|
Name |
Accession |
Description |
Interval |
E-value |
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-450 |
0e+00 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 770.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 1 MLDPILLRKDLQTVVDRLKSRGVDFDIARFNELESRRKAVQTETESQQARRNALAKQIGQLKGKGApeaEVQAVMAESQA 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGE---EAEALIAEVKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 81 LPARLKALEDELAQTQAQLNDLLMSVPNLPHASVPQGASSDENVEVRRWlpgaaderGIPAALGFEVRDHVAVGEPLG-L 159
Cdd:COG0172 78 LKEEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRW--------GEPREFDFEPKDHWELGEKLGiL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 160 DFDLAARLSGARFSFMRGQMARLHRALAQFMLDLQTgTHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFFVTKgggddep 239
Cdd:COG0172 150 DFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEG------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 240 kvdeqgnplarEDQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGSGGRDTRGMIRQHQFDKVEMVQIAHP 319
Cdd:COG0172 222 -----------DDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 320 EHSYEALEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRNAQ 399
Cdd:COG0172 291 EDSYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDED 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1142057827 400 NKPEYVHTLNGSGLAVGRALVAVLENCQQADGSVRVPAVLQPYMGGLTVLE 450
Cdd:COG0172 371 GKPEFVHTLNGSGLAVGRTLVAILENYQQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-451 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 753.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 1 MLDPILLRKDLQTVVDRLKSRGVDFDIARFNELESRRKAVQTETESQQARRNALAKQIGQLKGKGApeaEVQAVMAESQA 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGE---DAEALIAEVKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 81 LPARLKALEDELAQTQAQLNDLLMSVPNLPHASVPQGASSDENVEVRRWlpgaaderGIPAALGFEVRDHVAVGEPLG-L 159
Cdd:PRK05431 78 LKEEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRW--------GEPREFDFEPKDHWELGEKLGiL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 160 DFDLAARLSGARFSFMRGQMARLHRALAQFMLDLQTGTHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFFVTKgggddep 239
Cdd:PRK05431 150 DFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIED------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 240 kvdeqgnplarEDQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGSGGRDTRGMIRQHQFDKVEMVQIAHP 319
Cdd:PRK05431 223 -----------DDLYLIPTAEVPLTNLHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 320 EHSYEALEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRNA- 398
Cdd:PRK05431 292 EDSYAELEELTANAEEILQKLELPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEg 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1142057827 399 QNKPEYVHTLNGSGLAVGRALVAVLENCQQADGSVRVPAVLQPYMGGLTVLEP 451
Cdd:PRK05431 372 DGKPELVHTLNGSGLAVGRTLVAILENYQQADGSVTIPEVLRPYMGGLEVIPP 424
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-443 |
0e+00 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 543.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 1 MLDPILLRKDLQTVVDRLKSRGVDFDIA--RFNELESRRKAVQTETESQQARRNALAKQIGQLKGKGAPEAEvqAVMAES 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDIDleKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIE--EIKKEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 79 QALPARLKALEDELAQTQAQLNDLLMSVPNLPHASVPQGASSDENVEVRRWlpgaaderGIPAALGFEVRDHVAVGEPLG 158
Cdd:TIGR00414 79 KELKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRW--------GTPPVFDFKPKPHWELGEKLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 159 -LDFDLAARLSGARFSFMRGQMARLHRALAQFMLDLQTGtHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFfvtkgggdd 237
Cdd:TIGR00414 151 gLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEK-NGYQEIYPPYLVNEESLDGTGQLPKFEEDIF--------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 238 epKVDEqgnplarEDQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGSGGRDTRGMIRQHQFDKVEMVQIA 317
Cdd:TIGR00414 221 --KLED-------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 318 HPEHSYEALEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRN 397
Cdd:TIGR00414 292 KPEESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKD 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1142057827 398 AQN-KPEYVHTLNGSGLAVGRALVAVLENCQQADGSVRVPAVLQPYM 443
Cdd:TIGR00414 372 KNKgKNKYVHTLNGTALAIGRTIVAILENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
122-443 |
1.22e-161 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 457.79 E-value: 1.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 122 ENVEVRRWlpgaaderGIPAALGFEVRDHVAVGEPLG-LDFDLAARLSGARFSFMRGQMARLHRALAQFMLDLQTgTHGY 200
Cdd:cd00770 1 DNVEIRRW--------GEPRVFDFKPKDHVELGEKLDiLDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 201 TECYTPYIVNSSTLFGTGQLPKFKDDMFFVTkgggddepkvdeqgnplaREDQYLISTSEITLTSVVRETIVAGADLPLR 280
Cdd:cd00770 72 TPVIPPFLVRKEVMEGTGQLPKFDEQLYKVE------------------GEDLYLIATAEVPLAALHRDEILEEEELPLK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 281 LTAHTPCFRSEAGSGGRDTRGMIRQHQFDKVEMVQIAHPEHSYEALEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAK 360
Cdd:cd00770 134 YAGYSPCFRKEAGSAGRDTRGLFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 361 TYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRN-AQNKPEYVHTLNGSGLAVGRALVAVLENCQQADGSVRVPAVL 439
Cdd:cd00770 214 KYDIEAWMPGQGKYREISSCSNCTDFQARRLNIRYRDkKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVL 293
|
....
