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Conserved domains on  [gi|1622925213|ref|XP_001089182|]
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asparagine synthetase [glutamine-hydrolyzing] [Macaca mulatta]

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: 534.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   1 MCGIWALFGSD---DCLSVQCLSAMK-IAHRGPDAfrfENVNGYTNCCFGFHRLAVVDPLFGMQPI--RVKKypyLWLCY 74
Cdd:PRK09431    1 MCGIFGILDIKtdaDELRKKALEMSRlMRHRGPDW---SGIYASDNAILGHERLSIVDVNGGAQPLynEDGT---HVLAV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  75 NGEIYNYKKMQRHFE--FEYQTNVDGEIILHLYDKGGIEqTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTED 152
Cdd:PRK09431   75 NGEIYNHQELRAELGdkYAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEH 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 153 GFLAVCSEAKGLVtlkhsttPFLK-VEPFLPGHYevldLKPngkvASVEMVKYHHcRDEPLhalYDNVDklfpgfEIETV 231
Cdd:PRK09431  154 GNLYFASEMKALV-------PVCKtIKEFPPGHY----YWS----KDGEFVRYYQ-RDWFD---YDAVK------DNVTD 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 232 KNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAA--------TLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVA 303
Cdd:PRK09431  209 KNELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVA 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 304 NHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDNVVIFSGEGSDELTQGYIYFHKAPSP 383
Cdd:PRK09431  289 DHLGTVHHEIHFTVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNA 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 384 EEAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTPKNG-IEKHLLRETFEesNLIPKEI 462
Cdd:PRK09431  368 KEFHEETVRKLRALHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFE--GYLPESI 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 463 LWRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQIFERHYPGRA--------DWLS 534
Cdd:PRK09431  446 LWRQKEQFSDG---VGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVA 522
                         570       580       590
                  ....*....|....*....|....*....|..
gi 1622925213 535 HYWMP------KWINATDPSARTLTHYKSAAK 560
Cdd:PRK09431  523 CSSAKaiewdeAFKNMDDPSGRAVSGVHQSAY 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: 534.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   1 MCGIWALFGSD---DCLSVQCLSAMK-IAHRGPDAfrfENVNGYTNCCFGFHRLAVVDPLFGMQPI--RVKKypyLWLCY 74
Cdd:PRK09431    1 MCGIFGILDIKtdaDELRKKALEMSRlMRHRGPDW---SGIYASDNAILGHERLSIVDVNGGAQPLynEDGT---HVLAV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  75 NGEIYNYKKMQRHFE--FEYQTNVDGEIILHLYDKGGIEqTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTED 152
Cdd:PRK09431   75 NGEIYNHQELRAELGdkYAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEH 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 153 GFLAVCSEAKGLVtlkhsttPFLK-VEPFLPGHYevldLKPngkvASVEMVKYHHcRDEPLhalYDNVDklfpgfEIETV 231
Cdd:PRK09431  154 GNLYFASEMKALV-------PVCKtIKEFPPGHY----YWS----KDGEFVRYYQ-RDWFD---YDAVK------DNVTD 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 232 KNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAA--------TLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVA 303
Cdd:PRK09431  209 KNELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVA 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 304 NHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDNVVIFSGEGSDELTQGYIYFHKAPSP 383
Cdd:PRK09431  289 DHLGTVHHEIHFTVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNA 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 384 EEAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTPKNG-IEKHLLRETFEesNLIPKEI 462
Cdd:PRK09431  368 KEFHEETVRKLRALHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFE--GYLPESI 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 463 LWRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQIFERHYPGRA--------DWLS 534
Cdd:PRK09431  446 LWRQKEQFSDG---VGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVA 522
                         570       580       590
                  ....*....|....*....|....*....|..
gi 1622925213 535 HYWMP------KWINATDPSARTLTHYKSAAK 560
Cdd:PRK09431  523 CSSAKaiewdeAFKNMDDPSGRAVSGVHQSAY 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: 520.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   4 IWALFGSDDCLSVQ---CLS-AMKIAHRGPDAFRFENvnGYTNCCFGFHRLAVVDPLFGMQPIRVKKyPYLWLCYNGEIY 79
Cdd:TIGR01536   1 IAGFFDLDDKAVEEdeaIKRmSDTIAHRGPDASGIEY--KDGNAILGHRRLAIIDLSGGAQPMSNEG-KTYVIVFNGEIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  80 NYKKMQRHFE---FEYQTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMtEDGFLA 156
Cdd:TIGR01536  78 NHEELREELEakgYTFQTDSDTEVILHLYEEWG-EECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAY-DGGQLY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 157 VCSEAKGLVTLKhSTTPFLKVEPFLPGHYEVLDlkPNGKVASVEMVKYHHCRDEPLHALYDNVDKL------FPGFEIET 230
Cdd:TIGR01536 156 FASEIKALLAHP-NIKPFPDGAALAPGFGFVRV--PPPSTFFRGVFELEPGHDLPLDDDGLNIERYywerrdEHTDSEED 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 231 VKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqYPLQTFAIGMEDSPDLL---AARKVANHIG 307
Cdd:TIGR01536 233 LVDELRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR----GPVHTFSIGFEGSPDFDeskYARKVADHLG 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 308 SEHYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNTdNVVIFSGEGSDELTQGYIYFHKAPSPEEAE 387
Cdd:TIGR01536 309 TEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDG-VKVVLSGEGADELFGGYLYFHEAPAAEALR 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 388 EESERLLRELYLFDVLRA-DRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTpKNGIEKHLLRETFEEsnLIPKEILWRP 466
Cdd:TIGR01536 386 EELQYLDLELYMPGLLRRkDRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL-RDGKEKYLLREAFEG--YLPEEILWRP 462

