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Conserved domains on  [gi|296010852|ref|NP_001171548|]
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asparagine synthetase [glutamine-hydrolyzing] isoform c [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
asnB super family cl35830
asparagine synthetase B; Provisional
 7-472 6.93e-169

asparagine synthetase B; Provisional


The actual alignment was detected with superfamily member PRK09431:

Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 487.11  E-value: 6.93e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   7 FEYQTKVDGEIILHLYDKGGIEqTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVtlkh 86
Cdd:PRK09431  92 YAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEMKALV---- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  87 satPFLK-VEPFLPGHYevldLKPngkvASVEMVKYHHcRDVPLhalYDNVEklfpgfEIETVKNNLRILFNNAVKKRLM 165
Cdd:PRK09431 167 ---PVCKtIKEFPPGHY----YWS----KDGEFVRYYQ-RDWFD---YDAVK------DNVTDKNELRDALEAAVKKRLM 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 166 TDRRIGCLLSGGLDSSLVAA--------TLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEG 237
Cdd:PRK09431 226 SDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEG 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 238 IQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLF 317
Cdd:PRK09431 306 LDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMY 384

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 318 DVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNG-IEKHLLRETFEDsnLIPKEILWRPKEAFSDGitsVKN 396
Cdd:PRK09431 385 DCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFEG--YLPESILWRQKEQFSDG---VGY 459

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 397 SWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRA--------DWLSHYWMP------KWINAT 462
Cdd:PRK09431 460 SWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVACSSAKaiewdeAFKNMD 539

                        490
                 ....*....|
gi 296010852 463 DPSARTLTHY 472
Cdd:PRK09431 540 DPSGRAVSGV 549
 
Name Accession Description Interval E-value
asnB PRK09431
asparagine synthetase B; Provisional
 7-472 6.93e-169

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 487.11  E-value: 6.93e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   7 FEYQTKVDGEIILHLYDKGGIEqTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVtlkh 86
Cdd:PRK09431  92 YAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEMKALV---- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  87 satPFLK-VEPFLPGHYevldLKPngkvASVEMVKYHHcRDVPLhalYDNVEklfpgfEIETVKNNLRILFNNAVKKRLM 165
Cdd:PRK09431 167 ---PVCKtIKEFPPGHY----YWS----KDGEFVRYYQ-RDWFD---YDAVK------DNVTDKNELRDALEAAVKKRLM 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 166 TDRRIGCLLSGGLDSSLVAA--------TLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEG 237
Cdd:PRK09431 226 SDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEG 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 238 IQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLF 317
Cdd:PRK09431 306 LDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMY 384

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 318 DVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNG-IEKHLLRETFEDsnLIPKEILWRPKEAFSDGitsVKN 396
Cdd:PRK09431 385 DCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFEG--YLPESILWRQKEQFSDG---VGY 459

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 397 SWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRA--------DWLSHYWMP------KWINAT 462
Cdd:PRK09431 460 SWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVACSSAKaiewdeAFKNMD 539

                        490
                 ....*....|
gi 296010852 463 DPSARTLTHY 472
Cdd:PRK09431 540 DPSGRAVSGV 549
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
 1-387 7.93e-152

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: 440.62  E-value: 7.93e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852    1 MQQHFE---FEYQTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMtEDGFLAVCSE 77
Cdd:TIGR01536  82 LREELEakgYTFQTDSDTEVILHLYEEWG-EECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAY-DGGQLYFASE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   78 AKGLVTLKhSATPFLKVEPFLPGHYEVLDlkPNGKVASVEMVKYHHCRDVPLHALYDNVEKL------FPGFEIETVKNN 151
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFVRV--PPPSTFFRGVFELEPGHDLPLDDDGLNIERYywerrdEHTDSEEDLVDE 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  152 LRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqYPLQTFAIGMEDSPDLL---AARKVADHIGSEHY 228
Cdd:TIGR01536 237 LRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR----GPVHTFSIGFEGSPDFDeskYARKVADHLGTEHH 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  229 EVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNTdSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESE 308
Cdd:TIGR01536 313 EVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDG-VKVVLSGEGADELFGGYLYFHEAPAAEALREELQ 389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  309 RLLRELYLFDVLRA-DRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIpKNGIEKHLLRETFEDsnLIPKEILWRPKEAF 387
Cdd:TIGR01536 390 YLDLELYMPGLLRRkDRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL-RDGKEKYLLREAFEG--YLPEEILWRPKEGF 466
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 10-455 1.49e-103

