|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-430 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 813.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 1 MLDPNLLRNELDAVAVKLARRGFKLDLDLLRSQEERRKVLQVETETLQAERNSRSKSIGAAKARGEDIEPLRREVNELGD 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 81 KLDAAKAELDALQSEIRDYALTLPNLPDDAVPDGKDDSENLEVTRWGEPRQYDFAVRDHVDLGEMAGGLDFAAAVKLTGS 160
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 161 RFVVMKGQIARMHRALSQFMLDLHTEQHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHTrpleeeaDSSNYALIPTAEV 240
Cdd:PRK05431 161 RFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKI-------EDDDLYLIPTAEV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 241 PLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQLLN 320
Cdd:PRK05431 234 PLTNLHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 321 LPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCRSKADKKPRLVHTLNGSGLAVGRTLV 400
Cdd:PRK05431 314 LPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLV 393
|
410 420 430
....*....|....*....|....*....|
gi 727179761 401 AVLENYQQADGRIQVPEVLRPYMGGLEYIG 430
Cdd:PRK05431 394 AILENYQQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-430 |
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: 804.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 1 MLDPNLLRNELDAVAVKLARRGFKLDLDLLRSQEERRKVLQVETETLQAERNSRSKSIGAAKARGEDIEPLRREVNELGD 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 81 KLDAAKAELDALQSEIRDYALTLPNLPDDAVPDGKDDSENLEVTRWGEPRQYDFAVRDHVDLGEMAGGLDFAAAVKLTGS 160
Cdd:COG0172 81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 161 RFVVMKGQIARMHRALSQFMLDLHTEqHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHTrpleeEADssNYALIPTAEV 240
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHTE-HGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKI-----EGD--DLYLIPTAEV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 241 PLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQLLN 320
Cdd:COG0172 233 PLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 321 LPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCRSKaDKKPRLVHTLNGSGLAVGRTLV 400
Cdd:COG0172 313 LPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDE-DGKPEFVHTLNGSGLAVGRTLV 391
|
410 420 430
....*....|....*....|....*....|
gi 727179761 401 AVLENYQQADGRIQVPEVLRPYMGGLEYIG 430
Cdd:COG0172 392 AILENYQQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-423 |
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: 656.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 1 MLDPNLLRNELDAVAVKLARRG--FKLDLDLLRSQEERRKVLQVETETLQAERNSRSKSIGAAKARGED-IEPLRREVNE 77
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGlsVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 78 LGDKLDAAKAELDALQSEIRDYALTLPNLPDDAVPDGKDDSENLEVTRWGEPRQYDFAVRDHVDLGEMAGGLDFAAAVKL 157
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 158 TGSRFVVMKGQIARMHRALSQFMLDLHtEQHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHTRPLeeeadssNYALIPT 237
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLL-EKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDT-------DLYLIPT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 238 AEVPLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQ 317
Cdd:TIGR00414 233 AEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 318 LLNLPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCRSKADKKPRLVHTLNGSGLAVGR 397
Cdd:TIGR00414 313 ELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGR 392
|
410 420
....*....|....*....|....*.
gi 727179761 398 TLVAVLENYQQADGRIQVPEVLRPYM 423
Cdd:TIGR00414 393 TIVAILENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
119-423 |
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: 509.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 119 ENLEVTRWGEPRQYDFAVRDHVDLGEMAGGLDFAAAVKLTGSRFVVMKGQIARMHRALSQFMLDLHTEqHGYLEAYVPYL 198
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTK-RGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 199 VNHATLYGTGQLPKFGEDLFHTrpleeeaDSSNYALIPTAEVPLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDT 278
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKV-------EGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 279 RGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQLLNLPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISS 358
Cdd:cd00770 153 RGLFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727179761 359 CSNMWDFQARRMQARCRSKADKKPRLVHTLNGSGLAVGRTLVAVLENYQQADGRIQVPEVLRPYM 423
Cdd:cd00770 233 CSNCTDFQARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 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 ... |
225-406 |
1.77e-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: 161.04 E-value: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 225 EEADSSNYALIPTAEVPLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGsygRDTRGLIRMHQFDKVEMVQIVRPEDSMDA 304
Cdd:pfam00587 4 EDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 305 LEELTGHAEKVLQLLNLPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCRSKADKKpRL 384
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNES-KF 159
|
170 180
....*....|....*....|..
