|
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: 1173.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDLKSDPVELRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDVNNGAQPLYNAAHTHVLAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 81 HQALRQQLSDRYAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDEHGNLYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 161 EMKALVPVCRTIKEFPAGSYLWSQDGEIREYYRRDWFDYDSVKDNVTDATALRTALEESVKSHLMSDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 241 SVISAITKKYAARRVEDQERSEAWWPQLHSFAVGLEGSPDLRAAQEVANHLGTVHHEIHFTVQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 321 VTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLYFHKAPDAREFHEETVRKLLALHMFDCARANKAMSAWGVEA 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 401 RVPFLDKKFLDVAMRINPKDKMCGNGKMEKHIVRECFESYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAQQISDQQLET 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727168469 481 ARFRFPYNTPTSKEGYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDESFKKMDDPSGRAV-GVHQAAY 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: 543.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 4 IFGVLDLKSDPVELRKKALELSRLMRHRGPDWSGV-YASDKAILAHERLSIVDVNNGAQPLYNAAHTHVLAVNGEIYNHQ 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 83 ALRQQLSDR-YAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDeHGNLYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 162 MKALVPVCrTIKEFPAGSYLWSQDGEIR----EYYRRDWFDYDSVKDNVTDATA------------------------LR 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFVRvpppSTFFRGVFELEPGHDLPLDDDGlnieryywerrdehtdseedlvdeLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 214 TALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKYAARrvedqerseawwPQLHSFAVGLEGSPDL---RAAQEVANH 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 291 LGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLYFHKAPDAREF 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 371 HEETVRKLLALHMFDCARANKAMS-AWGVEARVPFLDKKFLDVAMRINPKDKMcgNGKMEKHIVRECFESYLPASVAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKDRMSmAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 727168469 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
1.68e-178 |
|
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: 514.77 E-value: 1.68e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDLKSDPveLRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDV-NNGAQPLYNAAHTHVLAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDFDGGA--DREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 80 NHQALRQQLSDR-YAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDEhGNLYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 159 ASEMKALVP---------------------------VCRTIKEFPAGSYLWSQDG---EIREYYRRDWFDYDSVKDNVTD 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 209 ATALRTALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKYAARRvedqerseawwpqLHSFAVGLEGSP--DLRAAQE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGP-------------LKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 287 VANHLGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMgIKMVLSGEGADEVFGGYLYFHKAP- 365
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAl 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 366 ------------------DAREFHEETVRKLLALHMF------DCARANKAMSAWGVEARVPFLDKKFLDVAMRINPKDK 421
Cdd:COG0367 382 llspdfaealggelvprlYAESGAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 422 McgNGKMEKHIVRECFESYLPASVAWRQKEQFSDGVGySWID-TLKEVAAQQISDQQLETARFrfpYNTptskegYLYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FDP------DAVRR 529
|
....*..
gi 727168469 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 |
4.48e-108 |
|
