|
Name |
Accession |
Description |
Interval |
E-value |
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
1-459 |
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: 847.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 1 MALKYTIEQLNAYAKRYGFVYQGSEIYGGLANTWDYGPLGVELKNNIKKFWWKRFVSQNKYNVGIDSSILLNPKVWEATG 80
Cdd:COG0423 1 MASEDTMEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSPIIMPPKVWEASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 81 HVAGFKDPLMDCKVCKARHRADNLIAQSSKsEVDADGWDYQKMYDYIIEHKIKCPNCGSVDYTEIREFNLMFKTSQGVTQ 160
Cdd:COG0423 81 HVDGFTDPLVDCKECKKRYRADHLIEEYLA-IEDAEGLSLEELEELIKENNIKCPNCGGKELTEVRQFNLMFKTNIGPVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 161 ESNNEIYLRPETAQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFCVPGTEMEWFGYWK 240
Cdd:COG0423 160 DESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVDPGTDNEWFAYWL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 241 NFAKEFLVEIGLKPESIKFYDHPAEKLSFYSNATTDVLYNFPWGFDELWGIASRTDYDLKRHQEYSGENLEYLDPVTNET 320
Cdd:COG0423 240 ALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDLTYFDPETGEK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 321 YLPYVIEPSLGVERLFLAVLLDNLEDETLeDGEIRTLLKINKELAPYQVNVLPLVKKY-HTEKSEEVYEQLMKNFVAFYD 399
Cdd:COG0423 320 YIPHVIEPSFGVDRLLLAFLEHAYTEEEV-DGEERTVLKLPPRLAPIKVAVLPLVKKDgLVEKAREIYDELRKAFNVEYD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 400 DAGNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLKKQFD 459
Cdd:COG0423 399 DSGSIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTIRDRDTMEQERVPIDELKAYLAELLK 458
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
6-458 |
0e+00 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 812.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 6 TIEQLNAYAKRYGFVYQGSEIYGGLANTWDYGPLGVELKNNIKKFWWKRFVSQNKYNVGIDSSILLNPKVWEATGHVAGF 85
Cdd:PRK04173 3 KMEKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSPIIMPPEVWEASGHVDNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 86 KDPLMDCKVCKARHRADNLIaQSSKSEVDADGWDyqKMYDYIIEHKIKCPNCGSVDYTEIREFNLMFKTSQGVTQESNNE 165
Cdd:PRK04173 83 SDPLVECKKCKKRYRADHLI-EELGIDAEGLSNE--ELKELIRENDIKCPECGGENWTEVRQFNLMFKTFIGPVEDSKSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 166 IYLRPETAQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFCVPGTEMEWFGYWKNFAKE 245
Cdd:PRK04173 160 GYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVKPGTDNEWFAYWIELRKN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 246 FLVEIGLKPESIKFYDHPAEKLSFYSNATTDVLYNFPWG--FDELWGIASRTDYDLKRHQEYSGENLEYLDP-VTNETYL 322
Cdd:PRK04173 240 WLLDLGIDPENLRFREHLPEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHSKHSGEDLSYFDDeTTGEKYI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 323 PYVIEPSLGVERLFLAVLLDNLEDETLEDGEIRTLLKINKELAPYQVNVLPLVKK-YHTEKSEEVYEQLMKNFVAFYDDA 401
Cdd:PRK04173 320 PYVIEPSAGLDRLLLAFLEDAYTEEELGGGDKRTVLRLPPALAPVKVAVLPLVKKeKLSEKAREIYAELRKDFNVDYDDS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308460433 402 GNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLKKQF 458
