|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
17-391 |
0e+00 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 736.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 17 SSR-LFLKPFTNTLTLGLFSR----HLQPRNKPLLVRAFSASAAVQDIPATQTSDSSVAaRPLWKAAIDFKWIRDNKEAV 91
Cdd:PLN02320 1 SSRfIFLKPFTNTLTLGPFSRltvsLLQRPHKPLLVRAFSASAAVQDIPATQKSDSSVA-RPQWKAAIDFKWIRDNKEAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 92 EINIRNRNSNANLEAVLQLYENMVNLQKEVERLREERNNVAKKMKGKLEPSERERLVEEGKNLKESLVTLEEDLVKLKDE 171
Cdd:PLN02320 80 AINIRNRNSNANLELVLELYENMLALQKEVERLRAERNAVANKMKGKLEPSERQALVEEGKNLKEGLVTLEEDLVKLTDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 172 LQHVAQSIPNMTHPDVPVGGEDSSAIRQEVGSPREFSFPIKDHLQLGKDLDLIDFDSAAEVSGSKFFYLKNEAVLLEMAL 251
Cdd:PLN02320 160 LQLEAQSIPNMTHPDVPVGGEDSSAVRKEVGSPREFSFPIKDHLQLGKELDLFDFDAAAEVSGSKFYYLKNEAVLLEMAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 252 LNWTLSQVMKKGYTPLTTPEIVRSSIVEKCGFQPRGDNTQVYSIDGTDQCLIGTAEIPVGGIHMDSILLESALPLKYIAF 331
Cdd:PLN02320 240 VNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNTQVYSIDGSDQCLIGTAEIPVGGIHMDSILLESALPLKYVAF 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 332 SHCFRTEAGAAGAATKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHF 391
Cdd:PLN02320 320 SHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHF 379
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
79-391 |
8.25e-116 |
|
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: 343.91 E-value: 8.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 79 IDFKWIRDNKEAVEINIRNRNSNANLEAVLQLYENMVNLQKEVERLREERNNVAKKM-KGKLEPSERERLVEEGKNLKES 157
Cdd:COG0172 2 LDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIgKAKKKGEEAEALIAEVKELKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 158 LVTLEEDLVKLKDELQHVAQSIPNMTHPDVPVGGEDSSA--IRqEVGSPREFSFPIKDHLQLGKDLDLIDFDSAAEVSGS 235
Cdd:COG0172 82 IKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNveVR-RWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 236 KFFYLKNEAVLLEMALLNWTLSQVMKKGYTPLTTPEIVRSSIVEKCGFQPRGDNtQVYSIDGTDQCLIGTAEIPVGGIHM 315
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEE-DLYKIEGDDLYLIPTAEVPLTNLHR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571443 316 DSILLESALPLKYIAFSHCFRTEAGAAGAATKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHF 391
Cdd:COG0172 240 DEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPY 315
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
197-391 |
6.23e-89 |
|
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: 270.97 E-value: 6.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 197 IRQEVGSPREFSFPIKDHLQLGKDLDLIDFDSAAEVSGSKFFYLKNEAVLLEMALLNWTLSQVMKKGYTPLTTPEIVRSS 276
Cdd:cd00770 4 EIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 277 IVEKCGFQPrGDNTQVYSIDGTDQCLIGTAEIPVGGIHMDSILLESALPLKYIAFSHCFRTEAGAAGAATKGLYRVHQFS 356
Cdd:cd00770 84 VMEGTGQLP-KFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVHQFE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 42571443 357 KAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHF 391
Cdd:cd00770 163 KVEQFVFTKPEESWEELEELISNAEEILQELGLPY 197
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
79-393 |
2.14e-86 |
|
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: 268.46 E-value: 2.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 79 IDFKWIRDNKEAV--EINIRNRNSNANLEAVLQLYENMVNLQKEVERLREERNNVAKKM--KGKLEPSERERLVEEGKNL 154
Cdd:TIGR00414 2 LDRKLLRNNPDLVkeSLKARGLSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIgkAKGQKKDKIEEIKKELKEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 155 KESLVTLEEDLVKLKDELQHVAQSIPNMTHPDVPVGGEDSSAIRQ-EVGSPREFSFPIKDHLQLGKDLDLIDFDSAAEVS 233
Cdd:TIGR00414 82 KEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVkRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 234 GSKFFYLKNEAVLLEMALLNWTLSQVMKKGYTPLTTPEIVRSSIVEKCGfQPRGDNTQVYSIDGTDQCLIGTAEIPVGGI 313
Cdd:TIGR00414 162 GSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTG-QLPKFEEDIFKLEDTDLYLIPTAEVPLTNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 314 HMDSILLESALPLKYIAFSHCFRTEAGAAGAATKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHFNR 393
Cdd:TIGR00414 241 HRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYRV 320
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
79-182 |
1.27e-25 |
|
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: 99.97 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 79 IDFKWIRDNKEAVEINIRNRN-SNANLEAVLQLYENMVNLQKEVERLREERNNVAKKM-KGKLEPSERERLVEEGKNLKE 156
Cdd:pfam02403 2 LDIKLIRENPEAVKESLKKRGvDVLDVDELLELDEKRRELQVELEELQAERNELSKEIgQAKKKKEDADALIAEVKELKD 81
|
90 100
....*....|....*....|....*.