                  ....
gi 1622925213 467 KEAF 470
Cdd:TIGR01536 463 KEGF 466
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
1-538 3.80e-127

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: 383.80  E-value: 3.80e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   1 MCGIWALFGSDDCLSVQCLSAM--KIAHRGPDAFRFEnVNGytNCCFGFHRLAVVDP-LFGMQPIRVKKYPYlWLCYNGE 77
Cdd:COG0367     1 MCGIAGIIDFDGGADREVLERMldALAHRGPDGSGIW-VDG--GVALGHRRLSIIDLsEGGHQPMVSEDGRY-VLVFNGE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  78 IYNYKK-----MQRHFEFeyQTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTED 152
Cdd:COG0367    77 IYNYRElraelEALGHRF--RTHSDTEVILHAYEEWG-EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 153 GFlAVCSEAKGLVTLKH---------------------STTPFLKVEPFLPGHYevLDLKPNGKVasvEMVKYHHCRDEP 211
Cdd:COG0367   154 GL-AFASELKALLAHPGvdreldpealaeyltlgyvpaPRTIFKGIRKLPPGHY--LTVDAGGEL---EIRRYWDLEFVP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 212 LHALYDnvdklfpgfeIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGME 291
Cdd:COG0367   228 HERSDS----------EEEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-----PLKTFSIGFE 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 292 DSP--DLLAARKVANHIGSEHYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNtdnV-VIFSGEGSD 368
Cdd:COG0367   293 DSAydESPYARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH---VkVVLSGEGAD 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 369 ELTQGYIYFHKAPSPEEAEEESERLLRE-----------------------LYLFDVL--RADRTTAAHGLELRVPFLDH 423
Cdd:COG0367   368 ELFGGYPRYREAALLLSPDFAEALGGELvprlyaesgaedplrrmlyldlkTYLPGDLlvKVDRMSMAHSLEVRVPFLDH 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 424 RFSSYYLSLPPEMRTpKNGIEKHLLRETFEesNLIPKEILWRPKEAFSDGItsvkNSWFK-ILQEYVEHQVDDAMManAA 502
Cdd:COG0367   448 RLVEFALSLPPELKL-RGGRGKYLLRKALE--GLLPDEVLDRPKQGFPVPL----GPWLRgPLREWLEDLLSDESL--AA 518
                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 1622925213 503 QKFpFNTpktkegYYYRQIFERHYPGRADWLSHYWM 538
Cdd:COG0367   519 RGL-FDP------DAVRRLLEEHLAGRRDHSRKLWS 547
Asn_synthase pfam00733
Asparagine synthase; This family is always found associated with pfam00310. Members of this ...
234-538 2.01e-89