gi 1142057827 440 QPYM 443
Cdd:cd00770 294 RPYM 297
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
251-425 |
1.85e-45 |
|
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: 156.03 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 251 EDQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGsggRDTRGMIRQHQFDKVEMVQIAHPEHSYEALEEMV 330
Cdd:pfam00587 9 DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 331 GHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRNAQNKPEYVHTLNG 410
Cdd:pfam00587 86 KLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHR 165
|
170
....*....|....*
gi 1142057827 411 SGLAVGRALVAVLEN 425
Cdd:pfam00587 166 AGLGVERFLAAILEN 180
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-450 |
0e+00 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 770.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 1 MLDPILLRKDLQTVVDRLKSRGVDFDIARFNELESRRKAVQTETESQQARRNALAKQIGQLKGKGApeaEVQAVMAESQA 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGE---EAEALIAEVKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 81 LPARLKALEDELAQTQAQLNDLLMSVPNLPHASVPQGASSDENVEVRRWlpgaaderGIPAALGFEVRDHVAVGEPLG-L 159
Cdd:COG0172 78 LKEEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRW--------GEPREFDFEPKDHWELGEKLGiL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 160 DFDLAARLSGARFSFMRGQMARLHRALAQFMLDLQTgTHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFFVTKgggddep 239
Cdd:COG0172 150 DFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEG------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 240 kvdeqgnplarEDQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGSGGRDTRGMIRQHQFDKVEMVQIAHP 319
Cdd:COG0172 222 -----------DDLYLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 320 EHSYEALEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRNAQ 399
Cdd:COG0172 291 EDSYEELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDED 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1142057827 400 NKPEYVHTLNGSGLAVGRALVAVLENCQQADGSVRVPAVLQPYMGGLTVLE 450
Cdd:COG0172 371 GKPEFVHTLNGSGLAVGRTLVAILENYQQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-451 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 753.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 1 MLDPILLRKDLQTVVDRLKSRGVDFDIARFNELESRRKAVQTETESQQARRNALAKQIGQLKGKGApeaEVQAVMAESQA 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGE---DAEALIAEVKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 81 LPARLKALEDELAQTQAQLNDLLMSVPNLPHASVPQGASSDENVEVRRWlpgaaderGIPAALGFEVRDHVAVGEPLG-L 159
Cdd:PRK05431 78 LKEEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRW--------GEPREFDFEPKDHWELGEKLGiL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 160 DFDLAARLSGARFSFMRGQMARLHRALAQFMLDLQTGTHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFFVTKgggddep 239
Cdd:PRK05431 150 DFERAAKVSGSRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIED------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 240 kvdeqgnplarEDQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGSGGRDTRGMIRQHQFDKVEMVQIAHP 319
Cdd:PRK05431 223 -----------DDLYLIPTAEVPLTNLHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 320 EHSYEALEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRNA- 398
Cdd:PRK05431 292 EDSYAELEELTANAEEILQKLELPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEg 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1142057827 399 QNKPEYVHTLNGSGLAVGRALVAVLENCQQADGSVRVPAVLQPYMGGLTVLEP 451
