|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-561 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 786.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 1 MCGIFAAF-KHEDIHNFKPKALQLSKKIRHRGPDWSGNAVMNSTIFVHERLAIVGLDSGAQPITSADGEYMLGVNGEIYN 79
Cdd:PRK09431 1 MCGIFGILdIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 80 HIQLR-EMCSDYKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRSSQSpeTVYF 158
Cdd:PRK09431 81 HQELRaELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHG--NLYF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 159 ASELKCLTDVCDSIISFPPGHVYDSETDKITRYFTPDWLDEKRIPSTPVDYHAIRHSLEKAVRKRLMAEVPYGVLLSGGL 238
Cdd:PRK09431 159 ASEMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 239 DSSLIAAIAARETEKANadanEDNNVDEkqlagiddqghlhtSGWSRLHSFAIGLPNAPDLQAARKVAKFIGSIHHEHTF 318
Cdd:PRK09431 239 DSSLISAIAKKYAARRI----EDDERSE--------------AWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 319 TLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFAQAPSAAEFHTESVQRVKN 398
Cdd:PRK09431 301 TVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 399 LHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIKPkeGRIEKYILRKAFDttdepdvkPYLPEEILWRQK 478
Cdd:PRK09431 381 LHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGN--GKMEKHILREAFE--------GYLPESILWRQK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 479 EQFSDGVGYSWIDGLRDTAERAISDAMFANPKADWGDDIPTTKEAYWYRLKFDAWFPQKTAADTVMR-------WIPKAD 551
Cdd:PRK09431 451 EQFSDGVGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGgpsvacsSAKAIE 530
|
570
....*....|....
gi 6321563 552 W-GCAE---DPSGR 561
Cdd:PRK09431 531 WdEAFKnmdDPSGR 544
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-508 |
2.75e-153 |
|
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: 451.21 E-value: 2.75e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 1 MCGIFAAFkHEDIHNFKPKALQLSKKIRHRGPDWSGNAVMNSTIFVHERLAIVGLDS-GAQPITSADGEYMLGVNGEIYN 79
Cdd:COG0367 1 MCGIAGII-DFDGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLSEgGHQPMVSEDGRYVLVFNGEIYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 80 HIQLRE--MCSDYKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGrssQSPETVY 157
Cdd:COG0367 80 YRELRAelEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYA---EDGGGLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 158 FASELKCLTD---------------------------VCDSIISFPPGHVYDSETD---KITRYFTPDWLDEKRIPSTPV 207
Cdd:COG0367 157 FASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 208 DYHAIRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAARETEKanadanednnvdekqlagiddqghlhtsgwsRLH 287
Cdd:COG0367 237 AVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-------------------------------PLK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 288 SFAIGLPNAP--DLQAARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLEtyDVTTIRASTPMFLLSRKIKAQgVKMVLS 365
Cdd:COG0367 286 TFSIGFEDSAydESPYARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 366 GEGSDEIFGGYLYFAQAPSAAE-------------------FHTESVQRVKNLHLA------DCLRANKSTMAWGLEARV 420
Cdd:COG0367 363 GEGADELFGGYPRYREAALLLSpdfaealggelvprlyaesGAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 421 PFLDKDFLQLCMNIDPNEKMikpkEGRIEKYILRKAFdttdepdvKPYLPEEILWRQKEQFSDGVGySWIDG-LRDTAER 499
Cdd:COG0367 443 PFLDHRLVEFALSLPPELKL----RGGRGKYLLRKAL--------EGLLPDEVLDRPKQGFPVPLG-PWLRGpLREWLED 509
|
....*....
