|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-553 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 1183.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDIKTDAGELRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDVNAGAQPLYNEKKTHALAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 81 HQALRAEYGDRYAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGHDEHGNFYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 161 EMKALVPVCRTIKEFPAGSYLWSQDGEIRPYYQRDWFDYEAVKDNVTDKAELRQALEESVKSHLMSDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 241 SVISAITKKFAARRVEDQERSEAWWPQLHSFAVGLEGAPDLKAAQEVANHLGTVHHEIHFTVQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 321 VTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKELHEETVRKLQALHMFDCARANKAMSAWGVEA 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 401 RVPFLDKKFLDVAMRINPQDKMCGNGKMEKHILRECFESYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAKQVSDQQLET 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955362 481 ASFRFPYNTPASKEAYLYREIFEELFPVPSAAECVPGGPSVACSSAKAIEWDESFKAMNDPSGRAV-GVHQSAY 553
Cdd:PRK09431 481 ARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAVsGVHQSAY 554
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-453 |
0e+00 |
|
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: 554.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 4 IFGVLDIKTDAGELRKKALELSRLMRHRGPDWSGV-YASDKAILAHERLSIVDVNAGAQPLYNEKKTHALAVNGEIYNHQ 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 83 ALRAEYGDR-YAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGHDeHGNFYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 162 MKALVPVCrTIKEFPAGSYLWSQDGEIRP----YYQRDWFDYEAVKDNVTD------------------------KAELR 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFVRVpppsTFFRGVFELEPGHDLPLDddglnieryywerrdehtdseedlVDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 214 QALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKFAARrvedqerseawwPQLHSFAVGLEGAPDL---KAAQEVANH 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 291 LGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKEL 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 371 HEETVRKLQALHMFDCARANKAMS-AWGVEARVPFLDKKFLDVAMRINPQDKMcgNGKMEKHILRECFESYLPASVAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKDRMSmAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 489955362 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
0e+00 |
|
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: 521.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDikTDAGELRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDV-NAGAQPLYNEKKTHALAVNGEIY 79
Cdd:COG0367 1 MCGIAGIID--FDGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 80 NHQALRAEYGDR-YAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGHDEhGNFYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 159 ASEMKALVP---------------------------VCRTIKEFPAGSYLWSQDG---EIRPYYQRDWFDYEAVKDNVTD 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 209 KAELRQALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKFAARRvedqerseawwpqLHSFAVGLEGAP--DLKAAQE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGP-------------LKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 287 VANHLGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMgIKMVLSGEGSDEVFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 367 AKEL-------------------HEETVRKLQALHMF------DCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDK 421
Cdd:COG0367 382 LLSPdfaealggelvprlyaesgAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 422 McgNGKMEKHILRECFESYLPASVAWRQKEQFSDGVGySWID-TLKEVAAKQVSDQQLETASFrfpYNTPAskeaylYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FDPDA------VRR 529
|
....*..
gi 489955362 501 IFEELFP 507
Cdd:COG0367 530 LLEEHLA 536
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
211-512 |
2.34e-109 |
|
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: 327.65 E-value: 2.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 211 ELRQALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKFAArrvedqerseawwPQLHSFAVGLEGA--PDLKAAQEVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEGRgyDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 289 NHLGTVHHEIHFTVQEGLDAIRDVIYHIETydVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHkapNAK 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 369 ELHEETVRKLQALHMFDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDKMCGNgkMEKHILRECFESYLPASVAWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955362 449 QKEQFSDGVGYSWID-TLKEVAAKQVSDQqletasfrfpyntPASKEAYLYREIFEELFPVPSAA 512
Cdd:pfam00733 221 PKEGFSAPVGDWKLRgPLRELAEDLLSDS-------------RLAKEGLLDREAVRELLDEHLAG 272
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
226-457 |
5.47e-93 |
|
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: 283.78 E-value: 5.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 226 SDVPYGVLLSGGLDSSVISAITKKFAARrvedqerseawwPQLHSFAVGLEG--APDLKAAQEVANHLGTVHHEIHFTVQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGspTPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 304 EGLDAIRDVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNA--KELHEETVRKLQAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955362 382 HMFDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDKMCGNGKMEKHILRECFESYLPASVAWRQKEQFSDGV 457
Cdd:cd01991 149 WTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-362 |
1.08e-28 |
|
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide bond-forming cyclase of lasso peptide biosynthesis systems, from a subgroup that contains primarily cyanobacterial examples. These proteins resemble the glutamine-hydrolyzing asparagine synthase AsnB (EC 6.3.5.4).
