|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-423 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 813.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 1 MLDVKMMRQNIEEVQEKLMTRGVKkETLAEFMELDENRRKLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKIAEMKEVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFP-LDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 81 GNIKALDTEIAEVDEKLKQIATTLPNLPHDSVPVGTDEEDNVEIRRWSEPRTFAFEPKPHWEIAENLDILDFERGAKVAG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 161 SRFVYYKGLGARLERAVYNFMLDQHIYEHGYTEMITPYIVNSKAMFGTGQFPKFKEDVFQLENTDLTLIPTAEVPLTNYY 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 241 NDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHLPYRVM 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 321 ALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYRDN-DGKIHYTHTLNGSGLAVGRTVAAILENY 399
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEgDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....
gi 1062443723 400 QNEDGSVTVPEALVPYMGNLKVIK 423
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-423 |
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: 813.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 1 MLDVKMMRQNIEEVQEKLMTRGVKkETLAEFMELDENRRKLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKIAEMKEVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFD-LDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 81 GNIKALDTEIAEVDEKLKQIATTLPNLPHDSVPVGTDEEDNVEIRRWSEPRTFAFEPKPHWEIAENLDILDFERGAKVAG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 161 SRFVYYKGLGARLERAVYNFMLDQHIyEHGYTEMITPYIVNSKAMFGTGQFPKFKEDVFQLENTDLTLIPTAEVPLTNYY 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 241 NDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHLPYRVM 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 321 ALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYRDNDGKIHYTHTLNGSGLAVGRTVAAILENYQ 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|...
gi 1062443723 401 NEDGSVTVPEALVPYMGNLKVIK 423
Cdd:COG0172 399 QADGSVRIPEVLRPYMGGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-416 |
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: 610.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 1 MLDVKMMRQNIEEVQEKLMTRGVKKETLAE-FMELDENRRKLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKI-AEMKE 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDIDLEkLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIkKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 79 VGGNIKALDTEIAEVDEKLKQIATTLPNLPHDSVPVGTDEEDNVEIRRWSEPRTFAFEPKPHWEIAENLDILDFERGAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 159 AGSRFVYYKGLGARLERAVYNFMLDQHIyEHGYTEMITPYIVNSKAMFGTGQFPKFKEDVFQLENTDLTLIPTAEVPLTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 239 YYNDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHLPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 319 VMALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYRD-NDGKIHYTHTLNGSGLAVGRTVAAILE 397
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDkNKGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 1062443723 398 NYQNEDGSVTVPEALVPYM 416
Cdd:TIGR00414 400 NYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-416 |
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: 537.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 120 DNVEIRRWSEPRTFAFEPKPHWEIAENLDILDFERGAKVAGSRFVYYKGLGARLERAVYNFMLDQHIyEHGYTEMITPYI 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 200 VNSKAMFGTGQFPKFKEDVFQLENTDLTLIPTAEVPLTNYYNDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 280 QFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHLPYRVMALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1062443723 360 QARRAMIRYRD-NDGKIHYTHTLNGSGLAVGRTVAAILENYQNEDGSVTVPEALVPYM 416
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 ... |
225-399 |
5.76e-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: 5.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 225 DLTLIPTAEVPLTNYYNDEILDGADLPIYFTALSPAFRSEAGsagRDTRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTA 304
Cdd:pfam00587 10 ELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 305 DAEDILKKLHLPYRVMALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYRDNDGKIHYTHTLNGS 384
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHRA 166
|
170
....*....|....*
gi 1062443723 385 GLAVGRTVAAILENY 399
Cdd:pfam00587 167 GLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-423 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 813.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 1 MLDVKMMRQNIEEVQEKLMTRGVKkETLAEFMELDENRRKLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKIAEMKEVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFP-LDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 81 GNIKALDTEIAEVDEKLKQIATTLPNLPHDSVPVGTDEEDNVEIRRWSEPRTFAFEPKPHWEIAENLDILDFERGAKVAG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 161 SRFVYYKGLGARLERAVYNFMLDQHIYEHGYTEMITPYIVNSKAMFGTGQFPKFKEDVFQLENTDLTLIPTAEVPLTNYY 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 241 NDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHLPYRVM 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 321 ALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYRDN-DGKIHYTHTLNGSGLAVGRTVAAILENY 399
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEgDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....
