|
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
|
|
| |