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: 324.57 E-value: 4.48e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 211 ALRTALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKYAArrvedqerseawwPQLHSFAVGLE--GSPDLRAAQEVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEgrGYDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 289 NHLGTVHHEIHFTVQEGLDAIRDVIYHIETydVTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLyFHKAPDAr 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYP-FYKGEDP- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 369 eFHEETVRKLLALHMFDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPKDKMCGNgkMEKHIVRECFESYLPASVAWR 448
Cdd:pfam00733 144 -LRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727168469 449 QKEQFSDGVGYSWID-TLKEVAAQQISDQqletarfrfpyntPTSKEGYLYREIFEELFPLPSAA 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 |
9.44e-91 |
|
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: 278.00 E-value: 9.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 226 SDVPYGVLLSGGLDSSVISAITKKYAARrvedqerseawwPQLHSFAVGLEGS--PDLRAAQEVANHLGTVHHEIHFTVQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 304 EGLDAIRDVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLYFHKAPDAR--EFHEETVRKLLAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRGweALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727168469 382 HMFDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPKDKMCGNGKMEKHIVRECFESYLPASVAWRQKEQFSDGV 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 |
7.81e-29 |
|
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: 121.25 E-value: 7.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDLKSDPVELRKKALELSRLMrHRGPDWSGVYASDKAILAH-------ERLSivdvnnGAQPLYNAAHTHVLA 73
Cdd:NF033535 1 MSGIVGIYYLDGRPVDREDLQQMVDILA-HRGPDGADIWCEGSVGLGHrmlwttpESLL------EKLPLVNQTGDLVIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 74 VNGEIYNHQALRQQLS-DRYAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDE 152
Cdd:NF033535 74 ADARIDNRDELISALQlNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 153 HGnLYVASEMKAL-----VPVC----------------------RTIKEFPAGSYLW-SQDG-EIREYYRRDWFDYDSVK 203
Cdd:NF033535 154 KR-FAFASEIKALlclpeVPRRlnevriadylalmledkvitfyQDIFRLPPAHSMTvSQSGlQIRSYWSLDPSRELRLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 204 DNVTDATALRTALEESVKSHLMSDVPYGVLLSGGLDSSVISAItkkyaARRVEDQERSeawwPQLHSFAVGLEGSP--DL 281
Cdd:NF033535 233 SDEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCV-----ARQLLAEEKK----APLHTFSNIFDKVTecDE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 282 RA-AQEVANHLGTVHHEIH---FTVQEGLDAIrdVIYHIETYdvttiraSTPMYLMSRKI----KAMGIKMVLSGEGADE 353
Cdd:NF033535 304 RPfINAVLEQGGLIPHYVHadqFGPLSDLEQI--FEYEDEPF-------LGPNHFLPWGLnraaQKEGVRILLDGFDGDS 374
|
410
....*....|
gi 727168469 354 -VFGGYLYFH 362
Cdd:NF033535 375 tVSHGHGYLT 384
|
|
| macrolact_Ik_Al |
NF033561 |
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology ... |
212-296 |
7.93e-04 |
|
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: 42.21 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 212 LRTALEESVKSHLMSDVPYGVLLSGGLDSSVISAItkkyAARRVEDQERSEAWwpQLHsfAVGLEGSPDLRAAQEVANHL 291
Cdd:NF033561 195 LRAALAAAVALRVDGAPPLSSDLSGGLDSTTLALL----AARCLPVGRRLTGV--TVH--PEGRTEGGDLDYARLAARAP 266
|
....*
gi 727168469 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: 1173.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDLKSDPVELRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDVNNGAQPLYNAAHTHVLAVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 81 HQALRQQLSDRYAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDEHGNLYVAS 160
Cdd:PRK09431 81 HQELRAELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 161 EMKALVPVCRTIKEFPAGSYLWSQDGEIREYYRRDWFDYDSVKDNVTDATALRTALEESVKSHLMSDVPYGVLLSGGLDS 240
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 241 SVISAITKKYAARRVEDQERSEAWWPQLHSFAVGLEGSPDLRAAQEVANHLGTVHHEIHFTVQEGLDAIRDVIYHIETYD 320
Cdd:PRK09431 241 SLISAIAKKYAARRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 321 VTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLYFHKAPDAREFHEETVRKLLALHMFDCARANKAMSAWGVEA 400