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: 319.86  E-value: 1.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  10 QTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFlAVCSEAKGLVTLKH--- 86
Cdd:COG0367   95 RTHSDTEVILHAYEEWG-EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGL-AFASELKALLAHPGvdr 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  87 ------------------SATPFLKVEPFLPGHYevLDLKPNGKVasvEMVKYHHCRDVPLHALYDnveklfpgfeIETV 148
Cdd:COG0367  173 eldpealaeyltlgyvpaPRTIFKGIRKLPPGHY--LTVDAGGEL---EIRRYWDLEFVPHERSDS----------EEEA 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 149 KNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGMEDSP--DLLAARKVADHIGSE 226
Cdd:COG0367  238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-----PLKTFSIGFEDSAydESPYARAVAEHLGTE 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 227 HYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKntDSVVIFSGEGSDELTQGYIYFHKAP---SPEKA 303
Cdd:COG0367  313 HHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLARE--HVKVVLSGEGADELFGGYPRYREAAlllSPDFA 388

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 304 EEESERLLREL--------------------YLFDVL--RADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIpKNGIE 361
Cdd:COG0367  389 EALGGELVPRLyaesgaedplrrmlyldlktYLPGDLlvKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELKL-RGGRG 467

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 362 KHLLRETFEDsnLIPKEILWRPKEAFSDGItsvkNSWFK-ILQEYVEHQVDDAMManAAQKFpFNTpktkegYYYRQVFE 440
Cdd:COG0367  468 KYLLRKALEG--LLPDEVLDRPKQGFPVPL----GPWLRgPLREWLEDLLSDESL--AARGL-FDP------DAVRRLLE 532

                        490
                 ....*....|....*
gi 296010852 441 RHYPGRADWLSHYWM 455
Cdd:COG0367  533 EHLAGRRDHSRKLWS 547
Asn_synthase pfam00733
Asparagine synthase; This family is always found associated with pfam00310. Members of this ...
 151-455 1.25e-92

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: 282.20  E-value: 1.25e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  151 NLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGME--DSPDLLAARKVADHIGSEHY 228
Cdd:pfam00733   1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPS-----PLHTFSIGFEgrGYDEAPYAREVAEHLGTDHH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  229 EVLFNSEEGIQALDEVIFSLETydITTVRASVGMYLISKYIRKnTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESE 308
Cdd:pfam00733  76 ELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARR-KGVKVVLSGEGADELFGGYPFYKGEDPLRRMLYLDL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  309 RLLrelYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIpKNGIEKHLLRETFEDsnLIPKEILWRPKEAFS 388
Cdd:pfam00733 153 KTL---LPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKL-RGGIEKYILREALEG--ILPDEILERPKEGFS 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010852  389 DGitsVKNSWFKI-LQEYVEHQVDDAmmanaaqkfpfntPKTKEGYYYRQVFERHYPGRADWLSHYWM 455
Cdd:pfam00733 227 AP---VGDWKLRGpLRELAEDLLSDS-------------RLAKEGLLDREAVRELLDEHLAGMLELWL 278
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 166-390 1.03e-75