Cdd:PRK04173 400 GSIGKRYRRQDEIGTPFCITVDFDTLEDNTVTIRDRDTMEQVRVKIDELKDYLAEKL 456
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
5-456 |
1.66e-175 |
|
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: 503.22 E-value: 1.66e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 5 YTIEQLNAYAKRYGFVYQGSEIYGGLANTWDYGPLGVELKNNIKKFWWKRFVsQNKYNVGIDSSILLNPKVWEATGHVAG 84
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFI-KNERVLEIDTPIITPEEVLKASGHVDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 85 FKDPLMDCKVCKARHRADNLIAQssKSEVDADGWDYQKMYDYIIEHKIKCPNCGSVDYTEIREFNLMFKTSQGVTQESnn 164
Cdd:TIGR00389 80 FTDWMVDCKSCKERFRADHLIEE--KLGKRLWGFSGPELNEVMEKYDINCPNCGGENLTEVRSFNLMFQTEIGVVGKR-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 165 EIYLRPETAQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFCVPG-TEMEWFGYWKN-- 241
Cdd:TIGR00389 156 KGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHPLdKSHPKFEEVKQdi 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 242 --------------------------------FAKEFLVEIGLKPESIKFYDHPAEKLSFYSNATTDVLYNFPWGFDELW 289
Cdd:TIGR00389 236 lpllprqmqesgigeavesgmienetlgyfiaRVKQFLLEIGINPDKLRFRQHDKNEMAHYAKDCWDFEFLTPYGWIECV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 290 GIASRTDYDLKRHQEYSGENLEYLDP------------------------------------------------------ 315
Cdd:TIGR00389 316 GIADRGDYDLTQHSKFSGKSLSVFDKldeprevtkweiepnkkkfgpkfrkdakkiesnlseddleereeeldkneveld 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 316 ------------VTNETYLPYVIEPSLGVERLFLAVLLDNLEDETLEDGEiRTLLKINKELAPYQVNVLPLVKKYH-TEK 382
Cdd:TIGR00389 396 kdlveiemvtevVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEVLDGEE-REVLRLPPHLAPIKVAVLPLVNKEElKEI 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308460433 383 SEEVYEQLMKN-FVAFYDDAGNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLKK 456
Cdd:TIGR00389 475 AKEIFQALRKTgIRIKYDDSGTIGKRYRRADEIGTPFCVTIDFETLEDETVTIRERDSMKQVRVKIKELPSYIKK 549
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
13-340 |
2.65e-118 |
|
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: 346.50 E-value: 2.65e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 13 YAKRYGFVYQGSEIYGGLANTWDYGPLGVELKNNIKKFWWKRFVSQNKYNVGIDSSILLNPkvweatghvagfkdplmdc 92
Cdd:cd00774 4 LAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPE------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 93 kvckarhradnliaqssksevdadgwdyqkmydyiiehkikcpncgsvdyteirefnLMFKTSQGVTQESNNEIYLRPET 172
Cdd:cd00774 65 ---------------------------------------------------------LMFKTSIGPVESGGNLGYLRPET 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 173 AQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFCVPGTEMEWFGYWKNFAKEFLVEIGL 252
Cdd:cd00774 88 AQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQ 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 253 KPESIKFYDHPAEKLSFYSNATTDVLYNFPWGFDELWGIASRTDYDLKRHQEYSGENLEYLDPVTnETYLPYVIEPSLGV 332
Cdd:cd00774 168 SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHYASDCWDAE-KLYVPGWIEVSGGA 246
|
....*...
