|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
81-570 |
4.05e-117 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 358.38 E-value: 4.05e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 81 CLDNHTEI--------------SDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDAIGKKNLYYTLDRGTY 146
Cdd:COG0367 76 EIYNYRELraelealghrfrthSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 147 YIA--PK-LTTLaPYHYHQLDLIALRDYLCCAFVPGTKTLWQNVQEIAQGTFLKI---PSHEITHYWQLKENIIEPYQPL 220
Cdd:COG0367 156 AFAseLKaLLAH-PGVDRELDPEALAEYLTLGYVPAPRTIFKGIRKLPPGHYLTVdagGELEIRRYWDLEFVPHERSDSE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 221 EWYGEKLRCLLEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKFHNSPVHTYSIHFGTETPNELEFSSLVAQHCQTEHH 300
Cdd:COG0367 235 EEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGPLKTFSIGFEDSAYDESPYARAVAEHLGTEHH 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 301 ILEITFKQMWELLPQTMLYLDNPIGDPLTVPNLLLGKLARENVQIILNGEGGDPCFGGpknqpmlinslYSRinhqdslk 380
Cdd:COG0367 315 EVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGG-----------YPR-------- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 381 aylisFQKCALDLPQLLKTEVWQTLVNQPcvfvDDLNAKINYLNRLMILNIKFKGADHILTKVNNLTQGAGLQGLSPLFD 460
Cdd:COG0367 376 -----YREAALLLSPDFAEALGGELVPRL----YAESGAEDPLRRMLYLDLKTYLPGDLLVKVDRMSMAHSLEVRVPFLD 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 461 RRIVDFSMQIPPEYKLSGVEEKAVFKNAVSNILPKEIIQRPKSGMMVPVQLGFRKYWQKQARKLLLNKNGEIANYINQDI 540
Cdd:COG0367 447 HRLVEFALSLPPELKLRGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLRGPLREWLEDLLSDESLAARGLFDPDA 526
|
490 500 510
....*....|....*....|....*....|..
gi 496700806 541 IRNWLD--FQGDtwGRYGVKLWLLVSLEIWLQ 570
Cdd:COG0367 527 VRRLLEehLAGR--RDHSRKLWSLLMLELWLR 556
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
89-504 |
4.05e-64 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 217.20 E-value: 4.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 89 SDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDAIGKKNLYYTLDRGTYYIA---------------PKLT 153
Cdd:TIGR01536 97 SDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQLYFAseikallahpnikpfPDGA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 154 TLAPYHYHQldlialrdylccaFVPGTKTLWQNVQEIAQG---TFLKIPSHEITHYWQLKEniiEPYQPLEWYGEKLRCL 230
Cdd:TIGR01536 177 ALAPGFGFV-------------RVPPPSTFFRGVFELEPGhdlPLDDDGLNIERYYWERRD---EHTDSEEDLVDELRSL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 231 LEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKFHNS-PVHTYSIHFGTE-TPNELEFSSLVAQHCQTEHHILEITFKQ 308
Cdd:TIGR01536 241 LEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPRgPVHTFSIGFEGSpDFDESKYARKVADHLGTEHHEVLFSVEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 309 MWELLPQTMLYLDNPIGDPLTVPNLLLGKLAREN-VQIILNGEGGDPCFGGpknqpmlinslYSRInhqdsLKAYlisfq 387
Cdd:TIGR01536 321 GLDALPEVIYHLEEPTTIRASIPLYLLSKLAREDgVKVVLSGEGADELFGG-----------YLYF-----HEAP----- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 388 kcaldlpqllktevwqtlvnqpcvFVDDLNAKINYLN--RLMILNIKFKGAdhiltkvnnLTQGAGLQGLSPLFDRRIVD 465
Cdd:TIGR01536 380 ------------------------AAEALREELQYLDleLYMPGLLRRKDR---------MSMAHSLEVRVPFLDHELVE 426
|
410 420 430
....*....|....*....|....*....|....*....
gi 496700806 466 FSMQIPPEYKLSGVEEKAVFKNAVSNILPKEIIQRPKSG 504
Cdd:TIGR01536 427 YALSIPPEMKLRDGKEKYLLREAFEGYLPEEILWRPKEG 465
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
226-570 |
3.33e-61 |
|
Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.
