|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-426 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 785.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 1 MLDIRLFRNEPDTVKSKIELRGDDPkVVDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKENADDVIAEMRTLG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPL-DVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 81 DDIKEKDSQLNEIDKKMTGILCRIPNLISDDVPQGESDEDNVEVKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKVSG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 161 ARFVYLTNEGAQLERALMNYMITKHTTQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNFY 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 241 RNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYRRV 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 321 ILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRFKRDKAAKPELAHTLNGSGLAVGRTFAAIVENY 400
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....*.
gi 613307394 401 QNEDGTVTIPEALVPFMGGKTQISKP 426
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIPPK 425
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-424 |
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: 784.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 1 MLDIRLFRNEPDTVKSKIELRGDDPKVvDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKENADDVIAEMRTLG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDV-DELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 81 DDIKEKDSQLNEIDKKMTGILCRIPNLISDDVPQGESDEDNVEVKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKVSG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 161 ARFVYLTNEGAQLERALMNYMITKHTtQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNFY 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 241 RNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYRRV 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 321 ILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRFkRDKAAKPELAHTLNGSGLAVGRTFAAIVENY 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRY-RDEDGKPEFVHTLNGSGLAVGRTLVAILENY 397
|
410 420
....*....|....*....|....
gi 613307394 401 QNEDGTVTIPEALVPFMGGKTQIS 424
Cdd:COG0172 398 QQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-417 |
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: 583.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 1 MLDIRLFRNEPDTVKSKIELRG-DDPKVVDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKEN-ADDVIAEMRT 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGlSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 79 LGDDIKEKDSQLNEIDKKMTGILCRIPNLISDDVPQGESDEDNVEVKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 159 SGARFVYLTNEGAQLERALMNYMITKHTtQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 239 FYRNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 319 RVILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRFKRDKAAKPELAHTLNGSGLAVGRTFAAIVE 398
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 613307394 399 NYQNEDGTVTIPEALVPFM 417
Cdd:TIGR00414 400 NYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-417 |
0e+00 |
|
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: 553.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 120 DNVEVKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKVSGARFVYLTNEGAQLERALMNYMITKHTtQHGYTEMMVPQL 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 200 VNADTMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNFYRNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 280 QFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYRRVILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 613307394 360 QARRANIRFKRDKAAKPELAHTLNGSGLAVGRTFAAIVENYQNEDGTVTIPEALVPFM 417
Cdd:cd00770 240 QARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 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 ... |
219-400 |
3.95e-47 |
|
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: 159.88 E-value: 3.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 219 FKVEKEG---LYTIPTAEVPLTNFYRNEIIQPGVLPEKFTGQSACFRSEAGsagRDTRGLIRLHQFDKVEMVRFEQPEDS 295
Cdd:pfam00587 1 YKVEDENgdeLALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 296 WNALEEMTTNAEAILEELGLPYRRVILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRFKrDKAAK 375
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYK-DEDNE 156
|
170 180
....*....|....*....|....*
gi 613307394 376 PELAHTLNGSGLAVGRTFAAIVENY 400
Cdd:pfam00587 157 SKFPYMIHRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-426 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 785.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 1 MLDIRLFRNEPDTVKSKIELRGDDPkVVDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKENADDVIAEMRTLG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPL-DVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 81 DDIKEKDSQLNEIDKKMTGILCRIPNLISDDVPQGESDEDNVEVKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKVSG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 161 ARFVYLTNEGAQLERALMNYMITKHTTQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNFY 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 241 RNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYRRV 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 321 ILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRFKRDKAAKPELAHTLNGSGLAVGRTFAAIVENY 400
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....*.
gi 613307394 401 QNEDGTVTIPEALVPFMGGKTQISKP 426
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIPPK 425
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-424 |
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: 784.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 1 MLDIRLFRNEPDTVKSKIELRGDDPKVvDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKENADDVIAEMRTLG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDV-DELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 81 DDIKEKDSQLNEIDKKMTGILCRIPNLISDDVPQGESDEDNVEVKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKVSG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 161 ARFVYLTNEGAQLERALMNYMITKHTtQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNFY 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 241 RNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYRRV 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 321 ILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRFkRDKAAKPELAHTLNGSGLAVGRTFAAIVENY 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRY-RDEDGKPEFVHTLNGSGLAVGRTLVAILENY 397
|
410 420
....*....|....*....|....