gi 6321563 500 AISDAMFAN 508
Cdd:COG0367 510 LLSDESLAA 518
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-481 |
1.12e-148 |
|
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: 436.00 E-value: 1.12e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 4 IFAAFKH-EDIHNFKPKALQLSKKIRHRGPDWSGnaVMNST---IFVHERLAIVGLDSGAQPITSADGEYMLGVNGEIYN 79
Cdd:TIGR01536 1 IAGFFDLdDKAVEEDEAIKRMSDTIAHRGPDASG--IEYKDgnaILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 80 HIQLREMCSD--YKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGrssQSPETVY 157
Cdd:TIGR01536 79 HEELREELEAkgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYA---YDGGQLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 158 FASELKCLTDVCDsIISFPPGHVYDSETDKIT-------------------RYFTPDWLDEKRIPSTPVDYHA------- 211
Cdd:TIGR01536 156 FASEIKALLAHPN-IKPFPDGAALAPGFGFVRvpppstffrgvfelepghdLPLDDDGLNIERYYWERRDEHTdseedlv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 212 --IRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAARETEKanadanednnvdekqlagiddqghlhtsgwSRLHSF 289
Cdd:TIGR01536 235 deLRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------------------------GPVHTF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 290 AIGLPNAPDLQ---AARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLEtyDVTTIRASTPMFLLSRKIKAQGVKMVLSG 366
Cdd:TIGR01536 285 SIGFEGSPDFDeskYARKVADHLGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 367 EGSDEIFGGYLYFAQAPSAAEFHTESVQRVKNLHLADCLRAN-KSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMikpKE 445
Cdd:TIGR01536 363 EGADELFGGYLYFHEAPAAEALREELQYLDLELYMPGLLRRKdRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL---RD 439
|
490 500 510
....*....|....*....|....*....|....*.
gi 6321563 446 GrIEKYILRKAFdttdepdvKPYLPEEILWRQKEQF 481
Cdd:TIGR01536 440 G-KEKYLLREAF--------EGYLPEEILWRPKEGF 466
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
211-547 |
5.56e-100 |
|
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: 304.15 E-value: 5.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 211 AIRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAARETEkanadanednnvdekqlagiddqghlhtsgwSRLHSFA 290
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------------------------SPLHTFS 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 291 IGLPNA--PDLQAARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLETydVTTIRASTPMFLLSRKIKAQGVKMVLSGEG 368
Cdd:pfam00733 50 IGFEGRgyDEAPYAREVAEHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 369 SDEIFGGYLYFaqaPSAAEFHTESVQRVKNLHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIkpkeGRI 448
Cdd:pfam00733 128 ADELFGGYPFY---KGEDPLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLR----GGI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 449 EKYILRKAFdttdepdvKPYLPEEILWRQKEQFSDGVGYSWIDG-LRDTAERAISDAmfanpkadwgddiPTTKEAYWYR 527
Cdd:pfam00733 201 EKYILREAL--------EGILPDEILERPKEGFSAPVGDWKLRGpLRELAEDLLSDS-------------RLAKEGLLDR 259
|
330 340
....*....|....*....|
gi 6321563 528 LKFDAWFPQKTAAdTVMRWI 547
Cdd:pfam00733 260 EAVRELLDEHLAG-MLELWL 278
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
226-485 |
1.23e-89 |
|
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: 275.69 E-value: 1.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 226 AEVPYGVLLSGGLDSSLIAAIAARETEKanadanednnvdekqlagiddqghlhtsgwSRLHSFAIGLPN--APDLQAAR 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------------------------TPIDLFTVGFEGspTPDRAAAR 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 304 KVAKFIGSIHHEHTFTLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFAQAP 383
Cdd:cd01991 51 RVAEELGTEHHEVEVTIEELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 384 SA--AEFHTESVQRVKNLHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIKPkeGRIEKYILRKAFdttd 461
Cdd:cd01991 131 LRgwEALEEELLRDLDRLWTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPR--GGGEKYILREAA---- 204
|
250 260
....*....|....*....|....
