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Conserved domains on  [gi|2392170]
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Chain B, GLYCYL-TRNA SYNTHETASE

Protein Classification

glycine--tRNA ligase( domain architecture ID 11417994)

glycine--tRNA ligase catalyzes the attachment of glycine to tRNA(Gly)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GRS1 COG0423
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ...
1-505 0e+00

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: 724.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    1 AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHE 80
Cdd:COG0423   3 SEDTMEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSPIIMPPKVWEASGHV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   81 ATFADPMVDNRITKKRYRLDHLLKEqpeevlkrlyramEVEEENLHALvqammqAPERAGGAMTAAGVLDPASGEPgDWT 160
Cdd:COG0423  83 DGFTDPLVDCKECKKRYRADHLIEE-------------YLAIEDAEGL------SLEELEELIKENNIKCPNCGGK-ELT 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  161 PPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEI 240
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  241 EYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHT 320
Cdd:COG0423 223 EFFVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQ 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  321 kdqealgitarvlrnEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELpNGEERIVLKLKPQLAPIK 400
Cdd:COG0423 303 ---------------EYSGKDLTYFDPETGEKYIPHVIEPSFGVDRLLLAFLEHAYTEEEV-DGEERTVLKLPPRLAPIK 366
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  401 VAVIPLVKnRPEITEYAKRLKARLLAlgLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGqskdgttrlKDTVTVR 480
Cdd:COG0423 367 VAVLPLVK-KDGLVEKAREIYDELRK--AFNVEYDDSGSIGRRYRRQDEIGTPFCVTVDFDTLE---------DNTVTIR 434
                       490       500
                ....*....|....*....|....*
gi 2392170  481 DRDTMEQIRLHVDELEGFLRERLRW 505
Cdd:COG0423 435 DRDTMEQERVPIDELKAYLAELLKG 459
 
Name Accession Description Interval E-value
GRS1 COG0423
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ...
1-505 0e+00

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: 724.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    1 AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHE 80
Cdd:COG0423   3 SEDTMEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSPIIMPPKVWEASGHV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   81 ATFADPMVDNRITKKRYRLDHLLKEqpeevlkrlyramEVEEENLHALvqammqAPERAGGAMTAAGVLDPASGEPgDWT 160
Cdd:COG0423  83 DGFTDPLVDCKECKKRYRADHLIEE-------------YLAIEDAEGL------SLEELEELIKENNIKCPNCGGK-ELT 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  161 PPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEI 240
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  241 EYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHT 320
Cdd:COG0423 223 EFFVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQ 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  321 kdqealgitarvlrnEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELpNGEERIVLKLKPQLAPIK 400
Cdd:COG0423 303 ---------------EYSGKDLTYFDPETGEKYIPHVIEPSFGVDRLLLAFLEHAYTEEEV-DGEERTVLKLPPRLAPIK 366
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  401 VAVIPLVKnRPEITEYAKRLKARLLAlgLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGqskdgttrlKDTVTVR 480
Cdd:COG0423 367 VAVLPLVK-KDGLVEKAREIYDELRK--AFNVEYDDSGSIGRRYRRQDEIGTPFCVTVDFDTLE---------DNTVTIR 434
                       490       500
                ....*....|....*....|....*
gi 2392170  481 DRDTMEQIRLHVDELEGFLRERLRW 505
Cdd:COG0423 435 DRDTMEQERVPIDELKAYLAELLKG 459
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
2-503 0e+00