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: 276.81  E-value: 2.01e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 234 NLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGME--DSPDLLAARKVANHIGSEHY 311
Cdd:pfam00733   1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPS-----PLHTFSIGFEgrGYDEAPYAREVAEHLGTDHH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 312 EVLFNSEEGIQALDEVIFSLETydITTVRASVGMYLISKYIRKnTDNVVIFSGEGSDELTQGYIYFHKAPSPEEAEEESE 391
Cdd:pfam00733  76 ELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARR-KGVKVVLSGEGADELFGGYPFYKGEDPLRRMLYLDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 392 RLLrelYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTpKNGIEKHLLRETFEesNLIPKEILWRPKEAFS 471
Cdd:pfam00733 153 KTL---LPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKL-RGGIEKYILREALE--GILPDEILERPKEGFS 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622925213 472 DGitsVKNSWFKI-LQEYVEHQVDDAmmanaaqkfpfntPKTKEGYYYRQIFERHYPGRADWLSHYWM 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 2.78e-72

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: 230.24  E-value: 2.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 249 TDRRIGCLLSGGLDSSLVAATLLKQLKEAqvqyPLQTFAIGMEDS--PDLLAARKVANHIGSEHYEVLFNSEEGIQALDE 326
Cdd:cd01991     1 SDVPVGVLLSGGLDSSLIAALAARLLPET----PIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEELLDALPD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 327 VIFSLETYDITTVRASVGMYLISKYIRKNTDNVVIfSGEGSDELTQGYIYFHKAPSPEEAEEESERLLREL--YLFDVLR 404
Cdd:cd01991    77 VILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVL-SGEGADELFGGYSRHRDAPLRGWEALEEELLRDLDrlWTRNLGR 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 405 ADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRT-PKNGIEKHLLRETFEesNLIPKEILWRPKEAFSDG 473
Cdd:cd01991   156 DDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIdPRGGGEKYILREAAR--DLLPDEIAWRPKRAIQFG 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: 534.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   1 MCGIWALFGSD---DCLSVQCLSAMK-IAHRGPDAfrfENVNGYTNCCFGFHRLAVVDPLFGMQPI--RVKKypyLWLCY 74
Cdd:PRK09431    1 MCGIFGILDIKtdaDELRKKALEMSRlMRHRGPDW---SGIYASDNAILGHERLSIVDVNGGAQPLynEDGT---HVLAV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  75 NGEIYNYKKMQRHFE--FEYQTNVDGEIILHLYDKGGIEqTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTED 152
Cdd:PRK09431   75 NGEIYNHQELRAELGdkYAFQTGSDCEVILALYQEKGPD-FLDDLDGMFAFALYDSEKDAYLIARDPIGIIPLYYGYDEH 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 153 GFLAVCSEAKGLVtlkhsttPFLK-VEPFLPGHYevldLKPngkvASVEMVKYHHcRDEPLhalYDNVDklfpgfEIETV 231
Cdd:PRK09431  154 GNLYFASEMKALV-------PVCKtIKEFPPGHY----YWS----KDGEFVRYYQ-RDWFD---YDAVK------DNVTD 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 232 KNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAA--------TLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVA 303
Cdd:PRK09431  209 KNELRDALEAAVKKRLMSDVPYGVLLSGGLDSSLISAiakkyaarRIEDDERSEAWWPQLHSFAVGLEGSPDLKAAREVA 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 304 NHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDNVVIFSGEGSDELTQGYIYFHKAPSP 383
Cdd:PRK09431  289 DHLGTVHHEIHFTVQEGLDALRDVIYHLETYDVTTIRASTPMYLMARKI-KAMGIKMVLSGEGADELFGGYLYFHKAPNA 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 384 EEAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTPKNG-IEKHLLRETFEesNLIPKEI 462
Cdd:PRK09431  368 KEFHEETVRKLRALHMYDCLRANKAMMAWGVEARVPFLDKEFLDVAMRINPEDKMCGNGkMEKHILREAFE--GYLPESI 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 463 LWRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQIFERHYPGRA--------DWLS 534
Cdd:PRK09431  446 LWRQKEQFSDG---VGYSWIDTLKEVAAEQVSDQQLATARFRFPYNTPTTKEAYLYREIFEELFPLPSaaecvpggPSVA 522
                         570       580       590
                  ....*....|....*....|....*....|..
gi 1622925213 535 HYWMP------KWINATDPSARTLTHYKSAAK 560
Cdd:PRK09431  523 CSSAKaiewdeAFKNMDDPSGRAVSGVHQSAY 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: 520.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   4 IWALFGSDDCLSVQ---CLS-AMKIAHRGPDAFRFENvnGYTNCCFGFHRLAVVDPLFGMQPIRVKKyPYLWLCYNGEIY 79
Cdd:TIGR01536   1 IAGFFDLDDKAVEEdeaIKRmSDTIAHRGPDASGIEY--KDGNAILGHRRLAIIDLSGGAQPMSNEG-KTYVIVFNGEIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  80 NYKKMQRHFE---FEYQTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMtEDGFLA 156
Cdd:TIGR01536  78 NHEELREELEakgYTFQTDSDTEVILHLYEEWG-EECVDRLDGMFAFALWDSEKGELFLARDRFGIKPLYYAY-DGGQLY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 157 VCSEAKGLVTLKhSTTPFLKVEPFLPGHYEVLDlkPNGKVASVEMVKYHHCRDEPLHALYDNVDKL------FPGFEIET 230
Cdd:TIGR01536 156 FASEIKALLAHP-NIKPFPDGAALAPGFGFVRV--PPPSTFFRGVFELEPGHDLPLDDDGLNIERYywerrdEHTDSEED 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 231 VKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqYPLQTFAIGMEDSPDLL---AARKVANHIG 307
Cdd:TIGR01536 233 LVDELRSLLEDAVKRRLVADVPVGVLLSGGLDSSLVAAIARREAPR----GPVHTFSIGFEGSPDFDeskYARKVADHLG 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 308 SEHYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNTdNVVIFSGEGSDELTQGYIYFHKAPSPEEAE 387
Cdd:TIGR01536 309 TEHHEVLFSVEEGLDALPEVIYHLE--EPTTIRASIPLYLLSKLAREDG-VKVVLSGEGADELFGGYLYFHEAPAAEALR 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 388 EESERLLRELYLFDVLRA-DRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTpKNGIEKHLLRETFEEsnLIPKEILWRP 466
Cdd:TIGR01536 386 EELQYLDLELYMPGLLRRkDRMSMAHSLEVRVPFLDHELVEYALSIPPEMKL-RDGKEKYLLREAFEG--YLPEEILWRP 462