gi 6321563 462 epdvKPYLPEEILWRQKEQFSDGV 485
Cdd:cd01991 205 ----RDLLPDEIAWRPKRAIQFGS 224
|
|
| macrolact_Ik_Al |
NF033561 |
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology ... |
176-249 |
1.83e-06 |
|
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: 50.68 E-value: 1.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321563 176 PPGHVYDSETDKITRYFTPDWLDEKRIPSTPVdyHAIRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAAR 249
Cdd:NF033561 161 PPGHRLTLPADGGAPRTPWWWRPDPRPGPDAV--ARLRAALAAAVALRVDGAPPLSSDLSGGLDSTTLALLAAR 232
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-561 |
0e+00 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 786.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 1 MCGIFAAF-KHEDIHNFKPKALQLSKKIRHRGPDWSGNAVMNSTIFVHERLAIVGLDSGAQPITSADGEYMLGVNGEIYN 79
Cdd:PRK09431 1 MCGIFGILdIKTDADELRKKALEMSRLMRHRGPDWSGIYASDNAILGHERLSIVDVNGGAQPLYNEDGTHVLAVNGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 80 HIQLR-EMCSDYKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRSSQSpeTVYF 158
Cdd:PRK09431 81 HQELRaELGDKYAFQTGSDCEVILALYQEKGPDFLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHG--NLYF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 159 ASELKCLTDVCDSIISFPPGHVYDSETDKITRYFTPDWLDEKRIPSTPVDYHAIRHSLEKAVRKRLMAEVPYGVLLSGGL 238
Cdd:PRK09431 159 ASEMKALVPVCKTIKEFPPGHYYWSKDGEFVRYYQRDWFDYDAVKDNVTDKNELRDALEAAVKKRLMSDVPYGVLLSGGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 239 DSSLIAAIAARETEKANadanEDNNVDEkqlagiddqghlhtSGWSRLHSFAIGLPNAPDLQAARKVAKFIGSIHHEHTF 318
Cdd:PRK09431 239 DSSLISAIAKKYAARRI----EDDERSE--------------AWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 319 TLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFAQAPSAAEFHTESVQRVKN 398
Cdd:PRK09431 301 TVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKIKAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 399 LHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIKPkeGRIEKYILRKAFDttdepdvkPYLPEEILWRQK 478
Cdd:PRK09431 381 LHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGN--GKMEKHILREAFE--------GYLPESILWRQK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 479 EQFSDGVGYSWIDGLRDTAERAISDAMFANPKADWGDDIPTTKEAYWYRLKFDAWFPQKTAADTVMR-------WIPKAD 551
Cdd:PRK09431 451 EQFSDGVGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSAAECVPGgpsvacsSAKAIE 530
|
570
....*....|....
gi 6321563 552 W-GCAE---DPSGR 561
Cdd:PRK09431 531 WdEAFKnmdDPSGR 544
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-561 |
0e+00 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 743.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 1 MCGIFAAFK-HEDIHNFKPKALQLSKKIRHRGPDWSGNAVMNST-----IFVHERLAIVGLDSGAQPITSADGEYMLGVN 74
Cdd:PTZ00077 1 MCGILAIFNsKGERHELRRKALELSKRLRHRGPDWSGIIVLENSpgtynILAHERLAIVDLSDGKQPLLDDDETVALMQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 75 GEIYNHIQLREMC--SDYKFQTFSDCEPIIPLYLEH-DIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRSSQ 151
Cdd:PTZ00077 81 GEIYNHWEIRPELekEGYKFSSNSDCEIIGHLYKEYgPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 152 SpeTVYFASELKCLTDVCDSIISFPPGHVYDS--ETDKITRYFTPDWLDEK-RIPSTPVDYHAIRHSLEKAVRKRLMAEV 228
Cdd:PTZ00077 161 G--SIWFSSELKALHDQCVEVKQFPPGHYYDQtkEKGEFVRYYNPNWHDFDhPIPTGEIDLEEIREALEAAVRKRLMGDV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 229 PYGVLLSGGLDSSLIAAIAARETEKANADanednnvdekqlagiddqghLHTSGWSRLHSFAIGLPNAPDLQAARKVAKF 308
Cdd:PTZ00077 239 PFGLFLSGGLDSSIVAAIVAKLIKNGEID--------------------LSKRGMPKLHSFCIGLEGSPDLKAARKVAEY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 309 IGSIHHEHTFTLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFAQAPSAAEF 388
Cdd:PTZ00077 299 LGTEHHEFTFTVEEGIDALPDVIYHTETYDVTTIRASTPMYLLSRRIKALGIKMVLSGEGSDELFGGYLYFHKAPNREEF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 389 HTESVQRVKNLHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIKPKEGRIEKYILRKAFDTTDepdvKPY 468
Cdd:PTZ00077 379 HRELVRKLHDLHKYDCLRANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFEGQMEKYILRKAFEGLE----KPY 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 469 LPEEILWRQKEQFSDGVGYSWIDGLRDTAERAISDAMFANPKADWGDDIPTTKEAYWYRLKFDAWFPQKTAADTV----- 543
Cdd:PTZ00077 455 LPDEILWRQKEQFSDGVGYSWIDGLKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTVpygps 534
|
570 580
....*....|....*....|....*.
