|
Name |
Accession |
Description |
Interval |
E-value |
| 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 496844763 1 MLDIKVFRNEPDYVKEKVRLRGMEPSVvDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKAMREVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDV-DELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 81 DKIKDLDAKLKEVKTEIEDKLARIPNFIHDDVPEGDSDEDNVEVKKWGTPREFDFDYKAHWDLVEDLKMANFERAAKVSG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 161 ARFVYLTNDGALLERALMNYMLTKHTtQNGYTEMMVPQLVNADSMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNYY 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 241 RDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLHQFDKVELVRFEKPEDSWNALEEMTENAESILEELGLPYRRV 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 321 ILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRFkRDKDAKPEFAHTLNGSGLAVGRTFAAIVENY 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRY-RDEDGKPEFVHTLNGSGLAVGRTLVAILENY 397
|
410 420
....*....|....*....|....
gi 496844763 401 QNEDGSITIPEALVPFMGGKTKIE 424
Cdd:COG0172 398 QQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-425 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 782.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 1 MLDIKVFRNEPDYVKEKVRLRGMePSVVDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKAMREVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGF-PLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 81 DKIKDLDAKLKEVKTEIEDKLARIPNFIHDDVPEGDSDEDNVEVKKWGTPREFDFDYKAHWDLVEDLKMANFERAAKVSG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 161 ARFVYLTNDGALLERALMNYMLTKHTTQNGYTEMMVPQLVNADSMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNYY 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 241 RDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLHQFDKVELVRFEKPEDSWNALEEMTENAESILEELGLPYRRV 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 321 ILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRFKRDKDAKPEFAHTLNGSGLAVGRTFAAIVENY 400
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....*
gi 496844763 401 QNEDGSITIPEALVPFMGGKTKIEP 425
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIPP 424
|
|
| 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: 592.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 1 MLDIKVFRNEPDYVKEKVRLRG-MEPSVVDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKA-MRE 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGlSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIKKeLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 79 VGDKIKDLDAKLKEVKTEIEDKLARIPNFIHDDVPEGDSDEDNVEVKKWGTPREFDFDYKAHWDLVEDLKMANFERAAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 159 SGARFVYLTNDGALLERALMNYMLTKHTtQNGYTEMMVPQLVNADSMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 239 YYRDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLHQFDKVELVRFEKPEDSWNALEEMTENAESILEELGLPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 319 RVILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRFKRDKDAKPEFAHTLNGSGLAVGRTFAAIVE 398
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 496844763 399 NYQNEDGSITIPEALVPFM 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: 544.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 120 DNVEVKKWGTPREFDFDYKAHWDLVEDLKMANFERAAKVSGARFVYLTNDGALLERALMNYMLTKHTtQNGYTEMMVPQL 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 200 VNADSMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNYYRDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 280 QFDKVELVRFEKPEDSWNALEEMTENAESILEELGLPYRRVILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 496844763 360 QARRANIRFKRDKDAKPEFAHTLNGSGLAVGRTFAAIVENYQNEDGSITIPEALVPFM 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 |
7.55e-48 |
|
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: 161.81 E-value: 7.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 219 FKVEKEG---LYTIPTAEVPLTNYYRDEVIQPGVLPEKFTGMSACFRSEAGsagRDTRGLIRLHQFDKVELVRFEKPEDS 295
Cdd:pfam00587 1 YKVEDENgdeLALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 296 WNALEEMTENAESILEELGLPYRRVILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRFKrDKDAK 375
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYK-DEDNE 156
|
170 180
....*....|....*....|....*
gi 496844763 376 PEFAHTLNGSGLAVGRTFAAIVENY 400
Cdd:pfam00587 157 SKFPYMIHRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| 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 496844763 1 MLDIKVFRNEPDYVKEKVRLRGMEPSVvDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKAMREVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDV-DELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 81 DKIKDLDAKLKEVKTEIEDKLARIPNFIHDDVPEGDSDEDNVEVKKWGTPREFDFDYKAHWDLVEDLKMANFERAAKVSG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 161 ARFVYLTNDGALLERALMNYMLTKHTtQNGYTEMMVPQLVNADSMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNYY 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 241 RDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLHQFDKVELVRFEKPEDSWNALEEMTENAESILEELGLPYRRV 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 321 ILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRFkRDKDAKPEFAHTLNGSGLAVGRTFAAIVENY 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRY-RDEDGKPEFVHTLNGSGLAVGRTLVAILENY 397
|
410 420
....*....|....*....|....
