVEL---AEQQ---GAEVEVISTDFEEGEQLLKAFGGIAAILRYRI 384
eRF1_2 pfam03464
eRF1 domain 2; The release factor eRF1 terminates protein biosynthesis by recognising stop ...
112-244 1.33e-58

eRF1 domain 2; The release factor eRF1 terminates protein biosynthesis by recognising stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known. The overall shape and dimensions of eRF1 resemble a tRNA molecule with domains 1, 2, and 3 of eRF1 corresponding to the anticodon loop, aminoacyl acceptor stem, and T stem of a tRNA molecule, respectively. The position of the essential GGQ motif at an exposed tip of domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase centre. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site. This family also includes other proteins for which the precise molecular function is unknown. Many of them are from Archaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification.


Pssm-ID: 397502  Cd Length: 133  Bit Score: 187.10  E-value: 1.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  112 KFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGL 191
Cdd:pfam03464   1 DYGAIVMDEGEATIGLLTGSRTEVLAKIEVSIPGKHGRGGQSARRFARLRDEARHNFYKKVGEAANQAFIHVDKDVVKGI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743310  192 VLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSN 244
Cdd:pfam03464  81 ILAGPGFTKEEFYDGDYLDAELKDKVIKLVDVSYGGEHGLNEALEKAADVLSD 133
 
Name Accession Description Interval E-value
aRF1/eRF1 TIGR03676
peptide chain release factor 1, archaeal and eukaryotic forms; Directs the termination of ...
1-384 4.93e-155

peptide chain release factor 1, archaeal and eukaryotic forms; Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. This model identifies both archaeal (aRF1) and eukaryotic (eRF1) of the protein. Also known as translation termination factor 1. [Protein synthesis, Translation factors]


Pssm-ID: 274719 [Multi-domain]  Cd Length: 403  Bit Score: 443.27  E-value: 4.93e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310    1 MISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNID 80
Cdd:TIGR03676  22 LISLYIPPDKQISDVVKQLRDEYSQAANIKSKQTRKNVQSAIESIMQRLKLYKKPPENGLVLFCGMVPTGGGKEKMETYV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310   81 FEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARL 160
Cdd:TIGR03676 102 IEPPEPINTYLYRCDSKFYLEPLEEMLEEKDVYGLIVLDRREATIGLLKGKRIEVLKELTSGVPGKHRAGGQSARRFERL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  161 RMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTE 240
Cdd:TIGR03676 182 IEIAAHEFYKRVGEAANEAFLPLKDKKLKGIIIGGPGPTKEEFAEGDYLHYELKKKIIGLVDVSYTGESGLRELVEKAED 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  241 VLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQ--GTEEEKilylTPEQE 318
Cdd:TIGR03676 262 ALKDLEYMKEKKLMERFFKELAKDTGLAAYGEDEVRKALEMGAVDTLLISEDLRKIRVTFKCPncGYEEEK----TVKPE 337
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634743310  319 KDKSHFTDKETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRV 384
Cdd:TIGR03676 338 EGDKSGTCPKCGSQLEIVEEEDIIEELSELAEESGAKVEIISTDTEEGEQLLKAFGGIAAILRYRV 403
eRF1 COG1503
Peptide chain release factor 1 (eRF1) [Translation, ribosomal structure and biogenesis]; ...
2-384 1.02e-101

