|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-577 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 1223.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILAVLGCVDNSQAKRSRIIELSRRLRHRGPDWSGLHCYEDCYLAHERLAIVDPTSGDQPLYNEDKTIAVTVNGEIYN 80
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTIVVTANGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 81 HKALRENLKSHQFRTGSDCEVIAHLYEEHGEEFVDMLDGMFAFVLLDTRDKSFIAARDAIGITPLYIGWGLDGSVWFASE 160
Cdd:PLN02549 81 HKELREKLKLHKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 161 MKALSDDCEQFMCFPPGHIYSSKQGGLRRWYNPPWFSEVVPSTPYDPLVVRNTFEKAVIKRLMTDVPFGVLLSGGLDSSL 240
Cdd:PLN02549 161 MKALCDDCERFEEFPPGHYYSSKAGGFRRWYNPPWFSESIPSTPYDPLVLREAFEKAVIKRLMTDVPFGVLLSGGLDSSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 241 VASVALRHLEKSEAACQWGSKLHTFCIGLKGSPDLKAGREVADYLGTRHHELHFTVQDGIDAIEEVIYHVETYDVTTIRA 320
Cdd:PLN02549 241 VASIAARHLAETKAARQWGQQLHSFCVGLEGSPDLKAAREVADYLGTVHHEFHFTVQEGIDAIEDVIYHLETYDVTTIRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 321 STPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKKEFHEETCRKIKALHQYDCLRANKSTSAWGVEARVPFLD 400
Cdd:PLN02549 321 STPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKEEFHKETCRKIKALHQYDCLRANKSTSAWGLEARVPFLD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 401 KEFINVAMSIDPEWKMIRPDLGRIEKWVLRNAFDDEKNPYLPKHILYRQKEQFSDGVGYSWIDGLKDHANKHVSETMLMN 480
Cdd:PLN02549 401 KEFIDVAMSIDPEWKMIRPGEGRIEKWVLRKAFDDEEDPYLPKHILWRQKEQFSDGVGYSWIDGLKAHAEKHVSDEMFAN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 481 ASFVFPDNTPLTKEAYYYRTIFEKFFPKSAARATVPGGPSVACSTAKAVEWDAAWSQNLDPSGRAALGVHVSAYGEDKTE 560
Cdd:PLN02549 481 ASFRYPHNTPTTKEAYYYRMIFEKHFPQDAARLTVPGGPSVACSTAKAVEWDAAWSKNLDPSGRAALGVHVAAYEEDVAA 560
|
570
....*....|....*..
gi 15238108 561 DSRPEKLQKLAEKTPAI 577
Cdd:PLN02549 561 DGAPAVPKAKKSKAPAI 577
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-554 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 930.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILAVLGCVDNSQAKRSRIIELSRRLRHRGPDWSGLHCYEDCYLAHERLAIVDPTSGDQPLYNEDKTIAVTVNGEIYN 80
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 81 HKALRENLKS-HQFRTGSDCEVIAHLYEEHGEEFVDMLDGMFAFVLLDTRDKSFIAARDAIGITPLYIGWGLDGSVWFAS 159
Cdd:PRK09431 81 HQELRAELGDkYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 160 EMKALSDDCEQFMCFPPGHIYSSKQGGLRRWYNPPWF-SEVVPSTPYDPLVVRNTFEKAVIKRLMTDVPFGVLLSGGLDS 238
Cdd:PRK09431 161 EMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFdYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGLDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 239 SLVASVALRHL----EKSEAACQWGSKLHTFCIGLKGSPDLKAGREVADYLGTRHHELHFTVQDGIDAIEEVIYHVETYD 314
Cdd:PRK09431 241 SLISAIAKKYAarriEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEGLDALRDVIYHLETYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 315 VTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKKEFHEETCRKIKALHQYDCLRANKSTSAWGVEA 394
Cdd:PRK09431 321 VTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMYDCLRANKAMMAWGVEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 395 RVPFLDKEFINVAMSIDPEWKMIRPdlGRIEKWVLRNAFDDeknpYLPKHILYRQKEQFSDGVGYSWIDGLKDHANKHVS 474
Cdd:PRK09431 401 RVPFLDKEFLDVAMRINPEDKMCGN--GKMEKHILREAFEG----YLPESILWRQKEQFSDGVGYSWIDTLKEVAAEQVS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 475 ETMLMNASFVFPDNTPLTKEAYYYRTIFEKFFPKSAARATVPGGPSVACSTAKAVEWDAAWSQNLDPSGRAALGVHVSAY 554
Cdd:PRK09431 475 DQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKNMDDPSGRAVSGVHQSAY 554
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-568 |