gi 1062443723 400 QNEDGSVTVPEALVPYMGNLKVIK 423
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-423 |
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: 813.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 1 MLDVKMMRQNIEEVQEKLMTRGVKkETLAEFMELDENRRKLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKIAEMKEVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFD-LDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 81 GNIKALDTEIAEVDEKLKQIATTLPNLPHDSVPVGTDEEDNVEIRRWSEPRTFAFEPKPHWEIAENLDILDFERGAKVAG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 161 SRFVYYKGLGARLERAVYNFMLDQHIyEHGYTEMITPYIVNSKAMFGTGQFPKFKEDVFQLENTDLTLIPTAEVPLTNYY 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 241 NDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHLPYRVM 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 321 ALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYRDNDGKIHYTHTLNGSGLAVGRTVAAILENYQ 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|...
gi 1062443723 401 NEDGSVTVPEALVPYMGNLKVIK 423
Cdd:COG0172 399 QADGSVRIPEVLRPYMGGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-416 |
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: 610.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 1 MLDVKMMRQNIEEVQEKLMTRGVKKETLAE-FMELDENRRKLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKI-AEMKE 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDIDLEkLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIkKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 79 VGGNIKALDTEIAEVDEKLKQIATTLPNLPHDSVPVGTDEEDNVEIRRWSEPRTFAFEPKPHWEIAENLDILDFERGAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 159 AGSRFVYYKGLGARLERAVYNFMLDQHIyEHGYTEMITPYIVNSKAMFGTGQFPKFKEDVFQLENTDLTLIPTAEVPLTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 239 YYNDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHLPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 319 VMALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYRD-NDGKIHYTHTLNGSGLAVGRTVAAILE 397
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDkNKGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 1062443723 398 NYQNEDGSVTVPEALVPYM 416
Cdd:TIGR00414 400 NYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-416 |
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: 537.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 120 DNVEIRRWSEPRTFAFEPKPHWEIAENLDILDFERGAKVAGSRFVYYKGLGARLERAVYNFMLDQHIyEHGYTEMITPYI 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 200 VNSKAMFGTGQFPKFKEDVFQLENTDLTLIPTAEVPLTNYYNDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 280 QFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHLPYRVMALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1062443723 360 QARRAMIRYRD-NDGKIHYTHTLNGSGLAVGRTVAAILENYQNEDGSVTVPEALVPYM 416
Cdd:cd00770 240 QARRLNIRYRDkKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-422 |
6.31e-123 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 364.03 E-value: 6.31e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 1 MLDVKMMRQ----NIEEVQEKLMTRGVKKETLAEFMELDENRRKLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKIAEM 76
Cdd:PLN02678 1 MLDINLFREekggDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 77 KEVGGNIKALDTEIAEVDEKLKQIATTLPNLPHDSVPVGTDEEDNVEIRRWSEPRtfaFEPKP--HWEIAENLDILDFER 154
Cdd:PLN02678 81 KELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKR---QEPKLknHVDLVELLGIVDTER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 155 GAKVAGSRFVYYKGLGARLERAVYNFMLDqHIYEHGYTEMITPYIVNSKAMFGTGQFPKFKEDVFQL--ENTDLTLIPTA 232
Cdd:PLN02678 158 GADVAGGRGYYLKGAGVLLNQALINFGLA-FLRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVtgEGDDKYLIATS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 233 EVPLTNYYNDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLHQFNKVEM--VKFSDVEHSYEELEKMTADAEDIL 310