Peptide chain release factor 1 (eRF1) [Translation, ribosomal structure and biogenesis]; Peptide chain release factor 1 (eRF1) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 441112 [Multi-domain]  Cd Length: 384  Bit Score: 306.82  E-value: 1.02e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310   2 ISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTeegkeKKVNIDF 81
Cdd:COG1503   26 LSLYIPPDPPISDVVNQLREELSQAKNIKSKQTRKNVQDALERIIERLKLYKKPPENGLAIFAGAVPT-----DMLTYVI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  82 EPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLR 161
Cdd:COG1503  101 EPPEPVRTFRYRCDSRFYLEPLEDMLEEKERYGLLVIDRREARIGLLRGGRIEELDELESEVPGKHRKGGQSQRRFERLI 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310 162 MEKRHNYVRKVAETAVQLFISGDkvnVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEV 241
Cdd:COG1503  181 EEAAHEFFKEVAEAANELFLRDK---LKGLIIGGPGPTKEEFLEGDYLHHRLRKKVLGLFDVSYTGEAGLRELVEKAEDL 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310 242 LSNVKFIQEKKLIGRYFDEISQDtGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQGTEEekilyltpEQEKDK 321
Cdd:COG1503  258 LKEQEREEEKELVEEFFEELAKG-GLAVYGLEEVLEALEMGAVDTLLISEDLRKPGVRCPCCGCLG--------EEECPC 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 634743310 322 SHFTDKETGQEhELIESMPLLewfANNYkkfGATLEIVTDKSQEGSQFVKGFGGIGGILRYRV 384
Cdd:COG1503  329 CGCGGEVEEEE-DLVDELVEL---AEQQ---GAEVEVISTDFEEGEQLLKAFGGIAAILRYRI 384
eRF1_2 pfam03464
eRF1 domain 2; The release factor eRF1 terminates protein biosynthesis by recognising stop ...
112-244 1.33e-58

eRF1 domain 2; The release factor eRF1 terminates protein biosynthesis by recognising stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known. The overall shape and dimensions of eRF1 resemble a tRNA molecule with domains 1, 2, and 3 of eRF1 corresponding to the anticodon loop, aminoacyl acceptor stem, and T stem of a tRNA molecule, respectively. The position of the essential GGQ motif at an exposed tip of domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase centre. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site. This family also includes other proteins for which the precise molecular function is unknown. Many of them are from Archaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification.


Pssm-ID: 397502  Cd Length: 133  Bit Score: 187.10  E-value: 1.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  112 KFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGL 191
Cdd:pfam03464   1 DYGAIVMDEGEATIGLLTGSRTEVLAKIEVSIPGKHGRGGQSARRFARLRDEARHNFYKKVGEAANQAFIHVDKDVVKGI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743310  192 VLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSN 244
Cdd:pfam03464  81 ILAGPGFTKEEFYDGDYLDAELKDKVIKLVDVSYGGEHGLNEALEKAADVLSD 133
eRF1_3 pfam03465
eRF1 domain 3; The release factor eRF1 terminates protein biosynthesis by recognising stop ...
247-384 8.64e-35

eRF1 domain 3; The release factor eRF1 terminates protein biosynthesis by recognising stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known. The overall shape and dimensions of eRF1 resemble a tRNA molecule with domains 1, 2, and 3 of eRF1 corresponding to the anticodon loop, aminoacyl acceptor stem, and T stem of a tRNA molecule, respectively. The position of the essential GGQ motif at an exposed tip of domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase centre. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site. This family also includes other proteins for which the precise molecular function is unknown. Many of them are from Archaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification.


Pssm-ID: 397503 [Multi-domain]  Cd Length: 100  Bit Score: 124.20  E-value: 8.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310  247 FIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVlhcqgteeekilyltpeQEKDKshftd 326
Cdd:pfam03465   1 IAQEKKLLEEFLEELAKDTGLAVYGVEEVLKALEMGAVETLLISDELLRSRDV-----------------ATRNK----- 58
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 634743310  327 ketgqeheliesmplLEWFANNYKKFGATLEIVTDKSQEGSQFvKGFGGIGGILRYRV 384
Cdd:pfam03465  59 ---------------IEWLVENAEESGGKVEIVSDESEEGEQL-KGFGGIAAILRYKV 100
eRF1_1 pfam03463
eRF1 domain 1; The release factor eRF1 terminates protein biosynthesis by recognising stop ...
1-103 2.40e-27

eRF1 domain 1; The release factor eRF1 terminates protein biosynthesis by recognising stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known. The overall shape and dimensions of eRF1 resemble a tRNA molecule with domains 1, 2, and 3 of eRF1 corresponding to the anticodon loop, aminoacyl acceptor stem, and T stem of a tRNA molecule, respectively. The position of the essential GGQ motif at an exposed tip of domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase centre. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site. This family also includes other proteins for which the precise molecular function is unknown. Many of them are from Archaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification.