0e+00 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 909.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILAVLGCVDNSQAKRSRIIELSRRLRHRGPDWSGLHCYE-----DCYLAHERLAIVDPTSGDQPLYNEDKTIAVTVN 75
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRKALELSKRLRHRGPDWSGIIVLEnspgtYNILAHERLAIVDLSDGKQPLLDDDETVALMQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 76 GEIYNHKALRENL--KSHQFRTGSDCEVIAHLYEEHGE-EFVDMLDGMFAFVLLDTRDKSFIAARDAIGITPLYIGWGLD 152
Cdd:PTZ00077 81 GEIYNHWEIRPELekEGYKFSSNSDCEIIGHLYKEYGPkDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 153 GSVWFASEMKALSDDCEQFMCFPPGHIYSS--KQGGLRRWYNPPWFSEVVPSTPY--DPLVVRNTFEKAVIKRLMTDVPF 228
Cdd:PTZ00077 161 GSIWFSSELKALHDQCVEVKQFPPGHYYDQtkEKGEFVRYYNPNWHDFDHPIPTGeiDLEEIREALEAAVRKRLMGDVPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 229 GVLLSGGLDSSLVASVALRHLEKSE--AACQWGSKLHTFCIGLKGSPDLKAGREVADYLGTRHHELHFTVQDGIDAIEEV 306
Cdd:PTZ00077 241 GLFLSGGLDSSIVAAIVAKLIKNGEidLSKRGMPKLHSFCIGLEGSPDLKAARKVAEYLGTEHHEFTFTVEEGIDALPDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 307 IYHVETYDVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKKEFHEETCRKIKALHQYDCLRANKS 386
Cdd:PTZ00077 321 IYHTETYDVTTIRASTPMYLLSRRIKALGIKMVLSGEGSDELFGGYLYFHKAPNREEFHRELVRKLHDLHKYDCLRANKA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 387 TSAWGVEARVPFLDKEFINVAMSIDPEWKMIRPDLGRIEKWVLRNAFDDEKNPYLPKHILYRQKEQFSDGVGYSWIDGLK 466
Cdd:PTZ00077 401 TMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFEGQMEKYILRKAFEGLEKPYLPDEILWRQKEQFSDGVGYSWIDGLK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 467 DHANKHVSETMLMNASFVFPDNTPLTKEAYYYRTIFEKFFPKSAARATVPGGPSVACSTAKAVEWDAAWSQNLDPSGRAA 546
Cdd:PTZ00077 481 EYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTVPYGPSIACSTEKALEWDESFKKNTDESGRAV 560
|
570 580
....*....|....*....|..
gi 15238108 547 LGVHVSAYgedKTEDSRPEKLQ 568
Cdd:PTZ00077 561 LSVHNDAK---QDSDVKEEDKS 579
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-507 |
9.73e-169 |
|
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: 490.89 E-value: 9.73e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILAVLGcvDNSQAKRSRIIELSRRLRHRGPDWSGLHCYEDCYLAHERLAIVDPTS-GDQPLYNEDKTIAVTVNGEIY 79
Cdd:COG0367 1 MCGIAGIID--FDGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLSEgGHQPMVSEDGRYVLVFNGEIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 80 NHKALRENLKS--HQFRTGSDCEVIAHLYEEHGEEFVDMLDGMFAFVLLDTRDKSFIAARDAIGITPLYIGWgLDGSVWF 157
Cdd:COG0367 79 NYRELRAELEAlgHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAE-DGGGLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 158 ASEMKAL-----------SDDCEQFMCF----------------PPGHIYSSKQGG---LRRWYNPPwFSEVVPSTPYDP 207
Cdd:COG0367 158 ASELKALlahpgvdreldPEALAEYLTLgyvpaprtifkgirklPPGHYLTVDAGGeleIRRYWDLE-FVPHERSDSEEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 208 LV--VRNTFEKAVIKRLMTDVPFGVLLSGGLDSSLVASVALRHLEKseaacqwgsKLHTFCIGLKGSP--DLKAGREVAD 283
Cdd:COG0367 237 AVeeLRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG---------PLKTFSIGFEDSAydESPYARAVAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 284 YLGTRHHELHFTVQDGIDAIEEVIYHVEtyDVTTIRASTPMFLMSRKIKSLgVKMVLSGEGSDEIFGGYLYFHKAPN--K 361
Cdd:COG0367 308 HLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLSGEGADELFGGYPRYREAALllS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 362 KEFHEETCRKIKA-----------------------LHQYDCLRANKSTSAWGVEARVPFLDKEFINVAMSIDPEWKMir 418
Cdd:COG0367 385 PDFAEALGGELVPrlyaesgaedplrrmlyldlktyLPGDLLVKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELKL-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 419 pdLGRIEKWVLRNAFDDeknpYLPKHILYRQKEQFSDGVGySWIDG-LKDHANKHVSETMLMNASFVfpdntpltkEAYY 497
Cdd:COG0367 463 --RGGRGKYLLRKALEG----LLPDEVLDRPKQGFPVPLG-PWLRGpLREWLEDLLSDESLAARGLF---------DPDA 526
