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Conserved domains on  [gi|591324615|ref|XP_007088348|]
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DNA polymerase subunit gamma-2, mitochondrial isoform X4 [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 ...
69-350 9.45e-74

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: 231.71  E-value: 9.45e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615  69 LLEICQRRHFFSGSRRQLSrhsLLSGCHpGFGPLGIELRKNLAAEWWSSVVVLREQVFPVDALHHEPGPLlpgdstFRLV 148
Cdd:cd00774    1 LVELAKRRGFVFPSSEIYG---GVAGFY-DYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELM------FKTS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 149 SAATlrellqdkelskeqlvafldNLLKTSGKLRENLLHGALEHYVNCLDLVNRRLPYGLAQIGVCFHPVSDTKQtpdGV 228
Cdd:cd00774   71 IGPV--------------------ESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRN---GL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 229 KRIGEKTEASLVWFTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFSSSDCQDEEG----RKGNKLYYNFPWGKEPIETLW 304
Cdd:cd00774  128 FRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELahyaNETLDYFYAFPHGFLELEGIA 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 591324615 305 NLGDHELLNMCPGN-ESQLHGRDGRKNVVPYVLSVSGNLDRGMLAYL 350
Cdd:cd00774  208 NRGDRFLQHHPNESaHYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
HGTP_anticodon super family cl00266
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
354-433 5.73e-39

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: 136.78  E-value: 5.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 354 FQLTESSFTRKKNLHRKVLKLHPCLAPVKVALDVGRGPTVELRQVCQGLFSELLENGISVWPGYLETVHSSLEQLYSNFD 433
Cdd:cd02426    1 AQLAELSDGRKKGRQRQVLKLHPCLAPYKVAIDCGKGDTAELRDLCQGLKNELREAGLSVWPGYLETQHSSLEQLLDKYD 80
 
Name Accession Description Interval E-value
GlyRS-like_core cd00774
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ...
69-350 9.45e-74

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: 231.71  E-value: 9.45e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615  69 LLEICQRRHFFSGSRRQLSrhsLLSGCHpGFGPLGIELRKNLAAEWWSSVVVLREQVFPVDALHHEPGPLlpgdstFRLV 148
Cdd:cd00774    1 LVELAKRRGFVFPSSEIYG---GVAGFY-DYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELM------FKTS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 149 SAATlrellqdkelskeqlvafldNLLKTSGKLRENLLHGALEHYVNCLDLVNRRLPYGLAQIGVCFHPVSDTKQtpdGV 228
Cdd:cd00774   71 IGPV--------------------ESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRN---GL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 229 KRIGEKTEASLVWFTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFSSSDCQDEEG----RKGNKLYYNFPWGKEPIETLW 304
Cdd:cd00774  128 FRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELahyaNETLDYFYAFPHGFLELEGIA 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 591324615 305 NLGDHELLNMCPGN-ESQLHGRDGRKNVVPYVLSVSGNLDRGMLAYL 350
Cdd:cd00774  208 NRGDRFLQHHPNESaHYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
Pol_gamma_b_Cterm cd02426
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ...
354-433 5.73e-39

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: 136.78  E-value: 5.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 354 FQLTESSFTRKKNLHRKVLKLHPCLAPVKVALDVGRGPTVELRQVCQGLFSELLENGISVWPGYLETVHSSLEQLYSNFD 433
Cdd:cd02426    1 AQLAELSDGRKKGRQRQVLKLHPCLAPYKVAIDCGKGDTAELRDLCQGLKNELREAGLSVWPGYLETQHSSLEQLLDKYD 80
GRS1 COG0423
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ...
67-384 7.89e-19

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: 88.24  E-value: 7.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615  67 EELLEICQRRHFFSGSrrqlsrhsllSGCHPG------FGPLGIELRKNLAAEWWSSVVVLREQVFPVDA---LH----- 132
Cdd:COG0423    8 EKIVSLAKRRGFVFPS----------SEIYGGlagfydYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSpiiMPpkvwe 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 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 591324615 187 -HGALE-----HY----------VNCLDLVN---RRLPYGLAQIGvcfhpvsdtKQ-----TP-DGVKRIGEKTEASLVW 241
Cdd:COG0423  154 nIGPVEdesstGYlrpetaqgifVNFKNVQRtarKKLPFGIAQIG---------KSfrneiTPrNFIFRTREFEQMELEF 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 242 FTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFS------------SSDCQDEEgrkgnklyYNFPWGKEPIETLWNLGDH 309
Cdd:COG0423  225 FVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRfrdhlpeelahyAKATWDIE--------YEFPFGWGELEGIAYRTDY 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 310 ELlnmcpGNESQLHGRD-------GRKNVVPYVLSVSGNLDRGMLAYLYDSFqlTESSFTRKKnlhRKVLKLHPCLAPVK 382
Cdd:COG0423  297 DL-----SRHQEYSGKDltyfdpeTGEKYIPHVIEPSFGVDRLLLAFLEHAY--TEEEVDGEE---RTVLKLPPRLAPIK 366