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 401 RVPFLDKKFLDVAMRINPKDKMCGNGKMEKHIVRECFESYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAQQISDQQLET 480
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGNGKMEKHILREAFEGYLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVSDQQLAT 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727168469 481 ARFRFPYNTPTSKEGYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDESFKKMDDPSGRAV-GVHQAAY 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: 837.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDLKSDPVELRKKALELSRLMRHRGPDWSGVYASDKA-----ILAHERLSIVDVNNGAQPLYNAAHTHVLAVN 75
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRKALELSKRLRHRGPDWSGIIVLENSpgtynILAHERLAIVDLSDGKQPLLDDDETVALMQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 76 GEIYNHQALRQQL-SDRYAFQTGSDCEVILALYQEKGP-DFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDEH 153
Cdd:PTZ00077 81 GEIYNHWEIRPELeKEGYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 154 GNLYVASEMKALVPVCRTIKEFPAGSYLWS--QDGEIREYYRRDWFDYDS-VKDNVTDATALRTALEESVKSHLMSDVPY 230
Cdd:PTZ00077 161 GSIWFSSELKALHDQCVEVKQFPPGHYYDQtkEKGEFVRYYNPNWHDFDHpIPTGEIDLEEIREALEAAVRKRLMGDVPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 231 GVLLSGGLDSSVISAITKKYaaRRVEDQERSEAWWPQLHSFAVGLEGSPDLRAAQEVANHLGTVHHEIHFTVQEGLDAIR 310
Cdd:PTZ00077 241 GLFLSGGLDSSIVAAIVAKL--IKNGEIDLSKRGMPKLHSFCIGLEGSPDLKAARKVAEYLGTEHHEFTFTVEEGIDALP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 311 DVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLYFHKAPDAREFHEETVRKLLALHMFDCARAN 390
Cdd:PTZ00077 319 DVIYHTETYDVTTIRASTPMYLLSRRIKALGIKMVLSGEGSDELFGGYLYFHKAPNREEFHRELVRKLHDLHKYDCLRAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 391 KAMSAWGVEARVPFLDKKFLDVAMRINPKDKMC--GNGKMEKHIVRECFE----SYLPASVAWRQKEQFSDGVGYSWIDT 464
Cdd:PTZ00077 399 KATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCnaFEGQMEKYILRKAFEglekPYLPDEILWRQKEQFSDGVGYSWIDG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 465 LKEVAAQQISDQQLETARFRFPYNTPTSKEGYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDESFKKMDDPSGR 544
Cdd:PTZ00077 479 LKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTVPYGPSIACSTEKALEWDESFKKNTDESGR 558
|
570
....*....|.
gi 727168469 545 AV-GVHQAAYK 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: 833.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDLKSDPVELRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDVNNGAQPLYNAAHTHVLAVNGEIYN 80
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTIVVTANGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 81 HQALRQQLSDrYAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDEHGNLYVAS 160
Cdd:PLN02549 81 HKELREKLKL-HKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 161 EMKALVPVCRTIKEFPAGSYLWSQDGEIREYYRRDWFDyDSVKDNVTDATALRTALEESVKSHLMSDVPYGVLLSGGLDS 240
Cdd:PLN02549 160 EMKALCDDCERFEEFPPGHYYSSKAGGFRRWYNPPWFS-ESIPSTPYDPLVLREAFEKAVIKRLMTDVPFGVLLSGGLDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 241 SVISAItkkyAARRVEDQERSEAWWPQLHSFAVGLEGSPDLRAAQEVANHLGTVHHEIHFTVQEGLDAIRDVIYHIETYD 320
Cdd:PLN02549 239 SLVASI----AARHLAETKAARQWGQQLHSFCVGLEGSPDLKAAREVADYLGTVHHEFHFTVQEGIDAIEDVIYHLETYD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 321 VTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLYFHKAPDAREFHEETVRKLLALHMFDCARANKAMSAWGVEA 400
Cdd:PLN02549 315 VTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKEEFHKETCRKIKALHQYDCLRANKSTSAWGLEA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 401 RVPFLDKKFLDVAMRINPKDKMC--GNGKMEKHIVRECFE----SYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAQQIS 474
Cdd:PLN02549 395 RVPFLDKEFIDVAMSIDPEWKMIrpGEGRIEKWVLRKAFDdeedPYLPKHILWRQKEQFSDGVGYSWIDGLKAHAEKHVS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 475 DQQLETARFRFPYNTPTSKEGYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDESFKKMDDPSGRAV-GVHQAAY 553
Cdd:PLN02549 475 DEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDAARLTVPGGPSVACSTAKAVEWDAAWSKNLDPSGRAAlGVHVAAY 554
|
.