|
570
....*....|
gi 15238108 498 YRTIFEKFFP 507
Cdd:COG0367 527 VRRLLEEHLA 536
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-453 |
5.12e-167 |
|
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: 482.99 E-value: 5.12e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 4 ILAVLGCVDNSQAKRSRIIELSRRLRHRGPDWSGL-HCYEDCYLAHERLAIVDPTSGDQPLYNEDKTIAVTVNGEIYNHK 82
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSDTIAHRGPDASGIeYKDGNAILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYNHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 83 ALRENL--KSHQFRTGSDCEVIAHLYEEHGEEFVDMLDGMFAFVLLDTRDKSFIAARDAIGITPLYIGwGLDGSVWFASE 160
Cdd:TIGR01536 81 ELREELeaKGYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYA-YDGGQLYFASE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 161 MKALSDDCE-----------QFMCF----------------PPGHIYSSKQGGLRRW-YNPPWFSEVVPSTPYDPLVVRN 212
Cdd:TIGR01536 160 IKALLAHPNikpfpdgaalaPGFGFvrvpppstffrgvfelEPGHDLPLDDDGLNIErYYWERRDEHTDSEEDLVDELRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 213 TFEKAVIKRLMTDVPFGVLLSGGLDSSLVASVALRHLEKSEaacqwgskLHTFCIGLKGSPDL---KAGREVADYLGTRH 289
Cdd:TIGR01536 240 LLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPRGP--------VHTFSIGFEGSPDFdesKYARKVADHLGTEH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 290 HELHFTVQDGIDAIEEVIYHVEtyDVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKKEFHEETC 369
Cdd:TIGR01536 312 HEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSGEGADELFGGYLYFHEAPAAEALREELQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 370 RKIKALHQYDCLRAN-KSTSAWGVEARVPFLDKEFINVAMSIDPEWKMirpdLGRIEKWVLRNAFDDeknpYLPKHILYR 448
Cdd:TIGR01536 390 YLDLELYMPGLLRRKdRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL----RDGKEKYLLREAFEG----YLPEEILWR 461
|
....*
gi 15238108 449 QKEQF 453
Cdd:TIGR01536 462 PKEGF 466
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
210-511 |
8.01e-104 |
|
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: 314.55 E-value: 8.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 210 VRNTFEKAVIKRLMTDVPFGVLLSGGLDSSLVASVALRHLEkseaacqwgSKLHTFCIGL--KGSPDLKAGREVADYLGT 287
Cdd:pfam00733 2 LRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP---------SPLHTFSIGFegRGYDEAPYAREVAEHLGT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 288 RHHELHFTVQDGIDAIEEVIYHVETydVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKApnkKEFHEE 367
Cdd:pfam00733 73 DHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEGADELFGGYPFYKGE---DPLRRM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 368 TCRKIKALHQYDCLRANKSTSAWGVEARVPFLDKEFINVAMSIDPEWKMIrpdlGRIEKWVLRNAFDDeknpYLPKHILY 447
Cdd:pfam00733 148 LYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLR----GGIEKYILREALEG----ILPDEILE 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15238108 448 RQKEQFSDGVGYSWIDG-LKDHANKHVSEtmlmnasfvfpdnTPLTKEAYYYRTIFEKFFPKSAA 511
Cdd:pfam00733 220 RPKEGFSAPVGDWKLRGpLRELAEDLLSD-------------SRLAKEGLLDREAVRELLDEHLA 271
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
224-457 |
6.11e-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: 284.17 E-value: 6.11e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 224 TDVPFGVLLSGGLDSSLVASVALRHLEKSeaacqwgsKLHTFCIGLKGS--PDLKAGREVADYLGTRHHELHFTVQDGID 301
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPET--------PIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEELLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 302 AIEEVIYHVETYDVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNK--KEFHEETCRKIKALHQYD 379