Pssm-ID: 395594 [Multi-domain] Cd Length: 279 Bit Score: 203.62 E-value: 3.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 226 KLRCLLEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKFHNSPVHTYSIHFGTETPNELEFSSLVAQHCQTEHHILEIT 305
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPSPLHTFSIGFEGRGYDEAPYAREVAEHLGTDHHELVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 306 FKQMWELLPQTMLYLDNPIGDPLTVPNLLLGKLARE-NVQIILNGEGGDPCFGGpknqpmlinslYSRINHQDslkayli 384
Cdd:pfam00733 81 PEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLARRkGVKVVLSGEGADELFGG-----------YPFYKGED------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 385 sfqkcaldlpqllktevwqtlvnqpcvfvddlnakinYLNRLMILNIKFKGADHILTkVNNLTQGAGLQGLSPLFDRRIV 464
Cdd:pfam00733 143 -------------------------------------PLRRMLYLDLKTLLPGDLLR-ADRMSMAHGLEVRVPFLDHRLV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 465 DFSMQIPPEYKLSGVEEKAVFKNAVSNILPKEIIQRPKSGMMVPVQ-LGFRKYWQKQARKLLLNKNGEIANYINQDIIRN 543
Cdd:pfam00733 185 EYALRLPPELKLRGGIEKYILREALEGILPDEILERPKEGFSAPVGdWKLRGPLRELAEDLLSDSRLAKEGLLDREAVRE 264
|
330 340
....*....|....*....|....*..
gi 496700806 544 WLDfqgdtwgrygvkLWLLVSLEIWLQ 570
Cdd:pfam00733 265 LLD------------EHLAGMLELWLR 279
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
244-509 |
2.20e-36 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 135.09 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 244 PVGVFLSGGLDSSSITALTRKFH-NSPVHTYSIHFGTETPNELEFSSLVAQHCQTEHHILEITFKQMWELLP--QTMLYL 320
Cdd:cd01991 4 PVGVLLSGGLDSSLIAALAARLLpETPIDLFTVGFEGSPTPDRAAARRVAEELGTEHHEVEVTIEELLDALPdvILIYPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 321 DNPIGDPLTVPNLLLGKLARENVQ-IILNGEGGDPCFGGpknqpmlinslYSRinhqdslkaYLISFQKCALDLPQLLKt 399
Cdd:cd01991 84 DTPMDLSIAIPLYFASRLAGKLGAkVVLSGEGADELFGG-----------YSR---------HRDAPLRGWEALEEELL- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 400 evwqtlvnqpcvfvddlnakiNYLNRLMILNikfkgadhiLTKVNNLTQGAGLQGLSPLFDRRIVDFSMQIPPEYKLS-- 477
Cdd:cd01991 143 ---------------------RDLDRLWTRN---------LGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDpr 192
|
250 260 270
....*....|....*....|....*....|..
gi 496700806 478 GVEEKAVFKNAVSNILPKEIIQRPKSGMMVPV 509
Cdd:cd01991 193 GGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
75-502 |
2.49e-35 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 139.66 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 75 QLLEKLCLDNH---TEiSDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDAIGKKNLYYTLD-RGTYYIAP 150
Cdd:PRK09431 82 QELRAELGDKYafqTG-SDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDeHGNLYFAS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 151 KLTTLAPyhyhQLDLIALrdylccaFVPGtktlwqnvqeiaqgtflkipsheitHYWQLKENIIEPYQPLEW--YG---- 224
Cdd:PRK09431 161 EMKALVP----VCKTIKE-------FPPG-------------------------HYYWSKDGEFVRYYQRDWfdYDavkd 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 225 -----EKLRCLLEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKFHNSPV-------------HTYSIhfGTETPNELE 286
Cdd:PRK09431 205 nvtdkNELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAIAKKYAARRIedderseawwpqlHSFAV--GLEGSPDLK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 287 FSSLVAQHCQTEHHILEITFKQMWELLPQTMLYLDNpiGDPLTV----PNLLLGKL-ARENVQIILNGEGGDPCFGG--- 358
Cdd:PRK09431 283 AAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLET--YDVTTIrastPMYLMARKiKAMGIKMVLSGEGADELFGGyly 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 359 PKNQPmlinslysriNHQDslkaylisFQKcaldlpqllktevwqtlvnqpcvfvdDLNAKINYLNRlmilnikfkgADh 438
