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Conserved domains on  [gi|33469123|ref|NP_036185|]
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asparagine synthetase [glutamine-hydrolyzing] isoform a [Mus musculus]

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
1-560 0e+00

asparagine synthetase B; Provisional


The actual alignment was detected with superfamily member PRK09431:

Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 568.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    1 MCGIWALFGSD---DCLSVQCLSAMK-IAHRGPDAfrfENVNGYTNCCFGFHRLAVVDPLFGMQPIRVRKYPyLWLCYNG 76
Cdd:PRK09431   1 MCGIFGILDIKtdaDELRKKALEMSRlMRHRGPDW---SGIYASDNAILGHERLSIVDVNGGAQPLYNEDGT-HVLAVNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   77 EIYNHKALQQRFE--FEYQTNVDGEIILHLYDKGGIEkTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:PRK09431  77 EIYNHQELRAELGdkYAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  155 LAVCSEAKGLVslkhsttPFLK-VEPFLPGHYevldLKPngkvASVEMVKYhhCTDEPLHaiYDSVEklfpgfDLETVKN 233
Cdd:PRK09431 156 LYFASEMKALV-------PVCKtIKEFPPGHY----YWS----KDGEFVRY--YQRDWFD--YDAVK------DNVTDKN 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  234 NLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAA--------SLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVANY 305
Cdd:PRK09431 211 ELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADH 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  306 IGSEHHEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEK 385
Cdd:PRK09431 291 LGTVHHEIHFTVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNAKE 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  386 AEEESERLLKELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIPKNG-IEKHLLRETFEDcnLLPKEILW 464
Cdd:PRK09431 370 FHEETVRKLRALHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFEG--YLPESILW 447
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  465 RPKEAFSDGitsVKNSWFKILQDYVEHQVDDEMMSAASQKFPFNTPKTKEGYFYRQIFERHYPGRA--------DWLTHY 536
Cdd:PRK09431 448 RQKEQFSDG---VGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVACS 524
                        570       580       590
                 ....*....|....*....|....*....|
gi 33469123  537 WMP------KWINATDPSARTLTHYKSAAK 560
Cdd:PRK09431 525 SAKaiewdeAFKNMDDPSGRAVSGVHQSAY 554
 
Name Accession Description Interval E-value
asnB PRK09431
asparagine synthetase B; Provisional
1-560 0e+00

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 568.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    1 MCGIWALFGSD---DCLSVQCLSAMK-IAHRGPDAfrfENVNGYTNCCFGFHRLAVVDPLFGMQPIRVRKYPyLWLCYNG 76
Cdd:PRK09431   1 MCGIFGILDIKtdaDELRKKALEMSRlMRHRGPDW---SGIYASDNAILGHERLSIVDVNGGAQPLYNEDGT-HVLAVNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   77 EIYNHKALQQRFE--FEYQTNVDGEIILHLYDKGGIEkTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:PRK09431  77 EIYNHQELRAELGdkYAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  155 LAVCSEAKGLVslkhsttPFLK-VEPFLPGHYevldLKPngkvASVEMVKYhhCTDEPLHaiYDSVEklfpgfDLETVKN 233
Cdd:PRK09431 156 LYFASEMKALV-------PVCKtIKEFPPGHY----YWS----KDGEFVRY--YQRDWFD--YDAVK------DNVTDKN 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  234 NLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAA--------SLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVANY 305
Cdd:PRK09431 211 ELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADH 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  306 IGSEHHEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEK 385
Cdd:PRK09431 291 LGTVHHEIHFTVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNAKE 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  386 AEEESERLLKELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIPKNG-IEKHLLRETFEDcnLLPKEILW 464
Cdd:PRK09431 370 FHEETVRKLRALHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFEG--YLPESILW 447
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  465 RPKEAFSDGitsVKNSWFKILQDYVEHQVDDEMMSAASQKFPFNTPKTKEGYFYRQIFERHYPGRA--------DWLTHY 536
Cdd:PRK09431 448 RQKEQFSDG---VGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVACS 524
                        570       580       590
                 ....*....|....*....|....*....|
gi 33469123  537 WMP------KWINATDPSARTLTHYKSAAK 560
Cdd:PRK09431 525 SAKaiewdeAFKNMDDPSGRAVSGVHQSAY 554
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
4-470 0e+00

asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273676 [Multi-domain]  Cd Length: 466  Bit Score: 534.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123     4 IWALFGSDDCLSVQ---CLS-AMKIAHRGPDAFRFENvnGYTNCCFGFHRLAVVDPLFGMQPIRVRKyPYLWLCYNGEIY 79
Cdd:TIGR01536   1 IAGFFDLDDKAVEEdeaIKRmSDTIAHRGPDASGIEY--KDGNAILGHRRLAIIDLSGGAQPMSNEG-KTYVIVFNGEIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    80 NHKALQQRFE---FEYQTNVDGEIILHLYDKGGiEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMtEDGFLA 156
Cdd:TIGR01536  78 NHEELREELEakgYTFQTDSDTEVILHLYEEWG-EECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAY-DGGQLY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   157 VCSEAKGLVSLKhSTTPFLKVEPFLPGHYEVLDlkPNGKVASVEMVKYHHCTDEPLHAIYDSVEKL------FPGFDLET 230
Cdd:TIGR01536 156 FASEIKALLAHP-NIKPFPDGAALAPGFGFVRV--PPPSTFFRGVFELEPGHDLPLDDDGLNIERYywerrdEHTDSEED 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   231 VKNNLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEaqvqYPLQTFAIGMEDSPDLL---AARKVANYIG 307
Cdd:TIGR01536 233 LVDELRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR----GPVHTFSIGFEGSPDFDeskYARKVADHLG 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   308 SEHHEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNTdSVVIFSGEGSDELTQGYIYFHKAPSPEKAE 387
Cdd:TIGR01536 309 TEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDG-VKVVLSGEGADELFGGYLYFHEAPAAEALR 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   388 EESERLLKELYLFDVLRA-DRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIpKNGIEKHLLRETFEDcnLLPKEILWRP 466
Cdd:TIGR01536 386 EELQYLDLELYMPGLLRRkDRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL-RDGKEKYLLREAFEG--YLPEEILWRP 462

                  ....
gi 33469123   467 KEAF 470
Cdd:TIGR01536 463 KEGF 466
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
1-538 1.86e-132

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: 397.29  E-value: 1.86e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   1 MCGIWALFGSDDCLSVQCLSAM--KIAHRGPDAFRFEnVNGytNCCFGFHRLAVVDP-LFGMQPIRVRKYPYlWLCYNGE 77
Cdd:COG0367   1 MCGIAGIIDFDGGADREVLERMldALAHRGPDGSGIW-VDG--GVALGHRRLSIIDLsEGGHQPMVSEDGRY-VLVFNGE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  78 IYNHKALQQRFE---FEYQTNVDGEIILHLYDKGGiEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:COG0367  77 IYNYRELRAELEalgHRFRTHSDTEVILHAYEEWG-EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 155 lAVCSEAKGLVSLKH---------------------STTPFLKVEPFLPGHYevLDLKPNGKVasvEMVKYHHctdeplh 213
Cdd:COG0367 156 -AFASELKALLAHPGvdreldpealaeyltlgyvpaPRTIFKGIRKLPPGHY--LTVDAGGEL---EIRRYWD------- 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 214 aiYDSVEKLFPGfDLETVKNNLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEaqvqyPLQTFAIGMEDS 293
Cdd:COG0367 223 --LEFVPHERSD-SEEEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-----PLKTFSIGFEDS 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 294 P--DLLAARKVANYIGSEHHEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKntDSVVIFSGEGSDELT 371
Cdd:COG0367 295 AydESPYARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLARE--HVKVVLSGEGADELF 370
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 372 QGYIYFHKAP---SPEKAEEESERLLKEL--------------------YLFDVL--RADRTTAAHGLELRVPFLDHRFS 426
Cdd:COG0367 371 GGYPRYREAAlllSPDFAEALGGELVPRLyaesgaedplrrmlyldlktYLPGDLlvKVDRMSMAHSLEVRVPFLDHRLV 450
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 427 SYYLSLPPDMRIpKNGIEKHLLRETFEDcnLLPKEILWRPKEAFSDGItsvkNSWFK-ILQDYVEHQVDDEmmSAASQKF 505
Cdd:COG0367 451 EFALSLPPELKL-RGGRGKYLLRKALEG--LLPDEVLDRPKQGFPVPL----GPWLRgPLREWLEDLLSDE--SLAARGL 521
                       570       580       590
                ....*....|....*....|....*....|...
gi 33469123 506 pFNTpktkegYFYRQIFERHYPGRADWLTHYWM 538
Cdd:COG0367 522 -FDP------DAVRRLLEEHLAGRRDHSRKLWS 547
Asn_synthase pfam00733
Asparagine synthase; This family is always found associated with pfam00310. Members of this ...
234-538 2.23e-97