gi 613307394 401 QNEDGTVTIPEALVPFMGGKTQIS 424
Cdd:COG0172 398 QQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-417 |
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: 583.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 1 MLDIRLFRNEPDTVKSKIELRG-DDPKVVDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKEN-ADDVIAEMRT 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGlSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 79 LGDDIKEKDSQLNEIDKKMTGILCRIPNLISDDVPQGESDEDNVEVKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 159 SGARFVYLTNEGAQLERALMNYMITKHTtQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 239 FYRNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 319 RVILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRFKRDKAAKPELAHTLNGSGLAVGRTFAAIVE 398
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 613307394 399 NYQNEDGTVTIPEALVPFM 417
Cdd:TIGR00414 400 NYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-417 |
0e+00 |
|
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: 553.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 120 DNVEVKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKVSGARFVYLTNEGAQLERALMNYMITKHTtQHGYTEMMVPQL 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 200 VNADTMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNFYRNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 280 QFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYRRVILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 613307394 360 QARRANIRFKRDKAAKPELAHTLNGSGLAVGRTFAAIVENYQNEDGTVTIPEALVPFM 417
Cdd:cd00770 240 QARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-421 |
6.70e-133 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 389.45 E-value: 6.70e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 1 MLDIRLFRNE----PDTVKSKIELRGDDPKVVDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKENADDVIAEM 76
Cdd:PLN02678 1 MLDINLFREEkggdPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 77 RTLGDDIKEKDSQLNEIDKKMTGILCRIPNLISDDVPQGESDEDNVEVKKWGTPReFSFEPKAHWDIVEELKMADFDRAA 156
Cdd:PLN02678 81 KELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKR-QEPKLKNHVDLVELLGIVDTERGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 157 KVSGARFVYLTNEGAQLERALMNYMITkHTTQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKVEKEG--LYTIPTAEV 234
Cdd:PLN02678 160 DVAGGRGYYLKGAGVLLNQALINFGLA-FLRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVTGEGddKYLIATSEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 235 PLTNFYRNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLHQFDKVEMVRFEQPED--SWNALEEMTTNAEAILEE 312
Cdd:PLN02678 239 PLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGneSWEMHEEMLKNSEDFYQS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 313 LGLPYRRVILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRF--KRDKAAKPELAHTLNGSGLAVG 390
Cdd:PLN02678 319 LGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYgqKKSNEQTKQYVHLLNSTLTATE 398
|
410 420 430
....*....|....*....|....*....|.
gi 613307394 391 RTFAAIVENYQNEDGtVTIPEALVPFMGGKT 421
Cdd:PLN02678 399 RTLCCILENYQTEDG-VRVPEVLQPFMGGIE 428
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-424 |
4.08e-94 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 292.21 E-value: 4.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 2 LDIRLFRNEPDTVKSKIELRGDDPKVvDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKENaDDVIAEMRTLGD 81
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRNSNANL-ELVLELYENMLALQKEVERLRAERNAVANKMKGKLEPSER-QALVEEGKNLKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 82 DIKEKDSQLNEIDKKMTGILCRIPNLISDDVPQGESDEDNVEvKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKVSGA 161
Cdd:PLN02320 145 GLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDSSAVR-KEVGSPREFSFPIKDHLQLGKELDLFDFDAAAEVSGS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 162 RFVYLTNEGAQLERALMNYMITKhTTQHGYTEMMVPQLVNADTMYGTGQLPKFEE-DLFKVEKEGLYTIPTAEVPLTNFY 240
Cdd:PLN02320 224 KFYYLKNEAVLLEMALVNWTLSE-VMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSIDGSDQCLIGTAEIPVGGIH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 241 RNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYRRV 320
Cdd:PLN02320 303 MDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHFKTL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 321 ILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRF----------KRDKAAKP--ELAHTLNGSGLA 388
Cdd:PLN02320 383 DMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYrpseppqtnpKKGKGSLGptKFVHTLNATACA 462
|
410 420 430
....*....|....*....|....*....|....*.
gi 613307394 389 VGRTFAAIVENYQNEDGTVTIPEALVPFMGGKTQIS 424
Cdd:PLN02320 463 VPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELIK 498
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
219-400 |
3.95e-47 |
|
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: 159.88 E-value: 3.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 219 FKVEKEG---LYTIPTAEVPLTNFYRNEIIQPGVLPEKFTGQSACFRSEAGsagRDTRGLIRLHQFDKVEMVRFEQPEDS 295
Cdd:pfam00587 1 YKVEDENgdeLALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 296 WNALEEMTTNAEAILEELGLPYRRVILCTGDIGFSASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRFKrDKAAK 375
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYK-DEDNE 156
|
170 180
....*....|....*....|....*
gi 613307394 376 PELAHTLNGSGLAVGRTFAAIVENY 400
Cdd:pfam00587 157 SKFPYMIHRAGLGVERFLAAILENN 181
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-107 |
6.16e-39 |
|
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: 135.79 E-value: 6.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 1 MLDIRLFRNEPDTVKSKIELRGDDPKVVDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKENADDVIAEMRTLG 80
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*..