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: 236.79  E-value: 1.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 166 TDRRIGCLLSGGLDSSLVAATLLKQLKEAqvqyPLQTFAIGMEDS--PDLLAARKVADHIGSEHYEVLFNSEEGIQALDE 243
Cdd:cd01991    1 SDVPVGVLLSGGLDSSLIAALAARLLPET----PIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEELLDALPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 244 VIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIfSGEGSDELTQGYIYFHKAPSPEKAEEESERLLREL--YLFDVLR 321
Cdd:cd01991   77 VILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVL-SGEGADELFGGYSRHRDAPLRGWEALEEELLRDLDrlWTRNLGR 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 322 ADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRI-PKNGIEKHLLRETFEDsnLIPKEILWRPKEAFSDG 390
Cdd:cd01991  156 DDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIdPRGGGEKYILREAARD--LLPDEIAWRPKRAIQFG 223
 
Name Accession Description Interval E-value
asnB PRK09431
asparagine synthetase B; Provisional
 7-472 6.93e-169

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 487.11  E-value: 6.93e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   7 FEYQTKVDGEIILHLYDKGGIEqTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVtlkh 86
Cdd:PRK09431  92 YAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGNLYFASEMKALV---- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  87 satPFLK-VEPFLPGHYevldLKPngkvASVEMVKYHHcRDVPLhalYDNVEklfpgfEIETVKNNLRILFNNAVKKRLM 165
Cdd:PRK09431 167 ---PVCKtIKEFPPGHY----YWS----KDGEFVRYYQ-RDWFD---YDAVK------DNVTDKNELRDALEAAVKKRLM 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 166 TDRRIGCLLSGGLDSSLVAA--------TLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEG 237
Cdd:PRK09431 226 SDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADHLGTVHHEIHFTVQEG 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 238 IQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLF 317
Cdd:PRK09431 306 LDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNAKEFHEETVRKLRALHMY 384

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 318 DVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNG-IEKHLLRETFEDsnLIPKEILWRPKEAFSDGitsVKN 396
Cdd:PRK09431 385 DCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFEG--YLPESILWRQKEQFSDG---VGY 459

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 397 SWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRA--------DWLSHYWMP------KWINAT 462
Cdd:PRK09431 460 SWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVACSSAKaiewdeAFKNMD 539

                        490
                 ....*....|
gi 296010852 463 DPSARTLTHY 472
Cdd:PRK09431 540 DPSGRAVSGV 549
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
 1-387 7.93e-152

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: 440.62  E-value: 7.93e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852    1 MQQHFE---FEYQTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMtEDGFLAVCSE 77
Cdd:TIGR01536  82 LREELEakgYTFQTDSDTEVILHLYEEWG-EECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAY-DGGQLYFASE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   78 AKGLVTLKhSATPFLKVEPFLPGHYEVLDlkPNGKVASVEMVKYHHCRDVPLHALYDNVEKL------FPGFEIETVKNN 151
Cdd:TIGR01536 160 IKALLAHP-NIKPFPDGAALAPGFGFVRV--PPPSTFFRGVFELEPGHDLPLDDDGLNIERYywerrdEHTDSEEDLVDE 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  152 LRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqYPLQTFAIGMEDSPDLL---AARKVADHIGSEHY 228
Cdd:TIGR01536 237 LRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR----GPVHTFSIGFEGSPDFDeskYARKVADHLGTEHH 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  229 EVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNTdSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESE 308
Cdd:TIGR01536 313 EVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDG-VKVVLSGEGADELFGGYLYFHEAPAAEALREELQ 389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  309 RLLRELYLFDVLRA-DRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIpKNGIEKHLLRETFEDsnLIPKEILWRPKEAF 387
Cdd:TIGR01536 390 YLDLELYMPGLLRRkDRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL-RDGKEKYLLREAFEG--YLPEEILWRPKEGF 466
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
 8-478 2.57e-137