gi 42571443 157 SLVTLEEDLVKLKDELQHVAQSIPNM 182
Cdd:pfam02403 82 ELKALEAELKELEAELDKLLLTIPNI 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
17-391 |
0e+00 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 736.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 17 SSR-LFLKPFTNTLTLGLFSR----HLQPRNKPLLVRAFSASAAVQDIPATQTSDSSVAaRPLWKAAIDFKWIRDNKEAV 91
Cdd:PLN02320 1 SSRfIFLKPFTNTLTLGPFSRltvsLLQRPHKPLLVRAFSASAAVQDIPATQKSDSSVA-RPQWKAAIDFKWIRDNKEAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 92 EINIRNRNSNANLEAVLQLYENMVNLQKEVERLREERNNVAKKMKGKLEPSERERLVEEGKNLKESLVTLEEDLVKLKDE 171
Cdd:PLN02320 80 AINIRNRNSNANLELVLELYENMLALQKEVERLRAERNAVANKMKGKLEPSERQALVEEGKNLKEGLVTLEEDLVKLTDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 172 LQHVAQSIPNMTHPDVPVGGEDSSAIRQEVGSPREFSFPIKDHLQLGKDLDLIDFDSAAEVSGSKFFYLKNEAVLLEMAL 251
Cdd:PLN02320 160 LQLEAQSIPNMTHPDVPVGGEDSSAVRKEVGSPREFSFPIKDHLQLGKELDLFDFDAAAEVSGSKFYYLKNEAVLLEMAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 252 LNWTLSQVMKKGYTPLTTPEIVRSSIVEKCGFQPRGDNTQVYSIDGTDQCLIGTAEIPVGGIHMDSILLESALPLKYIAF 331
Cdd:PLN02320 240 VNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNTQVYSIDGSDQCLIGTAEIPVGGIHMDSILLESALPLKYVAF 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 332 SHCFRTEAGAAGAATKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHF 391
Cdd:PLN02320 320 SHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHF 379
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
79-391 |
8.25e-116 |
|
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: 343.91 E-value: 8.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 79 IDFKWIRDNKEAVEINIRNRNSNANLEAVLQLYENMVNLQKEVERLREERNNVAKKM-KGKLEPSERERLVEEGKNLKES 157
Cdd:COG0172 2 LDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIgKAKKKGEEAEALIAEVKELKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 158 LVTLEEDLVKLKDELQHVAQSIPNMTHPDVPVGGEDSSA--IRqEVGSPREFSFPIKDHLQLGKDLDLIDFDSAAEVSGS 235
Cdd:COG0172 82 IKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNveVR-RWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 236 KFFYLKNEAVLLEMALLNWTLSQVMKKGYTPLTTPEIVRSSIVEKCGFQPRGDNtQVYSIDGTDQCLIGTAEIPVGGIHM 315
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEE-DLYKIEGDDLYLIPTAEVPLTNLHR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571443 316 DSILLESALPLKYIAFSHCFRTEAGAAGAATKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHF 391
Cdd:COG0172 240 DEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPY 315
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
79-391 |
2.84e-111 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 332.42 E-value: 2.84e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 79 IDFKWIRDNKEAVEINIRNRNSNANLEAVLQLYENMVNLQKEVERLREERNNVAKKM-KGKLEPSERERLVEEGKNLKES 157
Cdd:PRK05431 2 LDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIgQAKRKGEDAEALIAEVKELKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 158 LVTLEEDLVKLKDELQHVAQSIPNMTHPDVPVGGEDSSA--IRqEVGSPREFSFPIKDHLQLGKDLDLIDFDSAAEVSGS 235
Cdd:PRK05431 82 IKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNveVR-RWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 236 KFFYLKNEAVLLEMALLNWTLSQ-VMKKGYTPLTTPEIVRSSIVEKCGFQPRGDNtQVYSIDGTDQCLIGTAEIPVGGIH 314
Cdd:PRK05431 161 RFYVLKGDGARLERALIQFMLDLhTEEHGYTEVIPPYLVNEESMYGTGQLPKFEE-DLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571443 315 MDSILLESALPLKYIAFSHCFRTEAGAAGAATKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHF 391
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPY 316
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
197-391 |
6.23e-89 |
|
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: 270.97 E-value: 6.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 197 IRQEVGSPREFSFPIKDHLQLGKDLDLIDFDSAAEVSGSKFFYLKNEAVLLEMALLNWTLSQVMKKGYTPLTTPEIVRSS 276
Cdd:cd00770 4 EIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 277 IVEKCGFQPrGDNTQVYSIDGTDQCLIGTAEIPVGGIHMDSILLESALPLKYIAFSHCFRTEAGAAGAATKGLYRVHQFS 356
Cdd:cd00770 84 VMEGTGQLP-KFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVHQFE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 42571443 357 KAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHF 391
Cdd:cd00770 163 KVEQFVFTKPEESWEELEELISNAEEILQELGLPY 197
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
79-393 |
2.14e-86 |
|