gi 727168469 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: 543.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 4 IFGVLDLKSDPVELRKKALELSRLMRHRGPDWSGV-YASDKAILAHERLSIVDVNNGAQPLYNAAHTHVLAVNGEIYNHQ 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 83 ALRQQLSDR-YAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDeHGNLYVASE 161
Cdd:TIGR01536 81 ELREELEAKgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAYD-GGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 162 MKALVPVCrTIKEFPAGSYLWSQDGEIR----EYYRRDWFDYDSVKDNVTDATA------------------------LR 213
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFVRvpppSTFFRGVFELEPGHDLPLDDDGlnieryywerrdehtdseedlvdeLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 214 TALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKYAARrvedqerseawwPQLHSFAVGLEGSPDL---RAAQEVANH 290
Cdd:TIGR01536 239 SLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------GPVHTFSIGFEGSPDFdesKYARKVADH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 291 LGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLYFHKAPDAREF 370
Cdd:TIGR01536 307 LGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 371 HEETVRKLLALHMFDCARANKAMS-AWGVEARVPFLDKKFLDVAMRINPKDKMcgNGKMEKHIVRECFESYLPASVAWRQ 449
Cdd:TIGR01536 385 REELQYLDLELYMPGLLRRKDRMSmAHSLEVRVPFLDHELVEYALSIPPEMKL--RDGKEKYLLREAFEGYLPEEILWRP 462
|
....
gi 727168469 450 KEQF 453
Cdd:TIGR01536 463 KEGF 466
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
1.68e-178 |
|
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: 514.77 E-value: 1.68e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDLKSDPveLRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDV-NNGAQPLYNAAHTHVLAVNGEIY 79
Cdd:COG0367 1 MCGIAGIIDFDGGA--DREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLsEGGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 80 NHQALRQQLSDR-YAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDEhGNLYV 158
Cdd:COG0367 79 NYRELRAELEALgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDG-GGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 159 ASEMKALVP---------------------------VCRTIKEFPAGSYLWSQDG---EIREYYRRDWFDYDSVKDNVTD 208
Cdd:COG0367 158 ASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 209 ATALRTALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKYAARRvedqerseawwpqLHSFAVGLEGSP--DLRAAQE 286
Cdd:COG0367 238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKGP-------------LKTFSIGFEDSAydESPYARA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 287 VANHLGTVHHEIHFTVQEGLDAIRDVIYHIEtyDVTTIRASTPMYLMSRKIKAMgIKMVLSGEGADEVFGGYLYFHKAP- 365
Cdd:COG0367 305 VAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAAl 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 366 ------------------DAREFHEETVRKLLALHMF------DCARANKAMSAWGVEARVPFLDKKFLDVAMRINPKDK 421
Cdd:COG0367 382 llspdfaealggelvprlYAESGAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 422 McgNGKMEKHIVRECFESYLPASVAWRQKEQFSDGVGySWID-TLKEVAAQQISDQQLETARFrfpYNTptskegYLYRE 500
Cdd:COG0367 462 L--RGGRGKYLLRKALEGLLPDEVLDRPKQGFPVPLG-PWLRgPLREWLEDLLSDESLAARGL---FDP------DAVRR 529
|
....*..
gi 727168469 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 |
4.48e-108 |
|
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: 324.57 E-value: 4.48e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 211 ALRTALEESVKSHLMSDVPYGVLLSGGLDSSVISAITKKYAArrvedqerseawwPQLHSFAVGLE--GSPDLRAAQEVA 288
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------SPLHTFSIGFEgrGYDEAPYAREVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 289 NHLGTVHHEIHFTVQEGLDAIRDVIYHIETydVTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLyFHKAPDAr 368
Cdd:pfam00733 68 EHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYP-FYKGEDP- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 369 eFHEETVRKLLALHMFDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPKDKMCGNgkMEKHIVRECFESYLPASVAWR 448
Cdd:pfam00733 144 -LRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLRGG--IEKYILREALEGILPDEILER 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727168469 449 QKEQFSDGVGYSWID-TLKEVAAQQISDQqletarfrfpyntPTSKEGYLYREIFEELFPLPSAA 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 |