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 407.61  E-value: 2.57e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   8 EYQTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVtlKHS 87
Cdd:PLN02549  92 KFRTGSDCEVIAHLYEEHG-EEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGSVWFASEMKALC--DDC 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  88 AtpflKVEPFLPGHYEVLdlKPNGkvasveMVKYHHCR---DVPLHALYDNVEklfpgfeietvknnLRILFNNAVKKRL 164
Cdd:PLN02549 169 E----RFEEFPPGHYYSS--KAGG------FRRWYNPPwfsESIPSTPYDPLV--------------LREAFEKAVIKRL 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 165 MTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQY----PLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEGIQA 240
Cdd:PLN02549 223 MTDVPFGVLLSGGLDSSLVASIAARHLAETKAARqwgqQLHSFCVGLEGSPDLKAAREVADYLGTVHHEFHFTVQEGIDA 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 241 LDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIfSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVL 320
Cdd:PLN02549 303 IEDVIYHLETYDVTTIRASTPMFLMSRKIKSLGVKMVL-SGEGSDEIFGGYLYFHKAPNKEEFHKETCRKIKALHQYDCL 381

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 321 RADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNG---IEKHLLRETF--EDSNLIPKEILWRPKEAFSDGitsVK 395
Cdd:PLN02549 382 RANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMIRPGegrIEKWVLRKAFddEEDPYLPKHILWRQKEQFSDG---VG 458

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 396 NSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGR--------------ADWLSHYWMPKWINA 461
Cdd:PLN02549 459 YSWIDGLKAHAEKHVSDEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDaarltvpggpsvacSTAKAVEWDAAWSKN 538

                        490       500
                 ....*....|....*....|..
gi 296010852 462 TDPSARTLT--H---YKSAVKA 478
Cdd:PLN02549 539 LDPSGRAALgvHvaaYEEDVAA 560
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 6-477 2.94e-135

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 402.56  E-value: 2.94e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   6 EFEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLvtlk 85
Cdd:PTZ00077  97 GYKFSSNSDCEIIGHLYKEYGPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKAL---- 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  86 HSATpfLKVEPFLPGHYeVLDLKPNGkvasvEMVKYHHcrdvplhALYDNVEKLFPGFEIETVKnnLRILFNNAVKKRLM 165
Cdd:PTZ00077 173 HDQC--VEVKQFPPGHY-YDQTKEKG-----EFVRYYN-------PNWHDFDHPIPTGEIDLEE--IREALEAAVRKRLM 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 166 TDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYP------LQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEGIQ 239
Cdd:PTZ00077 236 GDVPFGLFLSGGLDSSIVAAIVAKLIKNGEIDLSkrgmpkLHSFCIGLEGSPDLKAARKVAEYLGTEHHEFTFTVEEGID 315

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 240 ALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDV 319
Cdd:PTZ00077 316 ALPDVIYHTETYDVTTIRASTPMYLLSRRI-KALGIKMVLSGEGSDELFGGYLYFHKAPNREEFHRELVRKLHDLHKYDC 394

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 320 LRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNG---IEKHLLRETFED--SNLIPKEILWRPKEAFSDGitsV 394
Cdd:PTZ00077 395 LRANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFegqMEKYILRKAFEGleKPYLPDEILWRQKEQFSDG---V 471

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 395 KNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLS-HY-------------WMPKWIN 460
Cdd:PTZ00077 472 GYSWIDGLKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTvPYgpsiacstekaleWDESFKK 551

                        490
                 ....*....|....*...
gi 296010852 461 ATDPSART-LTHYKSAVK 477
Cdd:PTZ00077 552 NTDESGRAvLSVHNDAKQ 569
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 10-455 1.49e-103

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: 319.86  E-value: 1.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  10 QTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFlAVCSEAKGLVTLKH--- 86
Cdd:COG0367   95 RTHSDTEVILHAYEEWG-EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGL-AFASELKALLAHPGvdr 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  87 ------------------SATPFLKVEPFLPGHYevLDLKPNGKVasvEMVKYHHCRDVPLHALYDnveklfpgfeIETV 148
Cdd:COG0367  173 eldpealaeyltlgyvpaPRTIFKGIRKLPPGHY--LTVDAGGEL---EIRRYWDLEFVPHERSDS----------EEEA 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 149 KNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGMEDSP--DLLAARKVADHIGSE 226
Cdd:COG0367  238 VEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-----PLKTFSIGFEDSAydESPYARAVAEHLGTE 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 227 HYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKntDSVVIFSGEGSDELTQGYIYFHKAP---SPEKA 303
Cdd:COG0367  313 HHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLARE--HVKVVLSGEGADELFGGYPRYREAAlllSPDFA 388