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: 268.46 E-value: 2.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 79 IDFKWIRDNKEAV--EINIRNRNSNANLEAVLQLYENMVNLQKEVERLREERNNVAKKM--KGKLEPSERERLVEEGKNL 154
Cdd:TIGR00414 2 LDRKLLRNNPDLVkeSLKARGLSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIgkAKGQKKDKIEEIKKELKEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 155 KESLVTLEEDLVKLKDELQHVAQSIPNMTHPDVPVGGEDSSAIRQ-EVGSPREFSFPIKDHLQLGKDLDLIDFDSAAEVS 233
Cdd:TIGR00414 82 KEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVkRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 234 GSKFFYLKNEAVLLEMALLNWTLSQVMKKGYTPLTTPEIVRSSIVEKCGfQPRGDNTQVYSIDGTDQCLIGTAEIPVGGI 313
Cdd:TIGR00414 162 GSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTG-QLPKFEEDIFKLEDTDLYLIPTAEVPLTNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 314 HMDSILLESALPLKYIAFSHCFRTEAGAAGAATKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHFNR 393
Cdd:TIGR00414 241 HRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYRV 320
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
79-389 |
3.19e-55 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 188.37 E-value: 3.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 79 IDFKWIRDNK----EAVEINIRNRNSNANL-EAVLQLYENMVNLQKEVERLREERN----NVAKKMKGKLEPSErerLVE 149
Cdd:PLN02678 2 LDINLFREEKggdpELIRESQRRRFASVELvDEVIALDKEWRQRQFELDSLRKEFNklnkEVAKLKIAKEDATE---LIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 150 EGKNLKESLVTLEEDLVKLKDELQHVAQSIPNMTHPDVPVGG-EDSSAIRQEVGSPReFSFPIKDHLQLGKDLDLIDFDS 228
Cdd:PLN02678 79 ETKELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNdEANNAVVRTWGEKR-QEPKLKNHVDLVELLGIVDTER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 229 AAEVSGSKFFYLKNEAVLLEMALLNWTLSQVMKKGYTPLTTPEIVRSSIVEKCGfQPRGDNTQVYSI--DGTDQCLIGTA 306
Cdd:PLN02678 158 GADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCA-QLAQFDEELYKVtgEGDDKYLIATS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 307 EIPVGGIHMDSILLESALPLKYIAFSHCFRTEAGAAGAATKGLYRVHQFSKAEMFVICQPEDSESF--HQELIQIEEDLF 384
Cdd:PLN02678 237 EQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGNESWemHEEMLKNSEDFY 316
|
....*
gi 42571443 385 TSLGL 389
Cdd:PLN02678 317 QSLGI 321
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
79-182 |
1.27e-25 |
|
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: 99.97 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 79 IDFKWIRDNKEAVEINIRNRN-SNANLEAVLQLYENMVNLQKEVERLREERNNVAKKM-KGKLEPSERERLVEEGKNLKE 156
Cdd:pfam02403 2 LDIKLIRENPEAVKESLKKRGvDVLDVDELLELDEKRRELQVELEELQAERNELSKEIgQAKKKKEDADALIAEVKELKD 81
|
90 100
....*....|....*....|....*.
gi 42571443 157 SLVTLEEDLVKLKDELQHVAQSIPNM 182
Cdd:pfam02403 82 ELKALEAELKELEAELDKLLLTIPNI 107
|
|
| 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 ... |
244-391 |
8.89e-14 |
|
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: 70.50 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 244 AVLLEMALLNWTLSQVMKKGYTPLTTPEIVRSSIVEKCGFQPRGDNtQVYSID-------GTDQCLIGTAEIPVGGIHMD 316
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRK-EMYTFEdkgrelrDTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571443 317 SILLESALPLKYIAFSHCFRTEAGAAgaatKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHF 391
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPV 150
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
301-397 |
9.83e-12 |
|
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: 63.20 E-value: 9.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 301 CLIGTAEIPVGGIHMDSILLESALPLKYIAFSHCFRTEAGAAgaaTKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIE 380
Cdd:pfam00587 12 ALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGD---TRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKLI 88
|
90
....*....|....*..
gi 42571443 381 EDLFTSLGLHFNRFRRS 397
Cdd:pfam00587 89 DRVYSRLGLEVRVVRLS 105
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
255-396 |
2.67e-04 |
|
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: 41.72 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571443 255 TLSQVMK-KGYTPLTTPEIVRSSIVEKCGFQPRgDNTQVYSIDGTDQCLIGTAEIPVGGIHMDSIlleSALPLKYIAFSH 333
Cdd:cd00768 8 KLRRFMAeLGFQEVETPIVEREPLLEKAGHEPK-DLLPVGAENEEDLYLRPTLEPGLVRLFVSHI---RKLPLRLAEIGP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571443 334 CFRTEAGaagaaTKGLYRVHQFSKAEMFVICQPEDSESFHQELIQIEEDLFTSLGLHFNRFRR 396
Cdd:cd00768 84 AFRNEGG-----RRGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIKLDIVFV 141
|
|
| |