9.44e-91 |
|
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: 278.00 E-value: 9.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 226 SDVPYGVLLSGGLDSSVISAITKKYAARrvedqerseawwPQLHSFAVGLEGS--PDLRAAQEVANHLGTVHHEIHFTVQ 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------TPIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 304 EGLDAIRDVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGADEVFGGYLYFHKAPDAR--EFHEETVRKLLAL 381
Cdd:cd01991 69 ELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRGweALEEELLRDLDRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727168469 382 HMFDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPKDKMCGNGKMEKHIVRECFESYLPASVAWRQKEQFSDGV 457
Cdd:cd01991 149 WTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGGEKYILREAARDLLPDEIAWRPKRAIQFGS 224
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-193 |
2.24e-81 |
|
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: 253.63 E-value: 2.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 2 CSIFGVLDLKSDPVeLRKKALELSRLMRHRGPDWSGVYASDKAILAHERLSIVDVNNGAQPLYNAAHTHVLAVNGEIYNH 81
Cdd:cd00712 1 CGIAGIIGLDGASV-DRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVLVFNGEIYNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 82 QALRQQLSDR-YAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDEhGNLYVAS 160
Cdd:cd00712 80 RELRAELEALgHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRDG-GGLAFAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727168469 161 EMKALVPVC---------------------------RTIKEFPAGSYLWSQDG--EIREYYR 193
Cdd:cd00712 159 ELKALLALPgvpreldeaalaeylafqyvpaprtifKGIRKLPPGHYLTVDPGgvEIRRYWD 220
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
48-167 |
4.05e-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: 178.87 E-value: 4.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 48 HERLSIVDVNNGAQPLYNAA-HTHVLAVNGEIYNHQALRQQLSDR-YAFQTGSDCEVILALYQ-EKGPDFLDDLQGMFAF 124
Cdd:pfam13537 1 HRRLSIIDLEGGAQPMVSSEdGRYVIVFNGEIYNYRELRAELEAKgYRFRTHSDTEVILHLYEaEWGEDCVDRLNGMFAF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 727168469 125 ALYDTEKDAYLIGRDHLGIIPLYMGHDEHGNLYVASEMKALVP 167
Cdd:pfam13537 81 AIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKALLA 123
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-181 |
2.72e-47 |
|
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: 164.54 E-value: 2.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 2 CSIFGVLDLKSDPVELRKKALELSRLMRHRGPDWSGVYASD---------------------------KAILAHERLSIV 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDgdglfvekragpvsdvaldlldeplksGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 55 DVNN--GAQPLYNAAHTHVLAVNGEIYNHQALRQQL-SDRYAFQTGSDCEVILALYQEKG---------PDFLDDLQGMF 122
Cdd:cd00352 81 GLPSeaNAQPFRSEDGRIALVHNGEIYNYRELREELeARGYRFEGESDSEVILHLLERLGregglfeavEDALKRLDGPF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 123 AFALYDTEKDAYLIGRDHLGIIPLYMGHDEHGNLYVASEMKALVPVC-RTIKEFPAGSYL 181
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
33-161 |
9.41e-46 |
|
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: 157.08 E-value: 9.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 33 PDWSGVYASDKAILAHERLSIVDV-NNGAQPLYNAAHTHVLAVNGEIYNHQALRQQLSDR-YAFQTGSDCEVILALYQEK 110
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLpDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADLgHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 727168469 111 GPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGhDEHGNLYVASE 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 |
7.81e-29 |
|
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: 121.25 E-value: 7.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDLKSDPVELRKKALELSRLMrHRGPDWSGVYASDKAILAH-------ERLSivdvnnGAQPLYNAAHTHVLA 73
Cdd:NF033535 1 MSGIVGIYYLDGRPVDREDLQQMVDILA-HRGPDGADIWCEGSVGLGHrmlwttpESLL------EKLPLVNQTGDLVIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 74 VNGEIYNHQALRQQLS-DRYAFQTGSDCEVILALYQEKGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDE 152