gi 6321563 544 --------MRWIPKadWGCAEDPSGR 561
Cdd:PTZ00077 535 iacstekaLEWDES--FKKNTDESGR 558
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-567 |
0e+00 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 733.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 1 MCGIFAAFK-HEDIHNFKPKALQLSKKIRHRGPDWSGNAVMNSTIFVHERLAIVGLDSGAQPITSADGEYMLGVNGEIYN 79
Cdd:PLN02549 1 MCGILAVLGcSDDSQAKRSRVLELSRRLRHRGPDWSGLYGNEDCYLAHERLAIMDPESGDQPLYNEDKTIVVTANGEIYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 80 HIQLREMCSDYKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRSSQSpeTVYFA 159
Cdd:PLN02549 81 HKELREKLKLHKFRTGSDCEVIAHLYEEHGEEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDG--SVWFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 160 SELKCLTDVCDSIISFPPGHVYDSETDKITRYFTPDWLDEkRIPSTPVDYHAIRHSLEKAVRKRLMAEVPYGVLLSGGLD 239
Cdd:PLN02549 159 SEMKALCDDCERFEEFPPGHYYSSKAGGFRRWYNPPWFSE-SIPSTPYDPLVLREAFEKAVIKRLMTDVPFGVLLSGGLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 240 SSLIAAIAARETEKANAdanednnvdekqlagiddqghlhTSGW-SRLHSFAIGLPNAPDLQAARKVAKFIGSIHHEHTF 318
Cdd:PLN02549 238 SSLVASIAARHLAETKA-----------------------ARQWgQQLHSFCVGLEGSPDLKAAREVADYLGTVHHEFHF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 319 TLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFAQAPSAAEFHTESVQRVKN 398
Cdd:PLN02549 295 TVQEGIDAIEDVIYHLETYDVTTIRASTPMFLMSRKIKSLGVKMVLSGEGSDEIFGGYLYFHKAPNKEEFHKETCRKIKA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 399 LHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIKPKEGRIEKYILRKAFDTTDepdvKPYLPEEILWRQK 478
Cdd:PLN02549 375 LHQYDCLRANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMIRPGEGRIEKWVLRKAFDDEE----DPYLPKHILWRQK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 479 EQFSDGVGYSWIDGLRDTAERAISDAMFANPKADWGDDIPTTKEAYWYRLKFDAWFPQKTAADTV-------------MR 545
Cdd:PLN02549 451 EQFSDGVGYSWIDGLKAHAEKHVSDEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDAARLTVpggpsvacstakaVE 530
|
570 580
....*....|....*....|...