Cdd:PLN02678 237 EQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQfcITSPNGNESWEMHEEMLKNSEDFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 311 KKLHLPYRVMALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYR---DNDGKIHYTHTLNGSGLA 387
Cdd:PLN02678 317 QSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYGqkkSNEQTKQYVHLLNSTLTA 396
|
410 420 430
....*....|....*....|....*....|....*
gi 1062443723 388 VGRTVAAILENYQNEDGsVTVPEALVPYMGNLKVI 422
Cdd:PLN02678 397 TERTLCCILENYQTEDG-VRVPEVLQPFMGGIEFL 430
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-423 |
8.22e-98 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 301.46 E-value: 8.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 2 LDVKMMRQNIEEVQEKLMTRGvKKETLAEFMELDENRRKLLVKSEELKKYRNDVSAEIaqlkRAKEDASAKIAEMKEvGG 81
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRN-SNANLELVLELYENMLALQKEVERLRAERNAVANKM----KGKLEPSERQALVEE-GK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 82 NIK----ALDTEIAEVDEKLKQIATTLPNLPHDSVPVGTdeEDNVEIRRW-SEPRTFAFEPKPHWEIAENLDILDFERGA 156
Cdd:PLN02320 141 NLKeglvTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGG--EDSSAVRKEvGSPREFSFPIKDHLQLGKELDLFDFDAAA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 157 KVAGSRFVYYKGLGARLERAVYNFMLDQhIYEHGYTEMITPYIVNSKAMFGTGQFPKFKE-DVFQLENTDLTLIPTAEVP 235
Cdd:PLN02320 219 EVSGSKFYYLKNEAVLLEMALVNWTLSE-VMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSIDGSDQCLIGTAEIP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 236 LTNYYNDEILDGADLPIYFTALSPAFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHL 315
Cdd:PLN02320 298 VGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 316 PYRVMALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYRDND-------------GKIHYTHTLN 382
Cdd:PLN02320 378 HFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRPSEppqtnpkkgkgslGPTKFVHTLN 457
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1062443723 383 GSGLAVGRTVAAILENYQNEDGSVTVPEALVPYMGNLKVIK 423
Cdd:PLN02320 458 ATACAVPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELIK 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 ... |
225-399 |
5.76e-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: 5.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 225 DLTLIPTAEVPLTNYYNDEILDGADLPIYFTALSPAFRSEAGsagRDTRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTA 304
Cdd:pfam00587 10 ELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 305 DAEDILKKLHLPYRVMALSTGDMGFSAAKTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRYRDNDGKIHYTHTLNGS 384
Cdd:pfam00587 87 LIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIHRA 166
|
170
....*....|....*
gi 1062443723 385 GLAVGRTVAAILENY 399
Cdd:pfam00587 167 GLGVERFLAAILENN 181
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-108 |
4.98e-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: 128.09 E-value: 4.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 1 MLDVKMMRQNIEEVQEKLMTRGVKKETLAEFMELDENRRKLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKIAEMKEVG 80
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*...
gi 1062443723 81 GNIKALDTEIAEVDEKLKQIATTLPNLP 108
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 ... |
170-396 |
7.66e-26 |
|
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: 104.78 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 170 GARLERAVYNFmLDQHIYEHGYTEMITPYIVNSKAMFGTGQFPKFKEDVFQLE-------NTDLTLIPTAEVPLTNYYND 242
Cdd:cd00670 1 GTALWRALERF-LDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEdkgrelrDTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 243 EILDGADLPIYFTALSPAFRSEAGSAgrdtRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTADAEDILKKLHLPYRVMAL 322
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 323 STGDMGFSAA--------KTYDLEVWIPAQDTYREISSCSNCEDFQARRAMIRyRDNDGKIHYTHTLNGSGLaVGRTVAA 394
Cdd:cd00670 156 DDPFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFGASFK-IDEDGGGRAHTGCGGAGG-EERLVLA 233
|
..