Cdd:PRK09431 361 FHKAP----------NAKE--------FHE--------------------------ETVRKLRALHM----------YD- 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496700806 439 iLTKVNNLTQGAGLQGLSPLFDRRIVDFSMQIPPEYKLSGVE--EKAVFKNAVSNILPKEIIQRPK 502
Cdd:PRK09431 386 -CLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkmEKHILREAFEGYLPESILWRQK 450
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
81-570 |
4.05e-117 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 358.38 E-value: 4.05e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 81 CLDNHTEI--------------SDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDAIGKKNLYYTLDRGTY 146
Cdd:COG0367 76 EIYNYRELraelealghrfrthSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 147 YIA--PK-LTTLaPYHYHQLDLIALRDYLCCAFVPGTKTLWQNVQEIAQGTFLKI---PSHEITHYWQLKENIIEPYQPL 220
Cdd:COG0367 156 AFAseLKaLLAH-PGVDRELDPEALAEYLTLGYVPAPRTIFKGIRKLPPGHYLTVdagGELEIRRYWDLEFVPHERSDSE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 221 EWYGEKLRCLLEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKFHNSPVHTYSIHFGTETPNELEFSSLVAQHCQTEHH 300
Cdd:COG0367 235 EEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGPLKTFSIGFEDSAYDESPYARAVAEHLGTEHH 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 301 ILEITFKQMWELLPQTMLYLDNPIGDPLTVPNLLLGKLARENVQIILNGEGGDPCFGGpknqpmlinslYSRinhqdslk 380
Cdd:COG0367 315 EVTVTPEDLLDALPDLVWHLDEPFADPSAVPTYLLSRLAREHVKVVLSGEGADELFGG-----------YPR-------- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 381 aylisFQKCALDLPQLLKTEVWQTLVNQPcvfvDDLNAKINYLNRLMILNIKFKGADHILTKVNNLTQGAGLQGLSPLFD 460
Cdd:COG0367 376 -----YREAALLLSPDFAEALGGELVPRL----YAESGAEDPLRRMLYLDLKTYLPGDLLVKVDRMSMAHSLEVRVPFLD 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 461 RRIVDFSMQIPPEYKLSGVEEKAVFKNAVSNILPKEIIQRPKSGMMVPVQLGFRKYWQKQARKLLLNKNGEIANYINQDI 540
Cdd:COG0367 447 HRLVEFALSLPPELKLRGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLGPWLRGPLREWLEDLLSDESLAARGLFDPDA 526
|
490 500 510
....*....|....*....|....*....|..
gi 496700806 541 IRNWLD--FQGDtwGRYGVKLWLLVSLEIWLQ 570
Cdd:COG0367 527 VRRLLEehLAGR--RDHSRKLWSLLMLELWLR 556
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
89-504 |
4.05e-64 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 217.20 E-value: 4.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 89 SDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDAIGKKNLYYTLDRGTYYIA---------------PKLT 153
Cdd:TIGR01536 97 SDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYDGGQLYFAseikallahpnikpfPDGA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 154 TLAPYHYHQldlialrdylccaFVPGTKTLWQNVQEIAQG---TFLKIPSHEITHYWQLKEniiEPYQPLEWYGEKLRCL 230
Cdd:TIGR01536 177 ALAPGFGFV-------------RVPPPSTFFRGVFELEPGhdlPLDDDGLNIERYYWERRD---EHTDSEEDLVDELRSL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 231 LEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKFHNS-PVHTYSIHFGTE-TPNELEFSSLVAQHCQTEHHILEITFKQ 308
Cdd:TIGR01536 241 LEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPRgPVHTFSIGFEGSpDFDESKYARKVADHLGTEHHEVLFSVEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 309 MWELLPQTMLYLDNPIGDPLTVPNLLLGKLAREN-VQIILNGEGGDPCFGGpknqpmlinslYSRInhqdsLKAYlisfq 387
Cdd:TIGR01536 321 GLDALPEVIYHLEEPTTIRASIPLYLLSKLAREDgVKVVLSGEGADELFGG-----------YLYF-----HEAP----- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 388 kcaldlpqllktevwqtlvnqpcvFVDDLNAKINYLN--RLMILNIKFKGAdhiltkvnnLTQGAGLQGLSPLFDRRIVD 465
Cdd:TIGR01536 380 ------------------------AAEALREELQYLDleLYMPGLLRRKDR---------MSMAHSLEVRVPFLDHELVE 426
|
410 420 430
....*....|....*....|....*....|....*....