gi 6321563 546 WipKADWGCAEDPSGRYAK-IHE 567
Cdd:PLN02549 531 W--DAAWSKNLDPSGRAALgVHV 551
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-508 |
2.75e-153 |
|
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: 451.21 E-value: 2.75e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 1 MCGIFAAFkHEDIHNFKPKALQLSKKIRHRGPDWSGNAVMNSTIFVHERLAIVGLDS-GAQPITSADGEYMLGVNGEIYN 79
Cdd:COG0367 1 MCGIAGII-DFDGGADREVLERMLDALAHRGPDGSGIWVDGGVALGHRRLSIIDLSEgGHQPMVSEDGRYVLVFNGEIYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 80 HIQLRE--MCSDYKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGrssQSPETVY 157
Cdd:COG0367 80 YRELRAelEALGHRFRTHSDTEVILHAYEEWGEDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYA---EDGGGLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 158 FASELKCLTD---------------------------VCDSIISFPPGHVYDSETD---KITRYFTPDWLDEKRIPSTPV 207
Cdd:COG0367 157 FASELKALLAhpgvdreldpealaeyltlgyvpaprtIFKGIRKLPPGHYLTVDAGgelEIRRYWDLEFVPHERSDSEEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 208 DYHAIRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAARETEKanadanednnvdekqlagiddqghlhtsgwsRLH 287
Cdd:COG0367 237 AVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-------------------------------PLK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 288 SFAIGLPNAP--DLQAARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLEtyDVTTIRASTPMFLLSRKIKAQgVKMVLS 365
Cdd:COG0367 286 TFSIGFEDSAydESPYARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH-VKVVLS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 366 GEGSDEIFGGYLYFAQAPSAAE-------------------FHTESVQRVKNLHLA------DCLRANKSTMAWGLEARV 420
Cdd:COG0367 363 GEGADELFGGYPRYREAALLLSpdfaealggelvprlyaesGAEDPLRRMLYLDLKtylpgdLLVKVDRMSMAHSLEVRV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 421 PFLDKDFLQLCMNIDPNEKMikpkEGRIEKYILRKAFdttdepdvKPYLPEEILWRQKEQFSDGVGySWIDG-LRDTAER 499
Cdd:COG0367 443 PFLDHRLVEFALSLPPELKL----RGGRGKYLLRKAL--------EGLLPDEVLDRPKQGFPVPLG-PWLRGpLREWLED 509
|
....*....
gi 6321563 500 AISDAMFAN 508
Cdd:COG0367 510 LLSDESLAA 518
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-481 |
1.12e-148 |
|
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: 436.00 E-value: 1.12e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 4 IFAAFKH-EDIHNFKPKALQLSKKIRHRGPDWSGnaVMNST---IFVHERLAIVGLDSGAQPITSADGEYMLGVNGEIYN 79
Cdd:TIGR01536 1 IAGFFDLdDKAVEEDEAIKRMSDTIAHRGPDASG--IEYKDgnaILGHRRLAIIDLSGGAQPMSNEGKTYVIVFNGEIYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 80 HIQLREMCSD--YKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGrssQSPETVY 157
Cdd:TIGR01536 79 HEELREELEAkgYTFQTDSDTEVILHLYEEWGEECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYA---YDGGQLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 158 FASELKCLTDVCDsIISFPPGHVYDSETDKIT-------------------RYFTPDWLDEKRIPSTPVDYHA------- 211
Cdd:TIGR01536 156 FASEIKALLAHPN-IKPFPDGAALAPGFGFVRvpppstffrgvfelepghdLPLDDDGLNIERYYWERRDEHTdseedlv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 212 --IRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAARETEKanadanednnvdekqlagiddqghlhtsgwSRLHSF 289
Cdd:TIGR01536 235 deLRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR------------------------------GPVHTF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 290 AIGLPNAPDLQ---AARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLEtyDVTTIRASTPMFLLSRKIKAQGVKMVLSG 366
Cdd:TIGR01536 285 SIGFEGSPDFDeskYARKVADHLGTEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDGVKVVLSG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 367 EGSDEIFGGYLYFAQAPSAAEFHTESVQRVKNLHLADCLRAN-KSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMikpKE 445
Cdd:TIGR01536 363 EGADELFGGYLYFHEAPAAEALREELQYLDLELYMPGLLRRKdRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL---RD 439
|
490 500 510
....*....|....*....|....*....|....*.