Cdd:cd01991 73 ALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAPLRgwEALEEELLRDLDRLWTRN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15238108 380 CLRANKSTSAWGVEARVPFLDKEFINVAMSIDPEWKMIRPDLGriEKWVLRNAFDDeknpYLPKHILYRQKEQFSDGV 457
Cdd:cd01991 153 LGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPRGGG--EKYILREAARD----LLPDEIAWRPKRAIQFGS 224
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-192 |
1.76e-84 |
|
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: 262.49 E-value: 1.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 2 CGILAVLGcVDNSQAKRSRIIELSRRLRHRGPDWSGLHCYEDCYLAHERLAIVDPTSGDQPLYNEDKTIAVTVNGEIYNH 81
Cdd:cd00712 1 CGIAGIIG-LDGASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVLVFNGEIYNY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 82 KALRENLKS--HQFRTGSDCEVIAHLYEEHGEEFVDMLDGMFAFVLLDTRDKSFIAARDAIGITPLYIGWGlDGSVWFAS 159
Cdd:cd00712 80 RELRAELEAlgHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRD-GGGLAFAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15238108 160 EMKALSDDCE----------------QFMC-----------FPPGHIYSSKQGG--LRRWYN 192
Cdd:cd00712 159 ELKALLALPGvpreldeaalaeylafQYVPaprtifkgirkLPPGHYLTVDPGGveIRRYWD 220
|
|
| eps_aminotran_1 |
TIGR03108 |
exosortase A system-associated amidotransferase 1; The predicted protein-sorting ... |
1-454 |
1.97e-64 |
|
exosortase A system-associated amidotransferase 1; The predicted protein-sorting transpeptidase that we call exosortase (see TIGR02602) has distinct subclasses that associated with different types of exopolysaccharide production loci. This model represents a distinct clade among a set of amidotransferases largely annotated (not necessarily accurately) as glutatime-hydrolyzing asparagine synthases. Members of this clade are essentially restricted to the characteristic exopolysaccharide (EPS) regions that contain the exosortase 1 genome (xrtA), in genomes that also have numbers of PEP-CTERM domain (TIGR02595) proteins.
Pssm-ID: 132152 [Multi-domain] Cd Length: 628 Bit Score: 222.30 E-value: 1.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILAVLGCVDNSQAKRSRIIELSRRLRHRGPDWSGLHCYEDCYLAHERLAIVDPTSGDQPLYNEDKTIAVTVNGEIYN 80
Cdd:TIGR03108 1 MCGITGIFDLTGQRPIDRDLLRRMNDAQAHRGPDGGGVHVEPGIGLGHRRLSIIDLSGGQQPLFNEDGSVVVVFNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 81 HKALRENLKS--HQFRTGSDCEVIAHLYEEHGEEFVDMLDGMFAFVLLDTRDKSFIAARDAIGITPLYIGWGLDGSVWFA 158
Cdd:TIGR03108 81 FQELVAELQAlgHVFRTRSDTEVIVHAWEEWGEACVERFRGMFAFALWDRNQETLFLARDRLGIKPLYYALLADGWFIFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 159 SEMKAL-----------SDDCEQFMCF----------------PPGHIYSSKQGG----LRRWYNPPwFSEVVPSTPYD- 206
Cdd:TIGR03108 161 SELKALtahpslpreldPLAVEDYFAYgyvpdprtifkgvkklEPGHTLTLRRGApparPRCYWDVS-FAPAAPLSEADa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 207 --PLVVRntFEKAVIKRLMTDVPFGVLLSGGLDSSLVasVALrhlekseAACQWGSKLHTFCIGLKGSPDLKA--GREVA 282
Cdd:TIGR03108 240 laELIER--LREAVRSRMVADVPLGAFLSGGVDSSAV--VAL-------MAGLSDTPVNTCSIAFDDPAFDESayARQVA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 283 DYLGTRHHELhfTVQDgiDAIEEVIYHVETYDVTTIRAST-PMFLMSRKIKSlGVKMVLSGEGSDEIFGGYL-------- 353
Cdd:TIGR03108 309 ERYGTNHRVE--TVDP--DDFSLVDRLAGLYDEPFADSSAlPTYRVCELARK-RVTVALSGDGGDELFAGYRryrwhmae 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 354 -------------------------------------------------YFHKA---PNK-------KEFH--------E 366
Cdd:TIGR03108 384 ervrgilplglrrplfgtlgrlypkadwaprmlrakttfqalardplegYFHSVsvlDNAlrrqlfsPDFRrelqgyraI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 367 ETCRKIKA---------LHQY---------DCL-RANKSTSAWGVEARVPFLDKEFINVAMSIDPEWKMirpdLGRIEKW 427
Cdd:TIGR03108 464 EVLRRHAAraptddalsLAQYldlktylpgDILtKVDRASMAHGLEVRVPLLDHRLVEWAAGLPPDLKL----RGGEGKY 539
|
570 580
....*....|....*....|....*..