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 716.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170     2 ASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEA 81
Cdd:PRK04173   1 MDKMEKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSPIIMPPEVWEASGHVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    82 TFADPMVDNRITKKRYRLDHLLkeqpEEVLKRLYRAMEVEEENLhalvqammqaperaggaMTAAGVLDPASGEPGdWTP 161
Cdd:PRK04173  81 NFSDPLVECKKCKKRYRADHLI----EELGIDAEGLSNEELKEL-----------------IRENDIKCPECGGEN-WTE 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   162 PRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIE 241
Cdd:PRK04173 139 VRQFNLMFKTFIGPVEDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   242 YFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSL--ELEGIAQRTDFDLGSH 319
Cdd:PRK04173 219 FFVKPGTDNEWFAYWIELRKNWLLDLGIDPENLRFREHLPEELAHYSKATWDIEYKFPFGRFwgELEGIANRTDYDLSRH 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   320 TKdqealgitarvlrneHSTQRLAY-RDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAP 398
Cdd:PRK04173 299 SK---------------HSGEDLSYfDDETTGEKYIPYVIEPSAGLDRLLLAFLEDAYTEEELGGGDKRTVLRLPPALAP 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   399 IKVAVIPLVKNRpEITEYAKRLKARLLAlgLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGqskdgttrlKDTVT 478
Cdd:PRK04173 364 VKVAVLPLVKKE-KLSEKAREIYAELRK--DFNVDYDDSGSIGKRYRRQDEIGTPFCITVDFDTLE---------DNTVT 431
                        490       500
                 ....*....|....*....|....*
gi 2392170   479 VRDRDTMEQIRLHVDELEGFLRERL 503
Cdd:PRK04173 432 IRDRDTMEQVRVKIDELKDYLAEKL 456
glyS_dimeric TIGR00389
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ...
3-503 3.10e-145

glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct from the two alpha and two beta chains of the tetrameric E. coli glycyl-tRNA synthetase. This enzyme is a homodimeric class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes His, Ser, Pro, and this set of glycyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273051 [Multi-domain]  Cd Length: 551  Bit Score: 427.73  E-value: 3.10e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170      3 SSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYErDDMEGLDASVLTHRLVLHYSGHEAT 82
Cdd:TIGR00389   1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKN-ERVLEIDTPIITPEEVLKASGHVDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170     83 FADPMVDNRITKKRYRLDHLLkeqpEEVLKRLYRAMEVEEENLhalvqammqaperaggAMTAAGVLDPASGEpGDWTPP 162
Cdd:TIGR00389  80 FTDWMVDCKSCKERFRADHLI----EEKLGKRLWGFSGPELNE----------------VMEKYDINCPNCGG-ENLTEV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    163 RYFNMMFQDLRGPRGGRglLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEY 242
Cdd:TIGR00389 139 RSFNLMFQTEIGVVGKR--KGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEF 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    243 FVRPGEDEY-WHRYWVEERLKWW----------------------------------QEMGLSRENLVPYQQPPESSAHY 287
Cdd:TIGR00389 217 FVHPLDKSHpKFEEVKQDILPLLprqmqesgigeavesgmienetlgyfiarvkqflLEIGINPDKLRFRQHDKNEMAHY 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    288 AKATVDILYRFPHGSLELEGIAQRTDFDLGSHTK-----------DQEALGITARVLRNEHSTQRLAYR----------- 345
Cdd:TIGR00389 297 AKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKfsgkslsvfdkLDEPREVTKWEIEPNKKKFGPKFRkdakkiesnls 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    346 -----------------------------DPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELpNGEERIVLKLKPQL 396
Cdd:TIGR00389 377 eddleereeeldkneveldkdlveiemvtEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEVL-DGEEREVLRLPPHL 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    397 APIKVAVIPLVkNRPEITEYAKRLkARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIgqsKDGttrlkdT 476
Cdd:TIGR00389 456 APIKVAVLPLV-NKEELKEIAKEI-FQALRKTGIRIKYDDSGTIGKRYRRADEIGTPFCVTIDFETL---EDE------T 524
                         570       580
                  ....*....|....*....|....*..
gi 2392170    477 VTVRDRDTMEQIRLHVDELEGFLRERL 503
Cdd:TIGR00389 525 VTIRERDSMKQVRVKIKELPSYIKKLL 551
GlyRS-like_core cd00774
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ...
8-372 6.69e-120