Cdd:PRK05431 372 DGKPELVHTLNGSGLAVGRTLVAILENYQQADGSVTIPEVLRPYMGGLEVIPP 424
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-443 |
0e+00 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 543.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 1 MLDPILLRKDLQTVVDRLKSRGVDFDIA--RFNELESRRKAVQTETESQQARRNALAKQIGQLKGKGAPEAEvqAVMAES 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDIDleKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIE--EIKKEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 79 QALPARLKALEDELAQTQAQLNDLLMSVPNLPHASVPQGASSDENVEVRRWlpgaaderGIPAALGFEVRDHVAVGEPLG 158
Cdd:TIGR00414 79 KELKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRW--------GTPPVFDFKPKPHWELGEKLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 159 -LDFDLAARLSGARFSFMRGQMARLHRALAQFMLDLQTGtHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFfvtkgggdd 237
Cdd:TIGR00414 151 gLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEK-NGYQEIYPPYLVNEESLDGTGQLPKFEEDIF--------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 238 epKVDEqgnplarEDQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGSGGRDTRGMIRQHQFDKVEMVQIA 317
Cdd:TIGR00414 221 --KLED-------TDLYLIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 318 HPEHSYEALEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRN 397
Cdd:TIGR00414 292 KPEESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKD 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1142057827 398 AQN-KPEYVHTLNGSGLAVGRALVAVLENCQQADGSVRVPAVLQPYM 443
Cdd:TIGR00414 372 KNKgKNKYVHTLNGTALAIGRTIVAILENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
122-443 |
1.22e-161 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 457.79 E-value: 1.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 122 ENVEVRRWlpgaaderGIPAALGFEVRDHVAVGEPLG-LDFDLAARLSGARFSFMRGQMARLHRALAQFMLDLQTgTHGY 200
Cdd:cd00770 1 DNVEIRRW--------GEPRVFDFKPKDHVELGEKLDiLDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 201 TECYTPYIVNSSTLFGTGQLPKFKDDMFFVTkgggddepkvdeqgnplaREDQYLISTSEITLTSVVRETIVAGADLPLR 280
Cdd:cd00770 72 TPVIPPFLVRKEVMEGTGQLPKFDEQLYKVE------------------GEDLYLIATAEVPLAALHRDEILEEEELPLK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 281 LTAHTPCFRSEAGSGGRDTRGMIRQHQFDKVEMVQIAHPEHSYEALEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAK 360
Cdd:cd00770 134 YAGYSPCFRKEAGSAGRDTRGLFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 361 TYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRN-AQNKPEYVHTLNGSGLAVGRALVAVLENCQQADGSVRVPAVL 439
Cdd:cd00770 214 KYDIEAWMPGQGKYREISSCSNCTDFQARRLNIRYRDkKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVL 293
|
....
gi 1142057827 440 QPYM 443
Cdd:cd00770 294 RPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-449 |
1.00e-92 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 287.76 E-value: 1.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 1 MLDPILLRKDlqtvvdrlksRGVDFDIARfnELESRR-----------------KAVQTETESQQARRNALAKQIGQLKG 63
Cdd:PLN02678 1 MLDINLFREE----------KGGDPELIR--ESQRRRfasvelvdevialdkewRQRQFELDSLRKEFNKLNKEVAKLKI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 64 KGAPEAEVqavMAESQALPARLKALEDELAQTQAQLNDLLMSVPNLPHASVPqgASSDE--NVEVRRWlpgaaDERGIPA 141
Cdd:PLN02678 69 AKEDATEL---IAETKELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVP--VSNDEanNAVVRTW-----GEKRQEP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 142 ALgfevRDHVAVGEPLGL-DFDLAARLSGARFSFMRGQMARLHRALAQFMLDLQTGtHGYTECYTPYIVNSSTLFGTGQL 220