gi 496700806 466 FSMQIPPEYKLSGVEEKAVFKNAVSNILPKEIIQRPKSG 504
Cdd:TIGR01536 427 YALSIPPEMKLRDGKEKYLLREAFEGYLPEEILWRPKEG 465
|
|
| eps_aminotran_1 |
TIGR03108 |
exosortase A system-associated amidotransferase 1; The predicted protein-sorting ... |
89-570 |
2.83e-63 |
|
exosortase A system-associated amidotransferase 1; The predicted protein-sorting transpeptidase that we call exosortase (see TIGR02602) has distinct subclasses that associated with different types of exopolysaccharide production loci. This model represents a distinct clade among a set of amidotransferases largely annotated (not necessarily accurately) as glutatime-hydrolyzing asparagine synthases. Members of this clade are essentially restricted to the characteristic exopolysaccharide (EPS) regions that contain the exosortase 1 genome (xrtA), in genomes that also have numbers of PEP-CTERM domain (TIGR02595) proteins.
Pssm-ID: 132152 [Multi-domain] Cd Length: 628 Bit Score: 219.22 E-value: 2.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 89 SDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDAIGKKNLYYT-LDRGTYYIAPKLTTLA--PYHYHQLDL 165
Cdd:TIGR03108 99 SDTEVIVHAWEEWGEACVERFRGMFAFALWDRNQETLFLARDRLGIKPLYYAlLADGWFIFGSELKALTahPSLPRELDP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 166 IALRDYLCCAFVPGTKTLWQNVQEIAQGTFLKI----PSHEITHYWQLKeniIEPYQPL--EWYGEKLRCLLEQVVKEYL 239
Cdd:TIGR03108 179 LAVEDYFAYGYVPDPRTIFKGVKKLEPGHTLTLrrgaPPARPRCYWDVS---FAPAAPLseADALAELIERLREAVRSRM 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 240 PENQPVGVFLSGGLDSSSITALTRKFHNSPVHTYSIHFGTETPNELEFSSLVAQHCQTEHHILEITFKQMWELLPQTMLY 319
Cdd:TIGR03108 256 VADVPLGAFLSGGVDSSAVVALMAGLSDTPVNTCSIAFDDPAFDESAYARQVAERYGTNHRVETVDPDDFSLVDRLAGLY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 320 lDNPIGDPLTVPNLLLGKLARENVQIILNGEGGDPCFGGPK-------------------NQPM--LINSLYSRINH--- 375
Cdd:TIGR03108 336 -DEPFADSSALPTYRVCELARKRVTVALSGDGGDELFAGYRryrwhmaeervrgilplglRRPLfgTLGRLYPKADWapr 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 376 ------------QDSLKAYlisFQKCALDLP----QLLKTEVWQTLVN-QPCVFVDDLNAKI---NYLNRLMILNIKFKG 435
Cdd:TIGR03108 415 mlrakttfqalaRDPLEGY---FHSVSVLDNalrrQLFSPDFRRELQGyRAIEVLRRHAARAptdDALSLAQYLDLKTYL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 436 ADHILTKVNNLTQGAGLQGLSPLFDRRIVDFSMQIPPEYKLSGVEEKAVFKNAVSNILPKEIIQRPKSGMMVPVQLGFRK 515
Cdd:TIGR03108 492 PGDILTKVDRASMAHGLEVRVPLLDHRLVEWAAGLPPDLKLRGGEGKYLLKKAMRPYLPDDVLYRPKMGFSVPLAAWFRG 571
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 496700806 516 YWQKQARKLLLNKNGEIANYINQDIIRNWLD-FQGDTWGrYGVKLWLLVSLEIWLQ 570
Cdd:TIGR03108 572 PLRERVRTLVLGETLAETGLFDPAFIRKLVDqHQSGRRD-YSAPLWSLLMFEAFLR 626
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
226-570 |
3.33e-61 |
|
Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.