gi 727179761 385 VHTLNGSGLAVGRTLVAVLENY 406
Cdd:pfam00587 160 PYMIHRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-430 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 813.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 1 MLDPNLLRNELDAVAVKLARRGFKLDLDLLRSQEERRKVLQVETETLQAERNSRSKSIGAAKARGEDIEPLRREVNELGD 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 81 KLDAAKAELDALQSEIRDYALTLPNLPDDAVPDGKDDSENLEVTRWGEPRQYDFAVRDHVDLGEMAGGLDFAAAVKLTGS 160
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 161 RFVVMKGQIARMHRALSQFMLDLHTEQHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHTrpleeeaDSSNYALIPTAEV 240
Cdd:PRK05431 161 RFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKI-------EDDDLYLIPTAEV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 241 PLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQLLN 320
Cdd:PRK05431 234 PLTNLHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 321 LPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCRSKADKKPRLVHTLNGSGLAVGRTLV 400
Cdd:PRK05431 314 LPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLV 393
|
410 420 430
....*....|....*....|....*....|
gi 727179761 401 AVLENYQQADGRIQVPEVLRPYMGGLEYIG 430
Cdd:PRK05431 394 AILENYQQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-430 |
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: 804.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 1 MLDPNLLRNELDAVAVKLARRGFKLDLDLLRSQEERRKVLQVETETLQAERNSRSKSIGAAKARGEDIEPLRREVNELGD 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 81 KLDAAKAELDALQSEIRDYALTLPNLPDDAVPDGKDDSENLEVTRWGEPRQYDFAVRDHVDLGEMAGGLDFAAAVKLTGS 160
Cdd:COG0172 81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 161 RFVVMKGQIARMHRALSQFMLDLHTEqHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHTrpleeEADssNYALIPTAEV 240
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHTE-HGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKI-----EGD--DLYLIPTAEV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 241 PLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQLLN 320
Cdd:COG0172 233 PLTNLHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 321 LPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCRSKaDKKPRLVHTLNGSGLAVGRTLV 400
Cdd:COG0172 313 LPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDE-DGKPEFVHTLNGSGLAVGRTLV 391
|
410 420 430
....*....|....*....|....*....|
gi 727179761 401 AVLENYQQADGRIQVPEVLRPYMGGLEYIG 430
Cdd:COG0172 392 AILENYQQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-423 |
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: 656.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 1 MLDPNLLRNELDAVAVKLARRG--FKLDLDLLRSQEERRKVLQVETETLQAERNSRSKSIGAAKARGED-IEPLRREVNE 77
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGlsVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 78 LGDKLDAAKAELDALQSEIRDYALTLPNLPDDAVPDGKDDSENLEVTRWGEPRQYDFAVRDHVDLGEMAGGLDFAAAVKL 157
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 158 TGSRFVVMKGQIARMHRALSQFMLDLHtEQHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHTRPLeeeadssNYALIPT 237
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLL-EKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDT-------DLYLIPT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 238 AEVPLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQ 317
Cdd:TIGR00414 233 AEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 318 LLNLPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCRSKADKKPRLVHTLNGSGLAVGR 397
Cdd:TIGR00414 313 ELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGR 392
|
410 420
....*....|....*....|....*.
gi 727179761 398 TLVAVLENYQQADGRIQVPEVLRPYM 423
Cdd:TIGR00414 393 TIVAILENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
119-423 |
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: 509.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 119 ENLEVTRWGEPRQYDFAVRDHVDLGEMAGGLDFAAAVKLTGSRFVVMKGQIARMHRALSQFMLDLHTEqHGYLEAYVPYL 198
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTK-RGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 199 VNHATLYGTGQLPKFGEDLFHTrpleeeaDSSNYALIPTAEVPLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDT 278
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKV-------EGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 279 RGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQLLNLPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISS 358
Cdd:cd00770 153 RGLFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727179761 359 CSNMWDFQARRMQARCRSKADKKPRLVHTLNGSGLAVGRTLVAVLENYQQADGRIQVPEVLRPYM 423
Cdd:cd00770 233 CSNCTDFQARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-429 |
3.20e-101 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 308.56 E-value: 3.20e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 1 MLDPNLLRNEL--DAVAVKLA-RRGFK----LDLDLLRSQEERRKvlQVETETLQAERNSRSKSIGAAKARGEDIEPLRR 73