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: 351.89  E-value: 6.69e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    8 LVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLvlhysgheatfadpm 87
Cdd:cd00774   1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPEL--------------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   88 vdnritkkryrldhllkeqpeevlkrlyrameveeenlhalvqammqaperaggamtaagvldpasgepgdwtppryfnm 167
Cdd:cd00774     --------------------------------------------------------------------------------
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  168 MFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPG 247
Cdd:cd00774  66 MFKTSIGPVESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPE 145
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  248 EDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHTKdqealg 327
Cdd:cd00774 146 KSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPN------ 219
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 2392170  328 itarvlrneHSTQRLAYRDPETgKWFVPYVIEPSAGVDRGVLALL 372
Cdd:cd00774 220 ---------ESAHYASDCWDAE-KLYVPGWIEVSGGADRTDYDLL 254
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
400-502 9.25e-25

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: 98.04  E-value: 9.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    400 KVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIgqskdgttrLKDTVTV 479
Cdd:pfam03129   1 QVVVIPLGEKAEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKEL---------EEGTVTV 71
                          90       100
                  ....*....|....*....|...
gi 2392170    480 RDRDTMEQIRLHVDELEGFLRER 502
Cdd:pfam03129  72 RRRDTGEQETVSLDELVEKLKEL 94
 
Name Accession Description Interval E-value
GRS1 COG0423
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ...
1-505 0e+00

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: 724.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    1 AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHE 80
Cdd:COG0423   3 SEDTMEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSPIIMPPKVWEASGHV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   81 ATFADPMVDNRITKKRYRLDHLLKEqpeevlkrlyramEVEEENLHALvqammqAPERAGGAMTAAGVLDPASGEPgDWT 160
Cdd:COG0423  83 DGFTDPLVDCKECKKRYRADHLIEE-------------YLAIEDAEGL------SLEELEELIKENNIKCPNCGGK-ELT 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  161 PPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEI 240
Cdd:COG0423 143 EVRQFNLMFKTNIGPVEDESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMEL 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  241 EYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHT 320
Cdd:COG0423 223 EFFVDPGTDNEWFAYWLALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQ 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  321 kdqealgitarvlrnEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELpNGEERIVLKLKPQLAPIK 400
Cdd:COG0423 303 ---------------EYSGKDLTYFDPETGEKYIPHVIEPSFGVDRLLLAFLEHAYTEEEV-DGEERTVLKLPPRLAPIK 366
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  401 VAVIPLVKnRPEITEYAKRLKARLLAlgLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGqskdgttrlKDTVTVR 480
Cdd:COG0423 367 VAVLPLVK-KDGLVEKAREIYDELRK--AFNVEYDDSGSIGRRYRRQDEIGTPFCVTVDFDTLE---------DNTVTIR 434
                       490       500
                ....*....|....*....|....*
gi 2392170  481 DRDTMEQIRLHVDELEGFLRERLRW 505
Cdd:COG0423 435 DRDTMEQERVPIDELKAYLAELLKG 459
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
2-503 0e+00

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 716.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170     2 ASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEA 81
Cdd:PRK04173   1 MDKMEKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSPIIMPPEVWEASGHVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    82 TFADPMVDNRITKKRYRLDHLLkeqpEEVLKRLYRAMEVEEENLhalvqammqaperaggaMTAAGVLDPASGEPGdWTP 161
Cdd:PRK04173  81 NFSDPLVECKKCKKRYRADHLI----EELGIDAEGLSNEELKEL-----------------IRENDIKCPECGGEN-WTE 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   162 PRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIE 241
Cdd:PRK04173 139 VRQFNLMFKTFIGPVEDSKSLGYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   242 YFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSL--ELEGIAQRTDFDLGSH 319
Cdd:PRK04173 219 FFVKPGTDNEWFAYWIELRKNWLLDLGIDPENLRFREHLPEELAHYSKATWDIEYKFPFGRFwgELEGIANRTDYDLSRH 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   320 TKdqealgitarvlrneHSTQRLAY-RDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAP 398
Cdd:PRK04173 299 SK---------------HSGEDLSYfDDETTGEKYIPYVIEPSAGLDRLLLAFLEDAYTEEELGGGDKRTVLRLPPALAP 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   399 IKVAVIPLVKNRpEITEYAKRLKARLLAlgLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGqskdgttrlKDTVT 478
Cdd:PRK04173 364 VKVAVLPLVKKE-KLSEKAREIYAELRK--DFNVDYDDSGSIGKRYRRQDEIGTPFCITVDFDTLE---------DNTVT 431
                        490       500
                 ....*....|....*....|....*
gi 2392170   479 VRDRDTMEQIRLHVDELEGFLRERL 503
Cdd:PRK04173 432 IRDRDTMEQVRVKIDELKDYLAEKL 456
PRK14894 PRK14894
glycyl-tRNA synthetase; Provisional
2-504 0e+00