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: 297.22  E-value: 2.23e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   234 NLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEaqvqyPLQTFAIGME--DSPDLLAARKVANYIGSEHH 311
Cdd:pfam00733   1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPS-----PLHTFSIGFEgrGYDEAPYAREVAEHLGTDHH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   312 EVLFNSEEGIQALDEVIFSLETydITTVRASVGMYLISKYIRKnTDSVVIFSGEGSDELTQGYIyFHKAPSPekAEEESE 391
Cdd:pfam00733  76 ELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARR-KGVKVVLSGEGADELFGGYP-FYKGEDP--LRRMLY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   392 RLLKELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIpKNGIEKHLLRETFEDcnLLPKEILWRPKEAFS 471
Cdd:pfam00733 150 LDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKL-RGGIEKYILREALEG--ILPDEILERPKEGFS 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33469123   472 DGitsVKNSWFKI-LQDYVEHQVDDEmmsaasqkfpfntPKTKEGYFYRQIFERHYPGRADWLTHYWM 538
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 ...
249-473 4.77e-81

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: 252.97  E-value: 4.77e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 249 TDRRIGCLLSGGLDSSLVAAsLLKQLKEAQvqyPLQTFAIGMEDS--PDLLAARKVANYIGSEHHEVLFNSEEGIQALDE 326
Cdd:cd01991   1 SDVPVGVLLSGGLDSSLIAA-LAARLLPET---PIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEELLDALPD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 327 VIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIfSGEGSDELTQGYIYFHKAPS--PEKAEEESERLLKELYLFDVLR 404
Cdd:cd01991  77 VILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVL-SGEGADELFGGYSRHRDAPLrgWEALEEELLRDLDRLWTRNLGR 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 405 ADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRI-PKNGIEKHLLRETFEDcnLLPKEILWRPKEAFSDG 473
Cdd:cd01991 156 DDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIdPRGGGEKYILREAARD--LLPDEIAWRPKRAIQFG 223
 
Name Accession Description Interval E-value
asnB PRK09431
asparagine synthetase B; Provisional
1-560 0e+00

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 568.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    1 MCGIWALFGSD---DCLSVQCLSAMK-IAHRGPDAfrfENVNGYTNCCFGFHRLAVVDPLFGMQPIRVRKYPyLWLCYNG 76
Cdd:PRK09431   1 MCGIFGILDIKtdaDELRKKALEMSRlMRHRGPDW---SGIYASDNAILGHERLSIVDVNGGAQPLYNEDGT-HVLAVNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   77 EIYNHKALQQRFE--FEYQTNVDGEIILHLYDKGGIEkTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:PRK09431  77 EIYNHQELRAELGdkYAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEHGN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  155 LAVCSEAKGLVslkhsttPFLK-VEPFLPGHYevldLKPngkvASVEMVKYhhCTDEPLHaiYDSVEklfpgfDLETVKN 233
Cdd:PRK09431 156 LYFASEMKALV-------PVCKtIKEFPPGHY----YWS----KDGEFVRY--YQRDWFD--YDAVK------DNVTDKN 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  234 NLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAA--------SLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVANY 305
Cdd:PRK09431 211 ELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVADH 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  306 IGSEHHEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEK 385
Cdd:PRK09431 291 LGTVHHEIHFTVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNAKE 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  386 AEEESERLLKELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIPKNG-IEKHLLRETFEDcnLLPKEILW 464
Cdd:PRK09431 370 FHEETVRKLRALHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFEG--YLPESILW 447
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  465 RPKEAFSDGitsVKNSWFKILQDYVEHQVDDEMMSAASQKFPFNTPKTKEGYFYRQIFERHYPGRA--------DWLTHY 536
Cdd:PRK09431 448 RQKEQFSDG---VGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVACS 524
                        570       580       590
                 ....*....|....*....|....*....|
gi 33469123  537 WMP------KWINATDPSARTLTHYKSAAK 560
Cdd:PRK09431 525 SAKaiewdeAFKNMDDPSGRAVSGVHQSAY 554
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
4-470 0e+00

asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273676 [Multi-domain]  Cd Length: 466  Bit Score: 534.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123     4 IWALFGSDDCLSVQ---CLS-AMKIAHRGPDAFRFENvnGYTNCCFGFHRLAVVDPLFGMQPIRVRKyPYLWLCYNGEIY 79
Cdd:TIGR01536   1 IAGFFDLDDKAVEEdeaIKRmSDTIAHRGPDASGIEY--KDGNAILGHRRLAIIDLSGGAQPMSNEG-KTYVIVFNGEIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    80 NHKALQQRFE---FEYQTNVDGEIILHLYDKGGiEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMtEDGFLA 156
Cdd:TIGR01536  78 NHEELREELEakgYTFQTDSDTEVILHLYEEWG-EECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAY-DGGQLY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   157 VCSEAKGLVSLKhSTTPFLKVEPFLPGHYEVLDlkPNGKVASVEMVKYHHCTDEPLHAIYDSVEKL------FPGFDLET 230
Cdd:TIGR01536 156 FASEIKALLAHP-NIKPFPDGAALAPGFGFVRV--PPPSTFFRGVFELEPGHDLPLDDDGLNIERYywerrdEHTDSEED 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   231 VKNNLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEaqvqYPLQTFAIGMEDSPDLL---AARKVANYIG 307
Cdd:TIGR01536 233 LVDELRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR----GPVHTFSIGFEGSPDFDeskYARKVADHLG 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   308 SEHHEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNTdSVVIFSGEGSDELTQGYIYFHKAPSPEKAE 387
Cdd:TIGR01536 309 TEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDG-VKVVLSGEGADELFGGYLYFHEAPAAEALR 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   388 EESERLLKELYLFDVLRA-DRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIpKNGIEKHLLRETFEDcnLLPKEILWRP 466
Cdd:TIGR01536 386 EELQYLDLELYMPGLLRRkDRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL-RDGKEKYLLREAFEG--YLPEEILWRP 462

                  ....
gi 33469123   467 KEAF 470
Cdd:TIGR01536 463 KEGF 466
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
1-559 7.41e-164

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 478.49  E-value: 7.41e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    1 MCGIWALFGSDDCLS-----VQCLSAmKIAHRGPDAFRFEnvnGYTNCCFGFHRLAVVDPLFGMQPIRVRKYPYLwLCYN 75
Cdd:PLN02549   1 MCGILAVLGCSDDSQakrsrVLELSR-RLRHRGPDWSGLY---GNEDCYLAHERLAIMDPESGDQPLYNEDKTIV-VTAN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   76 GEIYNHKALQQRFE-FEYQTNVDGEIILHLYDKGGiEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:PLN02549  76 GEIYNHKELREKLKlHKFRTGSDCEVIAHLYEEHG-EEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  155 LAVCSEAKGLVSlkhsttPFLKVEPFLPGHYEVLdlKPNGkvasveMVKYHH---CTDEPLHAIYDSVEklfpgfdletv 231
Cdd:PLN02549 155 VWFASEMKALCD------DCERFEEFPPGHYYSS--KAGG------FRRWYNppwFSESIPSTPYDPLV----------- 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  232 knnLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEAQVQY----PLQTFAIGMEDSPDLLAARKVANYIG 307
Cdd:PLN02549 210 ---LREAFEKAVIKRLMTDVPFGVLLSGGLDSSLVASIAARHLAETKAARqwgqQLHSFCVGLEGSPDLKAAREVADYLG 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  308 SEHHEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIfSGEGSDELTQGYIYFHKAPSPEKAE 387
Cdd:PLN02549 287 TVHHEFHFTVQEGIDAIEDVIYHLETYDVTTIRASTPMFLMSRKIKSLGVKMVL-SGEGSDEIFGGYLYFHKAPNKEEFH 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  388 EESERLLKELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIPKNG---IEKHLLRETF--EDCNLLPKEI 462
Cdd:PLN02549 366 KETCRKIKALHQYDCLRANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMIRPGegrIEKWVLRKAFddEEDPYLPKHI 445
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  463 LWRPKEAFSDGitsVKNSWFKILQDYVEHQVDDEMMSAASQKFPFNTPKTKEGYFYRQIFERHYPGRADWLT-------- 534
Cdd:PLN02549 446 LWRQKEQFSDG---VGYSWIDGLKAHAEKHVSDEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDAARLTvpggpsva 522
                        570       580       590
                 ....*....|....*....|....*....|.
gi 33469123  535 ------HYWMPKWINATDPSARTLTHYKSAA 559
Cdd:PLN02549 523 cstakaVEWDAAWSKNLDPSGRAALGVHVAA 553
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
1-560 4.57e-158