gi 1308460433 333 ERLFLAVL 340
Cdd:cd00774 247 DRTDYDLL 254
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
368-457 |
2.60e-24 |
|
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: 96.50 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 368 QVNVLPLVKKY--HTEKSEEVYEQLMKN--FVAFYDDAGNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQV 443
Cdd:pfam03129 1 QVVVIPLGEKAeeLEEYAQKLAEELRAAgiRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 1308460433 444 RVALKELNQYLKKQ 457
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GRS1 |
COG0423 |
Glycyl-tRNA synthetase, class II [Translation, ribosomal structure and biogenesis]; ... |
1-459 |
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: 847.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 1 MALKYTIEQLNAYAKRYGFVYQGSEIYGGLANTWDYGPLGVELKNNIKKFWWKRFVSQNKYNVGIDSSILLNPKVWEATG 80
Cdd:COG0423 1 MASEDTMEKIVSLAKRRGFVFPSSEIYGGLAGFYDYGPLGVELKNNIKEAWWKSFVQRRDDVVGIDSPIIMPPKVWEASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 81 HVAGFKDPLMDCKVCKARHRADNLIAQSSKsEVDADGWDYQKMYDYIIEHKIKCPNCGSVDYTEIREFNLMFKTSQGVTQ 160
Cdd:COG0423 81 HVDGFTDPLVDCKECKKRYRADHLIEEYLA-IEDAEGLSLEELEELIKENNIKCPNCGGKELTEVRQFNLMFKTNIGPVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 161 ESNNEIYLRPETAQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFCVPGTEMEWFGYWK 240
Cdd:COG0423 160 DESSTGYLRPETAQGIFVNFKNVQRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVDPGTDNEWFAYWL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 241 NFAKEFLVEIGLKPESIKFYDHPAEKLSFYSNATTDVLYNFPWGFDELWGIASRTDYDLKRHQEYSGENLEYLDPVTNET 320
Cdd:COG0423 240 ALRKKWLLSLGIDPENLRFRDHLPEELAHYAKATWDIEYEFPFGWGELEGIAYRTDYDLSRHQEYSGKDLTYFDPETGEK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 321 YLPYVIEPSLGVERLFLAVLLDNLEDETLeDGEIRTLLKINKELAPYQVNVLPLVKKY-HTEKSEEVYEQLMKNFVAFYD 399
Cdd:COG0423 320 YIPHVIEPSFGVDRLLLAFLEHAYTEEEV-DGEERTVLKLPPRLAPIKVAVLPLVKKDgLVEKAREIYDELRKAFNVEYD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 400 DAGNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLKKQFD 459
Cdd:COG0423 399 DSGSIGRRYRRQDEIGTPFCVTVDFDTLEDNTVTIRDRDTMEQERVPIDELKAYLAELLK 458
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
6-458 |
0e+00 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 812.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 6 TIEQLNAYAKRYGFVYQGSEIYGGLANTWDYGPLGVELKNNIKKFWWKRFVSQNKYNVGIDSSILLNPKVWEATGHVAGF 85
Cdd:PRK04173 3 KMEKIVSLAKRRGFVFPSSEIYGGLAGFWDYGPLGVELKNNIKRAWWKSFVQEREDVVGIDSPIIMPPEVWEASGHVDNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 86 KDPLMDCKVCKARHRADNLIaQSSKSEVDADGWDyqKMYDYIIEHKIKCPNCGSVDYTEIREFNLMFKTSQGVTQESNNE 165
Cdd:PRK04173 83 SDPLVECKKCKKRYRADHLI-EELGIDAEGLSNE--ELKELIRENDIKCPECGGENWTEVRQFNLMFKTFIGPVEDSKSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 166 IYLRPETAQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFCVPGTEMEWFGYWKNFAKE 245
Cdd:PRK04173 160 GYLRPETAQGIFVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNFIFRTREFEQMELEFFVKPGTDNEWFAYWIELRKN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 246 FLVEIGLKPESIKFYDHPAEKLSFYSNATTDVLYNFPWG--FDELWGIASRTDYDLKRHQEYSGENLEYLDP-VTNETYL 322