gi 15238108 428 VLRNAFDdeknPYLPKHILYRQKEQFS 454
Cdd:TIGR03108 540 LLKKAMR----PYLPDDVLYRPKMGFS 562
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
48-164 |
2.59e-58 |
|
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: 190.42 E-value: 2.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 48 HERLAIVDPTSGDQPLYN-EDKTIAVTVNGEIYNHKALRENLKS--HQFRTGSDCEVIAHLYE-EHGEEFVDMLDGMFAF 123
Cdd:pfam13537 1 HRRLSIIDLEGGAQPMVSsEDGRYVIVFNGEIYNYRELRAELEAkgYRFRTHSDTEVILHLYEaEWGEDCVDRLNGMFAF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15238108 124 VLLDTRDKSFIAARDAIGITPLYIGWGLDGSVWFASEMKAL 164
Cdd:pfam13537 81 AIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKAL 121
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-180 |
2.30e-56 |
|
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: 188.81 E-value: 2.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 2 CGILAVLGCVDNSQAKRSRIIELSRRLRHRGPDWSGLHCYED---------------------------CYLAHERLAIV 54
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDGdglfvekragpvsdvaldlldeplksgVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 55 DPTS--GDQPLYNEDKTIAVTVNGEIYNHKALRENLKS--HQFRTGSDCEVIAHLYEEHG---------EEFVDMLDGMF 121
Cdd:cd00352 81 GLPSeaNAQPFRSEDGRIALVHNGEIYNYRELREELEArgYRFEGESDSEVILHLLERLGregglfeavEDALKRLDGPF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 122 AFVLLDTRDKSFIAARDAIGITPLYIGWGLDGSVWFASEMKALSDDC-EQFMCFPPGHIY 180
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
33-160 |
8.95e-44 |
|
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: 152.07 E-value: 8.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 33 PDWSGLHCYEDCYLAHERLAIVD-PTSGDQPLYNEDKTIAVTVNGEIYNHKALRENLKS--HQFRTGSDCEVIAHLYEEH 109
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDlPDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADlgHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15238108 110 GEEFVDMLDGMFAFVLLDTRDKSFIAARDAIGITPLYIGWgLDGSVWFASE 160
Cdd:pfam13522 81 GEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGI-LGGGFVFASE 130
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-141 |
1.14e-13 |
|
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: 69.62 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILAVLGCVDNSQAKRSRIIELSRRLRHRGPDWSGLH-----CYEDCYLA---HERLAIVDPtsgdQPLYNEDKTIAV 72
Cdd:cd03766 1 MCGILCSVSPSGPHINSSLLSEELLPNLRNRGPDYLSTRqlsvtNWTLLFTSsvlSLRGDHVTR----QPLVDQSTGNVL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15238108 73 TVNGEIYNhkalrenlKSHQFRTGSDCEVIAHLYEEHGEEFVDMLD------GMFAFVLLDTRDKSFIAARDAIG 141
Cdd:cd03766 77 QWNGELYN--------IDGVEDEENDTEVIFELLANCSSESQDILDvlssieGPFAFIYYDASENKLYFGRDCLG 143
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-172 |
1.37e-13 |
|
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: 70.17 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 2 CGILAVLGcvdNSQAKrSRIIELSRRLRHRGPDWSGLHCYEDCYL---------------------------AHERLAiv 54