gi 1062443723 395 IL 396
Cdd:cd00670 234 LL 235
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
39-342 |
1.82e-07 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 53.10 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 39 RKLLVKSEELK-KYRNDVSAEIAQLKR-------AKEDASAKIaEMKEVGgnikalDTEIAE--VDEKLKQIATTLPNLP 108
Cdd:PRK00960 96 RGIEIDNYVITiPADGEKVIELEGLKVppcvveiEGEKGTIIL-IFKDVG------ESELKRniIDRAIKLVEEKLEKLE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 109 HDSVPVGTDEEDnvEIRRWSEPRTFAFEPKPHwEIAEnldildfERG-AKVAGSRFVYYKG-LGARLERAVYNFMLDQHI 186
Cdd:PRK00960 169 DLTFYVGKAEPG--TIVSESKKREITFDGDPT-EEAE-------KLGwVKRFPGRGQWFYTpPMTKLFRAFEKLVIEEVL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 187 YEHGYTEMITPYIVNSKAMFGTGQF------------PKFKEDVFQlENTDLTLIpTAEVPLTN---------------- 238
Cdd:PRK00960 239 KPLGFDECLFPKLIPLEVMYKMRYLeglpegmyyvcpPKRDPEYFE-EFVDEMMV-KKEVPIEKlkeklrdpgyvlapaq 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 239 ------YYNDEILDGADLPIYFTALS-PAFRSEAGSAgrdtRGLIRLHQFNKVEMVKFSDVEHSYEELEKMTADAEDILK 311
Cdd:PRK00960 317 cepfyqFFQGETVDVDELPIKFFDRSgWTYRWEGGGA----HGLERVNEFHRIEIVWLGTPEQVEEIRDELLKYAHILAE 392
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1062443723 312 KLHLPYRVMA-----------LSTGDMGFSAAKTYDLEVWIP 342
Cdd:PRK00960 393 KLDLEYWREVgddpfylegrgLEDRGIEFPDVPKYEMELWLP 434
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
181-397 |
3.51e-07 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 51.22 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 181 MLDQHIYEHGYTEMITPYIVNSKAMFGTGQFPK--------FKEDVFQLENTDLTLIPTAEVPLTNYYNDEILDGADLPI 252
Cdd:cd00772 41 VLDKMFKEHGAQNALFPFFILASFLEKEAEHDEgfskelavFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 253 YFTALSPAFRSEAgsagRDTRGLIRLHQFNKVEMVKF-SDVEHSYEELEKMTADAEDILKKL-HLPYRVMALSTGDMGFS 330
Cdd:cd00772 121 HLNQIGNKFRDEI----RPRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAEIARDLaAIDFIEGEADEGAKFAG 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 331 AAKTYDLEVWIpaQDTYREISSCSNC--EDF-QARRAMIRYRDNDGKIHYTHTlNGSGLAVGRTVAAILE 397
Cdd:cd00772 197 ASKSREFEALM--EDGKAKQAETGHIfgEGFaRAFDLKAKFLDKDGKEKFFEM-GCWGIGISRFIGAIIE 263
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
182-328 |
3.25e-06 |
|
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: 48.34 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 182 LDQHIYEHGYTEMITPyIVNSKAMF-GTGQFPKFKEDVFQL---ENTDLTLIPTAEVPLTNYYNDEILDGADLPIYFTAL 257
Cdd:cd00779 41 IREEMNKIGAQEILMP-ILQPAELWkESGRWDAYGPELLRLkdrHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQI 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1062443723 258 SPAFRSEAgsagRDTRGLIRLHQFNKVEMVKF-SDVEHSYEELEKMTADAEDILKKLHLPYRVMALSTGDMG 328
Cdd:cd00779 120 QTKFRDEI----RPRFGLMRGREFLMKDAYSFdIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIG 187
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
3-110 |
8.70e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.63 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 3 DVKMMRQNIEEVQEKLMTR-----------GVKKETLAEFMELDENRRKL----------LVK-SEELKKYRNDVSAEIA 60
Cdd:pfam05667 357 EIKKLESSIKQVEEELEELkeqneelekqyKVKKKTLDLLPDAEENIAKLqalvdasaqrLVElAGQWEKHRVPLIEEYR 436
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1062443723 61 QLKRAK----EDASAKIAEMKEVGGNIKALDTEIAEVDEKLKQIATTLPNLPHD 110
Cdd:pfam05667 437 ALKEAKsnkeDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKD 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2-105 |
3.35e-04 |
|
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: 41.83 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 2 LDVKMMRQNIEEVQEKLMTRGVKKETLAEFMELDENRR-------KLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKIA 74
Cdd:COG1579 66 LEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRrisdledEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
90 100 110
....*....|....*....|....*....|.