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 304 EEESERLLREL--------------------YLFDVL--RADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIpKNGIE 361
Cdd:COG0367  389 EALGGELVPRLyaesgaedplrrmlyldlktYLPGDLlvKVDRMSMAHSLEVRVPFLDHRLVEFALSLPPELKL-RGGRG 467

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 362 KHLLRETFEDsnLIPKEILWRPKEAFSDGItsvkNSWFK-ILQEYVEHQVDDAMManAAQKFpFNTpktkegYYYRQVFE 440
Cdd:COG0367  468 KYLLRKALEG--LLPDEVLDRPKQGFPVPL----GPWLRgPLREWLEDLLSDESL--AARGL-FDP------DAVRRLLE 532

                        490
                 ....*....|....*
gi 296010852 441 RHYPGRADWLSHYWM 455
Cdd:COG0367  533 EHLAGRRDHSRKLWS 547
Asn_synthase pfam00733
Asparagine synthase; This family is always found associated with pfam00310. Members of this ...
 151-455 1.25e-92

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: 282.20  E-value: 1.25e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  151 NLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGME--DSPDLLAARKVADHIGSEHY 228
Cdd:pfam00733   1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPS-----PLHTFSIGFEgrGYDEAPYAREVAEHLGTDHH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  229 EVLFNSEEGIQALDEVIFSLETydITTVRASVGMYLISKYIRKnTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESE 308
Cdd:pfam00733  76 ELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARR-KGVKVVLSGEGADELFGGYPFYKGEDPLRRMLYLDL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  309 RLLrelYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIpKNGIEKHLLRETFEDsnLIPKEILWRPKEAFS 388
Cdd:pfam00733 153 KTL---LPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKL-RGGIEKYILREALEG--ILPDEILERPKEGFS 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010852  389 DGitsVKNSWFKI-LQEYVEHQVDDAmmanaaqkfpfntPKTKEGYYYRQVFERHYPGRADWLSHYWM 455
Cdd:pfam00733 227 AP---VGDWKLRGpLRELAEDLLSDS-------------RLAKEGLLDREAVRELLDEHLAGMLELWL 278
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 166-390 1.03e-75

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: 236.79  E-value: 1.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 166 TDRRIGCLLSGGLDSSLVAATLLKQLKEAqvqyPLQTFAIGMEDS--PDLLAARKVADHIGSEHYEVLFNSEEGIQALDE 243
Cdd:cd01991    1 SDVPVGVLLSGGLDSSLIAALAARLLPET----PIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEELLDALPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 244 VIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIfSGEGSDELTQGYIYFHKAPSPEKAEEESERLLREL--YLFDVLR 321
Cdd:cd01991   77 VILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVL-SGEGADELFGGYSRHRDAPLRGWEALEEELLRDLDrlWTRNLGR 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 322 ADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRI-PKNGIEKHLLRETFEDsnLIPKEILWRPKEAFSDG 390
Cdd:cd01991  156 DDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIdPRGGGEKYILREAARD--LLPDEIAWRPKRAIQFG 223
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
 8-123 2.06e-26

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: 106.49  E-value: 2.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   8 EYQTKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTeDGFLAVCSEAKGLVTLKH- 86
Cdd:cd00712   92 RFRTHSDTEVILHLYEEWG-EDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRD-GGGLAFASELKALLALPGv 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296010852  87 --------------------SATPFLKVEPFLPGHYEVLDLKPngkvasVEMVKYHH 123
Cdd:cd00712  170 preldeaalaeylafqyvpaPRTIFKGIRKLPPGHYLTVDPGG------VEIRRYWD 220
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 5-102 2.08e-19

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: 86.73  E-value: 2.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   5 FEFEYQTkvDGEIILHLYDKGG--------IEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCS 76
Cdd:cd00352  121 YRFEGES--DSEVILHLLERLGregglfeaVEDALKRLDGPFAFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFAS 198