gi 6321563 446 GrIEKYILRKAFdttdepdvKPYLPEEILWRQKEQF 481
Cdd:TIGR01536 440 G-KEKYLLREAF--------EGYLPEEILWRPKEGF 466
|
|
| Asn_synthase |
pfam00733 |
Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
211-547 |
5.56e-100 |
|
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: 304.15 E-value: 5.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 211 AIRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAARETEkanadanednnvdekqlagiddqghlhtsgwSRLHSFA 290
Cdd:pfam00733 1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSP-------------------------------SPLHTFS 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 291 IGLPNA--PDLQAARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLETydVTTIRASTPMFLLSRKIKAQGVKMVLSGEG 368
Cdd:pfam00733 50 IGFEGRgyDEAPYAREVAEHLGTDHHELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARRKGVKVVLSGEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 369 SDEIFGGYLYFaqaPSAAEFHTESVQRVKNLHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIkpkeGRI 448
Cdd:pfam00733 128 ADELFGGYPFY---KGEDPLRRMLYLDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKLR----GGI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 449 EKYILRKAFdttdepdvKPYLPEEILWRQKEQFSDGVGYSWIDG-LRDTAERAISDAmfanpkadwgddiPTTKEAYWYR 527
Cdd:pfam00733 201 EKYILREAL--------EGILPDEILERPKEGFSAPVGDWKLRGpLRELAEDLLSDS-------------RLAKEGLLDR 259
|
330 340
....*....|....*....|
gi 6321563 528 LKFDAWFPQKTAAdTVMRWI 547
Cdd:pfam00733 260 EAVRELLDEHLAG-MLELWL 278
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
226-485 |
1.23e-89 |
|
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: 275.69 E-value: 1.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 226 AEVPYGVLLSGGLDSSLIAAIAARETEKanadanednnvdekqlagiddqghlhtsgwSRLHSFAIGLPN--APDLQAAR 303
Cdd:cd01991 1 SDVPVGVLLSGGLDSSLIAALAARLLPE------------------------------TPIDLFTVGFEGspTPDRAAAR 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 304 KVAKFIGSIHHEHTFTLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQGVKMVLSGEGSDEIFGGYLYFAQAP 383
Cdd:cd01991 51 RVAEELGTEHHEVEVTIEELLDALPDVILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVLSGEGADELFGGYSRHRDAP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 384 SA--AEFHTESVQRVKNLHLADCLRANKSTMAWGLEARVPFLDKDFLQLCMNIDPNEKMIKPkeGRIEKYILRKAFdttd 461
Cdd:cd01991 131 LRgwEALEEELLRDLDRLWTRNLGRDDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIDPR--GGGEKYILREAA---- 204
|
250 260
....*....|....*....|....
gi 6321563 462 epdvKPYLPEEILWRQKEQFSDGV 485
Cdd:cd01991 205 ----RDLLPDEIAWRPKRAIQFGS 224
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-193 |
6.09e-72 |
|
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: 229.75 E-value: 6.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 2 CGIFAAFKHEDIHNFKPKALQLSKKIRHRGPDWSGNAVMNSTIFVHERLAIVGLDSGAQPITSADGEYMLGVNGEIYNHI 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERMLDALAHRGPDGSGIWIDEGVALGHRRLSIIDLSGGAQPMVSEDGRLVLVFNGEIYNYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 82 QLREMCSD--YKFQTFSDCEPIIPLYLEHDIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRssqSPETVYFA 159
Cdd:cd00712 81 ELRAELEAlgHRFRTHSDTEVILHLYEEWGEDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGR---DGGGLAFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321563 160 SELKCLTDVCDS---------------------------IISFPPGHVY--DSETDKITRYFT 193
Cdd:cd00712 158 SELKALLALPGVpreldeaalaeylafqyvpaprtifkgIRKLPPGHYLtvDPGGVEIRRYWD 220