gi 496844763 401 QNEDGSITIPEALVPFMGGKTKIE 424
Cdd:COG0172 398 QQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-425 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 782.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 1 MLDIKVFRNEPDYVKEKVRLRGMePSVVDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKAMREVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGF-PLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 81 DKIKDLDAKLKEVKTEIEDKLARIPNFIHDDVPEGDSDEDNVEVKKWGTPREFDFDYKAHWDLVEDLKMANFERAAKVSG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 161 ARFVYLTNDGALLERALMNYMLTKHTTQNGYTEMMVPQLVNADSMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNYY 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 241 RDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLHQFDKVELVRFEKPEDSWNALEEMTENAESILEELGLPYRRV 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 321 ILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRFKRDKDAKPEFAHTLNGSGLAVGRTFAAIVENY 400
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....*
gi 496844763 401 QNEDGSITIPEALVPFMGGKTKIEP 425
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIPP 424
|
|
| 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: 592.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 1 MLDIKVFRNEPDYVKEKVRLRG-MEPSVVDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKA-MRE 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGlSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIKKeLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 79 VGDKIKDLDAKLKEVKTEIEDKLARIPNFIHDDVPEGDSDEDNVEVKKWGTPREFDFDYKAHWDLVEDLKMANFERAAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 159 SGARFVYLTNDGALLERALMNYMLTKHTtQNGYTEMMVPQLVNADSMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 239 YYRDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLHQFDKVELVRFEKPEDSWNALEEMTENAESILEELGLPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 319 RVILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRFKRDKDAKPEFAHTLNGSGLAVGRTFAAIVE 398
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 496844763 399 NYQNEDGSITIPEALVPFM 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: 544.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 120 DNVEVKKWGTPREFDFDYKAHWDLVEDLKMANFERAAKVSGARFVYLTNDGALLERALMNYMLTKHTtQNGYTEMMVPQL 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 200 VNADSMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNYYRDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 280 QFDKVELVRFEKPEDSWNALEEMTENAESILEELGLPYRRVILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 496844763 360 QARRANIRFKRDKDAKPEFAHTLNGSGLAVGRTFAAIVENYQNEDGSITIPEALVPFM 417
Cdd:cd00770 240 QARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-421 |
5.38e-140 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 407.55 E-value: 5.38e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 1 MLDIKVFRNE----PDYVKEKVRLRGMEPSVVDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKAM 76
Cdd:PLN02678 1 MLDINLFREEkggdPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 77 REVGDKIKDLDAKLKEVKTEIEDKLARIPNFIHDDVPEGDSDEDNVEVKKWGTPReFDFDYKAHWDLVEDLKMANFERAA 156
Cdd:PLN02678 81 KELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKR-QEPKLKNHVDLVELLGIVDTERGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 157 KVSGARFVYLTNDGALLERALMNYMLTkHTTQNGYTEMMVPQLVNADSMYGTGQLPKFEEDLFKVEKEG--LYTIPTAEV 234
Cdd:PLN02678 160 DVAGGRGYYLKGAGVLLNQALINFGLA-FLRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVTGEGddKYLIATSEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 235 PLTNYYRDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLHQFDKVELVRFEKPED--SWNALEEMTENAESILEE 312
Cdd:PLN02678 239 PLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGneSWEMHEEMLKNSEDFYQS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 313 LGLPYRRVILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRF--KRDKDAKPEFAHTLNGSGLAVG 390
Cdd:PLN02678 319 LGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYgqKKSNEQTKQYVHLLNSTLTATE 398
|
410 420 430
....*....|....*....|....*....|.
