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Conserved domains on  [gi|70887790|ref|NP_009146|]
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DNA polymerase subunit gamma-2 [Homo sapiens]

Protein Classification

proline--tRNA ligase( domain architecture ID 10217163)

proline--tRNA ligase catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pol_gamma_b_Cterm cd02426
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ...
354-481 1.06e-76

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: 236.16  E-value: 1.06e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 354 FQLTENSFTRKKNLHRKVLKLHPCLAPIKVALDVGRGPTLELRQVCQGLFNELLENGISVWPGYLETMQSSLEQLYSKYD 433
Cdd:cd02426   1 AQLAELSDGRKKGRQRQVLKLHPCLAPYKVAIDCGKGDTAELRDLCQGLKNELREAGLSVWPGYLETQHSSLEQLLDKYD 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 70887790 434 EMSILFTVLVTETTLENGLIHLRSRDTTMKEMMHISKLKDFLIKYISS 481
Cdd:cd02426  81 EMGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLLRYIAA 128
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 4.99e-76

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: 239.03  E-value: 4.99e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  69 LLEICQRRHFLSGSKQQLSrdsLLSGCHpGFGPLGVELRKNLAAEWWTSVVVFREQVFPVDALHHKPGPLlpgdsaFRLV 148
Cdd:cd00774   1 LVELAKRRGFVFPSSEIYG---GVAGFY-DYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELM------FKTS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 149 SAETLREilqdkelskeqlvaflenvlKTSGKLRENLLHGALEHYVNCLDLVNKRLPYGLAQIGVCFHPVFDTkqiRNGV 228
Cdd:cd00774  71 IGPVESG--------------------GNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISP---RNGL 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 229 KSIGEKTEASLVWFTPPRTSNQWLDFWLRHRLQWWRKFAMSPSNFSSSDCQDEEG----RKGNKLYYNFPWGKELIETLW 304
Cdd:cd00774 128 FRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELahyaNETLDYFYAFPHGFLELEGIA 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 70887790 305 NLGDHELLHMYPGN-VSKLHGRDGRKNVVPCVLSVNGDLDRGMLAYL 350
Cdd:cd00774 208 NRGDRFLQHHPNESaHYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
 
Name Accession Description Interval E-value
Pol_gamma_b_Cterm cd02426
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ...
354-481 1.06e-76

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: 236.16  E-value: 1.06e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 354 FQLTENSFTRKKNLHRKVLKLHPCLAPIKVALDVGRGPTLELRQVCQGLFNELLENGISVWPGYLETMQSSLEQLYSKYD 433
Cdd:cd02426   1 AQLAELSDGRKKGRQRQVLKLHPCLAPYKVAIDCGKGDTAELRDLCQGLKNELREAGLSVWPGYLETQHSSLEQLLDKYD 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 70887790 434 EMSILFTVLVTETTLENGLIHLRSRDTTMKEMMHISKLKDFLIKYISS 481
Cdd:cd02426  81 EMGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLLRYIAA 128
GlyRS-like_core cd00774
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ...
69-350 4.99e-76

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: 239.03  E-value: 4.99e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  69 LLEICQRRHFLSGSKQQLSrdsLLSGCHpGFGPLGVELRKNLAAEWWTSVVVFREQVFPVDALHHKPGPLlpgdsaFRLV 148
Cdd:cd00774   1 LVELAKRRGFVFPSSEIYG---GVAGFY-DYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELM------FKTS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 149 SAETLREilqdkelskeqlvaflenvlKTSGKLRENLLHGALEHYVNCLDLVNKRLPYGLAQIGVCFHPVFDTkqiRNGV 228
Cdd:cd00774  71 IGPVESG--------------------GNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISP---RNGL 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 229 KSIGEKTEASLVWFTPPRTSNQWLDFWLRHRLQWWRKFAMSPSNFSSSDCQDEEG----RKGNKLYYNFPWGKELIETLW 304
Cdd:cd00774 128 FRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELahyaNETLDYFYAFPHGFLELEGIA 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 70887790 305 NLGDHELLHMYPGN-VSKLHGRDGRKNVVPCVLSVNGDLDRGMLAYL 350
Cdd:cd00774 208 NRGDRFLQHHPNESaHYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
99-479 9.06e-27