Pssm-ID: 395594 [Multi-domain] Cd Length: 279 Bit Score: 203.62 E-value: 3.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 226 KLRCLLEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKFHNSPVHTYSIHFGTETPNELEFSSLVAQHCQTEHHILEIT 305
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPSPLHTFSIGFEGRGYDEAPYAREVAEHLGTDHHELVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 306 FKQMWELLPQTMLYLDNPIGDPLTVPNLLLGKLARE-NVQIILNGEGGDPCFGGpknqpmlinslYSRINHQDslkayli 384
Cdd:pfam00733 81 PEDLLDALPDVIWHLDEPFADPSAIPLYLLSRLARRkGVKVVLSGEGADELFGG-----------YPFYKGED------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 385 sfqkcaldlpqllktevwqtlvnqpcvfvddlnakinYLNRLMILNIKFKGADHILTkVNNLTQGAGLQGLSPLFDRRIV 464
Cdd:pfam00733 143 -------------------------------------PLRRMLYLDLKTLLPGDLLR-ADRMSMAHGLEVRVPFLDHRLV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 465 DFSMQIPPEYKLSGVEEKAVFKNAVSNILPKEIIQRPKSGMMVPVQ-LGFRKYWQKQARKLLLNKNGEIANYINQDIIRN 543
Cdd:pfam00733 185 EYALRLPPELKLRGGIEKYILREALEGILPDEILERPKEGFSAPVGdWKLRGPLRELAEDLLSDSRLAKEGLLDREAVRE 264
|
330 340
....*....|....*....|....*..
gi 496700806 544 WLDfqgdtwgrygvkLWLLVSLEIWLQ 570
Cdd:pfam00733 265 LLD------------EHLAGMLELWLR 279
|
|
| trio_amidotrans |
TIGR03104 |
asparagine synthase family amidotransferase; Members of this protein family are closely ... |
89-571 |
2.75e-52 |
|
asparagine synthase family amidotransferase; Members of this protein family are closely related to several isoforms of asparagine synthetase (glutamine amidotransferase) and typically have been given this name in genome annotation to date. Each is part of a conserved three-gene cassette sparsely distributed across at least twenty different species known so far, including alpha, beta, and gamma Proteobacteria, Mycobacterium, and Prosthecochloris, which is a member of the Chlorobi. The other two members of the cassette are a probable protease and a member of the GNAT family of acetyltransferases.
Pssm-ID: 274430 [Multi-domain] Cd Length: 589 Bit Score: 188.37 E-value: 2.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 89 SDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDAIGKKNLYYTLDRGTYYIAPKLTTL--APYHYHQLDLI 166
Cdd:TIGR03104 99 GDTEVILKAYHAWGRDCVSRFNGMFAFAIWERDSGRLLLARDRLGIKPLYYAEDAGRLRFASSLPALlaAGGVDTDIDPV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 167 ALRDYLCC-AFVPGTKTLWQNVQEIAQGTFLKI-PSHEITH--YWQL---KENIIEPYQPLEWYgEKLRCLLEQVVKEYL 239
Cdd:TIGR03104 179 ALHHYLTFhAVVPAPHTILKGVRKLPPATWMTVePDGSRTQrsYWSLdagRPADDAARTEADWQ-DAILEALRLAVKRRL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 240 PENQPVGVFLSGGLDSSSITALTRKFHNSPVHTYSIHF---GTETPNELEFSSLVAQHCQTEHHILEITFKQMWELLPQT 316
Cdd:TIGR03104 258 VADVPVGVLLSGGLDSSLIVGLLAEAGVDGLRTFSIGFedvGGEKGDEFEYSDIIAERFHTRHHKIRIPNHRVLPALPEA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 317 MLYLDNPIGDPLTVPNLLLGKLARENVQIILNGEGGDPCFGGPKNQPMLinslysRINHQDSLKAYLISFqkcaLDLPql 396
Cdd:TIGR03104 338 VAAMSEPMVSHDCVAFYLLSEEVSKHVKVVQSGQGADEVFGGYHWYPPL------AAGAGDPVAAYRRAF----FDRD-- 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 397 lkTEVWQTLVnQPCVFVDDLNAK-----------INYLNRLMILNIKFKGADHILTKVNNLTQGAGLQGLSPLFDRRIVD 465
Cdd:TIGR03104 406 --HAEYLEMV-GPRFHAEDVSGEfvadhfarpgaDTAVDQALRLDTTVMLVDDPVKRVDNMTMAWGLEARVPFLDHELVE 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 466 FSMQIPPEYKLsGVEEKAVFKNAVSNILPKEIIQRPKSGMMVPVQLGFRKYWQKQARKLLLNKNGEIANYINQDIIRNWL 545
Cdd:TIGR03104 483 LAARIPPELKL-ADGGKGVLKEAARGVIPSEVIDRPKGYFPVPALKYLRGPFLEWVRDALTSPAARERGLFQRAYVDRLL 561
|
490 500
....*....|....*....|....*..