Cdd:PLN02678 1 MLDINLFREEKggDPELIRESqRRRFAsvelVDEVIALDKEWRQR--QFELDSLRKEFNKLNKEVAKLKIAKEDATELIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 74 EVNELGDKLDAAKAELDALQSEIRDYALTLPNLPDDAVPDGKDDSENLEVTRWGEPRQyDFAVRDHVDLGEMAGGLDFAA 153
Cdd:PLN02678 79 ETKELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKRQ-EPKLKNHVDLVELLGIVDTER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 154 AVKLTGSRFVVMKGQIARMHRALSQFMLDLhTEQHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHtrpLEEEADSsNYa 233
Cdd:PLN02678 158 GADVAGGRGYYLKGAGVLLNQALINFGLAF-LRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYK---VTGEGDD-KY- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 234 LIPTAEVPLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDTRGLIRMHQFDKVEMVQIVRPED--SMDALEELTGH 311
Cdd:PLN02678 232 LIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGneSWEMHEEMLKN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 312 AEKVLQLLNLPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCRSK--ADKKPRLVHTLN 389
Cdd:PLN02678 312 SEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYGQKksNEQTKQYVHLLN 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 727179761 390 GSGLAVGRTLVAVLENYQQADGrIQVPEVLRPYMGGLEYI 429
Cdd:PLN02678 392 STLTATERTLCCILENYQTEDG-VRVPEVLQPFMGGIEFL 430
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-429 |
6.63e-85 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 268.33 E-value: 6.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 2 LDPNLLRNELDAVAVKLARRGFKLDLDLLRSQEERRKVLQVETETLQAERNSRsksigAAKARGEdIEPLRRE--VNE-- 77
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRNSNANLELVLELYENMLALQKEVERLRAERNAV-----ANKMKGK-LEPSERQalVEEgk 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 78 -LGDKLDAAKAELDALQSEIRDYALTLPNLPDDAVPDGKDDSENL--EVtrwGEPRQYDFAVRDHVDLGEMAGGLDFAAA 154
Cdd:PLN02320 141 nLKEGLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDSSAVrkEV---GSPREFSFPIKDHLQLGKELDLFDFDAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 155 VKLTGSRFVVMKGQIARMHRALSQFMLDlHTEQHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHTrpleeeADSSNYAL 234
Cdd:PLN02320 218 AEVSGSKFYYLKNEAVLLEMALVNWTLS-EVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNTQVYS------IDGSDQCL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 235 IPTAEVPLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGSYGRDTRGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEK 314
Cdd:PLN02320 291 IGTAEIPVGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEED 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 315 VLQLLNLPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCR-----------SKADKKP- 382
Cdd:PLN02320 371 LFTSLGLHFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRpseppqtnpkkGKGSLGPt 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 727179761 383 RLVHTLNGSGLAVGRTLVAVLENYQQADGRIQVPEVLRPYMGGLEYI 429
Cdd:PLN02320 451 KFVHTLNATACAVPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELI 497
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
225-406 |
1.77e-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: 161.04 E-value: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 225 EEADSSNYALIPTAEVPLTNLVRDEIVEEETLPLKMTAHTPCFRAEAGsygRDTRGLIRMHQFDKVEMVQIVRPEDSMDA 304
Cdd:pfam00587 4 EDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 305 LEELTGHAEKVLQLLNLPYRKVLLCTGDMGFGACKTYDLEVWLPAQNTYREISSCSNMWDFQARRMQARCRSKADKKpRL 384
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNES-KF 159
|
170 180
....*....|....*....|..
gi 727179761 385 VHTLNGSGLAVGRTLVAVLENY 406
Cdd:pfam00587 160 PYMIHRAGLGVERFLAAILENN 181
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-107 |
4.01e-36 |
|
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: 128.47 E-value: 4.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 1 MLDPNLLRNELDAVAVKLARRG-FKLDLDLLRSQEERRKVLQVETETLQAERNSRSKSIGAAKARGEDIEPLRREVNELG 79
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGvDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*...
gi 727179761 80 DKLDAAKAELDALQSEIRDYALTLPNLP 107
Cdd:pfam02403 81 DELKALEAELKELEAELDKLLLTIPNIP 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 ... |
169-403 |
6.86e-20 |
|
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: 88.22 E-value: 6.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 169 IARMHRALSQFMLDLHTEqHGYLEAYVPYLVNHATLYGTGQLPKFGEDLFHTRPLEEEADSSNYALIPTAEVPLTNLVRD 248
Cdd:cd00670 1 GTALWRALERFLDDRMAE-YGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 249 EIVEEETLPLKMTAHTPCFRAEAgsygRDTRGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQLLNLPYRKVLL 328
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEP----SGRRGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 329 CTGDMGFGAC--------KTYDLEVWLPAQNTYREISSCSNMWDFQARRmqARCRSKADKKPRLVHTLNGSGLaVGRTLV 400
Cdd:cd00670 156 DDPFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFG--ASFKIDEDGGGRAHTGCGGAGG-EERLVL 232
|
...