Pssm-ID: 468066 [Multi-domain] Cd Length: 668 Bit Score: 120.87 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGV--LDIKTDAGELRKKALELsrlMRHRGPDWSGVYASDKAILAH-------ERLSivdvnaGAQPLYNEKKTHA 71
Cdd:NF033535 1 MSGIVGIyyLDGRPVDREDLQQMVDI---LAHRGPDGADIWCEGSVGLGHrmlwttpESLL------EKLPLVNQTGDLV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 72 LAVNGEIYNHQALRAEYG-DRYAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGH 150
Cdd:NF033535 72 ITADARIDNRDELISALQlNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 151 DEHGnFYVASEMKAL-----VPVC----------------------RTIKEFPAGSYLW-SQDG-EIRPYYQRDwFDYEA 201
Cdd:NF033535 152 SDKR-FAFASEIKALlclpeVPRRlnevriadylalmledkvitfyQDIFRLPPAHSMTvSQSGlQIRSYWSLD-PSREL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 202 VKDNVTDKAE-LRQALEESVKSHLMSDVPYGVLLSGGLDSSVISAItkkfaARRVEDQERSeawwPQLHSFAVGLEgapD 280
Cdd:NF033535 230 RLDSDEEYAEaFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCV-----ARQLLAEEKK----APLHTFSNIFD---K 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 281 LKAAQE------VANHLGTVHHEIH---FTVQEGLDAIrdVIYHIETYdvttiraSTPMYLMSRKI----KAMGIKMVLS 347
Cdd:NF033535 298 VTECDErpfinaVLEQGGLIPHYVHadqFGPLSDLEQI--FEYEDEPF-------LGPNHFLPWGLnraaQKEGVRILLD 368
|
410
....*....|....*.
gi 489955362 348 GEGSDE-VFGGYLYFH 362
Cdd:NF033535 369 GFDGDStVSHGHGYLT 384
|
|
| macrolact_Ik_Al |
NF033561 |
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology ... |
212-296 |
2.79e-03 |
|
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology enzymes known to form the lactam bond of the isopeptide linkage of lasso peptides. This family includes the peptide cyclase involved in biosynthesis of the lasso peptide albusnodin. However, another member of this family belongs to the biosynthesis cassette for ikarugamycin, a macrolactam whose biosynthesis relies on a hybrid PKS/NRPS system, not a ribosomally produced peptide.
Pssm-ID: 468087 [Multi-domain] Cd Length: 561 Bit Score: 40.28 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 212 LRQALEESVKSHLMSDVPYGVLLSGGLDSSVISAItkkfAARRVEDQERSEAWwpQLHsfAVGLEGAPDLKAAQEVANHL 291
Cdd:NF033561 195 LRAALAAAVALRVDGAPPLSSDLSGGLDSTTLALL----AARCLPVGRRLTGV--TVH--PEGRTEGGDLDYARLAARAP 266
|
....*
gi 489955362 292 GTVHH 296
Cdd:NF033561 267 RIRHR 271
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-553 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 1183.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDIKTDAGELRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDVNAGAQPLYNEKKTHALAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 81 HQALRAEYGDRYAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGHDEHGNFYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 161 EMKALVPVCRTIKEFPAGSYLWSQDGEIRPYYQRDWFDYEAVKDNVTDKAELRQALEESVKSHLMSDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 241 SVISAITKKFAARRVEDQERSEAWWPQLHSFAVGLEGAPDLKAAQEVANHLGTVHHEIHFTVQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 321 VTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKELHEETVRKLQALHMFDCARANKAMSAWGVEA 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 401 RVPFLDKKFLDVAMRINPQDKMCGNGKMEKHILRECFESYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAKQVSDQQLET 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955362 481 ASFRFPYNTPASKEAYLYREIFEELFPVPSAAECVPGGPSVACSSAKAIEWDESFKAMNDPSGRAV-GVHQSAY 553
Cdd:PRK09431 481 ARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAVsGVHQSAY 554
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-554 |