Cdd:cd00714 1 CGIVGYIG---KREAV-DILLEGLKRLEYRGYDSAGIAVIGDGSLevvkavgkvanleeklaekplsghvgiGHTRWA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 55 dpTSGD------QPLYNEDKTIAVTVNGEIYNHKALRENLKS--HQFRTGSDCEVIAHLYEEH---GEEFVD-------M 116
Cdd:cd00714 75 --THGEptdvnaHPHRSCDGEIAVVHNGIIENYAELKEELEAkgYKFESETDTEVIAHLIEYYydgGLDLLEavkkalkR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15238108 117 LDGMFAFVLLDTRDK-SFIAARDAigiTPLYIGWGlDGSVWFASEMKALSDDCEQFM 172
Cdd:cd00714 153 LEGAYALAVISKDEPdEIVAARNG---SPLVIGIG-DGENFVASDAPALLEHTRRVI 205
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
56-160 |
2.92e-13 |
|
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: 71.98 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 56 PTSGD------QPLY--NEDKTIAVTVNGEIYNHKALRENL--KSHQFRTGSDCEVIAHL--YEEHGEEFVD-------M 116
Cdd:COG0034 81 STTGSsslenaQPFYvnSPFGSIALAHNGNLTNAEELREELeeEGAIFQTTSDTEVILHLiaRELTKEDLEEaikealrR 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15238108 117 LDGMFAFVLLdTRDKsFIAARDAIGITPLYIGWgLDGSVWFASE 160
Cdd:COG0034 161 VKGAYSLVIL-TGDG-LIAARDPNGIRPLVLGK-LEDGYVVASE 201
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-164 |
1.74e-11 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 66.62 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILAVLGcvdNSQAkrSRIIELS-RRLRHRGPDWSGLHCYE---------------------------DCYLAHERLa 52
Cdd:PLN02440 1 ECGVVGIFG---DPEA--SRLCYLGlHALQHRGQEGAGIVTVDgnrlqsitgnglvsdvfdeskldqlpgDIAIGHVRY- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 53 ivdPTSGD------QPLYNEDK--TIAVTVNGEIYNHKALR---ENLKSHqFRTGSDCEVIAHLYEEHGEEFVDM----- 116
Cdd:PLN02440 75 ---STAGAsslknvQPFVANYRfgSIGVAHNGNLVNYEELRaklEENGSI-FNTSSDTEVLLHLIAISKARPFFSrivda 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15238108 117 ---LDGMFAFVLLdTRDKSFiAARDAIGITPLYIGWGLDGSVWFASEMKAL 164
Cdd:PLN02440 151 cekLKGAYSMVFL-TEDKLV-AVRDPHGFRPLVMGRRSNGAVVFASETCAL 199
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
56-164 |
4.03e-11 |
|
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: 63.63 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 56 PTSGD------QPLYNE--DKTIAVTVNGEIYNHKALRENLKSHQ--FRTGSDCEVIAHL--YEEHGEEFVD-------M 116
Cdd:cd00715 74 STAGSsslenaQPFVVNspLGGIALAHNGNLVNAKELREELEEEGriFQTTSDSEVILHLiaRSLAKDDLFEaiidaleR 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15238108 117 LDGMFAFVLLdTRDKsFIAARDAIGITPLYIGWGLDGSVWFASEMKAL 164
Cdd:cd00715 154 VKGAYSLVIM-TADG-LIAVRDPHGIRPLVLGKLEGDGYVVASESCAL 199
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-159 |
4.08e-11 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 65.84 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILavlGCVDNSQAKrSRIIELSRRLRHRGPDWSG--------LHCY-------------EDCYL------AHERLAi 53
Cdd:PRK00331 1 MCGIV---GYVGQRNAA-EILLEGLKRLEYRGYDSAGiavlddggLEVRkavgkvanleaklEEEPLpgttgiGHTRWA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 54 vdpTSGD------QPLYNEDKTIAVTVNGEIYNHKALRENLKS--HQFRTGSDCEVIAHLYEEHGEEFVD---------- 115