Cdd:PLN02678 139 KL----KNHVDLVELLGIvDTERGADVAGGRGYYLKGAGVLLNQALINFGLAFLRK-RGYTPLQTPFFMRKDVMAKCAQL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 221 PKFKDDMFFVTkGGGDDepkvdeqgnplaredQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGSGGRDTR 300
Cdd:PLN02678 214 AQFDEELYKVT-GEGDD---------------KYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 301 GMIRQHQFDKVEMVQIAHPE--HSYEALEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREIS 378
Cdd:PLN02678 278 GIFRVHQFEKVEQFCITSPNgnESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELV 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1142057827 379 SVSNCETFQARRMQARFR---NAQNKPEYVHTLNGSGLAVGRALVAVLENCQQADGsVRVPAVLQPYMGGLTVL 449
Cdd:PLN02678 358 SCSNCTDYQSRRLEIRYGqkkSNEQTKQYVHLLNSTLTATERTLCCILENYQTEDG-VRVPEVLQPFMGGIEFL 430
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
7-451 |
5.02e-88 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 277.19 E-value: 5.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 7 LRKDLQTVVDRLKSRGVDFDIARFNELESRRKAVQTETESQQARRNALAKQigqLKGKGAPeAEVQAVMAESQALPARLK 86
Cdd:PLN02320 72 IRDNKEAVAINIRNRNSNANLELVLELYENMLALQKEVERLRAERNAVANK---MKGKLEP-SERQALVEEGKNLKEGLV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 87 ALEDELAQTQAQLNDLLMSVPNLPHASVPQGAssDENVEVRRwlpgaadERGIPAALGFEVRDHVAVGEPLGL-DFDLAA 165
Cdd:PLN02320 148 TLEEDLVKLTDELQLEAQSIPNMTHPDVPVGG--EDSSAVRK-------EVGSPREFSFPIKDHLQLGKELDLfDFDAAA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 166 RLSGARFSFMRGQMARLHRALAQFMLDlQTGTHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFFVTKGggddepkvdeqg 245
Cdd:PLN02320 219 EVSGSKFYYLKNEAVLLEMALVNWTLS-EVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNTQVYSIDG------------ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 246 nplarEDQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGSGGRDTRGMIRQHQFDKVEMVQIAHPEHSYEA 325
Cdd:PLN02320 286 -----SDQCLIGTAEIPVGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESF 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 326 LEEMVGHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRNAQNKP--- 402
Cdd:PLN02320 361 HEELIQIEEDLFTSLGLHFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRPSEPPQtnp 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1142057827 403 ----------EYVHTLNGSGLAVGRALVAVLENCQQADGSVRVPAVLQPYMGGLTVLEP 451
Cdd:PLN02320 441 kkgkgslgptKFVHTLNATACAVPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELIKP 499
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
251-425 |
1.85e-45 |
|
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: 156.03 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 251 EDQYLISTSEITLTSVVRETIVAGADLPLRLTAHTPCFRSEAGsggRDTRGMIRQHQFDKVEMVQIAHPEHSYEALEEMV 330
Cdd:pfam00587 9 DELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 331 GHAERVLQLLELPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWREISSVSNCETFQARRMQARFRNAQNKPEYVHTLNG 410
Cdd:pfam00587 86 KLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHR 165
|
170
....*....|....*
gi 1142057827 411 SGLAVGRALVAVLEN 425
Cdd:pfam00587 166 AGLGVERFLAAILEN 180
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-110 |
7.24e-32 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 117.30 E-value: 7.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 1 MLDPILLRKDLQTVVDRLKSRGVD-FDIARFNELESRRKAVQTETESQQARRNALAKQIGQLKGKGapeAEVQAVMAESQ 79
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDvLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKK---EDADALIAEVK 77
|
90 100 110
....*....|....*....|....*....|.
