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Conserved domains on  [gi|591324617|ref|XP_007088349|]
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DNA polymerase subunit gamma-2, mitochondrial isoform X5 [Panthera tigris]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
class_II_aaRS-like_core super family cl00268
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
69-318 9.57e-63

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


The actual alignment was detected with superfamily member cd00774:

Pssm-ID: 444800 [Multi-domain]  Cd Length: 254  Bit Score: 202.44  E-value: 9.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  69 LLEICQRRHFFSGSRRQLSrhsLLSGCHpGFGPLGIELRKNLAAEWWSSVVVLREQVFPVDALHHEPGPLlpgdstFRLV 148
Cdd:cd00774    1 LVELAKRRGFVFPSSEIYG---GVAGFY-DYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELM------FKTS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 149 SAATlrellqdkelskeqlvafldNLLKTSGKLRENLLHGALEHYVNCLDLVNRRLPYGLAQIGVCFHPVSDTKQtpdGV 228
Cdd:cd00774   71 IGPV--------------------ESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRN---GL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 229 KRIGEKTEASLVWFTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFSSSDCQDEEG----RKGNKLYYNFPWGKEPIETLW 304
Cdd:cd00774  128 FRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELahyaNETLDYFYAFPHGFLELEGIA 207
                        250
                 ....*....|....
gi 591324617 305 NLGDHELLNMCPGN 318
Cdd:cd00774  208 NRGDRFLQHHPNES 221
HGTP_anticodon super family cl00266
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
324-407 2.91e-48

HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).


The actual alignment was detected with superfamily member cd02426:

Pssm-ID: 469699 [Multi-domain]  Cd Length: 128  Bit Score: 160.66  E-value: 2.91e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 324 VCQGLFSELLENGISVWPGYLETVHSSLEQLYSKYDEMSILFTVLITEATLENGLIHLRSRDTTMKEMMHISKVKDFLIK 403
Cdd:cd02426   45 LCQGLKNELREAGLSVWPGYLETQHSSLEQLLDKYDEMGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLLR 124

                 ....
gi 591324617 404 YISS 407
Cdd:cd02426  125 YIAA 128
 
Name Accession Description Interval E-value
GlyRS-like_core cd00774
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ...
69-318 9.57e-63

Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a homodimer in eukaryotes, archaea and some bacteria and as a heterotetramer in the remainder of prokaryotes. It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP binding and hydrolysis. This alignment contains only sequences from the GlyRS form which homodimerizes. The heterotetramer glyQ is in a different family of class II aaRS. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the N-terminus of the accessory subunit of mitochondrial polymerase gamma (Pol gamma b). Pol gamma b stimulates processive DNA synthesis and is functional as a homodimer, which can associate with the catalytic subunit Pol gamma alpha to form a heterotrimer. Despite significant both structural and sequence similarity with GlyRS, Pol gamma b lacks conservation of several class II functional residues.


Pssm-ID: 238397 [Multi-domain]  Cd Length: 254  Bit Score: 202.44  E-value: 9.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  69 LLEICQRRHFFSGSRRQLSrhsLLSGCHpGFGPLGIELRKNLAAEWWSSVVVLREQVFPVDALHHEPGPLlpgdstFRLV 148
Cdd:cd00774    1 LVELAKRRGFVFPSSEIYG---GVAGFY-DYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELM------FKTS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 149 SAATlrellqdkelskeqlvafldNLLKTSGKLRENLLHGALEHYVNCLDLVNRRLPYGLAQIGVCFHPVSDTKQtpdGV 228
Cdd:cd00774   71 IGPV--------------------ESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRN---GL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 229 KRIGEKTEASLVWFTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFSSSDCQDEEG----RKGNKLYYNFPWGKEPIETLW 304
Cdd:cd00774  128 FRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELahyaNETLDYFYAFPHGFLELEGIA 207
                        250
                 ....*....|....
gi 591324617 305 NLGDHELLNMCPGN 318
Cdd:cd00774  208 NRGDRFLQHHPNES 221
Pol_gamma_b_Cterm cd02426
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ...
324-407 2.91e-48

C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for processivity. Polymerase gamma replicates and repairs mitochondrial DNA. The c-terminal domain of its B subunit is strikingly similar to the anticodon-binding domain of glycyl tRNA synthetase.