gi 496700806 546 DFQGDTWGRY-GVKLWLLVSLEIWLQV 571
Cdd:TIGR03104 562 ADPDGHLTPLrGSKLWQLALLELWLQR 588
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
244-509 |
2.20e-36 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 135.09 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 244 PVGVFLSGGLDSSSITALTRKFH-NSPVHTYSIHFGTETPNELEFSSLVAQHCQTEHHILEITFKQMWELLP--QTMLYL 320
Cdd:cd01991 4 PVGVLLSGGLDSSLIAALAARLLpETPIDLFTVGFEGSPTPDRAAARRVAEELGTEHHEVEVTIEELLDALPdvILIYPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 321 DNPIGDPLTVPNLLLGKLARENVQ-IILNGEGGDPCFGGpknqpmlinslYSRinhqdslkaYLISFQKCALDLPQLLKt 399
Cdd:cd01991 84 DTPMDLSIAIPLYFASRLAGKLGAkVVLSGEGADELFGG-----------YSR---------HRDAPLRGWEALEEELL- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 400 evwqtlvnqpcvfvddlnakiNYLNRLMILNikfkgadhiLTKVNNLTQGAGLQGLSPLFDRRIVDFSMQIPPEYKLS-- 477
Cdd:cd01991 143 ---------------------RDLDRLWTRN---------LGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDpr 192
|
250 260 270
....*....|....*....|....*....|..
gi 496700806 478 GVEEKAVFKNAVSNILPKEIIQRPKSGMMVPV 509
Cdd:cd01991 193 GGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
75-502 |
2.49e-35 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 139.66 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 75 QLLEKLCLDNH---TEiSDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDAIGKKNLYYTLD-RGTYYIAP 150
Cdd:PRK09431 82 QELRAELGDKYafqTG-SDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDeHGNLYFAS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 151 KLTTLAPyhyhQLDLIALrdylccaFVPGtktlwqnvqeiaqgtflkipsheitHYWQLKENIIEPYQPLEW--YG---- 224
Cdd:PRK09431 161 EMKALVP----VCKTIKE-------FPPG-------------------------HYYWSKDGEFVRYYQRDWfdYDavkd 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 225 -----EKLRCLLEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKFHNSPV-------------HTYSIhfGTETPNELE 286
Cdd:PRK09431 205 nvtdkNELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAIAKKYAARRIedderseawwpqlHSFAV--GLEGSPDLK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 287 FSSLVAQHCQTEHHILEITFKQMWELLPQTMLYLDNpiGDPLTV----PNLLLGKL-ARENVQIILNGEGGDPCFGG--- 358
Cdd:PRK09431 283 AAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLET--YDVTTIrastPMYLMARKiKAMGIKMVLSGEGADELFGGyly 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 359 PKNQPmlinslysriNHQDslkaylisFQKcaldlpqllktevwqtlvnqpcvfvdDLNAKINYLNRlmilnikfkgADh 438
Cdd:PRK09431 361 FHKAP----------NAKE--------FHE--------------------------ETVRKLRALHM----------YD- 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496700806 439 iLTKVNNLTQGAGLQGLSPLFDRRIVDFSMQIPPEYKLSGVE--EKAVFKNAVSNILPKEIIQRPK 502
Cdd:PRK09431 386 -CLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkmEKHILREAFEGYLPESILWRQK 450
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
62-502 |
2.42e-26 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 113.27 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 62 FIIMGDIWlsNRWQLLEKLCLDNH--TEISDQQIVAQLWEKYNHQSL-TMLLGMFNIVIWDRNQQELYLIRDAIGKKNLY 138
Cdd:PTZ00077 77 LMQNGEIY--NHWEIRPELEKEGYkfSSNSDCEIIGHLYKEYGPKDFwNHLDGMFATVIYDMKTNTFFAARDHIGIIPLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 139 YTLDR-GTYYIAPKLTTL--APYHYHQldlialrdylccaFVPGtkTLWQNVQEIaqgtflkipsHEITHY----WQLKE 211