                  ....
gi 1622925213 467 KEAF 470
Cdd:TIGR01536 463 KEGF 466
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
1-559 1.48e-153

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 452.30  E-value: 1.48e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   1 MCGIWALFGSDDCLS-----VQCLSAmKIAHRGPDAFRFEnvnGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLwLCYN 75
Cdd:PLN02549    1 MCGILAVLGCSDDSQakrsrVLELSR-RLRHRGPDWSGLY---GNEDCYLAHERLAIMDPESGDQPLYNEDKTIV-VTAN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  76 GEIYNYKKMQRHFE-FEYQTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGF 154
Cdd:PLN02549   76 GEIYNHKELREKLKlHKFRTGSDCEVIAHLYEEHG-EEFVDMLDGMFSFVLLDTRDNSFIAARDHIGITPLYIGWGLDGS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 155 LAVCSEAKGLVTlkhsttPFLKVEPFLPGHYEVLdlKPNGkvasveMVKYHhcrdEPlhalydnvdKLFPGFEIETVKN- 233
Cdd:PLN02549  155 VWFASEMKALCD------DCERFEEFPPGHYYSS--KAGG------FRRWY----NP---------PWFSESIPSTPYDp 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 234 -NLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQY----PLQTFAIGMEDSPDLLAARKVANHIGS 308
Cdd:PLN02549  208 lVLREAFEKAVIKRLMTDVPFGVLLSGGLDSSLVASIAARHLAETKAARqwgqQLHSFCVGLEGSPDLKAAREVADYLGT 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 309 EHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDNVVIfSGEGSDELTQGYIYFHKAPSPEEAEE 388
Cdd:PLN02549  288 VHHEFHFTVQEGIDAIEDVIYHLETYDVTTIRASTPMFLMSRKIKSLGVKMVL-SGEGSDEIFGGYLYFHKAPNKEEFHK 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 389 ESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTPKNG---IEKHLLRETF--EESNLIPKEIL 463
Cdd:PLN02549  367 ETCRKIKALHQYDCLRANKSTSAWGLEARVPFLDKEFIDVAMSIDPEWKMIRPGegrIEKWVLRKAFddEEDPYLPKHIL 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 464 WRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQIFERHYPGR-------------- 529
Cdd:PLN02549  447 WRQKEQFSDG---VGYSWIDGLKAHAEKHVSDEMFANASFRYPHNTPTTKEAYYYRMIFEKHFPQDaarltvpggpsvac 523
                         570       580       590
                  ....*....|....*....|....*....|
gi 1622925213 530 ADWLSHYWMPKWINATDPSARTLTHYKSAA 559
Cdd:PLN02549  524 STAKAVEWDAAWSKNLDPSGRAALGVHVAA 553
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
1-560 1.63e-150