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
47-167 |
1.53e-45 |
|
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: 156.52 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 47 HERLAIVGLDSGAQPIT-SADGEYMLGVNGEIYNHIQLREMCSD--YKFQTFSDCEPIIPLYLEHDI-DAPKYLDGMFAF 122
Cdd:pfam13537 1 HRRLSIIDLEGGAQPMVsSEDGRYVIVFNGEIYNYRELRAELEAkgYRFRTHSDTEVILHLYEAEWGeDCVDRLNGMFAF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6321563 123 CLYDSKKDRIVAARDPIGVVTLYMGRSSQSpeTVYFASELKCLTD 167
Cdd:pfam13537 81 AIWDRRRQRLFLARDRFGIKPLYYGRDDGG--RLLFASELKALLA 123
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-181 |
1.21e-41 |
|
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: 149.52 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 2 CGIFAAF-KHEDIHNFKPKALQLSKKIRHRGPDWSGNAVMN---------------------------STIFVHERLAIV 53
Cdd:cd00352 1 CGIFGIVgADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDgdglfvekragpvsdvaldlldeplksGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 54 GL--DSGAQPITSADGEYMLGVNGEIYNHIQLREMCSD--YKFQTFSDCEPIIPLYLEHD---------IDAPKYLDGMF 120
Cdd:cd00352 81 GLpsEANAQPFRSEDGRIALVHNGEIYNYRELREELEArgYRFEGESDSEVILHLLERLGregglfeavEDALKRLDGPF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321563 121 AFCLYDSKKDRIVAARDPIGVVTLYMGRSsqSPETVYFASELKCLTDVC-DSIISFPPGHVY 181
Cdd:cd00352 161 AFALWDGKPDRLFAARDRFGIRPLYYGIT--KDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
32-161 |
4.20e-33 |
|
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: 122.80 E-value: 4.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 32 PDWSGNAVMNSTIFVHERLAIVGL-DSGAQPITSADGEYMLGVNGEIYNHIQLREMCSD--YKFQTFSDCEPIIPLYLEH 108
Cdd:pfam13522 1 PDFSGIWVEGGVALGHVRLAIVDLpDAGNQPMLSRDGRLVLVHNGEIYNYGELREELADlgHAFRSRSDTEVLLALYEEW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 6321563 109 DIDAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGrssQSPETVYFASE 161
Cdd:pfam13522 81 GEDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYG---ILGGGFVFASE 130
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
1-181 |
6.26e-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: 67.31 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 1 MCGIFAA----FKHEDIHNFKPKALQLskkIRHRGPDWSGNAVMNSTI----FVHERLAIVGLDSGAQPITSADGEYMLG 72
Cdd:cd03766 1 MCGILCSvspsGPHINSSLLSEELLPN---LRNRGPDYLSTRQLSVTNwtllFTSSVLSLRGDHVTRQPLVDQSTGNVLQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 73 VNGEIYNHIQLREMCSD--YKFQTFSDCepiipLYLEHDI-DAPKYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRS 149
Cdd:cd03766 78 WNGELYNIDGVEDEENDteVIFELLANC-----SSESQDIlDVLSSIEGPFAFIYYDASENKLYFGRDCLGRRSLLYKLD 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 6321563 150 SQspetvyfASELkCLTDVCD--SIISF---PPGHVY 181
Cdd:cd03766 153 PN-------GFEL-SISSVSGssSGSGFqevLAGGIY 181
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-161 |
1.43e-08 |
|
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: 57.34 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 1 MCGIFAAFKHED--------IHnfkpkALQlskkirHRGPDWSGNAVMN-STIFVH---------------ERL----AI 52
Cdd:COG0034 7 ECGVFGIYGHEDvaqltyygLY-----ALQ------HRGQESAGIATSDgGRFHLHkgmglvsdvfdeedlERLkgniAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 53 -------VGlDSG---AQPIT--SADGEYMLGVNGEIYNHIQLREM--CSDYKFQTFSDCEPIIPL----YLEHDI---- 110
Cdd:COG0034 76 ghvrystTG-SSSlenAQPFYvnSPFGSIALAHNGNLTNAEELREEleEEGAIFQTTSDTEVILHLiareLTKEDLeeai 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6321563 111 -DAPKYLDGMFAFCLYDskKDRIVAARDPIGVVTLYMGRssqSPETVYFASE 161