Cdd:PTZ00077 155 IGYAKdGSIWFSSELKALhdQCVEVKQ-------------FPPG--HYYDQTKEK----------GEFVRYynpnWHDFD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 212 NIIEPYQPLEwygEKLRCLLEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKFHNSP-----------VHTYSIhfGTE 280
Cdd:PTZ00077 210 HPIPTGEIDL---EEIREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIVAKLIKNGeidlskrgmpkLHSFCI--GLE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 281 TPNELEFSSLVAQHCQTEHHILEITFKQMWELLPQTMLYL---DNPIGDPLTVPNLLLGKLARENVQIILNGEGGDPCFG 357
Cdd:PTZ00077 285 GSPDLKAARKVAEYLGTEHHEFTFTVEEGIDALPDVIYHTetyDVTTIRASTPMYLLSRRIKALGIKMVLSGEGSDELFG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 358 GpknqpmlinslysrinhqdslkaYLIsFQKcALDLPQllktevwqtlvnqpcvFVDDLNAKINYLNRLMILnikfkgad 437
Cdd:PTZ00077 365 G-----------------------YLY-FHK-APNREE----------------FHRELVRKLHDLHKYDCL-------- 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496700806 438 hiltKVNNLTQGAGLQGLSPLFDRRIVDFSMQIPPEYKLSGVEEK--------AVFKNAVSNILPKEIIQRPK 502
Cdd:PTZ00077 396 ----RANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFEGqmekyilrKAFEGLEKPYLPDEILWRQK 464
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
62-502 |
2.67e-26 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 113.32 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 62 FIIMGDIWlsNRWQLLEKLCLDNHTEISDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDAIGKKNLY--Y 139
Cdd:PLN02549 72 VTANGEIY--NHKELREKLKLHKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYigW 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 140 TLDrGTYYIAPKLTTLA----------PYHYhqldlialrdylccaFVPGTKTL--WQNVQEIAQgtflKIPSheithyw 207
Cdd:PLN02549 150 GLD-GSVWFASEMKALCddcerfeefpPGHY---------------YSSKAGGFrrWYNPPWFSE----SIPS------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 208 qlkeniiEPYQPLEwygekLRCLLEQVVKEYLPENQPVGVFLSGGLDSSSITALTRKF---------HNSPVHTYSIhfG 278
Cdd:PLN02549 203 -------TPYDPLV-----LREAFEKAVIKRLMTDVPFGVLLSGGLDSSLVASIAARHlaetkaarqWGQQLHSFCV--G 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 279 TETPNELEFSSLVAQHCQTEHHILEITFKQMWELLPQTMLYLDNPigDPLTV----PNLLLG-KLARENVQIILNGEGGD 353
Cdd:PLN02549 269 LEGSPDLKAAREVADYLGTVHHEFHFTVQEGIDAIEDVIYHLETY--DVTTIrastPMFLMSrKIKSLGVKMVLSGEGSD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 354 PCFGGpknqpmlinslysrinhqdslkaYLIsFQKCaldlPQllKTEvwqtlvnqpcvFVDDLNAKINYLNRLMILnikf 433
Cdd:PLN02549 347 EIFGG-----------------------YLY-FHKA----PN--KEE-----------FHKETCRKIKALHQYDCL---- 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496700806 434 kgadhiltKVNNLTQGAGLQGLSPLFDRRIVDFSMQIPPEYKL----SGVEEKAVFKNAVSN----ILPKEIIQRPK 502
Cdd:PLN02549 382 --------RANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMirpgEGRIEKWVLRKAFDDeedpYLPKHILWRQK 450
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
56-208 |
6.05e-24 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 100.32 E-value: 6.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 56 VSPKQRFIIM--GDIWlsNRWQL---LEKLCLDNHTEiSDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRD 130
Cdd:cd00712 62 VSEDGRLVLVfnGEIY--NYRELraeLEALGHRFRTH-SDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 131 AIGKKNLYYTLDRGTYYIA--PKLTTLAPYHYHQLDLIALRDYLCCAFVPGTKTLWQNVQEIAQGTFLKI--PSHEITHY 206
Cdd:cd00712 139 RFGIKPLYYGRDGGGLAFAseLKALLALPGVPRELDEAALAEYLAFQYVPAPRTIFKGIRKLPPGHYLTVdpGGVEIRRY 218
|
..