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 444.54  E-value: 1.63e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   1 MCGIWALFGSDDCLS-----VQCLSAmKIAHRGPDAFR---FENVNGYTNCcFGFHRLAVVDPLFGMQPIRVKKYPyLWL 72
Cdd:PTZ00077    1 MCGILAIFNSKGERHelrrkALELSK-RLRHRGPDWSGiivLENSPGTYNI-LAHERLAIVDLSDGKQPLLDDDET-VAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  73 CYNGEIYNYKKMQRHFE---FEYQTNVDGEIILHLYDKGGIEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAM 149
Cdd:PTZ00077   78 MQNGEIYNHWEIRPELEkegYKFSSNSDCEIIGHLYKEYGPKDFWNHLDGMFATVIYDMKTNTFFAARDHIGIIPLYIGY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 150 TEDGFLAVCSEAKGLvtlkhsTTPFLKVEPFLPGHYeVLDLKPNGkvasvEMVKYHHcrdeplhALYDNVDKLFPGFEIE 229
Cdd:PTZ00077  158 AKDGSIWFSSELKAL------HDQCVEVKQFPPGHY-YDQTKEKG-----EFVRYYN-------PNWHDFDHPIPTGEID 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 230 TVKnnLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYP------LQTFAIGMEDSPDLLAARKVA 303
Cdd:PTZ00077  219 LEE--IREALEAAVRKRLMGDVPFGLFLSGGLDSSIVAAIVAKLIKNGEIDLSkrgmpkLHSFCIGLEGSPDLKAARKVA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 304 NHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIrKNTDNVVIFSGEGSDELTQGYIYFHKAPSP 383
Cdd:PTZ00077  297 EYLGTEHHEFTFTVEEGIDALPDVIYHTETYDVTTIRASTPMYLLSRRI-KALGIKMVLSGEGSDELFGGYLYFHKAPNR 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 384 EEAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTPKNG---IEKHLLRETFE--ESNLI 458
Cdd:PTZ00077  376 EEFHRELVRKLHDLHKYDCLRANKATMAWGIEARVPFLDKDFLEYVMNIDPKYKMCNAFegqMEKYILRKAFEglEKPYL 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 459 PKEILWRPKEAFSDGitsVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQIFERHYPGRADWLS-HY- 536
Cdd:PTZ00077  456 PDEILWRQKEQFSDG---VGYSWIDGLKEYAEKKISDQEFSQASFLFPYNTPRTKEAYLYRQIFSKHFPSDSAALTvPYg 532
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 1622925213 537 ------------WMPKWINATDPSART-LTHYKSAAK 560
Cdd:PTZ00077  533 psiacstekaleWDESFKKNTDESGRAvLSVHNDAKQ 569
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
1-538 3.80e-127

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: 383.80  E-value: 3.80e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   1 MCGIWALFGSDDCLSVQCLSAM--KIAHRGPDAFRFEnVNGytNCCFGFHRLAVVDP-LFGMQPIRVKKYPYlWLCYNGE 77
Cdd:COG0367     1 MCGIAGIIDFDGGADREVLERMldALAHRGPDGSGIW-VDG--GVALGHRRLSIIDLsEGGHQPMVSEDGRY-VLVFNGE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  78 IYNYKK-----MQRHFEFeyQTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTED 152
Cdd:COG0367    77 IYNYRElraelEALGHRF--RTHSDTEVILHAYEEWG-EDCLERLNGMFAFAIWDRRERRLFLARDRFGIKPLYYAEDGG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 153 GFlAVCSEAKGLVTLKH---------------------STTPFLKVEPFLPGHYevLDLKPNGKVasvEMVKYHHCRDEP 211
Cdd:COG0367   154 GL-AFASELKALLAHPGvdreldpealaeyltlgyvpaPRTIFKGIRKLPPGHY--LTVDAGGEL---EIRRYWDLEFVP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 212 LHALYDnvdklfpgfeIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGME 291
Cdd:COG0367   228 HERSDS----------EEEAVEELRELLEDAVRRRLRADVPVGAFLSGGLDSSAIAALAARLSKG-----PLKTFSIGFE 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 292 DSP--DLLAARKVANHIGSEHYEVLFNSEEGIQALDEVIFSLEtyDITTVRASVGMYLISKYIRKNtdnV-VIFSGEGSD 368
Cdd:COG0367   293 DSAydESPYARAVAEHLGTEHHEVTVTPEDLLDALPDLVWHLD--EPFADPSAVPTYLLSRLAREH---VkVVLSGEGAD 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 369 ELTQGYIYFHKAPSPEEAEEESERLLRE-----------------------LYLFDVL--RADRTTAAHGLELRVPFLDH 423
Cdd:COG0367   368 ELFGGYPRYREAALLLSPDFAEALGGELvprlyaesgaedplrrmlyldlkTYLPGDLlvKVDRMSMAHSLEVRVPFLDH 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 424 RFSSYYLSLPPEMRTpKNGIEKHLLRETFEesNLIPKEILWRPKEAFSDGItsvkNSWFK-ILQEYVEHQVDDAMManAA 502
Cdd:COG0367   448 RLVEFALSLPPELKL-RGGRGKYLLRKALE--GLLPDEVLDRPKQGFPVPL----GPWLRgPLREWLEDLLSDESL--AA 518
                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 1622925213 503 QKFpFNTpktkegYYYRQIFERHYPGRADWLSHYWM 538
Cdd:COG0367   519 RGL-FDP------DAVRRLLEEHLAGRRDHSRKLWS 547
Asn_synthase pfam00733
Asparagine synthase; This family is always found associated with pfam00310. Members of this ...
234-538 2.01e-89