Pssm-ID: 460930 [Multi-domain]  Cd Length: 122  Bit Score: 104.88  E-value: 2.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310    1 MISLIIPPKDQISRVAKMLADEFGTASNIKSRVNR---LSVLGAITSVQQRLKLYNKvppNGLVVYCGTIVTEEG---KE 74
Cdd:pfam03463  15 LITLYPEPDDDLWHLYNLIRPGDGVAANTKRKVTRessERVLLALTIIVERLKFDKK---NGLLRVKGTIVEENEhvkLG 91
                          90       100
                  ....*....|....*....|....*....
gi 634743310   75 KKVNIDFEPFKPINTSLYlCDNKFHTEAL 103
Cdd:pfam03463  92 KYHTLDIEPPRPITIIKY-RWDKFALERL 119
PelA COG1537
Stalled ribosome rescue protein Dom34, pelota family [Translation, ribosomal structure and ...
163-385 3.52e-12

Stalled ribosome rescue protein Dom34, pelota family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441146 [Multi-domain]  Cd Length: 351  Bit Score: 67.14  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310 163 EKRHNYVRKVAETAVQLFISGDKVnvaglVLAGSADFKtelsqsDMFDQRLQSKV------LKLVDISYGGENGFNQAI- 235
Cdd:COG1537  174 RSREEFFEEIAKALKNVASDVDAI-----IVAGPGFTK------EDFAKYLKEKYpelakkIVVEDTSSGGERGVYEVLr 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310 236 -ELSTEVLSNVKFIQEKKLIGRYFDEISQDtGKYCFGVEDTLKALEMGAVEILIVYENLdimryvLHCQGTEE-EKILyl 313
Cdd:COG1537  243 rGAVDEILEESRIARESELVEELLERIAKD-GKVAYGLDEVKEAAEYGAVETLLVLDEL------LRSEDREDvDELL-- 313
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 634743310 314 tpeqekdkshftdketgqehELIESMpllewfannykkfGATLEIVTDKSQEGSQfVKGFGGIGGILRYRVD 385
Cdd:COG1537  314 --------------------NSVESM-------------GGKVVVVSSEFEPGKQ-LKALGGIAALLRYKIQ 351
baeRF_family10 pfam18854
Bacterial archaeo-eukaryotic release factor family 10; Bacterial family of the ...
99-217 4.01e-06

Bacterial archaeo-eukaryotic release factor family 10; Bacterial family of the archaeo-eukaryotic release factor superfamily. Likely to play roles in biological conflicts or regulation under stress conditions at the ribosome.


Pssm-ID: 436784  Cd Length: 143  Bit Score: 46.13  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743310   99 HTEALTALLSDDSKFGFIVIDGSGA-LFGTLQGNTREVLHkFTVDLPKKHGRGGQSAL----RFARLRMEKRHNYVRKVA 173
Cdd:pfam18854   2 YIAPLLEALDEYRRYGVVLVDRGGArLFEFFLGELREVEV-GQREVVGRTKTGGWPGLtsqdRFQRRRDNQARRFYKEAA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 634743310  174 ETAVQLFISGDkvnVAGLVLAGSADFKTELsqSDMFDQRLQSKV 217
Cdd:pfam18854  81 EVAARLLEERG---VERLVLGGDPAVTAAF--LDRLPKALRAKV 119
acVLRF1 pfam18859
Actinobacteria/chloroflexi VLRF1 release factor; Archaeo-eukaryotic release factor domain ...
126-195 6.37e-04

Actinobacteria/chloroflexi VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging to the VLRF1 clade, observed primarily in the actinbacteria and chloroflexi bacterial lineages. Contains a conserved glutamine residue in the release factor catalytic loop, suggesting it functions as an active peptidyl-tRNA hydrolase at the ribosome.


Pssm-ID: 436788 [Multi-domain]  Cd Length: 130  Bit Score: 39.46  E-value: 6.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 634743310  126 GTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEK-RHNyVRKVAETAVQLFISGdkvnVAGLVLAG 195
Cdd:pfam18859  16 GVYEGGELVASKVGRRDVQGRTAAGGWSQQRFARRRENQaDAA-LEAAADAAARVLLPR----AADVVLGG 81
 
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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