0e+00 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 838.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDIKTDAGELRKKALELSRLMRHRGPDWSGVYASDKA-----ILAHERLSIVDVNAGAQPLYNEKKTHALAVN 75
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRKALELSKRLRHRGPDWSGIIVLENSpgtynILAHERLAIVDLSDGKQPLLDDDETVALMQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 76 GEIYNHQALRAEY-GDRYAFQTGSDCEVILALYQEKGP-EFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGHDEH 153
Cdd:PTZ00077 81 GEIYNHWEIRPELeKEGYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 154 GNFYVASEMKALVPVCRTIKEFPAGSYLWS--QDGEIRPYYQRDWFDYEA-VKDNVTDKAELRQALEESVKSHLMSDVPY 230
Cdd:PTZ00077 161 GSIWFSSELKALHDQCVEVKQFPPGHYYDQtkEKGEFVRYYNPNWHDFDHpIPTGEIDLEEIREALEAAVRKRLMGDVPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 231 GVLLSGGLDSSVISAITKKFaaRRVEDQERSEAWWPQLHSFAVGLEGAPDLKAAQEVANHLGTVHHEIHFTVQEGLDAIR 310
Cdd:PTZ00077 241 GLFLSGGLDSSIVAAIVAKL--IKNGEIDLSKRGMPKLHSFCIGLEGSPDLKAARKVAEYLGTEHHEFTFTVEEGIDALP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 311 DVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKELHEETVRKLQALHMFDCARAN 390
Cdd:PTZ00077 319 DVIYHTETYDVTTIRASTPMYLLSRRIKALGIKMVLSGEGSDELFGGYLYFHKAPNREEFHRELVRKLHDLHKYDCLRAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 391 KAMSAWGVEARVPFLDKKFLDVAMRINPQDKMC--GNGKMEKHILRECFE----SYLPASVAWRQKEQFSDGVGYSWIDT 464
Cdd:PTZ00077 399 KATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCnaFEGQMEKYILRKAFEglekPYLPDEILWRQKEQFSDGVGYSWIDG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 465 LKEVAAKQVSDQQLETASFRFPYNTPASKEAYLYREIFEELFPVPSAAECVPGGPSVACSSAKAIEWDESFKAMNDPSGR 544
Cdd:PTZ00077 479 LKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTVPYGPSIACSTEKALEWDESFKKNTDESGR 558
|
570
....*....|.
gi 489955362 545 AV-GVHQSAYK 554
Cdd:PTZ00077 559 AVlSVHNDAKQ 569
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-554 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 832.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDIKTDAGELRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDVNAGAQPLYNEKKTHALAVNGEIYN 80
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTIVVTANGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 81 HQALRAEYGDrYAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGHDEHGNFYVAS 160
Cdd:PLN02549 81 HKELREKLKL-HKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 161 EMKALVPVCRTIKEFPAGSYLWSQDGEIRPYYQRDWFDyEAVKDNVTDKAELRQALEESVKSHLMSDVPYGVLLSGGLDS 240
Cdd:PLN02549 160 EMKALCDDCERFEEFPPGHYYSSKAGGFRRWYNPPWFS-ESIPSTPYDPLVLREAFEKAVIKRLMTDVPFGVLLSGGLDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 241 SVISAItkkfAARRVEDQERSEAWWPQLHSFAVGLEGAPDLKAAQEVANHLGTVHHEIHFTVQEGLDAIRDVIYHIETYD 320
Cdd:PLN02549 239 SLVASI----AARHLAETKAARQWGQQLHSFCVGLEGSPDLKAAREVADYLGTVHHEFHFTVQEGIDAIEDVIYHLETYD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 321 VTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKELHEETVRKLQALHMFDCARANKAMSAWGVEA 400
Cdd:PLN02549 315 VTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKEEFHKETCRKIKALHQYDCLRANKSTSAWGLEA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 401 RVPFLDKKFLDVAMRINPQDKMC--GNGKMEKHILRECFE----SYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAKQVS 474
Cdd:PLN02549 395 RVPFLDKEFIDVAMSIDPEWKMIrpGEGRIEKWVLRKAFDdeedPYLPKHILWRQKEQFSDGVGYSWIDGLKAHAEKHVS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 475 DQQLETASFRFPYNTPASKEAYLYREIFEELFPVPSAAECVPGGPSVACSSAKAIEWDESFKAMNDPSGRAV-GVHQSAY 553
Cdd:PLN02549 475 DEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDAARLTVPGGPSVACSTAKAVEWDAAWSKNLDPSGRAAlGVHVAAY 554
|
.