glycyl-tRNA synthetase; Provisional


Pssm-ID: 237851 [Multi-domain]  Cd Length: 539  Bit Score: 576.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170     2 ASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEA 81
Cdd:PRK14894   3 ATSLDQIVALAKRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEGLDAAILMNRLVWKYSGHEE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    82 TFADPMVDNRITKKRYRLDHLlkeqpeevlkrlyrameveeenlhalvqammqaperaggamtaAGVLdPASGEPgDWTP 161
Cdd:PRK14894  83 TFNDPLVDCRDCKMRWRADHI-------------------------------------------QGVC-PNCGSR-DLTE 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   162 PRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIE 241
Cdd:PRK14894 118 PRPFNMMFRTQIGPVADSDSFAYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIE 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   242 YFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPH-GSLELEGIAQRTDFDLGSHT 320
Cdd:PRK14894 198 YFVMPGTDEEWHQRWLEARLAWWEQIGIPRSRITIYDVPPDELAHYSKRTFDLMYDYPNiGVQEIEGIANRTDYDLGSHS 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   321 KDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTR---------------------- 378
Cdd:PRK14894 278 KDQEQLNLTARVNPNEDSTARLTYFDQASGRHVVPYVIEPSAGVGRCMLAVMCEGYAEeltkaipgeklaavgdaleafl 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   379 -----------------------------EELPNGEE----------------------------RIVLKLKPQLAPIKV 401
Cdd:PRK14894 358 ksvgrseklageardailargeallqalpERLPEVEQllampgadqielgkklrgqaqplidehyRTVLRLKPRLAPIKV 437
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   402 AVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTtrLKDTVTVRD 481
Cdd:PRK14894 438 AVFPLKRNHEGLVATAKAVRRQLQVGGRMRTVYDDTGAIGKLYRRQDEIGTPFCITVDFDTIGQGKDPA--LAGTVTVRD 515
                        570       580
                 ....*....|....*....|...
gi 2392170   482 RDTMEQIRLHVDELEGFLRERLR 504
Cdd:PRK14894 516 RDTMAQERVPISELEAYLRDRVS 538
glyS_dimeric TIGR00389
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ...
3-503 3.10e-145

glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct from the two alpha and two beta chains of the tetrameric E. coli glycyl-tRNA synthetase. This enzyme is a homodimeric class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes His, Ser, Pro, and this set of glycyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273051 [Multi-domain]  Cd Length: 551  Bit Score: 427.73  E-value: 3.10e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170      3 SSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYErDDMEGLDASVLTHRLVLHYSGHEAT 82
Cdd:TIGR00389   1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFIKN-ERVLEIDTPIITPEEVLKASGHVDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170     83 FADPMVDNRITKKRYRLDHLLkeqpEEVLKRLYRAMEVEEENLhalvqammqaperaggAMTAAGVLDPASGEpGDWTPP 162
Cdd:TIGR00389  80 FTDWMVDCKSCKERFRADHLI----EEKLGKRLWGFSGPELNE----------------VMEKYDINCPNCGG-ENLTEV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    163 RYFNMMFQDLRGPRGGRglLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEY 242
Cdd:TIGR00389 139 RSFNLMFQTEIGVVGKR--KGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEF 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    243 FVRPGEDEY-WHRYWVEERLKWW----------------------------------QEMGLSRENLVPYQQPPESSAHY 287
Cdd:TIGR00389 217 FVHPLDKSHpKFEEVKQDILPLLprqmqesgigeavesgmienetlgyfiarvkqflLEIGINPDKLRFRQHDKNEMAHY 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    288 AKATVDILYRFPHGSLELEGIAQRTDFDLGSHTK-----------DQEALGITARVLRNEHSTQRLAYR----------- 345
Cdd:TIGR00389 297 AKDCWDFEFLTPYGWIECVGIADRGDYDLTQHSKfsgkslsvfdkLDEPREVTKWEIEPNKKKFGPKFRkdakkiesnls 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    346 -----------------------------DPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELpNGEERIVLKLKPQL 396
Cdd:TIGR00389 377 eddleereeeldkneveldkdlveiemvtEVVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEVL-DGEEREVLRLPPHL 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    397 APIKVAVIPLVkNRPEITEYAKRLkARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIgqsKDGttrlkdT 476
Cdd:TIGR00389 456 APIKVAVLPLV-NKEELKEIAKEI-FQALRKTGIRIKYDDSGTIGKRYRRADEIGTPFCVTIDFETL---EDE------T 524
                         570       580
                  ....*....|....*....|....*..
gi 2392170    477 VTVRDRDTMEQIRLHVDELEGFLRERL 503
Cdd:TIGR00389 525 VTIRERDSMKQVRVKIKELPSYIKKLL 551
GlyRS-like_core cd00774
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ...
8-372 6.69e-120

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: 351.89  E-value: 6.69e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    8 LVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLvlhysgheatfadpm 87
Cdd:cd00774   1 LVELAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPEL--------------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   88 vdnritkkryrldhllkeqpeevlkrlyrameveeenlhalvqammqaperaggamtaagvldpasgepgdwtppryfnm 167
Cdd:cd00774     --------------------------------------------------------------------------------
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  168 MFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPG 247
Cdd:cd00774  66 MFKTSIGPVESGGNLGYLRPETAQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPE 145
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  248 EDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHTKdqealg 327
Cdd:cd00774 146 KSHPWFDYWADQRLKWLPKFAQSPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPN------ 219
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 2392170  328 itarvlrneHSTQRLAYRDPETgKWFVPYVIEPSAGVDRGVLALL 372
Cdd:cd00774 220 ---------ESAHYASDCWDAE-KLYVPGWIEVSGGADRTDYDLL 254
PLN02734 PLN02734
glycyl-tRNA synthetase
8-501 1.43e-96

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 306.67  E-value: 1.43e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170     8 LVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLkQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPM 87
Cdd:PLN02734  78 VVNTLERRLFYIPSFKIYGGVAGLYDYGPPGCAVKSNV-LAFWRQHFVLEENMLEVECPCVTPEVVLKASGHVDKFTDLM 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    88 VDNRITKKRYRLDHLLKEQPEEVL-KRLYRAMEVEEENLHALVQAMMQAPERAGGAMTAAGVLDPASGEPgdWTPPRYFN 166
Cdd:PLN02734 157 VKDEKTGTCFRADHLLKDFCEEKLeKDLTISAEKAAELKDVLAVLDDLSAEELGAKIKEYGIKAPDTKNP--LSDPYPFN 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   167 MMFQDLRGPRGGrgLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRP 246
Cdd:PLN02734 235 LMFQTSIGPSGL--SVGYMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVDP 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   247 gEDEYwHRYWVE------------------------------------ERLKWW--------QEMGLSRENLVPYQQPPE 282
Cdd:PLN02734 313 -EDKS-HPKFSEvadlefllfpreeqlggqkakpmrlgeavskgivnnETLGYFigrtylflTKLGIDKERLRFRQHLAN 390
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   283 SSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHT------------------------------------KDQ--- 323
Cdd:PLN02734 391 EMAHYAADCWDAEIECSYGWIECVGIADRSAYDLKAHSdkskvplvahekfaeprevevlvivpnkkelglafkGDQkvv 470
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   324 ----------EALGITARVLRNEHSTQRLAY-----------------RDPETGKWFVPYVIEPSAGVDRGVLALLAEAF 376
Cdd:PLN02734 471 vealeamnekEAMEMKAKLESKGEAEFYVCTlgkeveikknmvsiskeKKKEHQRVFTPSVIEPSFGIGRIIYCLFEHSF 550
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   377 -TReelPNGEERIVLKLKPQLAPIKVAVIPLVKNrPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFA 455
Cdd:PLN02734 551 yTR---PGDEQLNVFRFPPLVAPIKCTVFPLVQN-QQLNAVAKVISKELTAAGISHKIDITGTSIGKRYARTDELGVPFA 626
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*.
gi 2392170   456 VTVDYDTigqskdgttrlkdTVTVRDRDTMEQIRLHVDELEGFLRE 501
Cdd:PLN02734 627 VTVDSDG-------------SVTIRERDSKDQVRVPVEEVASVVKD 659
GlyRS_anticodon cd00858
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ...
371-504 2.37e-52