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: 276.81  E-value: 2.01e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 234 NLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEaqvqyPLQTFAIGME--DSPDLLAARKVANHIGSEHY 311
Cdd:pfam00733   1 ELRELLEDAVARRLRADVPVGAFLSGGLDSSSIAALAARQSPS-----PLHTFSIGFEgrGYDEAPYAREVAEHLGTDHH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 312 EVLFNSEEGIQALDEVIFSLETydITTVRASVGMYLISKYIRKnTDNVVIFSGEGSDELTQGYIYFHKAPSPEEAEEESE 391
Cdd:pfam00733  76 ELVVTPEDLLDALPDVIWHLDE--PFADPSAIPLYLLSRLARR-KGVKVVLSGEGADELFGGYPFYKGEDPLRRMLYLDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 392 RLLrelYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRTpKNGIEKHLLRETFEesNLIPKEILWRPKEAFS 471
Cdd:pfam00733 153 KTL---LPGDLLRADRMSMAHGLEVRVPFLDHRLVEYALRLPPELKL-RGGIEKYILREALE--GILPDEILERPKEGFS 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622925213 472 DGitsVKNSWFKI-LQEYVEHQVDDAmmanaaqkfpfntPKTKEGYYYRQIFERHYPGRADWLSHYWM 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 2.78e-72

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: 230.24  E-value: 2.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 249 TDRRIGCLLSGGLDSSLVAATLLKQLKEAqvqyPLQTFAIGMEDS--PDLLAARKVANHIGSEHYEVLFNSEEGIQALDE 326
Cdd:cd01991     1 SDVPVGVLLSGGLDSSLIAALAARLLPET----PIDLFTVGFEGSptPDRAAARRVAEELGTEHHEVEVTIEELLDALPD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 327 VIFSLETYDITTVRASVGMYLISKYIRKNTDNVVIfSGEGSDELTQGYIYFHKAPSPEEAEEESERLLREL--YLFDVLR 404
Cdd:cd01991    77 VILIYPTDTPMDLSIAIPLYFASRLAGKLGAKVVL-SGEGADELFGGYSRHRDAPLRGWEALEEELLRDLDrlWTRNLGR 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 405 ADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRT-PKNGIEKHLLRETFEesNLIPKEILWRPKEAFSDG 473
Cdd:cd01991   156 DDRVAMAHGLEARVPFLDEELVEFALSLPPSLKIdPRGGGEKYILREAAR--DLLPDEIAWRPKRAIQFG 223
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
2-206 6.18e-61