gi 489955362 554 K 554
Cdd:PLN02549 555 E 555
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-453 |
0e+00 |
|
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: 554.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 4 IFGVLDIKTDAGELRKKALELSRLMRHRGPDWSGV-YASDKAILAHERLSIVDVNAGAQPLYNEKKTHALAVNGEIYNHQ 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 83 ALRAEYGDR-YAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGHDeHGNFYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 162 MKALVPVCrTIKEFPAGSYLWSQDGEIRP----YYQRDWFDYEAVKDNVTD------------------------KAELR 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFVRVpppsTFFRGVFELEPGHDLPLDddglnieryywerrdehtdseedlVDELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 214 QALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKFAARrvedqerseawwPQLHSFAVGLEGAPDL---KAAQEVANH 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 291 LGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNAKEL 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 371 HEETVRKLQALHMFDCARANKAMS-AWGVEARVPFLDKKFLDVAMRINPQDKMcgNGKMEKHILRECFESYLPASVAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKDRMSmAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 489955362 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
0e+00 |
|
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: 521.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDikTDAGELRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDV-NAGAQPLYNEKKTHALAVNGEIY 79
Cdd:COG0367 1 MCGIAGIID--FDGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 80 NHQALRAEYGDR-YAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGHDEhGNFYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 159 ASEMKALVP---------------------------VCRTIKEFPAGSYLWSQDG---EIRPYYQRDWFDYEAVKDNVTD 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 209 KAELRQALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKFAARRvedqerseawwpqLHSFAVGLEGAP--DLKAAQE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGP-------------LKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 287 VANHLGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMgIKMVLSGEGSDEVFGGYLYFHKAPN 366
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 367 AKEL-------------------HEETVRKLQALHMF------DCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDK 421
Cdd:COG0367 382 LLSPdfaealggelvprlyaesgAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 422 McgNGKMEKHILRECFESYLPASVAWRQKEQFSDGVGySWID-TLKEVAAKQVSDQQLETASFrfpYNTPAskeaylYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FDPDA------VRR 529
|
....*..
gi 489955362 501 IFEELFP 507
Cdd:COG0367 530 LLEEHLA 536
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
211-512 |
2.34e-109 |
|
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: 327.65 E-value: 2.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 211 ELRQALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKFAArrvedqerseawwPQLHSFAVGLEGA--PDLKAAQEVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEGRgyDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 289 NHLGTVHHEIHFTVQEGLDAIRDVIYHIETydVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHkapNAK 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYK---GED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 369 ELHEETVRKLQALHMFDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDKMCGNgkMEKHILRECFESYLPASVAWR 448
Cdd:pfam00733 143 PLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955362 449 QKEQFSDGVGYSWID-TLKEVAAKQVSDQqletasfrfpyntPASKEAYLYREIFEELFPVPSAA 512
Cdd:pfam00733 221 PKEGFSAPVGDWKLRgPLRELAEDLLSDS-------------RLAKEGLLDREAVRELLDEHLAG 272
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
226-457 |
5.47e-93 |
|
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: 283.78 E-value: 5.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 226 SDVPYGVLLSGGLDSSVISAITKKFAARrvedqerseawwPQLHSFAVGLEG--APDLKAAQEVANHLGTVHHEIHFTVQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGspTPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 304 EGLDAIRDVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLYFHKAPNA--KELHEETVRKLQAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955362 382 HMFDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQDKMCGNGKMEKHILRECFESYLPASVAWRQKEQFSDGV 457
Cdd:cd01991 149 WTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-193 |
1.52e-83 |