Cdd:PRK00331 76 ---THGKpternaHPHTDCSGRIAVVHNGIIENYAELKEELLAkgHVFKSETDTEVIAHLIEEELKEGGDlleavrkalk 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15238108 116 MLDGMFAFVLLDTRDKS-FIAARDAigiTPLYIGWGlDGSVWFAS 159
Cdd:PRK00331 153 RLEGAYALAVIDKDEPDtIVAARNG---SPLVIGLG-EGENFLAS 193
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-164 |
5.22e-11 |
|
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: 65.42 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILAVLGcvdNSQAKrSRIIE-LsRRLRHRGPDWSGLhcyedCYLAHERLAIV---------------DPTSGDQ--- 61
Cdd:COG0449 1 MCGIVGYIG---KRDAA-PILLEgL-KRLEYRGYDSAGI-----AVLDDGGLEVRkavgklanleeklaeEPLSGTIgig 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 62 ----------------PLYNEDKTIAVTVNGEIYNHKALRENLKS--HQFRTGSDCEVIAHLYEEH---GEEFVD----- 115
Cdd:COG0449 71 htrwathgapsdenahPHTSCSGRIAVVHNGIIENYAELREELEAkgHTFKSETDTEVIAHLIEEYlkgGGDLLEavrka 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15238108 116 --MLDGMFAFVLLDTRDK-SFIAARDAigiTPLYIGWGlDGSVWFASEMKAL 164
Cdd:COG0449 151 lkRLEGAYALAVISADEPdRIVAARKG---SPLVIGLG-EGENFLASDVPAL 198
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
117-193 |
2.02e-10 |
|
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: 60.79 E-value: 2.02e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15238108 117 LDGMFAFVLLDTRDKSFIAARDAIGITPLYIGWGLDGSVWFASEMKALSDDC-EQFMCFPPGHIYSSkQGGLRRWYNP 193
Cdd:cd01910 125 LEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADGSVVFSDDVELVKASCgKSFAPFPKGCFFHS-EGGLRSFEHP 201
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
117-193 |
4.12e-10 |
|
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: 60.07 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 117 LDGMFAFVLLDTRDKSFIAARDAIGITPLYigWGL--DGSVWFASEMKALSDDC-EQFMCFPPGHIYSSkQGGLRRWYNP 193
Cdd:pfam12481 129 LEGKFAFVLYDSSTSTVFVASDADGSVPLY--WGIdaDGSLVFSDDIEIVKKGCgKSFAPFPKGCFFTS-SGGLRSFEHP 205
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
70-164 |
5.34e-09 |
|
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: 57.28 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 70 IAVTVNGEIYNHKALRENLKSH--QFRTGSDCEVIAH----LYEEHG-------------------------EEFVDMLD 118
Cdd:cd01907 105 IAVVHNGEISNYGSNREYLERFgyKFETETDTEVIAYyldlLLRKGGlpleyykhiirmpeeerelllalrlTYRLADLD 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15238108 119 GMFAFVLldTRDKSFIAARDAIGITPLYIGwGLDGSVWFASEMKAL 164
Cdd:cd01907 185 GPFTIIV--GTPDGFIVIRDRIKLRPAVVA-ETDDYVAIASEECAI 227
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
61-164 |
1.55e-07 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 53.88 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 61 QPLYNEDK--TIAVTVNGEIYNHKALRENL--KSHQFRTGSDCEVIAHL--------YEEHGEEFVDMLDGMFAFVLLdT 128
Cdd:PRK05793 101 QPLVANYKlgSIAIAHNGNLVNADVIRELLedGGRIFQTSIDSEVILNLiarsakkgLEKALVDAIQAIKGSYALVIL-T 179
|
90 100 110
....*....|....*....|....*....|....*.