                 ..
gi 591324615 383 VA 384
Cdd:COG0423  367 VA 368
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
67-384 5.34e-18

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 85.57  E-value: 5.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615  67 EELLEICQRRHFFSGSrrqlsrhsllSGCHPG------FGPLGIELRKNLAAEWWSSVVVLREQVFPVDA---LH----- 132
Cdd:PRK04173   5 EKIVSLAKRRGFVFPS----------SEIYGGlagfwdYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSpiiMPpevwe 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 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 591324615 189 ALE-----HY----------VNCLDLVN---RRLPYGLAQIGvcfhpvsdtKQ-----TP-DGVKRIGEKTEASLVWFTS 244
Cdd:PRK04173 152 PVEdskslGYlrpetaqgifVNFKNVLRtarKKLPFGIAQIG---------KSfrneiTPrNFIFRTREFEQMELEFFVK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 245 ARTAGQWLDFWLRHRLLWWRKFAKSPSNFS------------SSDCQDEEgrkgnklyYNFPWGKEPIEtLW---NLGDH 309
Cdd:PRK04173 223 PGTDNEWFAYWIELRKNWLLDLGIDPENLRfrehlpeelahySKATWDIE--------YKFPFGRFWGE-LEgiaNRTDY 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 310 ELlnmcpGNESQLHGRD--------GRKNVVPYVLSVSGNLDRGMLAYLYDSFQLTESSFTRKknlhRKVLKLHPCLAPV 381
Cdd:PRK04173 294 DL-----SRHSKHSGEDlsyfddetTGEKYIPYVIEPSAGLDRLLLAFLEDAYTEEELGGGDK----RTVLRLPPALAPV 364

                 ...
gi 591324615 382 KVA 384
Cdd:PRK04173 365 KVA 367
 
Name Accession Description Interval E-value
GlyRS-like_core cd00774
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ...
69-350 9.45e-74

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: 231.71  E-value: 9.45e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615  69 LLEICQRRHFFSGSRRQLSrhsLLSGCHpGFGPLGIELRKNLAAEWWSSVVVLREQVFPVDALHHEPGPLlpgdstFRLV 148
Cdd:cd00774    1 LVELAKRRGFVFPSSEIYG---GVAGFY-DYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELM------FKTS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 149 SAATlrellqdkelskeqlvafldNLLKTSGKLRENLLHGALEHYVNCLDLVNRRLPYGLAQIGVCFHPVSDTKQtpdGV 228
Cdd:cd00774   71 IGPV--------------------ESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRN---GL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 229 KRIGEKTEASLVWFTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFSSSDCQDEEG----RKGNKLYYNFPWGKEPIETLW 304
Cdd:cd00774  128 FRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELahyaNETLDYFYAFPHGFLELEGIA 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 591324615 305 NLGDHELLNMCPGN-ESQLHGRDGRKNVVPYVLSVSGNLDRGMLAYL 350
Cdd:cd00774  208 NRGDRFLQHHPNESaHYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
Pol_gamma_b_Cterm cd02426
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ...
354-433 5.73e-39

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: 136.78  E-value: 5.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 354 FQLTESSFTRKKNLHRKVLKLHPCLAPVKVALDVGRGPTVELRQVCQGLFSELLENGISVWPGYLETVHSSLEQLYSNFD 433
Cdd:cd02426    1 AQLAELSDGRKKGRQRQVLKLHPCLAPYKVAIDCGKGDTAELRDLCQGLKNELREAGLSVWPGYLETQHSSLEQLLDKYD 80
GRS1 COG0423
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ...
67-384 7.89e-19

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: 88.24  E-value: 7.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615  67 EELLEICQRRHFFSGSrrqlsrhsllSGCHPG------FGPLGIELRKNLAAEWWSSVVVLREQVFPVDA---LH----- 132
Cdd:COG0423    8 EKIVSLAKRRGFVFPS----------SEIYGGlagfydYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSpiiMPpkvwe 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 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 591324615 187 -HGALE-----HY----------VNCLDLVN---RRLPYGLAQIGvcfhpvsdtKQ-----TP-DGVKRIGEKTEASLVW 241
Cdd:COG0423  154 nIGPVEdesstGYlrpetaqgifVNFKNVQRtarKKLPFGIAQIG---------KSfrneiTPrNFIFRTREFEQMELEF 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 242 FTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFS------------SSDCQDEEgrkgnklyYNFPWGKEPIETLWNLGDH 309
Cdd:COG0423  225 FVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRfrdhlpeelahyAKATWDIE--------YEFPFGWGELEGIAYRTDY 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 310 ELlnmcpGNESQLHGRD-------GRKNVVPYVLSVSGNLDRGMLAYLYDSFqlTESSFTRKKnlhRKVLKLHPCLAPVK 382
Cdd:COG0423  297 DL-----SRHQEYSGKDltyfdpeTGEKYIPHVIEPSFGVDRLLLAFLEHAY--TEEEVDGEE---RTVLKLPPRLAPIK 366