|
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: 259.03 E-value: 1.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 2 CSIFGVLDIKtDAGELRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDVNAGAQPLYNEKKTHALAVNGEIYNH 81
Cdd:cd00712 1 CGIAGIIGLD-GASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVLVFNGEIYNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 82 QALRAEYGDR-YAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGHDEhGNFYVAS 160
Cdd:cd00712 80 RELRAELEALgHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDG-GGLAFAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955362 161 EMKALVPVC---------------------------RTIKEFPAGSYLWSQDG--EIRPYYQ 193
Cdd:cd00712 159 ELKALLALPgvpreldeaalaeylafqyvpaprtifKGIRKLPPGHYLTVDPGgvEIRRYWD 220
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
48-167 |
2.20e-54 |
|
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: 179.64 E-value: 2.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 48 HERLSIVDVNAGAQPLYN-EKKTHALAVNGEIYNHQALRAEYGDR-YAFQTGSDCEVILALYQ-EKGPEFLDDLQGMFAF 124
Cdd:pfam13537 1 HRRLSIIDLEGGAQPMVSsEDGRYVIVFNGEIYNYRELRAELEAKgYRFRTHSDTEVILHLYEaEWGEDCVDRLNGMFAF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489955362 125 ALYDSEKDAYLIGRDHIGIIPLYMGHDEHGNFYVASEMKALVP 167
Cdd:pfam13537 81 AIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKALLA 123
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-181 |
1.18e-48 |
|
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: 168.01 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 2 CSIFGVLDIKTDAGELRKKALELSRLMRHRGPDWSGVYASD---------------------------KAILAHERLSIV 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDgdglfvekragpvsdvaldlldeplksGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 55 DV--NAGAQPLYNEKKTHALAVNGEIYNHQALRAEYGDR-YAFQTGSDCEVILALYQEKG---------PEFLDDLQGMF 122
Cdd:cd00352 81 GLpsEANAQPFRSEDGRIALVHNGEIYNYRELREELEARgYRFEGESDSEVILHLLERLGregglfeavEDALKRLDGPF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 123 AFALYDSEKDAYLIGRDHIGIIPLYMGHDEHGNFYVASEMKALVPVC-RTIKEFPAGSYL 181
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
33-161 |
2.90e-47 |
|
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: 160.93 E-value: 2.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 33 PDWSGVYASDKAILAHERLSIVDV-NAGAQPLYNEKKTHALAVNGEIYNHQALRAEYGDR-YAFQTGSDCEVILALYQEK 110
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLpDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLgHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489955362 111 GPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGhDEHGNFYVASE 161
Cdd:pfam13522 81 GEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYG-ILGGGFVFASE 130
|
|
| lass_lactam_cya |
NF033535 |
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide ... |
1-362 |
1.08e-28 |
|
lasso peptide isopeptide bond-forming cyclase; Members of this family are the isopeptide bond-forming cyclase of lasso peptide biosynthesis systems, from a subgroup that contains primarily cyanobacterial examples. These proteins resemble the glutamine-hydrolyzing asparagine synthase AsnB (EC 6.3.5.4).
Pssm-ID: 468066 [Multi-domain] Cd Length: 668 Bit Score: 120.87 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGV--LDIKTDAGELRKKALELsrlMRHRGPDWSGVYASDKAILAH-------ERLSivdvnaGAQPLYNEKKTHA 71
Cdd:NF033535 1 MSGIVGIyyLDGRPVDREDLQQMVDI---LAHRGPDGADIWCEGSVGLGHrmlwttpESLL------EKLPLVNQTGDLV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 72 LAVNGEIYNHQALRAEYG-DRYAFQTGSDCEVILALYQEKGPEFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPLYMGH 150
Cdd:NF033535 72 ITADARIDNRDELISALQlNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 151 DEHGnFYVASEMKAL-----VPVC----------------------RTIKEFPAGSYLW-SQDG-EIRPYYQRDwFDYEA 201
Cdd:NF033535 152 SDKR-FAFASEIKALlclpeVPRRlnevriadylalmledkvitfyQDIFRLPPAHSMTvSQSGlQIRSYWSLD-PSREL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 202 VKDNVTDKAE-LRQALEESVKSHLMSDVPYGVLLSGGLDSSVISAItkkfaARRVEDQERSeawwPQLHSFAVGLEgapD 280
Cdd:NF033535 230 RLDSDEEYAEaFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCV-----ARQLLAEEKK----APLHTFSNIFD---K 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 281 LKAAQE------VANHLGTVHHEIH---FTVQEGLDAIrdVIYHIETYdvttiraSTPMYLMSRKI----KAMGIKMVLS 347
Cdd:NF033535 298 VTECDErpfinaVLEQGGLIPHYVHadqFGPLSDLEQI--FEYEDEPF-------LGPNHFLPWGLnraaQKEGVRILLD 368
|
410
....*....|....*.