Pssm-ID: 239106 [Multi-domain]  Cd Length: 128  Bit Score: 160.66  E-value: 2.91e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 324 VCQGLFSELLENGISVWPGYLETVHSSLEQLYSKYDEMSILFTVLITEATLENGLIHLRSRDTTMKEMMHISKVKDFLIK 403
Cdd:cd02426   45 LCQGLKNELREAGLSVWPGYLETQHSSLEQLLDKYDEMGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLLR 124

                 ....
gi 591324617 404 YISS 407
Cdd:cd02426  125 YIAA 128
PRK14894 PRK14894
glycyl-tRNA synthetase; Provisional
67-311 2.44e-12

glycyl-tRNA synthetase; Provisional


Pssm-ID: 237851 [Multi-domain]  Cd Length: 539  Bit Score: 68.49  E-value: 2.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  67 EELLEICQRRHFFSGSRRQlsrHSLLSGCHpGFGPLGIELRKNLAAEWWSSVVVLREQVFPVDAL------------HHE 134
Cdd:PRK14894   7 DQIVALAKRRGFIFPSSEI---YGGLQGVY-DYGPLGVELKNNIIADWWRTNVYERDDMEGLDAAilmnrlvwkysgHEE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 135 P--GPLLP---------GDSTFRLVSAATLRELLQDKELS---KEQLVAFLDNllKTSGKLRENLLHGALEHYVNCLDLV 200
Cdd:PRK14894  83 TfnDPLVDcrdckmrwrADHIQGVCPNCGSRDLTEPRPFNmmfRTQIGPVADS--DSFAYLRPETAQGIFVNFANVLATS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 201 NRRLPYGLAQIGVCFHpvsdTKQTP-DGVKRIGEKTEASLVWFTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFSSSDCQ 279
Cdd:PRK14894 161 ARKLPFGIAQVGKAFR----NEINPrNFLFRVREFEQMEIEYFVMPGTDEEWHQRWLEARLAWWEQIGIPRSRITIYDVP 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 591324617 280 DEE----GRKGNKLYYNFP-WGKEPIETLWNLGDHEL 311
Cdd:PRK14894 237 PDElahySKRTFDLMYDYPnIGVQEIEGIANRTDYDL 273
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
317-403 1.70e-11

Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.


Pssm-ID: 460819 [Multi-domain]  Cd Length: 94  Bit Score: 60.29  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  317 GNESQLHVCQGLFSELLENGISVwpgYLETVHSSLEQLYSKYDEMSILFTVLITEATLENGLIHLRSRDTTMKEMMHISK 396
Cdd:pfam03129  10 KAEELEEYAQKLAEELRAAGIRV---ELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQETVSLDE 86

                  ....*..
gi 591324617  397 VKDFLIK 403
Cdd:pfam03129  87 LVEKLKE 93
GRS1 COG0423
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ...
67-301 4.78e-07

Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; Glycyl-tRNA synthetase, class II is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440192 [Multi-domain]  Cd Length: 461  Bit Score: 51.65  E-value: 4.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  67 EELLEICQRRHFFSGSrrqlsrhsllSGCHPG------FGPLGIELRKNLAAEWWSSVVVLREQVFPVDA---LH----- 132
Cdd:COG0423    8 EKIVSLAKRRGFVFPS----------SEIYGGlagfydYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSpiiMPpkvwe 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 133 ---HEPG---PLLpgD-----STFR---LVSAATLRELLQDkeLSKEQLVAFL-DNLLK--TSGKL-----RE-NLL--- 186
Cdd:COG0423   78 asgHVDGftdPLV--DckeckKRYRadhLIEEYLAIEDAEG--LSLEELEELIkENNIKcpNCGGKeltevRQfNLMfkt 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 187 -HGALE-----HY----------VNCLDLVN---RRLPYGLAQIGvcfhpvsdtKQ-----TP-DGVKRIGEKTEASLVW 241
Cdd:COG0423  154 nIGPVEdesstGYlrpetaqgifVNFKNVQRtarKKLPFGIAQIG---------KSfrneiTPrNFIFRTREFEQMELEF 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 591324617 242 FTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFS------------SSDCQDEEgrkgnklyYNFPWGKEPIE 301
Cdd:COG0423  225 FVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRfrdhlpeelahyAKATWDIE--------YEFPFGWGELE 288
 
Name Accession Description Interval E-value
GlyRS-like_core cd00774
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ...
69-318 9.57e-63

Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a homodimer in eukaryotes, archaea and some bacteria and as a heterotetramer in the remainder of prokaryotes. It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP binding and hydrolysis. This alignment contains only sequences from the GlyRS form which homodimerizes. The heterotetramer glyQ is in a different family of class II aaRS. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the N-terminus of the accessory subunit of mitochondrial polymerase gamma (Pol gamma b). Pol gamma b stimulates processive DNA synthesis and is functional as a homodimer, which can associate with the catalytic subunit Pol gamma alpha to form a heterotrimer. Despite significant both structural and sequence similarity with GlyRS, Pol gamma b lacks conservation of several class II functional residues.