                         90       100
                 ....*....|....*....|....*.
gi 296010852  77 EAKGLVtlkhsATPFLKVEPFLPGHY 102
Cdd:cd00352  199 EPKALL-----ALPFKGVRRLPPGEL 219
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 10-81 7.10e-19

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: 82.18  E-value: 7.10e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296010852   10 QTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGL 81
Cdd:pfam13537  50 RTHSDTEVILHLYEAEWGEDCVDRLNGMFAFAIWDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKAL 121
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 11-72 2.40e-09

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: 55.39  E-value: 2.40e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296010852   11 TKVDGEIILHLYDKGGiEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFL 72
Cdd:pfam13522  66 SRSDTEVLLALYEEWG-EDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFV 126
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 9-84 5.44e-06

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 48.88  E-value: 5.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852   9 YQTKVDGEIILHL---YDKGGIEQ----TICMLDGVFAFVLLdTANKkvFLG-RDTYGVRPLFKAMTEDGFLaVCSEAKG 80
Cdd:PRK05793 137 FQTSIDSEVILNLiarSAKKGLEKalvdAIQAIKGSYALVIL-TEDK--LIGvRDPHGIRPLCLGKLGDDYI-LSSESCA 212


                 ....
gi 296010852  81 LVTL 84
Cdd:PRK05793 213 LDTI 216
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 10-77 1.75e-05

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: 46.94  E-value: 1.75e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296010852  10 QTKVDGEIILHL----YDKGGIEQTIC----MLDGVFAFVLLDtaNKKVFLGRDTYGVRPLFKAMTEDGFlAVCSE 77
Cdd:COG0034  129 QTTSDTEVILHLiareLTKEDLEEAIKealrRVKGAYSLVILT--GDGLIAARDPNGIRPLVLGKLEDGY-VVASE 201
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
 28-91 5.15e-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: 44.66  E-value: 5.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296010852   28 EQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLaVCSEAKGLVT--LKHSATPF 91
Cdd:pfam12481 123 DQVVRDLEGKFAFVLYDSSTSTVFVASDADGSVPLYWGIDADGSL-VFSDDIEIVKkgCGKSFAPF 187
Gn_AT_II_novel cd03766
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ...
 14-96 5.52e-05

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: 43.81  E-value: 5.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852  14 DGEIILHL-----YDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPL-FKAMTEDGFLAVCSeakglVTLKHS 87
Cdd:cd03766   94 DTEVIFELlancsSESQDILDVLSSIEGPFAFIYYDASENKLYFGRDCLGRRSLlYKLDPNGFELSISS-----VSGSSS 168


                 ....*....
gi 296010852  88 ATPFLKVEP 96
Cdd:cd03766  169 GSGFQEVLA 177
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
 28-78 7.56e-05

This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits.


Pssm-ID: 238891 [Multi-domain]  Cd Length: 224  Bit Score: 43.84  E-value: 7.56e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296010852  28 EQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEA 78
Cdd:cd01910  119 DQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADGSVVFSDDV 169
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 169-235 8.58e-05

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: 44.42  E-value: 8.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 169 RIGCLLSGGLDSSlVAATLLKqlkEAQVQYplqtFAIGM-----EDSP--------DLLAARKVADHIGSEHYEVLFNSE 235
Cdd:cd01998    1 KVAVAMSGGVDSS-VAAALLK---EQGYDV----IGVFMknwddEDNEkggccseeDIEDARRVADQLGIPLYVVDFSEE 72
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 172-230 2.45e-04

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: 42.22  E-value: 2.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 296010852  172 CLLSGGLDSSLVAATLLKQLKEAqvqYPLqTFAIGMEDSPDLLAARKVADHIGSEHYEV 230
Cdd:pfam06508   4 VLLSGGLDSTTCLAWAKKEGYEV---YAL-SFDYGQRHRKELECAKKIAKALGVEHKIL 58
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 168-232 9.74e-04