Cdd:PRK04173 240 WLLDLGIDPENLRFREHLPEELAHYSKATWDIEYKFPFGrfWGELEGIANRTDYDLSRHSKHSGEDLSYFDDeTTGEKYI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 323 PYVIEPSLGVERLFLAVLLDNLEDETLEDGEIRTLLKINKELAPYQVNVLPLVKK-YHTEKSEEVYEQLMKNFVAFYDDA 401
Cdd:PRK04173 320 PYVIEPSAGLDRLLLAFLEDAYTEEELGGGDKRTVLRLPPALAPVKVAVLPLVKKeKLSEKAREIYAELRKDFNVDYDDS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308460433 402 GNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLKKQF 458
Cdd:PRK04173 400 GSIGKRYRRQDEIGTPFCITVDFDTLEDNTVTIRDRDTMEQVRVKIDELKDYLAEKL 456
|
|
| glyS_dimeric |
TIGR00389 |
glycyl-tRNA synthetase, dimeric type; This model describes a glycyl-tRNA synthetase distinct ... |
5-456 |
1.66e-175 |
|
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: 503.22 E-value: 1.66e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 5 YTIEQLNAYAKRYGFVYQGSEIYGGLANTWDYGPLGVELKNNIKKFWWKRFVsQNKYNVGIDSSILLNPKVWEATGHVAG 84
Cdd:TIGR00389 1 VNMEVIMSLLKRRGFVFQSFEIYGGLAGFWDYGPLGAVLKNNIKNAWRKFFI-KNERVLEIDTPIITPEEVLKASGHVDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 85 FKDPLMDCKVCKARHRADNLIAQssKSEVDADGWDYQKMYDYIIEHKIKCPNCGSVDYTEIREFNLMFKTSQGVTQESnn 164
Cdd:TIGR00389 80 FTDWMVDCKSCKERFRADHLIEE--KLGKRLWGFSGPELNEVMEKYDINCPNCGGENLTEVRSFNLMFQTEIGVVGKR-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 165 EIYLRPETAQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFCVPG-TEMEWFGYWKN-- 241
Cdd:TIGR00389 156 KGYLRPETAQGIFINFKRLLQFFRRKLPFGVAQIGKSFRNEISPRNGLFRVREFEQAEIEFFVHPLdKSHPKFEEVKQdi 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 242 --------------------------------FAKEFLVEIGLKPESIKFYDHPAEKLSFYSNATTDVLYNFPWGFDELW 289
Cdd:TIGR00389 236 lpllprqmqesgigeavesgmienetlgyfiaRVKQFLLEIGINPDKLRFRQHDKNEMAHYAKDCWDFEFLTPYGWIECV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 290 GIASRTDYDLKRHQEYSGENLEYLDP------------------------------------------------------ 315
Cdd:TIGR00389 316 GIADRGDYDLTQHSKFSGKSLSVFDKldeprevtkweiepnkkkfgpkfrkdakkiesnlseddleereeeldkneveld 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 316 ------------VTNETYLPYVIEPSLGVERLFLAVLLDNLEDETLEDGEiRTLLKINKELAPYQVNVLPLVKKYH-TEK 382
Cdd:TIGR00389 396 kdlveiemvtevVHGEKYIPHVIEPSFGIDRIIYALLEHSYQEEVLDGEE-REVLRLPPHLAPIKVAVLPLVNKEElKEI 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308460433 383 SEEVYEQLMKN-FVAFYDDAGNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLKK 456
Cdd:TIGR00389 475 AKEIFQALRKTgIRIKYDDSGTIGKRYRRADEIGTPFCVTIDFETLEDETVTIRERDSMKQVRVKIKELPSYIKK 549
|
|
| PRK14894 |
PRK14894 |
glycyl-tRNA synthetase; Provisional |
6-455 |
4.93e-144 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 237851 [Multi-domain] Cd Length: 539 Bit Score: 422.49 E-value: 4.93e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 6 TIEQLNAYAKRYGFVYQGSEIYGGLANTWDYGPLGVELKNNIKKFWWKRFVSQNKYNVGIDSSILLNPKVWEATGHVAGF 85
Cdd:PRK14894 5 SLDQIVALAKRRGFIFPSSEIYGGLQGVYDYGPLGVELKNNIIADWWRTNVYERDDMEGLDAAILMNRLVWKYSGHEETF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 86 KDPLMDCKVCKARHRADNLiaqssksevdadgwdyqkmydyiiehKIKCPNCGSVDYTEIREFNLMFKTSQGVTQESNNE 165