Cdd:NF033535 74 ADARIDNRDELISALQlNNCPPEKITDSQLILAAYEKWGEQCPEHLLGDFAFAIWDKRKQQLFCARDHFGVKPFYYYQSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 153 HGnLYVASEMKAL-----VPVC----------------------RTIKEFPAGSYLW-SQDG-EIREYYRRDWFDYDSVK 203
Cdd:NF033535 154 KR-FAFASEIKALlclpeVPRRlnevriadylalmledkvitfyQDIFRLPPAHSMTvSQSGlQIRSYWSLDPSRELRLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 204 DNVTDATALRTALEESVKSHLMSDVPYGVLLSGGLDSSVISAItkkyaARRVEDQERSeawwPQLHSFAVGLEGSP--DL 281
Cdd:NF033535 233 SDEEYAEAFREIFTEAVRCRLRSAFPVGSHLSGGLDSSSITCV-----ARQLLAEEKK----APLHTFSNIFDKVTecDE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 282 RA-AQEVANHLGTVHHEIH---FTVQEGLDAIrdVIYHIETYdvttiraSTPMYLMSRKI----KAMGIKMVLSGEGADE 353
Cdd:NF033535 304 RPfINAVLEQGGLIPHYVHadqFGPLSDLEQI--FEYEDEPF-------LGPNHFLPWGLnraaQKEGVRILLDGFDGDS 374
|
410
....*....|
gi 727168469 354 -VFGGYLYFH 362
Cdd:NF033535 375 tVSHGHGYLT 384
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
60-161 |
2.32e-10 |
|
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: 62.73 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 60 AQPLYNAAHTHVLAV--NGEIYNHQALRQQLSDRYA-FQTGSDCEVILAL--YQEKGPDFLD-------DLQGMFAFALY 127
Cdd:COG0034 91 AQPFYVNSPFGSIALahNGNLTNAEELREELEEEGAiFQTTSDTEVILHLiaRELTKEDLEEaikealrRVKGAYSLVIL 170
|
90 100 110
....*....|....*....|....*....|....*
gi 727168469 128 DTEKdayLIG-RDHLGIIPLYMGHDEHGnLYVASE 161
Cdd:COG0034 171 TGDG---LIAaRDPNGIRPLVLGKLEDG-YVVASE 201
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
42-165 |
2.78e-10 |
|
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: 60.94 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 42 DKAIlAHERLS---IVDVNNgAQPLY-NAAHTHV-LAVNGEIYNHQALRQQLSDRYA-FQTGSDCEVILAL----YQEKG 111
Cdd:cd00715 65 NIAI-GHVRYStagSSSLEN-AQPFVvNSPLGGIaLAHNGNLVNAKELREELEEEGRiFQTTSDSEVILHLiarsLAKDD 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 112 P-----DFLDDLQGMFAFALYDTEKdayLIG-RDHLGIIPLYMGHDEHGNLYVASEMKAL 165
Cdd:cd00715 143 LfeaiiDALERVKGAYSLVIMTADG---LIAvRDPHGIRPLVLGKLEGDGYVVASESCAL 199
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
67-188 |
8.37e-10 |
|
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: 59.00 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 67 AHTHV-----LAV--NGEIYNHQALRQQLSDR-YAFQTGSDCEVI---LALYQEKGPDFLD-------DLQGMFAFALYD 128
Cdd:cd00714 84 AHPHRscdgeIAVvhNGIIENYAELKEELEAKgYKFESETDTEVIahlIEYYYDGGLDLLEavkkalkRLEGAYALAVIS 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727168469 129 TEKDAYLIG--RDHlgiiPLYMGHDEHGNlYVASEMKALVPVCRTIkefpagSYLwsQDGEI 188
Cdd:cd00714 164 KDEPDEIVAarNGS----PLVIGIGDGEN-FVASDAPALLEHTRRV------IYL--EDGDI 212
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-165 |
9.78e-09 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 57.74 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 2 CSIFGVLDlksdpvelrKKALELSRL-------MRHRGPDWSGVYASD-KAILAHERLSIV------------------- 54
Cdd:PRK05793 15 CGVFGVFS---------KNNIDVASLtyyglyaLQHRGQESAGIAVSDgEKIKVHKGMGLVsevfskeklkglkgnsaig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 55 ----------DVNNgAQPLYNAAHTHVLAV--NGEIYNHQALRQQLSDR-YAFQTGSDCEVILAL---YQEKG-----PD 113
Cdd:PRK05793 86 hvrysttgasDLDN-AQPLVANYKLGSIAIahNGNLVNADVIRELLEDGgRIFQTSIDSEVILNLiarSAKKGlekalVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 727168469 114 FLDDLQGMFAFALYDTEKdayLIG-RDHLGIIPLYMGHDEhGNLYVASEMKAL 165
Cdd:PRK05793 165 AIQAIKGSYALVILTEDK---LIGvRDPHGIRPLCLGKLG-DDYILSSESCAL 213
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-160 |
1.96e-08 |
|
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: 54.22 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDLKSDPVELRKKALELSRLMRHRGPDWSGV----YASDKAILAHERLSIVDVNNGAQPLYNAAHTHVLAVNG 76
Cdd:cd03766 1 MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYLSTrqlsVTNWTLLFTSSVLSLRGDHVTRQPLVDQSTGNVLQWNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 77 EIYNHQALRQQlsdryafqtGSDCEVILALYQE------KGPDFLDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGH 150
Cdd:cd03766 81 ELYNIDGVEDE---------ENDTEVIFELLANcssesqDILDVLSSIEGPFAFIYYDASENKLYFGRDCLGRRSLLYKL 151
|
170
....*....|.