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 463.80  E-value: 4.57e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    1 MCGIWALFGSDDCLS-----VQCLSAmKIAHRGPDAFR---FENVNGYTNCcFGFHRLAVVDPLFGMQPIRVRKYPyLWL 72
Cdd:PTZ00077   1 MCGILAIFNSKGERHelrrkALELSK-RLRHRGPDWSGiivLENSPGTYNI-LAHERLAIVDLSDGKQPLLDDDET-VAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   73 CYNGEIYNHKALQQRFE---FEYQTNVDGEIILHLYDKGGIEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAM 149
Cdd:PTZ00077  78 MQNGEIYNHWEIRPELEkegYKFSSNSDCEIIGHLYKEYGPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  150 TEDGFLAVCSEAKGLvslkhsTTPFLKVEPFLPGHYeVLDLKPNGkvasvEMVKYHHctdeplhAIYDSVEKLFPGFdlE 229
Cdd:PTZ00077 158 AKDGSIWFSSELKAL------HDQCVEVKQFPPGHY-YDQTKEKG-----EFVRYYN-------PNWHDFDHPIPTG--E 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  230 TVKNNLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEAQVQYP------LQTFAIGMEDSPDLLAARKVA 303
Cdd:PTZ00077 217 IDLEEIREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIVAKLIKNGEIDLSkrgmpkLHSFCIGLEGSPDLKAARKVA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  304 NYIGSEHHEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDSVVIFSGEGSDELTQGYIYFHKAPSP 383
Cdd:PTZ00077 297 EYLGTEHHEFTFTVEEGIDALPDVIYHTETYDVTTIRASTPMYLLSRRI-KALGIKMVLSGEGSDELFGGYLYFHKAPNR 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  384 EKAEEESERLLKELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIPKNG---IEKHLLRETFEDCN--LL 458
Cdd:PTZ00077 376 EEFHRELVRKLHDLHKYDCLRANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFegqMEKYILRKAFEGLEkpYL 455
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  459 PKEILWRPKEAFSDGitsVKNSWFKILQDYVEHQVDDEMMSAASQKFPFNTPKTKEGYFYRQIFERHYPGRADWLT-HY- 536
Cdd:PTZ00077 456 PDEILWRQKEQFSDG---VGYSWIDGLKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTvPYg 532
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 33469123  537 ------------WMPKWINATDPSART-LTHYKSAAK 560
Cdd:PTZ00077 533 psiacstekaleWDESFKKNTDESGRAvLSVHNDAKQ 569
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
1-538 1.86e-132

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: 397.29  E-value: 1.86e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   1 MCGIWALFGSDDCLSVQCLSAM--KIAHRGPDAFRFEnVNGytNCCFGFHRLAVVDP-LFGMQPIRVRKYPYlWLCYNGE 77
Cdd:COG0367   1 MCGIAGIIDFDGGADREVLERMldALAHRGPDGSGIW-VDG--GVALGHRRLSIIDLsEGGHQPMVSEDGRY-VLVFNGE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  78 IYNHKALQQRFE---FEYQTNVDGEIILHLYDKGGiEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:COG0367  77 IYNYRELRAELEalgHRFRTHSDTEVILHAYEEWG-EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 155 lAVCSEAKGLVSLKH---------------------STTPFLKVEPFLPGHYevLDLKPNGKVasvEMVKYHHctdeplh 213
Cdd:COG0367 156 -AFASELKALLAHPGvdreldpealaeyltlgyvpaPRTIFKGIRKLPPGHY--LTVDAGGEL---EIRRYWD------- 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 214 aiYDSVEKLFPGfDLETVKNNLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEaqvqyPLQTFAIGMEDS 293
Cdd:COG0367 223 --LEFVPHERSD-SEEEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-----PLKTFSIGFEDS 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 294 P--DLLAARKVANYIGSEHHEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKntDSVVIFSGEGSDELT 371
Cdd:COG0367 295 AydESPYARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLARE--HVKVVLSGEGADELF 370
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 372 QGYIYFHKAP---SPEKAEEESERLLKEL--------------------YLFDVL--RADRTTAAHGLELRVPFLDHRFS 426
Cdd:COG0367 371 GGYPRYREAAlllSPDFAEALGGELVPRLyaesgaedplrrmlyldlktYLPGDLlvKVDRMSMAHSLEVRVPFLDHRLV 450
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 427 SYYLSLPPDMRIpKNGIEKHLLRETFEDcnLLPKEILWRPKEAFSDGItsvkNSWFK-ILQDYVEHQVDDEmmSAASQKF 505
Cdd:COG0367 451 EFALSLPPELKL-RGGRGKYLLRKALEG--LLPDEVLDRPKQGFPVPL----GPWLRgPLREWLEDLLSDE--SLAARGL 521
                       570       580       590
                ....*....|....*....|....*....|...
gi 33469123 506 pFNTpktkegYFYRQIFERHYPGRADWLTHYWM 538
Cdd:COG0367 522 -FDP------DAVRRLLEEHLAGRRDHSRKLWS 547
Asn_synthase pfam00733
Asparagine synthase; This family is always found associated with pfam00310. Members of this ...
234-538 2.23e-97