gi 727179761 401 AVL 403
Cdd:cd00670 233 ALL 235
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
168-397 |
1.24e-13 |
|
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: 69.45 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 168 QIARMHRALSQFMldlhtEQHGYLEAYVPYLVNHATLYGTGQLPKfgeDLFHTRPLEEEadssNYALIPTAEvplTNLVR 247
Cdd:cd00768 1 IRSKIEQKLRRFM-----AELGFQEVETPIVEREPLLEKAGHEPK---DLLPVGAENEE----DLYLRPTLE---PGLVR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 248 DEIVEEETLPLKMTAHTPCFRAEAGSygrdtRGLIRMHQFDKVEMVQIVRPEDSMDALEELTGHAEKVLQLL--NLPYRK 325
Cdd:cd00768 66 LFVSHIRKLPLRLAEIGPAFRNEGGR-----RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALgiKLDIVF 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727179761 326 VLLCTGDMGFG-ACKTYDLEVWLPaQNTYREISSCSNMWDFQARRMQARCRSKADKKpRLVHTLNGsGLAVGR 397
Cdd:cd00768 141 VEKTPGEFSPGgAGPGFEIEVDHP-EGRGLEIGSGGYRQDEQARAADLYFLDEALEY-RYPPTIGF-GLGLER 210
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
168-348 |
5.68e-12 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 67.35 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 168 QIARMHRALSQFMLDLHTEQHGYLEAYVPYLVNHATLYGTGQL------------PKFGEDLF----------HTRPLE- 224
Cdd:PRK00960 221 PMTKLFRAFEKLVIEEVLKPLGFDECLFPKLIPLEVMYKMRYLeglpegmyyvcpPKRDPEYFeefvdemmvkKEVPIEk 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 225 --EEADSSNYALIPTAEVPLTNLVRDEIVEEETLPLKMTAHT-PCFRAEAGSygrdTRGLIRMHQFDKVEMVQIVRPEDS 301
Cdd:PRK00960 301 lkEKLRDPGYVLAPAQCEPFYQFFQGETVDVDELPIKFFDRSgWTYRWEGGG----AHGLERVNEFHRIEIVWLGTPEQV 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 727179761 302 MDALEELTGHAEKVLQLLNLPY-RKV----------LLCTGDMGFGACKTYDLEVWLP 348
Cdd:PRK00960 377 EEIRDELLKYAHILAEKLDLEYwREVgddpfylegrGLEDRGIEFPDVPKYEMELWLP 434
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
186-404 |
6.57e-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: 44.10 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 186 EQHGYLEAYVPyLVNHATLY-GTGQLPKFGEDLFHTRpleeeaDSSN--YALIPTAEVPLTNLVRDEIVEEETLPLKMTA 262
Cdd:cd00779 46 NKIGAQEILMP-ILQPAELWkESGRWDAYGPELLRLK------DRHGkeFLLGPTHEEVITDLVANEIKSYKQLPLNLYQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 263 HTPCFRAEAgsygRDTRGLIR--------MHQFDkvemvqiVRPEDSMDALEELTGHAEKVLQLLNLPYRKVLLCTGDMG 334
Cdd:cd00779 119 IQTKFRDEI----RPRFGLMRgreflmkdAYSFD-------IDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIG 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727179761 335 FGACKTYDLEVWLPAQNTYrEISSCSNMWDFQARRMQARCrSKADKKPRLVHTlnGS-GLAVGRTLVAVLE 404
Cdd:cd00779 188 GSLSHEFHVLSPLKITKGI-EVGHIFQLGTKYSKALGATF-LDENGKPKPLEM--GCyGIGVSRLLAAIIE 254
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
178-404 |
8.88e-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.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 43.90 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 178 QFMLDLHTEQHGYLEAYVPYLVNHATLYGTGQLPKFGE-DLFHTRPLEEEADSSNYALIPTAEVPLTNLVRDEIVEEETL 256
Cdd:cd00772 39 ENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSkELAVFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 257 PLKMTAHTPCFRAEAgsygRDTRGLIRMHQFDKVE--MVQIVRPEDSMDALEELTGHAEKVLQLLNLPYRKVLLCTGDMG 334
Cdd:cd00772 119 PQHLNQIGNKFRDEI----RPRFGFLRAREFIMKDghSAHADAEEADEEFLNMLSAYAEIARDLAAIDFIEGEADEGAKF 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727179761 335 FGACKTYDLEVWLpaQNTYREISSCSNMWDFQARRMQARCRSKADK--KPRLVHTlNGSGLAVGRTLVAVLE 404
Cdd:cd00772 195 AGASKSREFEALM--EDGKAKQAETGHIFGEGFARAFDLKAKFLDKdgKEKFFEM-GCWGIGISRFIGAIIE 263
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
5-109 |
1.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179761 5 NLLRNELDAVAVKLARRGFKLDLDLLRSQEERRKVLQVETETLQAERNSRSKSIGAAKAR-----GEDIEPLRREVNELG 79
Cdd:COG4913 272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngGDRLEQLEREIERLE 351
|
90 100 110
....*....|....*....|....*....|
gi 727179761 80 DKLDAAKAELDALQSEIRDYALTLPNLPDD 109
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEE 381
|
|
| |