Cdd:COG0034 155 kEALRRVKGAYSLVILT--GDGLIAARDPNGIRPLVLGK---LEDGYVVASE 201
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-161 |
2.31e-07 |
|
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: 52.08 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 2 CGIFAAFKHEDI--------HnfkpkALQlskkirHRGPDWSGNAVMNS-TIFVH------------ERLAIVGLDSG-- 58
Cdd:cd00715 1 CGVFGIYGAEDAarltylglY-----ALQ------HRGQESAGIATSDGkRFHTHkgmglvsdvfdeEKLRRLPGNIAig 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 59 --------------AQPI--TSADGEYMLGVNGEIYNHIQLREMC--SDYKFQTFSDCEPIIPL---YLEHD------ID 111
Cdd:cd00715 70 hvrystagssslenAQPFvvNSPLGGIALAHNGNLVNAKELREELeeEGRIFQTTSDSEVILHLiarSLAKDdlfeaiID 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6321563 112 APKYLDGMFAFCLYDskKDRIVAARDPIGVVTLYMGRssQSPETVYFASE 161
Cdd:cd00715 150 ALERVKGAYSLVIMT--ADGLIAVRDPHGIRPLVLGK--LEGDGYVVASE 195
|
|
| macrolact_Ik_Al |
NF033561 |
albusnodin/ikarugamycin family macrolactam cyclase; Members of this family show homology ... |
176-249 |
1.83e-06 |
|
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: 50.68 E-value: 1.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321563 176 PPGHVYDSETDKITRYFTPDWLDEKRIPSTPVdyHAIRHSLEKAVRKRLMAEVPYGVLLSGGLDSSLIAAIAAR 249
Cdd:NF033561 161 PPGHRLTLPADGGAPRTPWWWRPDPRPGPDAV--ARLRAALAAAVALRVDGAPPLSSDLSGGLDSTTLALLAAR 232
|
|
| Wali7 |
cd01910 |
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
114-185 |
7.43e-06 |
|
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: 47.30 E-value: 7.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321563 114 KYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRSSQSpeTVYFASELKCLTDVC-DSIISFPPGHVYDSET 185
Cdd:cd01910 123 KDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADG--SVVFSDDVELVKASCgKSFAPFPKGCFFHSEG 193
|
|
| DUF3700 |
pfam12481 |
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
114-185 |
2.52e-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: 45.82 E-value: 2.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321563 114 KYLDGMFAFCLYDSKKDRIVAARDPIGVVTLYMGRSSQSpeTVYFASELKCLTDVC-DSIISFPPGHVYDSET 185
Cdd:pfam12481 127 RDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWGIDADG--SLVFSDDIEIVKKGCgKSFAPFPKGCFFTSSG 197
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-161 |
3.79e-05 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 46.21 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 1 MCGIFAAFKHEDIHNFKPKALQlskKIRHRGPDWSGNAVMN-------------STIFVHERLAIVGLDSG--------- 58
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLH---ALQHRGQEGAGIVTVDgnrlqsitgnglvSDVFDESKLDQLPGDIAighvrysta 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321563 59 -------AQPITSAdgeYMLGV-----NGEIYNHIQLREMCSDYK--FQTFSDCEPIIPL--------YLEHDIDAPKYL 116
Cdd:PLN02440 78 gasslknVQPFVAN---YRFGSigvahNGNLVNYEELRAKLEENGsiFNTSSDTEVLLHLiaiskarpFFSRIVDACEKL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6321563 117 DGMFAfCLYDSKkDRIVAARDPIGVVTLYMGRssQSPETVYFASE 161
Cdd:PLN02440 155 KGAYS-MVFLTE-DKLVAVRDPHGFRPLVMGR--RSNGAVVFASE 195
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
209-249 |
8.86e-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: 39.06 E-value: 8.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6321563 209 YHAIRHSLEKAVRKRLMAEVpygVL-LSGGLDSSLIAAIAAR 249
Cdd:COG0171 270 YDALVLGLRDYVRKNGFKGV---VLgLSGGIDSALVAALAVD 308
|
|
| |