gi 489955362 348 GEGSDE-VFGGYLYFH 362
Cdd:NF033535 369 GFDGDStVSHGHGYLT 384
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-161 |
1.12e-09 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 60.81 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDiKTDAGELRKKALelsRLMRHRGPDWSG-VYASDKAILAHERLSIV-DV-----------NAG-------- 59
Cdd:COG0034 7 ECGVFGIYG-HEDVAQLTYYGL---YALQHRGQESAGiATSDGGRFHLHKGMGLVsDVfdeedlerlkgNIAighvryst 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 60 --------AQPLYNEKKTHALAV--NGEIYNHQALRAEYGDRYA-FQTGSDCEVILAL---YQEKGPEF------LDDLQ 119
Cdd:COG0034 83 tgssslenAQPFYVNSPFGSIALahNGNLTNAEELREELEEEGAiFQTTSDTEVILHLiarELTKEDLEeaikeaLRRVK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489955362 120 GMFAFALYDSEKdayLIG-RDHIGIIPLYMGHDEHGnFYVASE 161
Cdd:COG0034 163 GAYSLVILTGDG---LIAaRDPNGIRPLVLGKLEDG-YVVASE 201
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
60-165 |
2.71e-09 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 60 AQPLYNEKKTHALAV--NGEIYNHQALRAEYGDRYA-FQTGSDCEVILAL----YQEKGPE-----FLDDLQGMFAFALY 127
Cdd:cd00715 84 AQPFVVNSPLGGIALahNGNLVNAKELREELEEEGRiFQTTSDSEVILHLiarsLAKDDLFeaiidALERVKGAYSLVIM 163
|
90 100 110
....*....|....*....|....*....|....*....
gi 489955362 128 DSEKdayLIG-RDHIGIIPLYMGHDEHGNFYVASEMKAL 165
Cdd:cd00715 164 TADG---LIAvRDPHGIRPLVLGKLEGDGYVVASESCAL 199
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-165 |
4.88e-08 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 55.43 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 2 CSIFGVLDiktdagelrKKALELSRL-------MRHRGPDWSGVYASD-KAILAHERLSIV-DV-----------NAG-- 59
Cdd:PRK05793 15 CGVFGVFS---------KNNIDVASLtyyglyaLQHRGQESAGIAVSDgEKIKVHKGMGLVsEVfskeklkglkgNSAig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 60 --------------AQPLYNEKKTH--ALAVNGEIYNHQALRAEYGDR-YAFQTGSDCEVILAL---YQEKGPEF----- 114
Cdd:PRK05793 86 hvrysttgasdldnAQPLVANYKLGsiAIAHNGNLVNADVIRELLEDGgRIFQTSIDSEVILNLiarSAKKGLEKalvda 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489955362 115 LDDLQGMFAFALYDSEKdayLIG-RDHIGIIPLYMGHDEhGNFYVASEMKAL 165
Cdd:PRK05793 166 IQAIKGSYALVILTEDK---LIGvRDPHGIRPLCLGKLG-DDYILSSESCAL 213
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
55-188 |
6.24e-08 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 53.22 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 55 DVNAgaQPLYNEKKTHALAVNGEIYNHQALRAEYGDR-YAFQTGSDCEVI---LALYQEKGPEFLD-------DLQGMFA 123
Cdd:cd00714 81 DVNA--HPHRSCDGEIAVVHNGIIENYAELKEELEAKgYKFESETDTEVIahlIEYYYDGGLDLLEavkkalkRLEGAYA 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955362 124 FALYDSEKDAYLIG--RDHigiiPLYMGHDEHGNFyVASEMKALVPVCRTIkefpagSYLwsQDGEI 188
Cdd:cd00714 159 LAVISKDEPDEIVAarNGS----PLVIGIGDGENF-VASDAPALLEHTRRV------IYL--EDGDI 212
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-168 |
1.45e-07 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 53.91 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDiktDAGELRKKALELSRLmRHRGPDWSGVYASDKAILaHER--LSIV-DV--------------------- 56
Cdd:PLN02440 1 ECGVVGIFG---DPEASRLCYLGLHAL-QHRGQEGAGIVTVDGNRL-QSItgNGLVsDVfdeskldqlpgdiaighvrys 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 57 NAG------AQPLYNEKKTHALAV--NGEIYNHQALRAEYGDRYA-FQTGSDCEVILALYQE-KGPEFLD-------DLQ 119
Cdd:PLN02440 76 TAGasslknVQPFVANYRFGSIGVahNGNLVNYEELRAKLEENGSiFNTSSDTEVLLHLIAIsKARPFFSrivdaceKLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489955362 120 GmfAFALYDSEKDAYLIGRDHIGIIPLYMGHDEHGNFYVASEMKALVPV 168
Cdd:PLN02440 156 G--AYSMVFLTEDKLVAVRDPHGFRPLVMGRRSNGAVVFASETCALDLI 202
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
55-188 |