gi 1142057827 80 ALPARLKALEDELAQTQAQLNDLLMSVPNLP 110
Cdd:pfam02403 78 ELKDELKALEAELKELEAELDKLLLTIPNIP 108
|
|
| 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 ... |
182-423 |
7.21e-19 |
|
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: 85.52 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 182 LHRALAQFmLDLQTGTHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFFVTkgggddEPKVDEQGNPLaredqYLISTSEI 261
Cdd:cd00670 4 LWRALERF-LDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFE------DKGRELRDTDL-----VLRPAACE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 262 TLTSVVRETIVAGADLPLRLTAHTPCFRSEAgsggRDTRGMIRQHQFDKVEMVQIAHPEHSYEALEEMVGHAERVLQLLE 341
Cdd:cd00670 72 PIYQIFSGEILSYRALPLRLDQIGPCFRHEP----SGRRGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 342 LPYRVMLLCTGDMGFGSA--------KTYDLEVWLPAQDTWREISSVSNCETFQARRmqARFRNAQNKPEYVHTLNGSGL 413
Cdd:cd00670 148 LPVRVVVADDPFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFG--ASFKIDEDGGGRAHTGCGGAG 225
|
250
....*....|
gi 1142057827 414 AVGRALVAVL 423
Cdd:cd00670 226 GEERLVLALL 235
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
181-417 |
1.61e-11 |
|
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: 63.68 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 181 RLHRALAQFMldlqtGTHGYTECYTPYIVNSSTLFGTGQlpkfkddmffvtkgggddEPKVDEQGNPLAREDQYLISTSE 260
Cdd:cd00768 4 KIEQKLRRFM-----AELGFQEVETPIVEREPLLEKAGH------------------EPKDLLPVGAENEEDLYLRPTLE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 261 ITLTSVVRETIvagADLPLRLTAHTPCFRSEAGSggrdtRGMIRQHQFDKVEmVQIAH-PEHSYEALEEMVGHAERVLQL 339
Cdd:cd00768 61 PGLVRLFVSHI---RKLPLRLAEIGPAFRNEGGR-----RGLRRVREFTQLE-GEVFGeDGEEASEFEELIELTEELLRA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 340 LE--LPYRVMLLCTGDMGFGSAK-TYDLEVWLPaQDTWREISSVSNCETFQARRMQARFRNAQNKPEYVHTLNGsGLAVG 416
Cdd:cd00768 132 LGikLDIVFVEKTPGEFSPGGAGpGFEIEVDHP-EGRGLEIGSGGYRQDEQARAADLYFLDEALEYRYPPTIGF-GLGLE 209
|
.
gi 1142057827 417 R 417
Cdd:cd00768 210 R 210
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
178-381 |
3.24e-11 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 65.04 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 178 QMARLHRALAQFMLDLQTGTHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFFVTKgggddePKVDeqgnPLARED--QYL 255
Cdd:PRK00960 221 PMTKLFRAFEKLVIEEVLKPLGFDECLFPKLIPLEVMYKMRYLEGLPEGMYYVCP------PKRD----PEYFEEfvDEM 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 256 ISTSEIT---LTSVVRETI-------------------VAGADLPLRLTAHT-PCFRSEagSGGrdTRGMIRQHQFDKVE 312
Cdd:PRK00960 291 MVKKEVPiekLKEKLRDPGyvlapaqcepfyqffqgetVDVDELPIKFFDRSgWTYRWE--GGG--AHGLERVNEFHRIE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 313 MVQIAHPEHSYEALEEMVGHAERVLQLLELPYRVM-----------LLCTGDMGFGSAKTYDLEVWLP---AQDTWREIS 378
Cdd:PRK00960 367 IVWLGTPEQVEEIRDELLKYAHILAEKLDLEYWREvgddpfylegrGLEDRGIEFPDVPKYEMELWLPyrgDERKWVAVT 446
|
...
gi 1142057827 379 SVS 381
Cdd:PRK00960 447 SAN 449
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
188-424 |
2.89e-07 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 51.60 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 188 QFMLDLQTGTHGYTECYTPYIVNSSTLFGTGQLPKFKDDMFFVTKGGGDDEPKvdeqgNPLAredqyLISTSEITLTSVV 267
Cdd:cd00772 39 ENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELAVFKDAGDEELE-----EDFA-----LRPTLEENIGEIA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 268 RETIVAGADLPLRLTAHTPCFRSEAgsggRDTRGMIRQHQFdkveMVQIAHPEH-SYEALEEMV-----GHAERVLQLLE 341
Cdd:cd00772 109 AKFIKSWKDLPQHLNQIGNKFRDEI----RPRFGFLRAREF----IMKDGHSAHaDAEEADEEFlnmlsAYAEIARDLAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 342 LPYRVMLLCTGDMGFGSAKTYDLEVWLPAQDTWR-EISSVSNCETFQARRMQARFRNAQNKPEYVHTlNGSGLAVGRALV 420
Cdd:cd00772 181 IDFIEGEADEGAKFAGASKSREFEALMEDGKAKQaETGHIFGEGFARAFDLKAKFLDKDGKEKFFEM-GCWGIGISRFIG 259
|
....
gi 1142057827 421 AVLE 424
Cdd:cd00772 260 AIIE 263
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1-99 |
1.37e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 1 MLDPILLRKDLQTVVDRLK--SRGVDFDIARFNELESRRKAVQTETESQQARRNALAKQIGQLKGKgapEAEVQAVMAES 78
Cdd:COG3883 104 YLDVLLGSESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAELEAQQAEQ 180
|
90 100
....*....|....*....|.