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 40.31  E-value: 9.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296010852  168 RRIGCLLSGGLDSSlVAATLLK----QLKEAQVQYPLQTFAIGMEDSP----DLLAARKVADHIGSEHYEVLF 232
Cdd:pfam03054   1 MKVVVAMSGGVDSS-VAAYLLKeqghNVIGVFMKNWDEEQSLDEEGKCcseeDLADAQRVCEQLGIPLYVVNF 72
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 174-230 1.71e-03

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 40.23  E-value: 1.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296010852 174 LSGGLDSSLVAATLLKQLKEAQVqyplqtFAIGM--EDSP--DLLAARKVADHIGSEHYEV 230
Cdd:cd00553   30 LSGGIDSAVVAALAVRALGAENV------LALIMpsRYSSkeTRDDAKALAENLGIEYRTI 84
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 169-235 2.69e-03

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 40.04  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 169 RIGCLLSGGLDSSlVAATLLKQlkeaqvqyplQ-------TFAIGMEDSP----------DLLAARKVADHIGSEHYEVL 231
Cdd:COG0482    2 RVVVGMSGGVDSS-VAAALLKE----------QgyevigvTMKLWDDDDAsgsggccsleDIEDARRVADKLGIPHYVVD 70


                 ....
gi 296010852 232 FNSE 235
Cdd:COG0482   71 FEEE 74
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 172-230 5.34e-03

7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440368 [Multi-domain]  Cd Length: 223  Bit Score: 38.22  E-value: 5.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296010852 172 CLLSGGLDSSLVAATLLKQLKEAqvqYPLqTFAIG----MEdspdLLAARKVADHIGS-EHYEV 230
Cdd:COG0603    7 VLLSGGLDSTTCLAWALARGYEV---YAL-SFDYGqrhrKE----LEAARRIAKALGVgEHKVI 62
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 169-245 8.34e-03

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 37.57  E-value: 8.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 169 RIGCLLSGGLDSSlVAATLLKQLKEaQVQYPLQTFAI-------GMEDSpDLLAARKVADHIGSEHYEVLFNSEEGIqAL 241
Cdd:cd01713   20 RVAVGLSGGKDST-VLLYVLKELNK-RHDYGVELIAVtidegikGYRDD-SLEAARKLAEEYGIPLEIVSFEDEFGF-TL 95


                 ....
gi 296010852 242 DEVI 245
Cdd:cd01713   96 DELI 99
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 174-264 8.40e-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: 38.67  E-value: 8.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010852 174 LSGGLDSSLVAATLLKQLKEAQVqyplqtFAIGM--EDSPD--LLAARKVADHIGSEHYEVlfNSEEGIQALDEVI---F 246
Cdd:COG0171  293 LSGGIDSALVAALAVDALGPENV------LGVTMpsRYTSDesLEDAEELAENLGIEYEEI--DITPAVEAFLEALphaF 364

                         90       100
                 ....*....|....*....|....
gi 296010852 247 SLETYDITT------VRASVGMYL 264
Cdd:COG0171  365 GGELDDVAEenlqarIRMVILMAL 388
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
 10-77 9.14e-03

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: 37.83  E-value: 9.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296010852  10 QTKVDGEIILHL----YDKGGIEQTIC----MLDGVFAFVLLDtaNKKVFLGRDTYGVRPLFKAMTEDGFLAVCSE 77
Cdd:cd00715  122 QTTSDSEVILHLiarsLAKDDLFEAIIdaleRVKGAYSLVIMT--ADGLIAVRDPHGIRPLVLGKLEGDGYVVASE 195
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 172-230 9.75e-03

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 37.59  E-value: 9.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296010852 172 CLLSGGLDSSLVAATLLKQLKEAqvqYPLqTFAIG-----MEDSpdllAARKVADHIGSEHYEV 230
Cdd:cd01995    5 VLLSGGLDSTTLLYWALKEGYEV---HAL-TFDYGqrhakEELE----AAKLIAKLLGIEHKVI 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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