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: 173.13  E-value: 2.37e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  371 LLAEAFTREElpNGEERIVLKLKPQLAPIKVAVIPLVKnRPEITEYAKRLKARLLALGLgRVLYEDTGNIGKAYRRHDEV 450
Cdd:cd00858   1 LLEHSFRVRE--GDEGRIVLRLPPALAPIKVAVLPLVK-RDELVEIAKEISEELRELGF-SVKYDDSGSIGRRYARQDEI 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 2392170  451 GTPFAVTVDYDTIGqskdgttrlKDTVTVRDRDTMEQIRLHVDELEGFLRERLR 504
Cdd:cd00858  77 GTPFCVTVDFDTLE---------DGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
Gly_His_Pro_Ser_Thr_tRS_core cd00670
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ...
160-372 5.45e-49

Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.


Pssm-ID: 238359 [Multi-domain]  Cd Length: 235  Bit Score: 168.34  E-value: 5.45e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  160 TPPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATsRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQME 239
Cdd:cd00670  40 HLDGYRKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSGEILSY-RALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVE 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  240 IEYFVRPGEDEYWHRYWVEERLKWWQEMGLsreNLVPYQQPPESSA--------HYAKATVDILYRFPH--GSLELEGIA 309
Cdd:cd00670 119 YVVFGEPEEAEEERREWLELAEEIARELGL---PVRVVVADDPFFGrggkrgldAGRETVVEFELLLPLpgRAKETAVGS 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2392170  310 QRTDFDLGSHTKdqealgitarvlrnehstqrlayRDPETGKWFVPYVIEPSAGVDRGVLALL 372
Cdd:cd00670 196 ANVHLDHFGASF-----------------------KIDEDGGGRAHTGCGGAGGEERLVLALL 235
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
163-366 3.11e-39

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.


Pssm-ID: 238391 [Multi-domain]  Cd Length: 211  Bit Score: 141.49  E-value: 3.11e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  163 RYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLdatsRKLGFGIAQIGKAFRNEITPRNFiFRVREFEQMEIEY 242
Cdd:cd00768  33 EKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHI----RKLPLRLAEIGPAFRNEGGRRGL-RRVREFTQLEGEV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  243 FVRPGEDEYWHRYWVEERLKWWQEMGLsRENLVPYQQPPES-SAHYAKATVDILYRFP-HGSLELEGIAQRTDFDLGSHT 320
Cdd:cd00768 108 FGEDGEEASEFEELIELTEELLRALGI-KLDIVFVEKTPGEfSPGGAGPGFEIEVDHPeGRGLEIGSGGYRQDEQARAAD 186
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 2392170  321 KdqealgitarvlrnehstqrlaYRDPETGKWFVPYVIEPSAGVDR 366
Cdd:cd00768 187 L----------------------YFLDEALEYRYPPTIGFGLGLER 210
HGTP_anticodon cd00738
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
398-500 1.15e-30