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: 200.48  E-value: 6.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   2 CGIWALFGSD---DCLSVQCLSAMKIAHRGPDAFRFENVNGytnCCFGFHRLAVVDPLFGMQPIRVKKyPYLWLCYNGEI 78
Cdd:cd00712     1 CGIAGIIGLDgasVDRATLERMLDALAHRGPDGSGIWIDEG---VALGHRRLSIIDLSGGAQPMVSED-GRLVLVFNGEI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  79 YNYKKMQRHFEFEY---QTNVDGEIILHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTeDGFL 155
Cdd:cd00712    77 YNYRELRAELEALGhrfRTHSDTEVILHLYEEWG-EDCLERLNGMFAFALWDKRKRRLFLARDRFGIKPLYYGRD-GGGL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622925213 156 AVCSEAKGLVTLKHST---------------------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 1.44e-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: 138.35  E-value: 1.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   2 CGIWALFGSDDCLSVQCL----SAMKIAHRGPDAF------------------------RFENVNGYTNCCFGFHRLAVV 53
Cdd:cd00352     1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAgiavydgdglfvekragpvsdvalDLLDEPLKSGVALGHVRLATN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  54 DP--LFGMQPIRVKKYPYlWLCYNGEIYNYKKMQRHFE---FEYQTNVDGEIILHLYDKGG--------IEQTVCMLDGV 120
Cdd:cd00352    81 GLpsEANAQPFRSEDGRI-ALVHNGEIYNYRELREELEargYRFEGESDSEVILHLLERLGregglfeaVEDALKRLDGP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622925213 121 FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLkhsttPFLKVEPFLPGHY 185
Cdd:cd00352   160 FAFALWDGKPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLAL-----PFKGVRRLPPGEL 219
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
49-164 1.21e-31

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: 118.39  E-value: 1.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  49 RLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNYKKMQRHFE---FEYQTNVDGEIILHLYDKGGIEQTVCMLDGVFAFVL 125
Cdd:pfam13537   3 RLSIIDLEGGAQPMVSSEDGRYVIVFNGEIYNYRELRAELEakgYRFRTHSDTEVILHLYEAEWGEDCVDRLNGMFAFAI 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622925213 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 1.52e-18

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: 81.97  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  29 PDAFRFEnvngYTNCC-FGFHRLAVVD-PLFGMQPIRVkkyPY--LWLCYNGEIYNYKKMQRHFE---FEYQTNVDGEII 101
Cdd:pfam13522   1 PDFSGIW----VEGGVaLGHVRLAIVDlPDAGNQPMLS---RDgrLVLVHNGEIYNYGELREELAdlgHAFRSRSDTEVL 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622925213 102 LHLYDKGGiEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFL 155
Cdd:pfam13522  74 LALYEEWG-EDCLERLRGMFAFAIWDRRRRTLFLARDRLGIKPLYYGILGGGFV 126
Gn_AT_II_novel cd03766
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ...
1-179 1.61e-17

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: 80.41  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   1 MCGIWALFG--SDDCLSVQCLSAMK--IAHRGPDAFRFENVN-GYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLwLCYN 75
Cdd:cd03766     1 MCGILCSVSpsGPHINSSLLSEELLpnLRNRGPDYLSTRQLSvTNWTLLFTSSVLSLRGDHVTRQPLVDQSTGNV-LQWN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  76 GEIYNYKKMqrhfefEYQTNvDGEIILHL-----YDKGGIEQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPL-FKAM 149
Cdd:cd03766    80 GELYNIDGV------EDEEN-DTEVIFELlancsSESQDILDVLSSIEGPFAFIYYDASENKLYFGRDCLGRRSLlYKLD 152
                         170       180       190
                  ....*....|....*....|....*....|
gi 1622925213 150 TEDGFLAVCSeakglVTLKHSTTPFLKVEP 179
Cdd:cd03766   153 PNGFELSISS-----VSGSSSGSGFQEVLA 177
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
60-160 1.90e-08

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


Pssm-ID: 439804 [Multi-domain]  Cd Length: 464  Bit Score: 56.95  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  60 QPIRVKkYPYLW--LCYNGEIYNYKKMQRHFE---FEYQTNVDGEIILHL----YDKGGIEQTVC----MLDGVFAFVLL 126
Cdd:COG0034    92 QPFYVN-SPFGSiaLAHNGNLTNAEELREELEeegAIFQTTSDTEVILHLiareLTKEDLEEAIKealrRVKGAYSLVIL 170
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622925213 127 DtaNKKVFLGRDTYGVRPLFKAMTEDGFlAVCSE 160
Cdd:COG0034   171 T--GDGLIAARDPNGIRPLVLGKLEDGY-VVASE 201
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
56-167 7.98e-08

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 55.04  E-value: 7.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  56 LFGMQPIRVK-KYPYLWLCYNGEIYNYKKMQRHFEFE---YQTNVDGEIILHL---YDKGGIEQTV--CMLD--GVFAFV 124
Cdd:PRK05793   97 LDNAQPLVANyKLGSIAIAHNGNLVNADVIRELLEDGgriFQTSIDSEVILNLiarSAKKGLEKALvdAIQAikGSYALV 176
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622925213 125 LLdTANKkvFLG-RDTYGVRPLFKAMTEDGFLaVCSEAKGLVTL 167
Cdd:PRK05793  177 IL-TEDK--LIGvRDPHGIRPLCLGKLGDDYI-LSSESCALDTI 216
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
60-160 1.63e-06