Pssm-ID: 238397 [Multi-domain]  Cd Length: 254  Bit Score: 202.44  E-value: 9.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  69 LLEICQRRHFFSGSRRQLSrhsLLSGCHpGFGPLGIELRKNLAAEWWSSVVVLREQVFPVDALHHEPGPLlpgdstFRLV 148
Cdd:cd00774    1 LVELAKRRGFVFPSSEIYG---GVAGFY-DYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELM------FKTS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 149 SAATlrellqdkelskeqlvafldNLLKTSGKLRENLLHGALEHYVNCLDLVNRRLPYGLAQIGVCFHPVSDTKQtpdGV 228
Cdd:cd00774   71 IGPV--------------------ESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRN---GL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 229 KRIGEKTEASLVWFTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFSSSDCQDEEG----RKGNKLYYNFPWGKEPIETLW 304
Cdd:cd00774  128 FRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELahyaNETLDYFYAFPHGFLELEGIA 207
                        250
                 ....*....|....
gi 591324617 305 NLGDHELLNMCPGN 318
Cdd:cd00774  208 NRGDRFLQHHPNES 221
Pol_gamma_b_Cterm cd02426
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ...
324-407 2.91e-48

C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for processivity. Polymerase gamma replicates and repairs mitochondrial DNA. The c-terminal domain of its B subunit is strikingly similar to the anticodon-binding domain of glycyl tRNA synthetase.


Pssm-ID: 239106 [Multi-domain]  Cd Length: 128  Bit Score: 160.66  E-value: 2.91e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 324 VCQGLFSELLENGISVWPGYLETVHSSLEQLYSKYDEMSILFTVLITEATLENGLIHLRSRDTTMKEMMHISKVKDFLIK 403
Cdd:cd02426   45 LCQGLKNELREAGLSVWPGYLETQHSSLEQLLDKYDEMGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLLR 124

                 ....
gi 591324617 404 YISS 407
Cdd:cd02426  125 YIAA 128
HGTP_anticodon cd00738
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
311-401 6.89e-25

HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).


Pssm-ID: 238379 [Multi-domain]  Cd Length: 94  Bit Score: 97.47  E-value: 6.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 311 LLNMCPGNESQLHVCQGLFSELLENGISVWPGYLEtvhSSLEQLYSKYDEMSILFTVLITEATLENGLIHLRSRDTTMKE 390
Cdd:cd00738    6 IVPLTDPRVEAREYAQKLLNALLANGIRVLYDDRE---RKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGESE 82
                         90
                 ....*....|.
gi 591324617 391 MMHISKVKDFL 401
Cdd:cd00738   83 TLHVDELPEFL 93
PRK14894 PRK14894
glycyl-tRNA synthetase; Provisional
67-311 2.44e-12

glycyl-tRNA synthetase; Provisional


Pssm-ID: 237851 [Multi-domain]  Cd Length: 539  Bit Score: 68.49  E-value: 2.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  67 EELLEICQRRHFFSGSRRQlsrHSLLSGCHpGFGPLGIELRKNLAAEWWSSVVVLREQVFPVDAL------------HHE 134
Cdd:PRK14894   7 DQIVALAKRRGFIFPSSEI---YGGLQGVY-DYGPLGVELKNNIIADWWRTNVYERDDMEGLDAAilmnrlvwkysgHEE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 135 P--GPLLP---------GDSTFRLVSAATLRELLQDKELS---KEQLVAFLDNllKTSGKLRENLLHGALEHYVNCLDLV 200
Cdd:PRK14894  83 TfnDPLVDcrdckmrwrADHIQGVCPNCGSRDLTEPRPFNmmfRTQIGPVADS--DSFAYLRPETAQGIFVNFANVLATS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 201 NRRLPYGLAQIGVCFHpvsdTKQTP-DGVKRIGEKTEASLVWFTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFSSSDCQ 279
Cdd:PRK14894 161 ARKLPFGIAQVGKAFR----NEINPrNFLFRVREFEQMEIEYFVMPGTDEEWHQRWLEARLAWWEQIGIPRSRITIYDVP 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 591324617 280 DEE----GRKGNKLYYNFP-WGKEPIETLWNLGDHEL 311
Cdd:PRK14894 237 PDElahySKRTFDLMYDYPnIGVQEIEGIANRTDYDL 273
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
317-403 1.70e-11

Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.