gi 727168469 151 DEHG-NLYVAS 160
Cdd:cd03766 152 DPNGfELSISS 162
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
67-188 |
1.71e-07 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 53.89 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 67 AHTHV-----LAV--NGEIYNHQALRQQLSDR-YAFQTGSDCEVI---LALYQEKGPDFLD-------DLQGMFAFAlyd 128
Cdd:PRK00331 85 AHPHTdcsgrIAVvhNGIIENYAELKEELLAKgHVFKSETDTEVIahlIEEELKEGGDLLEavrkalkRLEGAYALA--- 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727168469 129 tekdayLIGRDHLGII-------PLYMGHDEHGNlYVASEMKALVPVCRTIkefpagSYLwsQDGEI 188
Cdd:PRK00331 162 ------VIDKDEPDTIvaarngsPLVIGLGEGEN-FLASDALALLPYTRRV------IYL--EDGEI 213
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-168 |
7.38e-07 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 51.60 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 1 MCSIFGVLDlksDPVELRKKALELSRLmRHRGPDWSGVYASDKAILaHER--LSIV-DVNN------------------- 58
Cdd:PLN02440 1 ECGVVGIFG---DPEASRLCYLGLHAL-QHRGQEGAGIVTVDGNRL-QSItgNGLVsDVFDeskldqlpgdiaighvrys 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 59 --------GAQPLY-NAAHTHV-LAVNGEIYNHQALRQQLSDRYA-FQTGSDCEVILALYQE-KGPDFLD-------DLQ 119
Cdd:PLN02440 76 tagasslkNVQPFVaNYRFGSIgVAHNGNLVNYEELRAKLEENGSiFNTSSDTEVLLHLIAIsKARPFFSrivdaceKLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 727168469 120 GmfAFALYDTEKDAYLIGRDHLGIIPLYMGHDEHGNLYVASEMKALVPV 168
Cdd:PLN02440 156 G--AYSMVFLTEDKLVAVRDPHGFRPLVMGRRSNGAVVFASETCALDLI 202
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-169 |
1.83e-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: 49.57 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 2 CSIFGVLDLKSDPV--ELRKKALELsrlMRHRGPDWSG---VYASDKA-------------------------------- 44
Cdd:cd01907 1 CGIFGIMSKDGEPFvgALLVEMLDA---MQERGPGDGAgfaLYGDPDAfvyssgkdmevfkgvgypediarrydleeykg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 45 --ILAHERL---SIVDVNnGAQP--LYNAAHTHvlavNGEIYNHQALRQQLSDR-YAFQTGSDCEVI------------- 103
Cdd:cd01907 78 yhWIAHTRQptnSAVWWY-GAHPfsIGDIAVVH----NGEISNYGSNREYLERFgYKFETETDTEVIayyldlllrkggl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 104 -------------------LALYQEKGPDFLDdlqGMFAFALydTEKDAYLIGRDHLGIIPLYMGHDEhGNLYVASEMKA 164
Cdd:cd01907 153 pleyykhiirmpeeerellLALRLTYRLADLD---GPFTIIV--GTPDGFIVIRDRIKLRPAVVAETD-DYVAIASEECA 226
|
....*
gi 727168469 165 LVPVC 169
Cdd:cd01907 227 IREIP 231
|
|
| AANH_superfamily |
cd01984 |
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ... |
230-275 |
7.57e-06 |
|
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: 43.23 E-value: 7.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 727168469 230 YGVLLSGGLDSSVISAITKKYAARrvedqerseaWWPQLHSFAVGL 275
Cdd:cd01984 1 ILVPLSGGEDSSIALKHAKKFKTS----------KAEEVVVVHVGE 36
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
76-186 |
1.25e-05 |
|
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: 46.59 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 76 GEIYNHQALRQQlsdrYAFQTGSDcEVILAL--YQ---EKGP---DF-LDDLQGMFAFALYDTEKDAYLIGRDHLGIIPL 146