gi 15238108 129 RDKsFIAARDAIGITPLYIGwGLDGSVWFASEMKAL 164
Cdd:PRK05793 180 EDK-LIGVRDPHGIRPLCLG-KLGDDYILSSESCAL 213
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-204 |
1.67e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 50.79 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 1 MCGILAVLGCVDNSQAkrsrIIELSRRLRHRGPDWSGL-------------HCYE----DCY-----------------L 46
Cdd:PTZ00295 24 CCGIVGYLGNEDASKI----LLEGIEILQNRGYDSCGIstissggelkttkYASDgttsDSIeilkeklldshknstigI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 47 AHERLAIVDPTSgDQ---PLYNEDKTIAVTVNGEIYNHKALRENL--KSHQFRTGSDCEVIAHL---YEEHGEEFVDM-- 116
Cdd:PTZ00295 100 AHTRWATHGGKT-DEnahPHCDYKKRIALVHNGTIENYVELKSELiaKGIKFRSETDSEVIANLiglELDQGEDFQEAvk 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 117 -----LDGMFAFVLLDTRDK-SFIAARDAigiTPLYIGWGlDGSVWFASEMKALSDDCEQFMCFPPGHIYSSKQGGLRRW 190
Cdd:PTZ00295 179 saisrLQGTWGLCIIHKDNPdSLIVARNG---SPLLVGIG-DDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDL 254
|
250
....*....|....*...
gi 15238108 191 YNPPWF----SEVVPSTP 204
Cdd:PTZ00295 255 YTQRRVekipEEVIEKSP 272
|
|
| macrolact_Ik_Al |
NF033561 |
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology ... |
138-292 |
4.17e-05 |
|
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: 46.44 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 138 DAIGITPLYI-GWGlDGSVWfASEMKALS------DDCEQFMC----------------F------PPGH-IYSSKQGGL 187
Cdd:NF033561 97 DPAGACPVYTtRTD-GGWVW-SSSARALAgltgapVDAWRLAAallapsvpalaagrsaFagveqvPPGHrLTLPADGGA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 188 RRWynpPWFSEVVPSTPYDPLV-VRNTFEKAVIKRLMTDVPFGVLLSGGLDSSLVASVALRHLekSEAACQWGSKLHTfc 266
Cdd:NF033561 175 PRT---PWWWRPDPRPGPDAVArLRAALAAAVALRVDGAPPLSSDLSGGLDSTTLALLAARCL--PVGRRLTGVTVHP-- 247
|
170 180
....*....|....*....|....*.
gi 15238108 267 IGLKGSPDLKAGREVADYLGTRHHEL 292
Cdd:NF033561 248 EGRTEGGDLDYARLAARAPRIRHRLL 273
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
230-292 |
4.71e-05 |
|
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.
Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 44.92 E-value: 4.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15238108 230 VLLSGGLDSSLVASVALRHLEKSEAAcqwgsklhTFCIGLKGSPDLKAGREVADYLGTRHHEL 292
Cdd:pfam06508 4 VLLSGGLDSTTCLAWAKKEGYEVYAL--------SFDYGQRHRKELECAKKIAKALGVEHKIL 58
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
230-291 |
7.87e-04 |
|
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 41.30 E-value: 7.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15238108 230 VLLSGGLDSSLVASVALRHlekseaacqwGSKLH--TFCIGLKGSPDLKAGREVADYLGTRHHE 291
Cdd:COG0603 7 VLLSGGLDSTTCLAWALAR----------GYEVYalSFDYGQRHRKELEAARRIAKALGVGEHK 60
|
|
| betaLS_CarA_N |
cd01909 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_betaLS-type. Carbapenam ... |
76-165 |
7.92e-04 |
|
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: 40.94 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 76 GEIYNHKALRENLKSHQFRTG--SDCEVIAHLYEEHGEEFVDMLDGMFAFVlLDTRDKSFIAARDAIGITPLYIgwGLDG 153
Cdd:cd01909 58 GELYNRDELRSLLGAGEGRSAvlGDAELLLLLLTRLGLHAFRLAEGDFCFF-IEDGNGRLTLATDHAGSVPVYL--VQAG 134
|
90
....*....|..
gi 15238108 154 SVWFASEMKALS 165
Cdd:cd01909 135 EVWATTELKLLA 146
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
210-326 |
1.08e-03 |
|
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 41.76 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238108 210 VRNT-FEKAVIkrlmtdvpfGvlLSGGLDSSLVASVALRHLEKSeaacqwgsklHTFCIGL--KGSPD--LKAGREVADY 284
Cdd:COG0171 281 VRKNgFKGVVL---------G--LSGGIDSALVAALAVDALGPE----------NVLGVTMpsRYTSDesLEDAEELAEN 339
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15238108 285 LGTRHHELHftVQDGIDAIEEVIYHV---ETYDVTT------IRASTPMFL 326
Cdd:COG0171 340 LGIEYEEID--ITPAVEAFLEALPHAfggELDDVAEenlqarIRMVILMAL 388
|
|
| |