gi 496844763 391 RTFAAIVENYQNEDGsITIPEALVPFMGGKT 421
Cdd:PLN02678 399 RTLCCILENYQTEDG-VRVPEVLQPFMGGIE 428
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-425 |
1.04e-95 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 296.45 E-value: 1.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 2 LDIKVFRNEPDYVKEKVRLRGMEPSVvDEVLELDAKSREYINETEQLKAERNKaseeIAQKKRNKEDADDAiKAMREVGD 81
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRNSNANL-ELVLELYENMLALQKEVERLRAERNA----VANKMKGKLEPSER-QALVEEGK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 82 KIKDLDAKLKEVKTEIEDKLAR----IPNFIHDDVPEGDSDEDNVEvKKWGTPREFDFDYKAHWDLVEDLKMANFERAAK 157
Cdd:PLN02320 141 NLKEGLVTLEEDLVKLTDELQLeaqsIPNMTHPDVPVGGEDSSAVR-KEVGSPREFSFPIKDHLQLGKELDLFDFDAAAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 158 VSGARFVYLTNDGALLERALMNYMLTKhTTQNGYTEMMVPQLVNADSMYGTGQLPKFEE-DLFKVEKEGLYTIPTAEVPL 236
Cdd:PLN02320 220 VSGSKFYYLKNEAVLLEMALVNWTLSE-VMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSIDGSDQCLIGTAEIPV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 237 TNYYRDEVIQPGVLPEKFTGMSACFRSEAGSAGRDTRGLIRLHQFDKVELVRFEKPEDSWNALEEMTENAESILEELGLP 316
Cdd:PLN02320 299 GGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLH 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 317 YRRVILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRF----------KRDKDAKP--EFAHTLNG 384
Cdd:PLN02320 379 FKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYrpseppqtnpKKGKGSLGptKFVHTLNA 458
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 496844763 385 SGLAVGRTFAAIVENYQNEDGSITIPEALVPFMGGKTKIEP 425
Cdd:PLN02320 459 TACAVPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELIKP 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 ... |
219-400 |
7.55e-48 |
|
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: 161.81 E-value: 7.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 219 FKVEKEG---LYTIPTAEVPLTNYYRDEVIQPGVLPEKFTGMSACFRSEAGsagRDTRGLIRLHQFDKVELVRFEKPEDS 295
Cdd:pfam00587 1 YKVEDENgdeLALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 296 WNALEEMTENAESILEELGLPYRRVILCTGDIGFGASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRFKrDKDAK 375
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYK-DEDNE 156
|
170 180
....*....|....*....|....*
gi 496844763 376 PEFAHTLNGSGLAVGRTFAAIVENY 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 ... |
1-106 |
1.36e-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: 129.63 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 1 MLDIKVFRNEPDYVKEKVRLRGMEPSVVDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKAMREVG 80
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*.
gi 496844763 81 DKIKDLDAKLKEVKTEIEDKLARIPN 106
Cdd:pfam02403 81 DELKALEAELKELEAELDKLLLTIPN 106
|
|
| 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 |
1.67e-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: 103.62 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 170 GALLERALMNyMLTKHTTQNGYTEMMVPQLVNADSMYGTGQLPKFEEDLFKVEKEG-------LYTIPTAEVPLTNYYRD 242
Cdd:cd00670 1 GTALWRALER-FLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGrelrdtdLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 243 EVIQPGVLPEKFTGMSACFRSEAGSAgrdtRGLIRLHQFDKVELVRFEKPEDSWNALEEMTENAESILEELGLPYRRVIL 322
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 323 CTGDIGFG--------ASKTYDLEVWLPSYNEYKEISSCSNVTDFQARRANIRFKRDKDakpEFAHTLNGSGLAVGRTFA 394
Cdd:cd00670 156 DDPFFGRGgkrgldagRETVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDEDGG---GRAHTGCGGAGGEERLVL 232
|
..