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 112.53  E-value: 9.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790   99 FGPLGVELRKNLAAEWWTSVVVFREQVFPVDAlhhkpgP-LLPGD----------------------SAFR---LVsAET 152
Cdd:PRK04173  33 YGPLGVELKNNIKRAWWKSFVQEREDVVGIDS------PiIMPPEvweasghvdnfsdplveckkckKRYRadhLI-EEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  153 LREILQDKELSKEQLVAFLENVLKTSGK--LRE----NLL----HGALE-----HY----------VNCLDLVN---KRL 204
Cdd:PRK04173 106 GIDAEGLSNEELKELIRENDIKCPECGGenWTEvrqfNLMfktfIGPVEdskslGYlrpetaqgifVNFKNVLRtarKKL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  205 PYGLAQIGVCFH----PvfdtkqiRNGVKSIGEKTEASLVWFTPPRTSNQWLDFWLRHRLQWWRKFAMSPSNFS------ 274
Cdd:PRK04173 186 PFGIAQIGKSFRneitP-------RNFIFRTREFEQMELEFFVKPGTDNEWFAYWIELRKNWLLDLGIDPENLRfrehlp 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  275 ------SSDCQDEEgrkgnklyYNFPWGKELIEtLW---NLGDHELL-HMypgnvsKLHGRD--------GRKNVVPCVL 336
Cdd:PRK04173 259 eelahySKATWDIE--------YKFPFGRFWGE-LEgiaNRTDYDLSrHS------KHSGEDlsyfddetTGEKYIPYVI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  337 --SVnGdLDRGMLAYLYDSFQLTENSFTRKknlhRKVLKLHPCLAPIKVA-LdvgrgPTL---ELRQVCQGLFNELLENg 410
Cdd:PRK04173 324 epSA-G-LDRLLLAFLEDAYTEEELGGGDK----RTVLRLPPALAPVKVAvL-----PLVkkeKLSEKAREIYAELRKD- 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887790  411 ISVWpgYLETmqSSLEQLYSKYDEMSILFTVLVTETTLENGLIHLRSRDTTMKEMMHISKLKDFLIKYI 479
Cdd:PRK04173 392 FNVD--YDDS--GSIGKRYRRQDEIGTPFCITVDFDTLEDNTVTIRDRDTMEQVRVKIDELKDYLAEKL 456
GRS1 COG0423
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ...
67-483 3.62e-24

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: 104.80  E-value: 3.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  67 EALLEICQRRHFLSGSkqqlsrdsllSGCHPG------FGPLGVELRKNLAAEWWTSVVVFREQVFPVDA--LHHKP--- 135
Cdd:COG0423   8 EKIVSLAKRRGFVFPS----------SEIYGGlagfydYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSpiIMPPKvwe 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 136 --G-------PLLpgD-----SAFR---LVSAETLREILQDkeLSKEQLVAFL-ENVLK--TSGKL-----RE-NLL--- 186
Cdd:COG0423  78 asGhvdgftdPLV--DckeckKRYRadhLIEEYLAIEDAEG--LSLEELEELIkENNIKcpNCGGKeltevRQfNLMfkt 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 187 -HGALE-----HY----------VNCLDLVN---KRLPYGLAQIGVCFH----PvfdtkqiRNGVKSIGEKTEASLVWFT 243
Cdd:COG0423 154 nIGPVEdesstGYlrpetaqgifVNFKNVQRtarKKLPFGIAQIGKSFRneitP-------RNFIFRTREFEQMELEFFV 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 244 PPRTSNQWLDFWLRHRLQWWRKFAMSPSNFS------------SSDCQDEEgrkgnklyYNFPWGKELIETLWNLGDHEL 311
Cdd:COG0423 227 DPGTDNEWFAYWLALRKKWLLSLGIDPENLRfrdhlpeelahyAKATWDIE--------YEFPFGWGELEGIAYRTDYDL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 312 L-HMypgnvsKLHGRD-------GRKNVVPCVL--SVnGdLDRGMLAYLYDSFqlTENSFTRKKnlhRKVLKLHPCLAPI 381
Cdd:COG0423 299 SrHQ------EYSGKDltyfdpeTGEKYIPHVIepSF-G-VDRLLLAFLEHAY--TEEEVDGEE---RTVLKLPPRLAPI 365
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 382 KVA---LdVGRGptlELRQVCQGLFNELLENgISVwpGYLETmqSSLEQLYSKYDEMSILFTVLVTETTLENGLIHLRSR 458
Cdd:COG0423 366 KVAvlpL-VKKD---GLVEKAREIYDELRKA-FNV--EYDDS--GSIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTIRDR 436
                       490       500
                ....*....|....*....|....*
gi 70887790 459 DTTMKEMMHISKLKDFLIKYISSAK 483
Cdd:COG0423 437 DTMEQERVPIDELKAYLAELLKGER 461
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
382-477 5.80e-13