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: 297.22  E-value: 2.23e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   234 NLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEaqvqyPLQTFAIGME--DSPDLLAARKVANYIGSEHH 311
Cdd:pfam00733   1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPS-----PLHTFSIGFEgrGYDEAPYAREVAEHLGTDHH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   312 EVLFNSEEGIQALDEVIFSLETydITTVRASVGMYLISKYIRKnTDSVVIFSGEGSDELTQGYIyFHKAPSPekAEEESE 391
Cdd:pfam00733  76 ELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARR-KGVKVVLSGEGADELFGGYP-FYKGEDP--LRRMLY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   392 RLLKELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIpKNGIEKHLLRETFEDcnLLPKEILWRPKEAFS 471
Cdd:pfam00733 150 LDLKTLLPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKL-RGGIEKYILREALEG--ILPDEILERPKEGFS 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33469123   472 DGitsVKNSWFKI-LQDYVEHQVDDEmmsaasqkfpfntPKTKEGYFYRQIFERHYPGRADWLTHYWM 538
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 ...
249-473 4.77e-81

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: 252.97  E-value: 4.77e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 249 TDRRIGCLLSGGLDSSLVAAsLLKQLKEAQvqyPLQTFAIGMEDS--PDLLAARKVANYIGSEHHEVLFNSEEGIQALDE 326
Cdd:cd01991   1 SDVPVGVLLSGGLDSSLIAA-LAARLLPET---PIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEELLDALPD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 327 VIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIfSGEGSDELTQGYIYFHKAPS--PEKAEEESERLLKELYLFDVLR 404
Cdd:cd01991  77 VILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVL-SGEGADELFGGYSRHRDAPLrgWEALEEELLRDLDRLWTRNLGR 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 405 ADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRI-PKNGIEKHLLRETFEDcnLLPKEILWRPKEAFSDG 473
Cdd:cd01991 156 DDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIdPRGGGEKYILREAARD--LLPDEIAWRPKRAIQFG 223
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
2-206 1.03e-60

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: 200.09  E-value: 1.03e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   2 CGIWALFGSD---DCLSVQCLSAMKIAHRGPDAFRFENVNGytnCCFGFHRLAVVDPLFGMQPIRVRKyPYLWLCYNGEI 78
Cdd:cd00712   1 CGIAGIIGLDgasVDRATLERMLDALAHRGPDGSGIWIDEG---VALGHRRLSIIDLSGGAQPMVSED-GRLVLVFNGEI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  79 YNHKALQQRFEFEY---QTNVDGEIILHLYDKGGiEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTeDGFL 155
Cdd:cd00712  77 YNYRELRAELEALGhrfRTHSDTEVILHLYEEWG-EDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRD-GGGL 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33469123 156 AVCSEAKGLVSLKHST---------------------TPFLKVEPFLPGHYEVLDLKPngkvasVEMVKYHH 206
Cdd:cd00712 155 AFASELKALLALPGVPreldeaalaeylafqyvpaprTIFKGIRKLPPGHYLTVDPGG------VEIRRYWD 220
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
2-185 1.61e-37

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: 137.97  E-value: 1.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   2 CGIWALFGSDDCLSVQCL----SAMKIAHRGPDAF------------------------RFENVNGYTNCCFGFHRLAVV 53
Cdd:cd00352   1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAgiavydgdglfvekragpvsdvalDLLDEPLKSGVALGHVRLATN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  54 DP--LFGMQPIRVRKYPYlWLCYNGEIYNHKALQQRFE---FEYQTNVDGEIILHLYDKGG--------IEKTICMLDGV 120
Cdd:cd00352  81 GLpsEANAQPFRSEDGRI-ALVHNGEIYNYRELREELEargYRFEGESDSEVILHLLERLGregglfeaVEDALKRLDGP 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33469123 121 FAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVSLkhsttPFLKVEPFLPGHY 185
Cdd:cd00352 160 FAFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLAL-----PFKGVRRLPPGEL 219
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
49-164 2.94e-32