gi 496700806 207 WQ 208
Cdd:cd00712 219 WD 220
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
54-144 |
6.94e-12 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 62.54 E-value: 6.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 54 FSVSPKQRFIIM--GDIWlsNRWQLLEKLCLDNHT--EISDQQIVAQLWEK-YNHQSLTMLLGMFNIVIWDRNQQELYLI 128
Cdd:pfam13537 16 MVSSEDGRYVIVfnGEIY--NYRELRAELEAKGYRfrTHSDTEVILHLYEAeWGEDCVDRLNGMFAFAIWDRRRQRLFLA 93
|
90
....*....|....*.
gi 496700806 129 RDAIGKKNLYYTLDRG 144
Cdd:pfam13537 94 RDRFGIKPLYYGRDDG 109
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
56-149 |
4.01e-11 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 60.78 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 56 VSPKQRFIIM--GDIWlsNRWQLLEKLCLDNHTEI--SDQQIVAQLWEKYNHQSLTMLLGMFNIVIWDRNQQELYLIRDA 131
Cdd:pfam13522 33 LSRDGRLVLVhnGEIY--NYGELREELADLGHAFRsrSDTEVLLALYEEWGEDCLERLRGMFAFAIWDRRRRTLFLARDR 110
|
90
....*....|....*...
gi 496700806 132 IGKKNLYYTLDRGTYYIA 149
Cdd:pfam13522 111 LGIKPLYYGILGGGFVFA 128
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
56-149 |
1.13e-09 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 58.61 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 56 VSPKQRFIIM--GDIWlsNRWQLLEKLCLDNHT--EISDQQIVAQLWEKYNH---------QSLTMLLGMFNIVIWDRNQ 122
Cdd:cd00352 92 RSEDGRIALVhnGEIY--NYRELREELEARGYRfeGESDSEVILHLLERLGRegglfeaveDALKRLDGPFAFALWDGKP 169
|
90 100
....*....|....*....|....*...
gi 496700806 123 QELYLIRDAIGKKNLYYTLDR-GTYYIA 149
Cdd:cd00352 170 DRLFAARDRFGIRPLYYGITKdGGLVFA 197
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
247-306 |
1.68e-03 |
|
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 40.14 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496700806 247 VFLSGGLDSSSITALTRKfHNSPVHTYSIHFGTETPNELEFSSLVAQHCQ-TEHHILEITF 306
Cdd:COG0603 7 VLLSGGLDSTTCLAWALA-RGYEVYALSFDYGQRHRKELEAARRIAKALGvGEHKVIDLDF 66
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
247-306 |
3.63e-03 |
|
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.
Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 39.14 E-value: 3.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496700806 247 VFLSGGLDSSSITALTRKfHNSPVHTYSIHFGTETPNELEFSSLVAQHCQTEHHILEITF 306
Cdd:pfam06508 4 VLLSGGLDSTTCLAWAKK-EGYEVYALSFDYGQRHRKELECAKKIAKALGVEHKILDLDF 62
|
|
| QueC-like |
cd01995 |
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
247-306 |
5.98e-03 |
|
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467499 [Multi-domain] Cd Length: 208 Bit Score: 38.36 E-value: 5.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496700806 247 VFLSGGLDSSSITALTRKfHNSPVHTYSIHFGTET-PNELEFSSLVAQHCQTEHHILEITF 306
Cdd:cd01995 5 VLLSGGLDSTTLLYWALK-EGYEVHALTFDYGQRHaKEELEAAKLIAKLLGIEHKVIDLSF 64
|
|
| |