1.70e-07 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 53.86 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 55 DVNAgaQPLYNEKKTHALAVNGEIYNHQALRAEYGDR-YAFQTGSDCEVI---LALYQEKGPEFLD-------DLQGMFA 123
Cdd:COG0449 82 DENA--HPHTSCSGRIAVVHNGIIENYAELREELEAKgHTFKSETDTEVIahlIEEYLKGGGDLLEavrkalkRLEGAYA 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955362 124 FAlydsekdayLIGRDHIGII-------PLYMGHDEHGNFyVASEMKALVPVCRTIkefpagSYLwsQDGEI 188
Cdd:COG0449 160 LA---------VISADEPDRIvaarkgsPLVIGLGEGENF-LASDVPALLPYTRRV------IYL--EDGEI 213
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-160 |
9.59e-07 |
|
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its function has not yet been determined. 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: 239735 [Multi-domain] Cd Length: 181 Bit Score: 49.21 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDIKTDAGELRKKALELSRLMRHRGPDWSGV----YASDKAILAHERLSIVDVNAGAQPLYNEKKTHALAVNG 76
Cdd:cd03766 1 MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYLSTrqlsVTNWTLLFTSSVLSLRGDHVTRQPLVDQSTGNVLQWNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 77 EIYNHQALRAEygdryafqtGSDCEVILALYQE---KGPEFLD---DLQGMFAFALYD-SEKDAYLiGRDHIGIIPLYMG 149
Cdd:cd03766 81 ELYNIDGVEDE---------ENDTEVIFELLANcssESQDILDvlsSIEGPFAFIYYDaSENKLYF-GRDCLGRRSLLYK 150
|
170
....*....|..
gi 489955362 150 HDEHG-NFYVAS 160
Cdd:cd03766 151 LDPNGfELSISS 162
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-169 |
1.38e-06 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including 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). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 49.96 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 2 CSIFGVLDiKTDA---GELRKKALELsrlMRHRGPDWSG---VYASDKA------------------------------- 44
Cdd:cd01907 1 CGIFGIMS-KDGEpfvGALLVEMLDA---MQERGPGDGAgfaLYGDPDAfvyssgkdmevfkgvgypediarrydleeyk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 45 ---ILAHERL---SIVDVnAGAQP--LYNEKKTHalavNGEIYNHQALRaEY--GDRYAFQTGSDCEVILALYQEKGPEF 114
Cdd:cd01907 77 gyhWIAHTRQptnSAVWW-YGAHPfsIGDIAVVH----NGEISNYGSNR-EYleRFGYKFETETDTEVIAYYLDLLLRKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 115 -----------------------------LDDLQGMFAFALydSEKDAYLIGRDHIGIIPLYMGHDEhGNFYVASEMKAL 165
Cdd:cd01907 151 glpleyykhiirmpeeerelllalrltyrLADLDGPFTIIV--GTPDGFIVIRDRIKLRPAVVAETD-DYVAIASEECAI 227
|
....
gi 489955362 166 VPVC 169
Cdd:cd01907 228 REIP 231
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
72-188 |
5.98e-06 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 48.89 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 72 LAV--NGEIYNHQALRAEYGDR-YAFQTGSDCEVI---LALYQEKGPEFLD-------DLQGMFAFAlydsekdayLIGR 138
Cdd:PRK00331 95 IAVvhNGIIENYAELKEELLAKgHVFKSETDTEVIahlIEEELKEGGDLLEavrkalkRLEGAYALA---------VIDK 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489955362 139 DHIGII-------PLYMGHDEHGNFyVASEMKALVPVCRTIkefpagSYLwsQDGEI 188
Cdd:PRK00331 166 DEPDTIvaarngsPLVIGLGEGENF-LASDALALLPYTRRV------IYL--EDGEI 213
|
|
| AANH_superfamily |
cd01984 |
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ... |
230-275 |
1.10e-05 |
|
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467489 [Multi-domain] Cd Length: 56 Bit Score: 42.85 E-value: 1.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489955362 230 YGVLLSGGLDSSVISAITKKFAARrvedqerseaWWPQLHSFAVGL 275
Cdd:cd01984 1 ILVPLSGGEDSSIALKHAKKFKTS----------KAEEVVVVHVGE 36
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
76-191 |
9.87e-05 |
|
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of 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). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits.