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: 120.32  E-value: 2.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    49 RLAVVDPLFGMQPIRVRKYPYLWLCYNGEIYNHKALQQRFE---FEYQTNVDGEIILHLYDKGGIEKTICMLDGVFAFIL 125
Cdd:pfam13537   3 RLSIIDLEGGAQPMVSSEDGRYVIVFNGEIYNYRELRAELEakgYRFRTHSDTEVILHLYEAEWGEDCVDRLNGMFAFAI 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 33469123   126 LDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGL 164
Cdd:pfam13537  83 WDRRRQRLFLARDRFGIKPLYYGRDDGGRLLFASELKAL 121
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
29-155 5.13e-20

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: 86.21  E-value: 5.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    29 PDAFRFEnvngYTNCC-FGFHRLAVVD-PLFGMQPIRVRkYPYLWLCYNGEIYNHKALQQRFE---FEYQTNVDGEIILH 103
Cdd:pfam13522   1 PDFSGIW----VEGGVaLGHVRLAIVDlPDAGNQPMLSR-DGRLVLVHNGEIYNYGELREELAdlgHAFRSRSDTEVLLA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 33469123   104 LYDKGGiEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGFL 155
Cdd:pfam13522  76 LYEEWG-EDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFV 126
Gn_AT_II_novel cd03766
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ...
1-179 3.05e-18

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: 82.72  E-value: 3.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   1 MCGIWALFG--SDDCLSVQCLSAMK--IAHRGPDAFRFENVN-GYTNCCFGFHRLAVVDPLFGMQPIRVRKYPYLwLCYN 75
Cdd:cd03766   1 MCGILCSVSpsGPHINSSLLSEELLpnLRNRGPDYLSTRQLSvTNWTLLFTSSVLSLRGDHVTRQPLVDQSTGNV-LQWN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  76 GEIYNHKALqqrfefEYQTNvDGEIILHL-----YDKGGIEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPL-FKAM 149
Cdd:cd03766  80 GELYNIDGV------EDEEN-DTEVIFELlancsSESQDILDVLSSIEGPFAFIYYDASENKLYFGRDCLGRRSLlYKLD 152
                       170       180       190
                ....*....|....*....|....*....|
gi 33469123 150 TEDGFLAVCSeakglVSLKHSTTPFLKVEP 179
Cdd:cd03766 153 PNGFELSISS-----VSGSSSGSGFQEVLA 177
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
60-160 4.88e-09

Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439804 [Multi-domain]  Cd Length: 464  Bit Score: 58.50  E-value: 4.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  60 QPIrVRKYPYLW--LCYNGEIYNHKALQQRFE---FEYQTNVDGEIILHL----YDKGGIEKTIC----MLDGVFAFILL 126
Cdd:COG0034  92 QPF-YVNSPFGSiaLAHNGNLTNAEELREELEeegAIFQTTSDTEVILHLiareLTKEDLEEAIKealrRVKGAYSLVIL 170
                        90       100       110
                ....*....|....*....|....*....|....
gi 33469123 127 DtaNKKVFLGRDTYGVRPLFKAMTEDGFlAVCSE 160
Cdd:COG0034 171 T--GDGLIAARDPNGIRPLVLGKLEDGY-VVASE 201
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
56-164 3.13e-08

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 56.20  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   56 LFGMQPIRVR-KYPYLWLCYNGEIYNHKALQQRFEFE---YQTNVDGEIILHL---YDKGGIEK----TICMLDGVFAFI 124
Cdd:PRK05793  97 LDNAQPLVANyKLGSIAIAHNGNLVNADVIRELLEDGgriFQTSIDSEVILNLiarSAKKGLEKalvdAIQAIKGSYALV 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 33469123  125 LLdTANKkvFLG-RDTYGVRPLFKAMTEDGFLaVCSEAKGL 164
Cdd:PRK05793 177 IL-TEDK--LIGvRDPHGIRPLCLGKLGDDYI-LSSESCAL 213
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
60-160 8.26e-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: 50.54  E-value: 8.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123  60 QPIRVRkYP--YLWLCYNGEIYNHKALQQRFEFE---YQTNVDGEIILHL----YDKGGIEKTIC----MLDGVFAFILL 126
Cdd:cd00715  85 QPFVVN-SPlgGIALAHNGNLVNAKELREELEEEgriFQTTSDSEVILHLiarsLAKDDLFEAIIdaleRVKGAYSLVIM 163
                        90       100       110
                ....*....|....*....|....*....|....
gi 33469123 127 DtaNKKVFLGRDTYGVRPLFKAMTEDGFLAVCSE 160
Cdd:cd00715 164 T--ADGLIAVRDPHGIRPLVLGKLEGDGYVVASE 195
PLN02440 PLN02440
amidophosphoribosyltransferase
1-160 1.13e-05