Pssm-ID: 460819 [Multi-domain]  Cd Length: 94  Bit Score: 60.29  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  317 GNESQLHVCQGLFSELLENGISVwpgYLETVHSSLEQLYSKYDEMSILFTVLITEATLENGLIHLRSRDTTMKEMMHISK 396
Cdd:pfam03129  10 KAEELEEYAQKLAEELRAAGIRV---ELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQETVSLDE 86

                  ....*..
gi 591324617  397 VKDFLIK 403
Cdd:pfam03129  87 LVEKLKE 93
GRS1 COG0423
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ...
67-301 4.78e-07

Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; Glycyl-tRNA synthetase, class II is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440192 [Multi-domain]  Cd Length: 461  Bit Score: 51.65  E-value: 4.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  67 EELLEICQRRHFFSGSrrqlsrhsllSGCHPG------FGPLGIELRKNLAAEWWSSVVVLREQVFPVDA---LH----- 132
Cdd:COG0423    8 EKIVSLAKRRGFVFPS----------SEIYGGlagfydYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSpiiMPpkvwe 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 133 ---HEPG---PLLpgD-----STFR---LVSAATLRELLQDkeLSKEQLVAFL-DNLLK--TSGKL-----RE-NLL--- 186
Cdd:COG0423   78 asgHVDGftdPLV--DckeckKRYRadhLIEEYLAIEDAEG--LSLEELEELIkENNIKcpNCGGKeltevRQfNLMfkt 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 187 -HGALE-----HY----------VNCLDLVN---RRLPYGLAQIGvcfhpvsdtKQ-----TP-DGVKRIGEKTEASLVW 241
Cdd:COG0423  154 nIGPVEdesstGYlrpetaqgifVNFKNVQRtarKKLPFGIAQIG---------KSfrneiTPrNFIFRTREFEQMELEF 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 591324617 242 FTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFS------------SSDCQDEEgrkgnklyYNFPWGKEPIE 301
Cdd:COG0423  225 FVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRfrdhlpeelahyAKATWDIE--------YEFPFGWGELE 288
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
67-311 7.33e-06

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 47.82  E-value: 7.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617  67 EELLEICQRRHFFSGSrrqlsrhsllSGCHPG------FGPLGIELRKNLAAEWWSSVVVLREQVFPVDA---LH----- 132
Cdd:PRK04173   5 EKIVSLAKRRGFVFPS----------SEIYGGlagfwdYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSpiiMPpevwe 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 133 ---HEPG---PLLpgDST-----FR---LVSAAtLRELLQDKELSKEQLVAFLDNLLKTSGK--LRE----NLL----HG 188
Cdd:PRK04173  75 asgHVDNfsdPLV--ECKkckkrYRadhLIEEL-GIDAEGLSNEELKELIRENDIKCPECGGenWTEvrqfNLMfktfIG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 189 ALE-----HY----------VNCLDLVN---RRLPYGLAQIGvcfhpvsdtKQ-----TP-DGVKRIGEKTEASLVWFTS 244
Cdd:PRK04173 152 PVEdskslGYlrpetaqgifVNFKNVLRtarKKLPFGIAQIG---------KSfrneiTPrNFIFRTREFEQMELEFFVK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324617 245 ARTAGQWLDFWLRHRLLWWRKFAKSPSNFS------------SSDCQDEEgrkgnklyYNFPWGKEPIEtLW---NLGDH 309
Cdd:PRK04173 223 PGTDNEWFAYWIELRKNWLLDLGIDPENLRfrehlpeelahySKATWDIE--------YKFPFGRFWGE-LEgiaNRTDY 293

                 ..
gi 591324617 310 EL 311
Cdd:PRK04173 294 DL 295
GlyRS_anticodon cd00858
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ...
328-405 7.34e-04

GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238435 [Multi-domain]  Cd Length: 121  Bit Score: 39.08  E-value: 7.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 591324617 328 LFSELLENGISVwpGYLETVhsSLEQLYSKYDEMSILFTVLITEATLENGLIHLRSRDTTMKEMMHISKVKDFLIKYI 405
Cdd:cd00858   47 ISEELRELGFSV--KYDDSG--SIGRRYARQDEIGTPFCVTVDFDTLEDGTVTIRERDSMRQVRVKIEELPSYLRELI 120
 
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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