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: 64.53  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790   382 KVALDVGRGPTLELRQVCQGLFNELLENGISVwpgYLETMQSSLEQLYSKYDEMSILFTVLVTETTLENGLIHLRSRDTT 461
Cdd:pfam03129   1 QVVVIPLGEKAEELEEYAQKLAEELRAAGIRV---ELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTG 77
                          90
                  ....*....|....*.
gi 70887790   462 MKEMMHISKLKDFLIK 477
Cdd:pfam03129  78 EQETVSLDELVEKLKE 93
 
Name Accession Description Interval E-value
Pol_gamma_b_Cterm cd02426
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ...
354-481 1.06e-76

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: 236.16  E-value: 1.06e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 354 FQLTENSFTRKKNLHRKVLKLHPCLAPIKVALDVGRGPTLELRQVCQGLFNELLENGISVWPGYLETMQSSLEQLYSKYD 433
Cdd:cd02426   1 AQLAELSDGRKKGRQRQVLKLHPCLAPYKVAIDCGKGDTAELRDLCQGLKNELREAGLSVWPGYLETQHSSLEQLLDKYD 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 70887790 434 EMSILFTVLVTETTLENGLIHLRSRDTTMKEMMHISKLKDFLIKYISS 481
Cdd:cd02426  81 EMGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLLRYIAA 128
GlyRS-like_core cd00774
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ...
69-350 4.99e-76

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: 239.03  E-value: 4.99e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  69 LLEICQRRHFLSGSKQQLSrdsLLSGCHpGFGPLGVELRKNLAAEWWTSVVVFREQVFPVDALHHKPGPLlpgdsaFRLV 148
Cdd:cd00774   1 LVELAKRRGFVFPSSEIYG---GVAGFY-DYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPELM------FKTS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 149 SAETLREilqdkelskeqlvaflenvlKTSGKLRENLLHGALEHYVNCLDLVNKRLPYGLAQIGVCFHPVFDTkqiRNGV 228
Cdd:cd00774  71 IGPVESG--------------------GNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISP---RNGL 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 229 KSIGEKTEASLVWFTPPRTSNQWLDFWLRHRLQWWRKFAMSPSNFSSSDCQDEEG----RKGNKLYYNFPWGKELIETLW 304
Cdd:cd00774 128 FRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELahyaNETLDYFYAFPHGFLELEGIA 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 70887790 305 NLGDHELLHMYPGN-VSKLHGRDGRKNVVPCVLSVNGDLDRGMLAYL 350
Cdd:cd00774 208 NRGDRFLQHHPNESaHYASDCWDAEKLYVPGWIEVSGGADRTDYDLL 254
HGTP_anticodon cd00738
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
380-475 2.58e-31

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: 115.96  E-value: 2.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 380 PIKVALDVGRGPTLELRQVCQGLFNELLENGISVWPGYLetmQSSLEQLYSKYDEMSILFTVLVTETTLENGLIHLRSRD 459
Cdd:cd00738   1 PIDVAIVPLTDPRVEAREYAQKLLNALLANGIRVLYDDR---ERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRD 77
                        90
                ....*....|....*.
gi 70887790 460 TTMKEMMHISKLKDFL 475
Cdd:cd00738  78 TGESETLHVDELPEFL 93
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
99-479 9.06e-27