gi 1142057827 79 QALPARLKALEDELAQTQAQL 99
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAEL 201
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
180-236 |
5.05e-04 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 42.33 E-value: 5.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1142057827 180 ARLHRALAQFMLDLQTgTHGYTECYTPYIVNSStLFGT-GQLPKFKDDMFFVTKGGGD 236
Cdd:COG0441 271 AIIRRELEDYIREKHR-KAGYQEVKTPHILDRE-LWETsGHWDHYRENMFPTESDGEE 326
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7-103 |
9.84e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 7 LRKDLQTVVDRLKSRGvdfdiARFNELESRRKAVQTETESQQARRNALAKQIGQLkgkgapEAEVQAVMAESQALPARLK 86
Cdd:COG4942 25 AEAELEQLQQEIAELE-----KELAALKKEEKALLKQLAALERRIAALARRIRAL------EQELAALEAELAELEKEIA 93
|
90
....*....|....*..
gi 1142057827 87 ALEDELAQTQAQLNDLL 103
Cdd:COG4942 94 ELRAELEAQKEELAELL 110
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
180-234 |
2.04e-03 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 39.84 E-value: 2.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1142057827 180 ARLHRALAQFMLDLQTgTHGYTECYTPYIVNSStLFGT-GQLPKFKDDMFFVTKGG 234
Cdd:cd00771 30 AIIRNELEDFLRELQR-KRGYQEVETPIIYNKE-LWETsGHWDHYRENMFPFEEED 83
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
148-229 |
3.14e-03 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 40.12 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 148 RDHVAVGEPLGLdFDLAARLSGARFSFMRGQMARlhRALAQFMLDLQTgTHGYTECYTPYIVNSSTLFGTGQLPKFKDDM 227
Cdd:PRK12444 245 RNHRKLGKELEL-FMFSEEAPGMPFYLPKGQIIR--NELEAFLREIQK-EYNYQEVRTPFMMNQELWERSGHWDHYKDNM 320
|
..
gi 1142057827 228 FF 229
Cdd:PRK12444 321 YF 322
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
32-102 |
3.90e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 3.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1142057827 32 ELESRRKAVQTETESQQARRNALAKQIGQLkgkgapEAEVQAVMAESQALPARLKALEDELAQTQAQLNDL 102
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKAL------LKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
8-102 |
4.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 8 RKDLQTVVDRLKSRgvdfdIARFNELESRRKAVQTETESQQARRNALAKQIGQLkgkgapEAEVQAVMAESQALPARLKA 87
Cdd:COG4372 72 RSELEQLEEELEEL-----NEQLQAAQAELAQAQEELESLQEEAEELQEELEEL------QKERQDLEQQRKQLEAQIAE 140
|
90
....*....|....*
gi 1142057827 88 LEDELAQTQAQLNDL 102
Cdd:COG4372 141 LQSEIAEREEELKEL 155
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
198-350 |
5.84e-03 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 38.35 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 198 HGYTECYTPYIVNSSTLfgtgQLPK-----FKDDMFFVTKGGGDdepKVDEqgnPLAredqyLISTSEITLTSVVRETIV 272
Cdd:cd00778 49 TGHENVYFPLLIPESEL----EKEKehiegFAPEVAWVTHGGLE---ELEE---PLA-----LRPTSETAIYPMFSKWIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142057827 273 AGADLPLRLTAHTPCFRSEAgsggRDTRGMIRQHQFdkveMVQIAHPEHSY--EALEEmvghaerVLQLLELPYRVM--L 348
Cdd:cd00778 114 SYRDLPLKINQWVNVFRWET----KTTRPFLRTREF----LWQEGHTAHATeeEAEEE-------VLQILDLYKEFYedL 178
|
..
gi 1142057827 349 LC 350
Cdd:cd00778 179 LA 180
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
28-98 |
9.43e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 37.90 E-value: 9.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1142057827 28 ARFNELESRRKAVQTETESQQARRNALA--KQIGQLKGKGAPEAEVQA-VMAESQALP-ARLKALEDELAQTQAQ 98
Cdd:TIGR02794 89 ARQKELEQRAAAEKAAKQAEQAAKQAEEkqKQAEEAKAKQAAEAKAKAeAEAERKAKEeAAKQAEEEAKAKAAAE 163
|
|
| |