Cdd:PRK14894 85 NDPLVDCRDCKMRWRADHI--------------------------QGVCPNCGSRDLTEPRPFNMMFRTQIGPVADSDSF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 166 IYLRPETAQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFCVPGTEMEWFGYWKNFAKE 245
Cdd:PRK14894 139 AYLRPETAQGIFVNFANVLATSARKLPFGIAQVGKAFRNEINPRNFLFRVREFEQMEIEYFVMPGTDEEWHQRWLEARLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 246 FLVEIGLKPESIKFYDHPAEKLSFYSNATTDVLYNFP-WGFDELWGIASRTDYDLKRH---------------QEYSGEN 309
Cdd:PRK14894 219 WWEQIGIPRSRITIYDVPPDELAHYSKRTFDLMYDYPnIGVQEIEGIANRTDYDLGSHskdqeqlnltarvnpNEDSTAR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 310 LEYLDPVTNETYLPYVIEPSLGVERLFLAVLL--------------------DNLE-----------------DETLEDG 352
Cdd:PRK14894 299 LTYFDQASGRHVVPYVIEPSAGVGRCMLAVMCegyaeeltkaipgeklaavgDALEaflksvgrseklagearDAILARG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 353 E------------------------------------------IRTLLKINKELAPYQVNVLPLvKKYHTE---KSEEVY 387
Cdd:PRK14894 379 EallqalperlpeveqllampgadqielgkklrgqaqplidehYRTVLRLKPRLAPIKVAVFPL-KRNHEGlvaTAKAVR 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308460433 388 EQLM--KNFVAFYDDAGNIGRRYRRADAIGTPFCVTIDNQTLEDD-------TVTVRDRDTMEQVRVALKELNQYLK 455
Cdd:PRK14894 458 RQLQvgGRMRTVYDDTGAIGKLYRRQDEIGTPFCITVDFDTIGQGkdpalagTVTVRDRDTMAQERVPISELEAYLR 534
|
|
| GlyRS-like_core |
cd00774 |
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
13-340 |
2.65e-118 |
|
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: 346.50 E-value: 2.65e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 13 YAKRYGFVYQGSEIYGGLANTWDYGPLGVELKNNIKKFWWKRFVSQNKYNVGIDSSILLNPkvweatghvagfkdplmdc 92
Cdd:cd00774 4 LAKRRGFVFPSSEIYGGVAGFYDYGPLGVELKNNIKSAWRKSFVLEEEDMLEIDSPIITPE------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 93 kvckarhradnliaqssksevdadgwdyqkmydyiiehkikcpncgsvdyteirefnLMFKTSQGVTQESNNEIYLRPET 172
Cdd:cd00774 65 ---------------------------------------------------------LMFKTSIGPVESGGNLGYLRPET 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 173 AQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFCVPGTEMEWFGYWKNFAKEFLVEIGL 252
Cdd:cd00774 88 AQGIFVNFKNLLEFNRRKLPFGVAQIGKSFRNEISPRNGLFRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQ 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 253 KPESIKFYDHPAEKLSFYSNATTDVLYNFPWGFDELWGIASRTDYDLKRHQEYSGENLEYLDPVTnETYLPYVIEPSLGV 332
Cdd:cd00774 168 SPENLRLTDHEKEELAHYANETLDYFYAFPHGFLELEGIANRGDRFLQHHPNESAHYASDCWDAE-KLYVPGWIEVSGGA 246
|
....*...
gi 1308460433 333 ERLFLAVL 340
Cdd:cd00774 247 DRTDYDLL 254
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
25-456 |
2.41e-62 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 214.22 E-value: 2.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 25 EIYGGLANTWDYGPLGVELKNNIKKFWWKRFV-SQNKYNVgiDSSILLNPKVWEATGHVAGFKDpLM-------DC---- 92
Cdd:PLN02734 93 KIYGGVAGLYDYGPPGCAVKSNVLAFWRQHFVlEENMLEV--ECPCVTPEVVLKASGHVDKFTD-LMvkdektgTCfrad 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 93 ----KVCKARHRADNLIAQSSKSEVD-----ADGWDYQKMYDYIIEHKIKCPNCGSvDYTEIREFNLMFKTSQGVTQESN 163