gi 1062443723 75 EMKEVggnIKALDTEIAEVDEKLKQIATTLP 105
Cdd:COG1579 146 ELDEE---LAELEAELEELEAEREELAAKIP 173
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
170-349 |
2.96e-03 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 39.75 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 170 GARleraVYNFMLD---QHIYEHGYTEMITPYIVNSKAMFGTGQFPKFKED--VFQLENTDLTLIPTAEVPLTNYYNDEI 244
Cdd:PLN02908 320 GAR----IYNKLMDfirEQYWERGYDEVITPNIYNMDLWETSGHAAHYKENmfVFEIEKQEFGLKPMNCPGHCLMFAHRV 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 245 LDGADLPIYFTALSPAFRSEAGSAgrdTRGLIRLHQFNKvemvkfsDVEHSYEELEKMTADAEDILKKLHLPYRV----- 319
Cdd:PLN02908 396 RSYRELPLRLADFGVLHRNELSGA---LTGLTRVRRFQQ-------DDAHIFCREDQIKDEVKGVLDFLDYVYEVfgfty 465
|
170 180 190
....*....|....*....|....*....|.
gi 1062443723 320 -MALSTGDMGFSAaktyDLEVWIPAQDTYRE 349
Cdd:PLN02908 466 eLKLSTRPEKYLG----DLETWDKAEAALTE 492
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
139-399 |
5.13e-03 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 38.69 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 139 PHWEIAENLDILDFERGAKvAGSRFVYYKGlgARLERAVYNFMLDQHIyEHGYTEMITPYIVNSKAMFGTGQFPKFKEDV 218
Cdd:cd00771 1 DHRRLGGELELFFFFDEAG-PGLPFWLPKG--AIIRNELEDFLRELQR-KRGYQEVETPIIYNKELWETSGHWDHYRENM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 219 F--QLENTDLTLIPTAEVPLTNYYNDEILDGADLPIYFTALSPAFRSEA-GSAGrdtrGLIRL--------HQFNKVEMV 287
Cdd:cd00771 77 FpfEEEDEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQsGALH----GLTRVrgftqddaHIFCTPDQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062443723 288 K----------------FSDVEHSY-------------EELEKMTADAEDILKKLHLPYRVMAlstGDMGFsaaktYDLE 338
Cdd:cd00771 153 KeeikgvldlikevysdFGFFDYKVelstrpekfigsdEVWEKAEAALREALEEIGLPYEINE---GEGAF-----YGPK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062443723 339 VWIPAQDTYREISSCSNCE-DFQ-ARRAMIRYRDNDGKIHY---TH-TLNGSglaVGRTVAAILENY 399
Cdd:cd00771 225 IDFHVKDALGREWQCSTIQlDFNlPERFDLTYIGEDGEKKRpvmIHrAILGS---IERFIGILIEHY 288
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
33-101 |
6.27e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 6.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062443723 33 ELDENRRKLLVKSEELKKYRNDVSAEIAQLKRAKEDASAKIAEMKEVGGNIKALDTEIAEVDEKLKQIA 101
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
|
| |