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 48.14  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123    1 MCGIWALFGSDDCLSVQCLSAMKIAHRGPDA--------FRFENV--NGYTNCCFGFHRLAVVDPLFGMQPIR------- 63
Cdd:PLN02440   1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGagivtvdgNRLQSItgNGLVSDVFDESKLDQLPGDIAIGHVRystagas 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   64 --------VRKYPY--LWLCYNGEIYNHKALQQRFEFE---YQTNVDGEIILHLYDKG-------GIEKTICMLDGVFAF 123
Cdd:PLN02440  81 slknvqpfVANYRFgsIGVAHNGNLVNYEELRAKLEENgsiFNTSSDTEVLLHLIAISkarpffsRIVDACEKLKGAYSM 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33469123  124 ILLdtANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSE 160
Cdd:PLN02440 161 VFL--TEDKLVAVRDPHGFRPLVMGRRSNGAVVFASE 195
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
117-174 5.20e-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: 5.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123   117 LDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGFLaVCSEAKGLV--SLKHSTTPF 174
Cdd:pfam12481 129 LEGKFAFVLYDSSTSTVFVASDADGSVPLYWGIDADGSL-VFSDDIEIVkkGCGKSFAPF 187
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
117-174 1.30e-04

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: 43.45  E-value: 1.30e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33469123 117 LDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEA---KGlvSLKHSTTPF 174
Cdd:cd01910 125 LEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADGSVVFSDDVelvKA--SCGKSFAPF 183
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
255-313 2.67e-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: 42.60  E-value: 2.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 33469123   255 CLLSGGLDSSLVAASLLKQLKEAqvqYPLqTFAIGMEDSPDLLAARKVANYIGSEHHEV 313
Cdd:pfam06508   4 VLLSGGLDSTTCLAWAKKEGYEV---YAL-SFDYGQRHRKELECAKKIAKALGVEHKIL 58
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
252-328 9.16e-04

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: 40.65  E-value: 9.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 252 RIGCLLSGGLDSSlVAASLLKQLKEaQVQYPLQTFAI-------GMEDSpDLLAARKVANYIGSEHHEVLFNSEEGIqAL 324
Cdd:cd01713  20 RVAVGLSGGKDST-VLLYVLKELNK-RHDYGVELIAVtidegikGYRDD-SLEAARKLAEEYGIPLEIVSFEDEFGF-TL 95

                ....
gi 33469123 325 DEVI 328
Cdd:cd01713  96 DELI 99
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
255-314 1.23e-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: 40.53  E-value: 1.23e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33469123 255 CLLSGGLDSSLVAASLLKQLKEAqvqYPLqTFAIG----MEdspdLLAARKVANYIGSEHHEVL 314
Cdd:COG0603   7 VLLSGGLDSTTCLAWALARGYEV---YAL-SFDYGqrhrKE----LEAARRIAKALGVGEHKVI 62
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
252-318 1.29e-03

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 41.34  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469123 252 RIGCLLSGGLDSSlVAASLLKqlkEAQVQYplqtFAIGM-----EDSP--------DLLAARKVANYIGSEHHEVLFNSE 318
Cdd:cd01998   1 KVAVAMSGGVDSS-VAAALLK---EQGYDV----IGVFMknwddEDNEkggccseeDIEDARRVADQLGIPLYVVDFSEE 72
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
251-315 3.87e-03

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: 38.77  E-value: 3.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33469123   251 RRIGCLLSGGLDSSlVAASLLK----QLKEAQVQYPLQTFAIGMEDSP----DLLAARKVANYIGSEHHEVLF 315
Cdd:pfam03054   1 MKVVVAMSGGVDSS-VAAYLLKeqghNVIGVFMKNWDEEQSLDEEGKCcseeDLADAQRVCEQLGIPLYVVNF 72
 
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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