Cdd:PLN02734 170 hllkDFCEEKLEKDLTISAEKAAELKdvlavLDDLSAEELGAKIKEYGIKAPDTKN-PLSDPYPFNLMFQTSIGPSGLSV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 164 NeiYLRPETAQGIFLNFKNIVRTSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFC------------VPGT 231
Cdd:PLN02734 249 G--YMRPETAQGIFVNFRDLYYYNGGKLPFAAAQIGQAFRNEISPRQGLLRVREFTLAEIEHFVdpedkshpkfseVADL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 232 EM------------------------------EWFGYWKNFAKEFLVEIGLKPESIKFYDHPAEKLSFYSNATTDVLYNF 281
Cdd:PLN02734 327 EFllfpreeqlggqkakpmrlgeavskgivnnETLGYFIGRTYLFLTKLGIDKERLRFRQHLANEMAHYAADCWDAEIEC 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 282 PWGFDELWGIASRTDYDLKRHQEYSG---------------------------------------ENLEYLD-------- 314
Cdd:PLN02734 407 SYGWIECVGIADRSAYDLKAHSDKSKvplvahekfaeprevevlvivpnkkelglafkgdqkvvvEALEAMNekeamemk 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 315 ----------------------------------PVTNETYLPYVIEPSLGVERLFLAVLLDNLedETLEDGEIRTLLKI 360
Cdd:PLN02734 487 akleskgeaefyvctlgkeveikknmvsiskekkKEHQRVFTPSVIEPSFGIGRIIYCLFEHSF--YTRPGDEQLNVFRF 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 361 NKELAPYQVNVLPLVKKYH-TEKSEEVYEQLMKNFVAFYDD--AGNIGRRYRRADAIGTPFCVTIDNqtleDDTVTVRDR 437
Cdd:PLN02734 565 PPLVAPIKCTVFPLVQNQQlNAVAKVISKELTAAGISHKIDitGTSIGKRYARTDELGVPFAVTVDS----DGSVTIRER 640
|
570
....*....|....*....
gi 1308460433 438 DTMEQVRVALKELNQYLKK 456
Cdd:PLN02734 641 DSKDQVRVPVEEVASVVKD 659
|
|
| GlyRS_anticodon |
cd00858 |
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ... |
347-456 |
4.32e-48 |
|
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: 161.19 E-value: 4.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 347 ETLEDGEIRTLLKINKELAPYQVNVLPLVKKYH-TEKSEEVYEQLMKN-FVAFYDDAGNIGRRYRRADAIGTPFCVTIDN 424
Cdd:cd00858 7 RVREGDEGRIVLRLPPALAPIKVAVLPLVKRDElVEIAKEISEELRELgFSVKYDDSGSIGRRYARQDEIGTPFCVTVDF 86
|
90 100 110
....*....|....*....|....*....|..
gi 1308460433 425 QTLEDDTVTVRDRDTMEQVRVALKELNQYLKK 456
Cdd:cd00858 87 DTLEDGTVTIRERDSMRQVRVKIEELPSYLRE 118
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
368-457 |
2.60e-24 |
|
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: 96.50 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 368 QVNVLPLVKKY--HTEKSEEVYEQLMKN--FVAFYDDAGNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQV 443
Cdd:pfam03129 1 QVVVIPLGEKAeeLEEYAQKLAEELRAAgiRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 1308460433 444 RVALKELNQYLKKQ 457
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
146-335 |
3.81e-24 |
|
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: 99.88 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 146 REFNLMFKTSQGVTQESNNEIYLRPETAQGIFLNFKNIVRtsrkKVPFGIGQVGKSFRNEITPgNFVFRTREFEQMELEF 225
Cdd:cd00768 33 EKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIR----KLPLRLAEIGPAFRNEGGR-RGLRRVREFTQLEGEV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 226 FCVPGTEMEWFGYWKNFAKEFLVEIGLKPESIKFYDHPAEKLSFYSNATTDVLYNFPWG-FDELWGIASRTDYDLKRHQE 304
Cdd:cd00768 108 FGEDGEEASEFEELIELTEELLRALGIKLDIVFVEKTPGEFSPGGAGPGFEIEVDHPEGrGLEIGSGGYRQDEQARAADL 187
|
170 180 190
....*....|....*....|....*....|..