                 ..
gi 591324615 383 VA 384
Cdd:COG0423  367 VA 368
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
67-384 5.34e-18

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 85.57  E-value: 5.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615  67 EELLEICQRRHFFSGSrrqlsrhsllSGCHPG------FGPLGIELRKNLAAEWWSSVVVLREQVFPVDA---LH----- 132
Cdd:PRK04173   5 EKIVSLAKRRGFVFPS----------SEIYGGlagfwdYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSpiiMPpevwe 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 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 591324615 189 ALE-----HY----------VNCLDLVN---RRLPYGLAQIGvcfhpvsdtKQ-----TP-DGVKRIGEKTEASLVWFTS 244
Cdd:PRK04173 152 PVEdskslGYlrpetaqgifVNFKNVLRtarKKLPFGIAQIG---------KSfrneiTPrNFIFRTREFEQMELEFFVK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 245 ARTAGQWLDFWLRHRLLWWRKFAKSPSNFS------------SSDCQDEEgrkgnklyYNFPWGKEPIEtLW---NLGDH 309
Cdd:PRK04173 223 PGTDNEWFAYWIELRKNWLLDLGIDPENLRfrehlpeelahySKATWDIE--------YKFPFGRFWGE-LEgiaNRTDY 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 310 ELlnmcpGNESQLHGRD--------GRKNVVPYVLSVSGNLDRGMLAYLYDSFQLTESSFTRKknlhRKVLKLHPCLAPV 381
Cdd:PRK04173 294 DL-----SRHSKHSGEDlsyfddetTGEKYIPYVIEPSAGLDRLLLAFLEDAYTEEELGGGDK----RTVLRLPPALAPV 364

                 ...
gi 591324615 382 KVA 384
Cdd:PRK04173 365 KVA 367
PRK14894 PRK14894
glycyl-tRNA synthetase; Provisional
67-359 1.10e-16

glycyl-tRNA synthetase; Provisional


Pssm-ID: 237851 [Multi-domain]  Cd Length: 539  Bit Score: 81.97  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615  67 EELLEICQRRHFFSGSRRQlsrHSLLSGCHpGFGPLGIELRKNLAAEWWSSVVVLREQVFPVDAL------------HHE 134
Cdd:PRK14894   7 DQIVALAKRRGFIFPSSEI---YGGLQGVY-DYGPLGVELKNNIIADWWRTNVYERDDMEGLDAAilmnrlvwkysgHEE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 135 P--GPLLP---------GDSTFRLVSAATLRELLQDKELS---KEQLVAFLDNllKTSGKLRENLLHGALEHYVNCLDLV 200
Cdd:PRK14894  83 TfnDPLVDcrdckmrwrADHIQGVCPNCGSRDLTEPRPFNmmfRTQIGPVADS--DSFAYLRPETAQGIFVNFANVLATS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 201 NRRLPYGLAQIGVCFHpvsdTKQTP-DGVKRIGEKTEASLVWFTSARTAGQWLDFWLRHRLLWWRKFAKSPSNFSSSDCQ 279
Cdd:PRK14894 161 ARKLPFGIAQVGKAFR----NEINPrNFLFRVREFEQMEIEYFVMPGTDEEWHQRWLEARLAWWEQIGIPRSRITIYDVP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 591324615 280 DEE----GRKGNKLYYNFP-WGKEPIE-----TLWNLGDH----ELLNMC----PGNES----QLHGRDGRKNVVPYVLS 337
Cdd:PRK14894 237 PDElahySKRTFDLMYDYPnIGVQEIEgianrTDYDLGSHskdqEQLNLTarvnPNEDStarlTYFDQASGRHVVPYVIE 316
                        330       340
                 ....*....|....*....|....
gi 591324615 338 VSGNLDRGMLAYLYDSF--QLTES 359
Cdd:PRK14894 317 PSAGVGRCMLAVMCEGYaeELTKA 340
HGTP_anticodon cd00738
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
380-433 2.52e-09

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: 53.94  E-value: 2.52e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 591324615 380 PVKVALDVGRGPTVELRQVCQGLFSELLENGISVWPGYLEtvhSSLEQLYSNFD 433
Cdd:cd00738    1 PIDVAIVPLTDPRVEAREYAQKLLNALLANGIRVLYDDRE---RKIGKKFREAD 51
GlyRS_anticodon cd00858
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ...
356-413 7.45e-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: 7.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 591324615 356 LTESSFTRKKNLH-RKVLKLHPCLAPVKVALdvgrGPTV---ELRQVCQGLFSELLENGISV 413
Cdd:cd00858    1 LLEHSFRVREGDEgRIVLRLPPALAPIKVAV----LPLVkrdELVEIAKEISEELRELGFSV 58
 
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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