gi 496844763 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 |
1.66e-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: 74.85 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 173 LERALMNYMltkhtTQNGYTEMMVPQLVNADSMYGTGQLPKfEEDLFKVEKEGLYTIPTAEVPLTNYYRDEVIQPgvLPE 252
Cdd:cd00768 5 IEQKLRRFM-----AELGFQEVETPIVEREPLLEKAGHEPK-DLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRK--LPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 253 KFTGMSACFRSEAGSagrdtRGLIRLHQFDKVELVRFEKPEDSWNALEEMTENAESILEELG--LPYRRVILCTGDIGFG 330
Cdd:cd00768 77 RLAEIGPAFRNEGGR-----RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGikLDIVFVEKTPGEFSPG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496844763 331 -ASKTYDLEVWLPSyNEYKEISSCSNVTDFQARRANIRFkRDKDAKPEFAHTLNGsGLAVGR 391
Cdd:cd00768 152 gAGPGFEIEVDHPE-GRGLEIGSGGYRQDEQARAADLYF-LDEALEYRYPPTIGF-GLGLER 210
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
173-342 |
6.66e-09 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 57.72 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 173 LERALMNYMLTKHTTQNGYTEMMVPQLVNADSMYGTGQL------------PKFEEDLF-------KVEKEglytIPTAE 233
Cdd:PRK00960 225 LFRAFEKLVIEEVLKPLGFDECLFPKLIPLEVMYKMRYLeglpegmyyvcpPKRDPEYFeefvdemMVKKE----VPIEK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 234 V-----------------PLTNYYRDEVIQPGVLPEKFTGMSA-CFRSEAGSAgrdtRGLIRLHQFDKVELVRFEKPEDS 295
Cdd:PRK00960 301 LkeklrdpgyvlapaqcePFYQFFQGETVDVDELPIKFFDRSGwTYRWEGGGA----HGLERVNEFHRIEIVWLGTPEQV 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496844763 296 WNALEEMTENAESILEELGLPYRRVILCT-----------GDIGFGASKTYDLEVWLP 342
Cdd:PRK00960 377 EEIRDELLKYAHILAEKLDLEYWREVGDDpfylegrgledRGIEFPDVPKYEMELWLP 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
29-104 |
3.81e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 3.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496844763 29 DEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKAMREvgdKIKDLDAKLKEVKTEIEDKLARI 104
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEERREEL 88
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
190-398 |
1.55e-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 prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 39.87 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 190 GYTEMMVPQLVNADSMYGTGQLPKFEEDLFKV----EKEGLYTiPTAEVPLTNYYRDEVIQPGVLPEKFTGMSACFRSEA 265
Cdd:cd00779 49 GAQEILMPILQPAELWKESGRWDAYGPELLRLkdrhGKEFLLG-PTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 266 gsagRDTRGLIRLHQFDKVELVRFEK-PEDSWNALEEMTENAESILEELGLPYRRVILCTGDIGFGASKTYDLevwLPSY 344
Cdd:cd00779 128 ----RPRFGLMRGREFLMKDAYSFDIdEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHV---LSPL 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496844763 345 NEYKEI------------SSCSNVTdFQarranirfkrDKDAKPEFAHTlnGS-GLAVGRTFAAIVE 398
Cdd:cd00779 201 KITKGIevghifqlgtkySKALGAT-FL----------DENGKPKPLEM--GCyGIGVSRLLAAIIE 254
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-104 |
4.82e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 15 KEKVRLRGMEPSVVDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKA----MREVGDKIKDLDAKL 90
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkseLKELEARIEELEEDL 774
|
90
....*....|....
gi 496844763 91 KEVKTEIEDKLARI 104
Cdd:TIGR02169 775 HKLEEALNDLEARL 788
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
43-104 |
8.29e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.60 E-value: 8.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496844763 43 NETEQLKAERNKASEEIAQKKRNKEDADDAIKAMREvgdKIKDLDAKLKEVKTEIEDKLARI 104
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKT---ELEDLEKEIKRLELEIEEVEARI 75
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
37-104 |
8.52e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.60 E-value: 8.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496844763 37 KSREY---INETEQLKAERNKASEEIAQKKRNKEDADDAIKAMREvgdKIKDLDAKLKEVKTEIEDKLARI 104
Cdd:COG1579 87 NNKEYealQKEIESLKRRISDLEDEILELMERIEELEEELAELEA---ELAELEAELEEKKAELDEELAEL 154
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
33-103 |
8.77e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 37.97 E-value: 8.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496844763 33 ELDAKSREYINETEQLKAERNKASEEIAQKKRNKEDADDAIKAMREVGDKIKD--LDAKLKEVKTEIEDKLAR 103
Cdd:COG1340 206 ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRekEKEELEEKAEEIFEKLKK 278
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
17-105 |
9.92e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.14 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496844763 17 KVRLRGMepSVVDEVLELDAKSREYINETEQLKAERNKASEEIAQKKRNKE-DADDAIKAMREVGDKIKDLDAKLKEVKT 95
Cdd:COG0542 401 RVRMEID--SKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELaELEEELEALKARWEAEKELIEEIQELKE 478
|
90
....*....|
gi 496844763 96 EIEDKLARIP 105
Cdd:COG0542 479 ELEQRYGKIP 488
|
|
| |