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 112.53  E-value: 9.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790   99 FGPLGVELRKNLAAEWWTSVVVFREQVFPVDAlhhkpgP-LLPGD----------------------SAFR---LVsAET 152
Cdd:PRK04173  33 YGPLGVELKNNIKRAWWKSFVQEREDVVGIDS------PiIMPPEvweasghvdnfsdplveckkckKRYRadhLI-EEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  153 LREILQDKELSKEQLVAFLENVLKTSGK--LRE----NLL----HGALE-----HY----------VNCLDLVN---KRL 204
Cdd:PRK04173 106 GIDAEGLSNEELKELIRENDIKCPECGGenWTEvrqfNLMfktfIGPVEdskslGYlrpetaqgifVNFKNVLRtarKKL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  205 PYGLAQIGVCFH----PvfdtkqiRNGVKSIGEKTEASLVWFTPPRTSNQWLDFWLRHRLQWWRKFAMSPSNFS------ 274
Cdd:PRK04173 186 PFGIAQIGKSFRneitP-------RNFIFRTREFEQMELEFFVKPGTDNEWFAYWIELRKNWLLDLGIDPENLRfrehlp 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  275 ------SSDCQDEEgrkgnklyYNFPWGKELIEtLW---NLGDHELL-HMypgnvsKLHGRD--------GRKNVVPCVL 336
Cdd:PRK04173 259 eelahySKATWDIE--------YKFPFGRFWGE-LEgiaNRTDYDLSrHS------KHSGEDlsyfddetTGEKYIPYVI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  337 --SVnGdLDRGMLAYLYDSFQLTENSFTRKknlhRKVLKLHPCLAPIKVA-LdvgrgPTL---ELRQVCQGLFNELLENg 410
Cdd:PRK04173 324 epSA-G-LDRLLLAFLEDAYTEEELGGGDK----RTVLRLPPALAPVKVAvL-----PLVkkeKLSEKAREIYAELRKD- 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887790  411 ISVWpgYLETmqSSLEQLYSKYDEMSILFTVLVTETTLENGLIHLRSRDTTMKEMMHISKLKDFLIKYI 479
Cdd:PRK04173 392 FNVD--YDDS--GSIGKRYRRQDEIGTPFCITVDFDTLEDNTVTIRDRDTMEQVRVKIDELKDYLAEKL 456
GRS1 COG0423
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ...
67-483 3.62e-24

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: 104.80  E-value: 3.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  67 EALLEICQRRHFLSGSkqqlsrdsllSGCHPG------FGPLGVELRKNLAAEWWTSVVVFREQVFPVDA--LHHKP--- 135
Cdd:COG0423   8 EKIVSLAKRRGFVFPS----------SEIYGGlagfydYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSpiIMPPKvwe 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 136 --G-------PLLpgD-----SAFR---LVSAETLREILQDkeLSKEQLVAFL-ENVLK--TSGKL-----RE-NLL--- 186
Cdd:COG0423  78 asGhvdgftdPLV--DckeckKRYRadhLIEEYLAIEDAEG--LSLEELEELIkENNIKcpNCGGKeltevRQfNLMfkt 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 187 -HGALE-----HY----------VNCLDLVN---KRLPYGLAQIGVCFH----PvfdtkqiRNGVKSIGEKTEASLVWFT 243
Cdd:COG0423 154 nIGPVEdesstGYlrpetaqgifVNFKNVQRtarKKLPFGIAQIGKSFRneitP-------RNFIFRTREFEQMELEFFV 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 244 PPRTSNQWLDFWLRHRLQWWRKFAMSPSNFS------------SSDCQDEEgrkgnklyYNFPWGKELIETLWNLGDHEL 311
Cdd:COG0423 227 DPGTDNEWFAYWLALRKKWLLSLGIDPENLRfrdhlpeelahyAKATWDIE--------YEFPFGWGELEGIAYRTDYDL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 312 L-HMypgnvsKLHGRD-------GRKNVVPCVL--SVnGdLDRGMLAYLYDSFqlTENSFTRKKnlhRKVLKLHPCLAPI 381
Cdd:COG0423 299 SrHQ------EYSGKDltyfdpeTGEKYIPHVIepSF-G-VDRLLLAFLEHAY--TEEEVDGEE---RTVLKLPPRLAPI 365
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 382 KVA---LdVGRGptlELRQVCQGLFNELLENgISVwpGYLETmqSSLEQLYSKYDEMSILFTVLVTETTLENGLIHLRSR 458
Cdd:COG0423 366 KVAvlpL-VKKD---GLVEKAREIYDELRKA-FNV--EYDDS--GSIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTIRDR 436
                       490       500
                ....*....|....*....|....*
gi 70887790 459 DTTMKEMMHISKLKDFLIKYISSAK 483
Cdd:COG0423 437 DTMEQERVPIDELKAYLAELLKGER 461
PRK14894 PRK14894
glycyl-tRNA synthetase; Provisional
67-475 6.16e-16