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: 49.77  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  60 QPIRVKkYP--YLWLCYNGEIYNYKKMQ-------RHFefeyQTNVDGEIILHL----YDKG----GIEQTVCMLDGVFA 122
Cdd:cd00715    85 QPFVVN-SPlgGIALAHNGNLVNAKELReeleeegRIF----QTTSDSEVILHLiarsLAKDdlfeAIIDALERVKGAYS 159
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622925213 123 FVLLDtaNKKVFLGRDTYGVRPLFKAMTEDGFLAVCSE 160
Cdd:cd00715   160 LVIMT--ADGLIAVRDPHGIRPLVLGKLEGDGYVVASE 195
PLN02440 PLN02440
amidophosphoribosyltransferase
1-160 9.20e-06

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 48.14  E-value: 9.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213   1 MCGIWALFGSDDCLSVQCLSAMKIAHRGPDA--------FRFENV--NGYTNCCFGFHRLAVVDPLFGMQPIR------- 63
Cdd:PLN02440    1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGagivtvdgNRLQSItgNGLVSDVFDESKLDQLPGDIAIGHVRystagas 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  64 --------VKKYPY--LWLCYNGEIYNYKKMQ-------RHFefeyQTNVDGEIILHLYDKG-------GIEQTVCMLDG 119
Cdd:PLN02440   81 slknvqpfVANYRFgsIGVAHNGNLVNYEELRakleengSIF----NTSSDTEVLLHLIAISkarpffsRIVDACEKLKG 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622925213 120 VFAFVLLdtANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSE 160
Cdd:PLN02440  157 AYSMVFL--TEDKLVAVRDPHGFRPLVMGRRSNGAVVFASE 195
DUF3700 pfam12481
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ...
48-174 2.24e-05

Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains.


Pssm-ID: 403619 [Multi-domain]  Cd Length: 228  Bit Score: 45.82  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213  48 HRL-AVVDPLFGMqpirvkkypylwlcYNGEIYNYKKMQRHFEFEYQTNvdgEIIL------HLYDKG--GIEQTVCMLD 118
Cdd:pfam12481  68 PRLfAVVDDIFCL--------------FQGHLENLASLKQQYGLSKGAN---EAMIvieayrTLRDRGpyPADQVVRDLE 130
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622925213 119 GVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLaVCSEAKGLVT--LKHSTTPF 174
Cdd:pfam12481 131 GKFAFVLYDSSTSTVFVASDADGSVPLYWGIDADGSL-VFSDDIEIVKkgCGKSFAPF 187
Wali7 cd01910
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ...
111-161 4.24e-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: 44.99  E-value: 4.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622925213 111 EQTVCMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEA 161
Cdd:cd01910   119 DQVVKDLEGSFAFVLYDKKTSTVFVASDADGSVPLYWGIAADGSVVFSDDV 169
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
252-318 2.26e-04

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: 43.65  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622925213 252 RIGCLLSGGLDSSlVAATLLKqlkEAQVQYplqtFAIGM-----EDSP--------DLLAARKVANHIGSEHYEVLFNSE 318
Cdd:cd01998     1 KVAVAMSGGVDSS-VAAALLK---EQGYDV----IGVFMknwddEDNEkggccseeDIEDARRVADQLGIPLYVVDFSEE 72
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
255-313 6.21e-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: 41.45  E-value: 6.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622925213 255 CLLSGGLDSSLVAATLLKQLKEAqvqYPLqTFAIGMEDSPDLLAARKVANHIGSEHYEV 313
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 ...
251-315 1.27e-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: 40.31  E-value: 1.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622925213 251 RRIGCLLSGGLDSSlVAATLLK----QLKEAQVQYPLQTFAIGMEDSP----DLLAARKVANHIGSEHYEVLF 315
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 ...
257-313 2.11e-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: 2.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622925213 257 LSGGLDSSLVAATLLKQLKEAQVqyplqtFAIGM--EDSP--DLLAARKVANHIGSEHYEV 313
Cdd:cd00553    30 LSGGIDSAVVAALAVRALGAENV------LALIMpsRYSSkeTRDDAKALAENLGIEYRTI 84
 
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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