gi 613307394 81 DDIKEKDSQLNEIDKKMTGILCRIPNL 107
Cdd:pfam02403 81 DELKALEAELKELEAELDKLLLTIPNI 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 ... |
170-396 |
5.57e-25 |
|
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: 102.47 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 170 GAQLERALMNyMITKHTTQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKVEKEG-------LYTIPTAEVPLTNFYRN 242
Cdd:cd00670 1 GTALWRALER-FLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGrelrdtdLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 243 EIIQPGVLPEKFTGQSACFRSEAGSAgrdtRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYRRVIL 322
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 323 CTGDIGFS--------ASKTYDLEVWLPSYNDYKEISSCSNCTDFQARRANIRFKRDKAAKpelAHTLNGSGLAVGRTFA 394
Cdd:cd00670 156 DDPFFGRGgkrgldagRETVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDEDGGGR---AHTGCGGAGGEERLVL 232
|
..
gi 613307394 395 AI 396
Cdd:cd00670 233 AL 234
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
173-391 |
7.77e-15 |
|
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: 72.92 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 173 LERALMNYMitkhtTQHGYTEMMVPQLVNADTMYGTGQLPKfEEDLFKVEKEGLYTI-PTAEVPLTNFYRNEIIQpgvLP 251
Cdd:cd00768 5 IEQKLRRFM-----AELGFQEVETPIVEREPLLEKAGHEPK-DLLPVGAENEEDLYLrPTLEPGLVRLFVSHIRK---LP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 252 EKFTGQSACFRSEAGSagrdtRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELG--LPYRRVILCTGDIGF 329
Cdd:cd00768 76 LRLAEIGPAFRNEGGR-----RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGikLDIVFVEKTPGEFSP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613307394 330 S-ASKTYDLEVWLPSyNDYKEISSCSNCTDFQARRANIRFkRDKAAKPELAHTLNGsGLAVGR 391
Cdd:cd00768 151 GgAGPGFEIEVDHPE-GRGLEIGSGGYRQDEQARAADLYF-LDEALEYRYPPTIGF-GLGLER 210
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
171-349 |
3.90e-10 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 61.57 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 171 AQLERALMNYMITKHTTQHGYTEMMVPQLVNADTMYGTGQL------------PKFEEDLF-------KVEKEglytIPT 231
Cdd:PRK00960 223 TKLFRAFEKLVIEEVLKPLGFDECLFPKLIPLEVMYKMRYLeglpegmyyvcpPKRDPEYFeefvdemMVKKE----VPI 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 232 AEV-----------------PLTNFYRNEIIQPGVLPEKFTGQSA-CFRSEAGSAgrdtRGLIRLHQFDKVEMVRFEQPE 293
Cdd:PRK00960 299 EKLkeklrdpgyvlapaqcePFYQFFQGETVDVDELPIKFFDRSGwTYRWEGGGA----HGLERVNEFHRIEIVWLGTPE 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613307394 294 DSWNALEEMTTNAEAILEELGLPYRRVILCT-----------GDIGFSASKTYDLEVWLPSYNDYKE 349
Cdd:PRK00960 375 QVEEIRDELLKYAHILAEKLDLEYWREVGDDpfylegrgledRGIEFPDVPKYEMELWLPYRGDERK 441
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
182-335 |
1.17e-05 |
|
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 prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 46.42 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 182 ITKHTTQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKV----EKEGLYTiPTAEVPLTNFYRNEIIQPGVLPEKFTGQ 257
Cdd:cd00779 41 IREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLkdrhGKEFLLG-PTHEEVITDLVANEIKSYKQLPLNLYQI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307394 258 SACFRSEAgsagRDTRGLIRLHQFDKVEMVRF----EQPEDSWNALEEMTTNaeaILEELGLPYRRVILCTGDIGFSASK 333
Cdd:cd00779 120 QTKFRDEI----RPRFGLMRGREFLMKDAYSFdideESLEETYEKMYQAYSR---IFKRLGLPFVKVEADSGAIGGSLSH 192
|
..
gi 613307394 334 TY 335
Cdd:cd00779 193 EF 194
|
|
| |