Pssm-ID: 238891 [Multi-domain] Cd Length: 224 Bit Score: 43.84 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 76 GEIYNHQALRAEYGdryafQTGSDCEVILAL--YQ---EKGP----EFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPL 146
Cdd:cd01910 79 GHLDNLGSLKQQYG-----LSKTANEAMLVIeaYRtlrDRGPypadQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPL 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489955362 147 YMGHDEHGNFYVASEMKALVPVC-RTIKEFPAGSYLWSqDGEIRPY 191
Cdd:cd01910 154 YWGIAADGSVVFSDDVELVKASCgKSFAPFPKGCFFHS-EGGLRSF 198
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-188 |
1.21e-04 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 45.01 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 1 MCSIFGVLDiktdAGELRKKALELSRLMRHRGPDWSGV-------------YASDKA------IL--------------- 46
Cdd:PTZ00295 24 CCGIVGYLG----NEDASKILLEGIEILQNRGYDSCGIstissggelkttkYASDGTtsdsieILkeklldshknstigi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 47 AHERL----SIVDVNAgaQPLYNEKKTHALAVNGEIYNHQALRAEYGDR-YAFQTGSDCEVI---LALYQEKGPEFLD-- 116
Cdd:PTZ00295 100 AHTRWathgGKTDENA--HPHCDYKKRIALVHNGTIENYVELKSELIAKgIKFRSETDSEVIanlIGLELDQGEDFQEav 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955362 117 -----DLQGMFAFALYDSEKDAYLIGRDHIGiiPLYMGHDEHGnFYVASEMKALVpvcRTIKEfpagsYLWSQDGEI 188
Cdd:PTZ00295 178 ksaisRLQGTWGLCIIHKDNPDSLIVARNGS--PLLVGIGDDS-IYVASEPSAFA---KYTNE-----YISLKDGEI 243
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
76-186 |
1.51e-04 |
|
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.
Pssm-ID: 403619 [Multi-domain] Cd Length: 228 Bit Score: 43.51 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 76 GEIYNHQALRAEYGdryaFQTGSDcEVILAL--YQ---EKGP----EFLDDLQGMFAFALYDSEKDAYLIGRDHIGIIPL 146
Cdd:pfam12481 83 GHLENLASLKQQYG----LSKGAN-EAMIVIeaYRtlrDRGPypadQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489955362 147 YMGHDEHGNFYVASEMKALVPVC-RTIKEFPAGSYLWSQDG 186
Cdd:pfam12481 158 YWGIDADGSLVFSDDIEIVKKGCgKSFAPFPKGCFFTSSGG 198
|
|
| macrolact_Ik_Al |
NF033561 |
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology ... |
212-296 |
2.79e-03 |
|
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology enzymes known to form the lactam bond of the isopeptide linkage of lasso peptides. This family includes the peptide cyclase involved in biosynthesis of the lasso peptide albusnodin. However, another member of this family belongs to the biosynthesis cassette for ikarugamycin, a macrolactam whose biosynthesis relies on a hybrid PKS/NRPS system, not a ribosomally produced peptide.
Pssm-ID: 468087 [Multi-domain] Cd Length: 561 Bit Score: 40.28 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955362 212 LRQALEESVKSHLMSDVPYGVLLSGGLDSSVISAItkkfAARRVEDQERSEAWwpQLHsfAVGLEGAPDLKAAQEVANHL 291
Cdd:NF033561 195 LRAALAAAVALRVDGAPPLSSDLSGGLDSTTLALL----AARCLPVGRRLTGV--TVH--PEGRTEGGDLDYARLAARAP 266
|
....*
gi 489955362 292 GTVHH 296
Cdd:NF033561 267 RIRHR 271
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
232-301 |
4.41e-03 |
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MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family 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: 467502 [Multi-domain] Cd Length: 349 Bit Score: 39.41 E-value: 4.41e-03
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....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955362 232 VLLSGGLDSSVISAITKK--FAARRV-------EDQERSEAWWPQlhsfavglegapDLKAAQEVANHLGTVHHEIHFT 301
Cdd:cd01998 4 VAMSGGVDSSVAAALLKEqgYDVIGVfmknwddEDNEKGGCCSEE------------DIEDARRVADQLGIPLYVVDFS 70
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