glycyl-tRNA synthetase; Provisional


Pssm-ID: 237851 [Multi-domain]  Cd Length: 539  Bit Score: 80.43  E-value: 6.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790   67 EALLEICQRRHFLSGSKQQLSRdslLSGCHpGFGPLGVELRKNLAAEWWTSVVVFREQVFPVDAlhhkpgPLLPGDSAFR 146
Cdd:PRK14894   7 DQIVALAKRRGFIFPSSEIYGG---LQGVY-DYGPLGVELKNNIIADWWRTNVYERDDMEGLDA------AILMNRLVWK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  147 LVS-AETLREILQDKELSKEQLVA-FLENVLKTSGK----------------------------LRENLLHGALEHYVNC 196
Cdd:PRK14894  77 YSGhEETFNDPLVDCRDCKMRWRAdHIQGVCPNCGSrdlteprpfnmmfrtqigpvadsdsfayLRPETAQGIFVNFANV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  197 LDLVNKRLPYGLAQIGVCFHPVFDTkqiRNGVKSIGEKTEASLVWFTPPRTSNQWLDFWLRHRLQWWRKFAMSPSNFSSS 276
Cdd:PRK14894 157 LATSARKLPFGIAQVGKAFRNEINP---RNFLFRVREFEQMEIEYFVMPGTDEEWHQRWLEARLAWWEQIGIPRSRITIY 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  277 DCQDEE----GRKGNKLYYNFP-WGKELIE-----TLWNLGDH----ELLHMYP------GNVSKL--HGRDGRKNVVPC 334
Cdd:PRK14894 234 DVPPDElahySKRTFDLMYDYPnIGVQEIEgianrTDYDLGSHskdqEQLNLTArvnpneDSTARLtyFDQASGRHVVPY 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  335 VLSVNGDLDRGMLAYLYDSF--QLTE------------------NSFTRKKNL--------------------------- 367
Cdd:PRK14894 314 VIEPSAGVGRCMLAVMCEGYaeELTKaipgeklaavgdaleaflKSVGRSEKLageardailargeallqalperlpeve 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790  368 ----------------------------HRKVLKLHPCLAPIKVALdvgrgptLELRQVCQGL------FNELLENGISV 413
Cdd:PRK14894 394 qllampgadqielgkklrgqaqplidehYRTVLRLKPRLAPIKVAV-------FPLKRNHEGLvatakaVRRQLQVGGRM 466
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887790  414 WPGYLETmqSSLEQLYSKYDEMSILFTVLVTETTLEN-------GLIHLRSRDTTMKEMMHISKLKDFL 475
Cdd:PRK14894 467 RTVYDDT--GAIGKLYRRQDEIGTPFCITVDFDTIGQgkdpalaGTVTVRDRDTMAQERVPISELEAYL 533
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
382-477 5.80e-13

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: 64.53  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790   382 KVALDVGRGPTLELRQVCQGLFNELLENGISVwpgYLETMQSSLEQLYSKYDEMSILFTVLVTETTLENGLIHLRSRDTT 461
Cdd:pfam03129   1 QVVVIPLGEKAEELEEYAQKLAEELRAAGIRV---ELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTG 77
                          90
                  ....*....|....*.
gi 70887790   462 MKEMMHISKLKDFLIK 477
Cdd:pfam03129  78 EQETVSLDELVEKLKE 93
GlyRS_anticodon cd00858
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ...
356-479 3.78e-11

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: 60.26  E-value: 3.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887790 356 LTENSFTRKKNLH-RKVLKLHPCLAPIKVALdvgrGPTL---ELRQVCQGLFNELLENGISVwpGYLETmqSSLEQLYSK 431
Cdd:cd00858   1 LLEHSFRVREGDEgRIVLRLPPALAPIKVAV----LPLVkrdELVEIAKEISEELRELGFSV--KYDDS--GSIGRRYAR 72
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 70887790 432 YDEMSILFTVLVTETTLENGLIHLRSRDTTMKEMMHISKLKDFLIKYI 479
Cdd:cd00858  73 QDEIGTPFCVTVDFDTLEDGTVTIRERDSMRQVRVKIEELPSYLRELI 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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