gi 1308460433 305 YS-GENLEYLdpvtnetyLPYVIEPSLGVERL 335
Cdd:cd00768 188 YFlDEALEYR--------YPPTIGFGLGLERL 211
|
|
| 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 ... |
148-340 |
2.72e-21 |
|
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: 92.45 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 148 FNLMFKTSQGVTQESNNEIYLRPETAQGIFLNFKNIVRtSRKKVPFGIGQVGKSFRNEITPGNFVFRTREFEQMELEFFC 227
Cdd:cd00670 45 RKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSGEIL-SYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVVFG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 228 VPGTEMEWFGYW----KNFAKEFLVEIGLKPESIKFYDHPA-EKLSFYSNATTDVLYNFPwGFDELWGIAS---RTDYDL 299
Cdd:cd00670 124 EPEEAEEERREWlelaEEIARELGLPVRVVVADDPFFGRGGkRGLDAGRETVVEFELLLP-LPGRAKETAVgsaNVHLDH 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1308460433 300 KRHQEYSGENLEylDPVtnetylPYVIEPSLGVERLFLAVL 340
Cdd:cd00670 203 FGASFKIDEDGG--GRA------HTGCGGAGGEERLVLALL 235
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
366-455 |
7.74e-17 |
|
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: 75.51 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 366 PYQVNVLPLVKKYH--TEKSEEVYEQLMKNFV-AFYDDAG-NIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTME 441
Cdd:cd00738 1 PIDVAIVPLTDPRVeaREYAQKLLNALLANGIrVLYDDRErKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|....
gi 1308460433 442 QVRVALKELNQYLK 455
Cdd:cd00738 81 SETLHVDELPEFLV 94
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
329-459 |
2.30e-08 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 55.90 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 329 SLGVERLFLAvlldnLEDETLEDGEIRTLlkinkelapyQVNVLPLvkkyhTEKSEEVYEQLMKNF------VAFYDDAG 402
Cdd:COG0124 305 AIGLERLLLL-----LEELGLLPAAEPPP----------DVYVVPL-----GEEARAEALKLAQELraagirVELDLGGR 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308460433 403 NIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLKKQFD 459
Cdd:COG0124 365 KLKKQLKYADKSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
362-456 |
2.76e-08 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 55.86 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 362 KELAPYQVNVLPLVKKYHT--EKSEEVYEQLMKNFV-AFYDDagnigrRYRR-----ADA--IGTPFCVTIDNQTLEDDT 431
Cdd:PRK09194 464 KAIAPFDVHIVPVNMKDEEvkELAEKLYAELQAAGIeVLLDD------RKERpgvkfADAdlIGIPHRIVVGDRGLAEGI 537
|
90 100
....*....|....*....|....*
gi 1308460433 432 VTVRDRDTMEQVRVALKELNQYLKK 456
Cdd:PRK09194 538 VEYKDRRTGEKEEVPVDELVEFLKA 562
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
309-457 |
3.96e-08 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 55.65 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 309 NLEYLDPVTNETYlPYVIE--PSLGVERlFLAVLLDNLEDETlEDGEIRTLlkiNKELAPYQVNVLPlVKKYHTEKSEEV 386
Cdd:PRK03991 446 GIKYVDENGEEKY-PIILHcsPTGSIER-VIYALLEKAAKEE-EEGKVPML---PTWLSPTQVRVIP-VSERHLDYAEEV 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308460433 387 YEQLMKN-FVAFYDDAG-NIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLKKQ 457
Cdd:PRK03991 519 ADKLEAAgIRVDVDDRDeSLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEELIERIKEE 591
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
366-455 |
4.04e-08 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. 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.
Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 50.67 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 366 PYQVNVLPLVKKY--HTEKSEEVYEQLMKNFV-AFYDDAGN-IGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTME 441
Cdd:cd00861 1 PFDVVIIPMNMKDevQQELAEKLYAELQAAGVdVLLDDRNErPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTGE 80
|
90
....*....|....