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: 114.42  E-value: 1.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  398 PIKVAVIPLVKNRPEITEYAKRLKARLLALGLgRVLYEDTG-NIGKAYRRHDEVGTPFAVTVDYDTIGqskdgttrlKDT 476
Cdd:cd00738   1 PIDVAIVPLTDPRVEAREYAQKLLNALLANGI-RVLYDDRErKIGKKFREADLRGVPFAVVVGEDELE---------NGK 70
                        90       100
                ....*....|....*....|....
gi 2392170  477 VTVRDRDTMEQIRLHVDELEGFLR 500
Cdd:cd00738  71 VTVKSRDTGESETLHVDELPEFLV 94
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
400-502 9.25e-25

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: 98.04  E-value: 9.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    400 KVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIgqskdgttrLKDTVTV 479
Cdd:pfam03129   1 QVVVIPLGEKAEELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKEL---------EEGTVTV 71
                          90       100
                  ....*....|....*....|...
gi 2392170    480 RDRDTMEQIRLHVDELEGFLRER 502
Cdd:pfam03129  72 RRRDTGEQETVSLDELVEKLKEL 94
Pol_gamma_b_Cterm cd02426
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ...
367-499 6.18e-08

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: 51.27  E-value: 6.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  367 GVLALLAeaFTREElpnGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLgRV----LYEDTGNIGK 442
Cdd:cd02426   1 AQLAELS--DGRKK---GRQRQVLKLHPCLAPYKVAIDCGKGDTAELRDLCQGLKNELREAGL-SVwpgyLETQHSSLEQ 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2392170  443 AYRRHDEVGTPFAVTVDYDTIgqsKDGTTRLkdtvtvRDRDTMEQIRLHVDELEGFL 499
Cdd:cd02426  75 LLDKYDEMGVLFTLLISEQTL---ENGLLQL------RSRDTTLKETIHISDLPDYL 122
ProRS_anticodon_zinc cd00862
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ...
390-503 9.57e-06

ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS 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, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.


Pssm-ID: 238439 [Multi-domain]  Cd Length: 202  Bit Score: 46.52  E-value: 9.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170  390 LKLKPQLAPIKVAVIPLVK---NRPEITEYAKRLKARLLALGLgRVLYEDTGNIGKAYRRHD-EV-GTPFAVtvdydTIG 464
Cdd:cd00862   2 LVLPPRVAPIQVVIVPIGIkdeKREEVLEAADELAERLKAAGI-RVHVDDRDNYTPGWKFNDwELkGVPLRI-----EIG 75
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2392170  465 qSKDgttRLKDTVTVRDRDTMEQIRLHVDELEGFLRERL 503
Cdd:cd00862  76 -PRD---LEKNTVVIVRRDTGEKKTVPLAELVEKVPELL 110
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
395-504 1.52e-04

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 44.30  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170   395 QLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLgRVLYEDtgnigkayRrhDE-----------VGTPFAVTVdydti 463
Cdd:PRK09194 465 AIAPFDVHIVPVNMKDEEVKELAEKLYAELQAAGI-EVLLDD--------R--KErpgvkfadadlIGIPHRIVV----- 528
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 2392170   464 gqskdGTTRLKD-TVTVRDRDTMEQIRLHVDELEGFLRERLR 504
Cdd:PRK09194 529 -----GDRGLAEgIVEYKDRRTGEKEEVPVDELVEFLKALKK 565
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
184-270 2.82e-03

tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.


Pssm-ID: 395469 [Multi-domain]  Cd Length: 181  Bit Score: 38.93  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392170    184 YLRPETAQGIFVNFKNVLDaTSRKLGFGIAQIGKAFRNEiTPRNF--IFRVREFEQMEIEYFVRPGE--DEYwhRYWVEE 259
Cdd:pfam00587  12 ALKPTNEPGHTLLFREEGL-RSKDLPLKLAQFGTCFRHE-ASGDTrgLIRVRQFHQDDAHIFHAPGQspDEL--EDYIKL 87
                          90
                  ....*....|.
gi 2392170    260 RLKWWQEMGLS 270
Cdd:pfam00587  88 IDRVYSRLGLE 98
 
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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