Cdd:pfam12481 83 GHLENLASLKQQ----YGLSKGAN-EAMIVIeaYRtlrDRGPypaDQvVRDLEGKFAFVLYDSSTSTVFVASDADGSVPL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 727168469 147 YMGHDEHGNLYVASEMKALVPVC-RTIKEFPAGSYLWSQDG 186
Cdd:pfam12481 158 YWGIDADGSLVFSDDIEIVKKGCgKSFAPFPKGCFFTSSGG 198
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
115-191 |
3.47e-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: 45.38 E-value: 3.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727168469 115 LDDLQGMFAFALYDTEKDAYLIGRDHLGIIPLYMGHDEHGNLYVASEMKALVPVC-RTIKEFPAGSYLWSqDGEIREY 191
Cdd:cd01910 122 VKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADGSVVFSDDVELVKASCgKSFAPFPKGCFFHS-EGGLRSF 198
|
|
| macrolact_Ik_Al |
NF033561 |
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology ... |
212-296 |
7.93e-04 |
|
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: 42.21 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 212 LRTALEESVKSHLMSDVPYGVLLSGGLDSSVISAItkkyAARRVEDQERSEAWwpQLHsfAVGLEGSPDLRAAQEVANHL 291
Cdd:NF033561 195 LRAALAAAVALRVDGAPPLSSDLSGGLDSTTLALL----AARCLPVGRRLTGV--TVH--PEGRTEGGDLDYARLAARAP 266
|
....*
gi 727168469 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 |
2.17e-03 |
|
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: 40.57 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727168469 232 VLLSGGLDSSVISAITKK--YAARRV-------EDQERSEAWWPQlhsfavglegspDLRAAQEVANHLGTVHHEIHFT 301
Cdd:cd01998 4 VAMSGGVDSSVAAALLKEqgYDVIGVfmknwddEDNEKGGCCSEE------------DIEDARRVADQLGIPLYVVDFS 70
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
69-165 |
3.60e-03 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam synthetase (CarA) is an ATP/Mg2+-dependent enzyme that catalyzes the formation of the beta-lactam ring in (5R)-carbapenem-3-carboxylic acid biosynthesis. CarA is homologous to beta-lactam synthetase (beta-LS), which is involved in the biosynthesis of clavulanic acid, a clinically important beta-lactamase inhibitor. CarA and beta-LS each have two distinct domains, an N-terminal Ntn hydrolase domain and a C-terminal synthetase domain, a domain architecture similar to that of the class-B asparagine synthetases (AS-B's). The N-terminal domain of these enzymes hydrolyzes glutamine to glutamate and ammonia. CarA forms a homotetramer while betaLS forms a heterodimer. The N-terminal folds of CarA and beta-LS are similar to those of other class II glutamine amidotransferases including lucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and glutamate synthase (GltS). This fold is also somwhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238890 [Multi-domain] Cd Length: 199 Bit Score: 39.01 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727168469 69 THVLAvnGEIYNHQALRQQLSdryAFQTGS----DCEVILALYQEKGPDFLDDLQGMFAFALyDTEKDAYLIGRDHLGII 144
Cdd:cd01909 53 TAYLI--GELYNRDELRSLLG---AGEGRSavlgDAELLLLLLTRLGLHAFRLAEGDFCFFI-EDGNGRLTLATDHAGSV 126
|
90 100
....*....|....*....|.
gi 727168469 145 PLYMGHDehGNLYVASEMKAL 165
Cdd:cd01909 127 PVYLVQA--GEVWATTELKLL 145
|
|
| |