gi 1308460433 442 QVRVALKELNQYLK 455
Cdd:cd00861 81 KEEISIDELLEFLQ 94
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
401-455 |
1.08e-06 |
|
HisRS Histidyl-anticodon binding domain. HisRS 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: 238436 [Multi-domain] Cd Length: 91 Bit Score: 46.76 E-value: 1.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1308460433 401 AGNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLK 455
Cdd:cd00859 37 GRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVALDELVEELK 91
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
158-343 |
1.60e-06 |
|
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: 48.18 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 158 VTQESNNEIYLRPETAQGIFLNFKNIVRTSrKKVPFGIGQVGKSFRNEiTPGNF--VFRTREFEQMELEFFCVPGTEM-E 234
Cdd:pfam00587 3 VEDENGDELALKPTNEPGHTLLFREEGLRS-KDLPLKLAQFGTCFRHE-ASGDTrgLIRVRQFHQDDAHIFHAPGQSPdE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 235 WFGYWKnFAKEFLVEIGLKPESIKFYDHPaeKLSFYSNaTTDVLYNFPwGFDELWGIAS-RTDYDlkrhQEYSGENLEYL 313
Cdd:pfam00587 81 LEDYIK-LIDRVYSRLGLEVRVVRLSNSD--GSAFYGP-KLDFEVVFP-SLGKQRQTGTiQNDGF----RLPRRLGIRYK 151
|
170 180 190
....*....|....*....|....*....|.
gi 1308460433 314 DPvTNETYLPYVIEPS-LGVERlFLAVLLDN 343
Cdd:pfam00587 152 DE-DNESKFPYMIHRAgLGVER-FLAAILEN 180
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
366-450 |
6.96e-06 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS 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: 238437 [Multi-domain] Cd Length: 91 Bit Score: 44.42 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 366 PYQVNVLPlVKKYHTEKSEEVYEQLMK-NFVAFYDDAGN-IGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQV 443
Cdd:cd00860 1 PVQVVVIP-VTDEHLDYAKEVAKKLSDaGIRVEVDLRNEkLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79
|
....*..
gi 1308460433 444 RVALKEL 450
Cdd:cd00860 80 SMSLDEF 86
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
364-460 |
1.63e-05 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 46.76 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 364 LAPYQVNVLPlVKKYHTEKSEEVYEQLMKNF--VAFYDDAGNIGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTME 441
Cdd:PRK14938 272 LNPIQVRILP-VKKDFLDFSIQVAERLRKEGirVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRANNE 350
|
90
....*....|....*....
gi 1308460433 442 QVRVALKELNQYLKKQFDL 460
Cdd:PRK14938 351 QKSMTVEELVKEIKRADEL 369
|
|
| Pol_gamma_b_Cterm |
cd02426 |
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ... |
337-458 |
1.32e-04 |
|
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: 41.64 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 337 LAVLLDnledeTLEDGEIRTLLKINKELAPYQVNVLplVKKYHTEKSEEVYEQLMKNFVA---------FYDDAGNIGRR 407
Cdd:cd02426 3 LAELSD-----GRKKGRQRQVLKLHPCLAPYKVAID--CGKGDTAELRDLCQGLKNELREaglsvwpgyLETQHSSLEQL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1308460433 408 YRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTMEQVRVALKELNQYLKKQF 458
Cdd:cd02426 76 LDKYDEMGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYLLRYI 126
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
358-459 |
1.58e-04 |
|
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: 42.67 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 358 LKINKELAPYQVNVLPLVKKYHT-----EKSEEVYEQLMK-NFVAFYDDAGNI--GRRYRRADAIGTPFCVTIDNQTLED 429
Cdd:cd00862 2 LVLPPRVAPIQVVIVPIGIKDEKreevlEAADELAERLKAaGIRVHVDDRDNYtpGWKFNDWELKGVPLRIEIGPRDLEK 81
|
90 100 110
....*....|....*....|....*....|
gi 1308460433 430 DTVTVRDRDTMEQVRVALKELNQYLKKQFD 459
Cdd:cd00862 82 NTVVIVRRDTGEKKTVPLAELVEKVPELLD 111
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
364-457 |
2.33e-04 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 43.58 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460433 364 LAPYQVNVLPLVKKYHTEKSEEVYEQLMKNFVAFYDDAGN--IGRRYRRADAIGTPFCVTIDNQTLEDDTVTVRDRDTME 441
Cdd:PRK12444 539 LAPVQVKVIPVSNAVHVQYADEVADKLAQAGIRVERDERDekLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEK 618
|
90
....*....|....*.
gi 1308460433 442 QVRVALKELNQYLKKQ 457
Cdd:PRK12444 619 SEVIELDMFVESIKEE 634
|
|
| |
