|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
1-299 |
5.79e-151 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 424.91 E-value: 5.79e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 1 MRIGVIMGGVSSEKQVSIMTGNEMIAHLDKNKYEIVPI-TLNEKMDLIEKAKdIDFALLALHGKYGEDGTVQGTLESLGI 79
Cdd:PRK01372 5 GKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPIdPGEDIAAQLKELG-FDRVFNALHGRGGEDGTIQGLLELLGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 80 PYSGSNMLSSGICMDKNISKKILRYEGVETPDWIELTKMADLKLDDLDKlGFPLVVKPNSGGSSVGVKIVNDKNELISML 159
Cdd:PRK01372 84 PYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKL-GLPLVVKPAREGSSVGVSKVKEEDELQAAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 160 ETVFEWDSEVVIEKYIKGDEITCSIFDGKHLPIVSIRHAAEFFDYNAKY-DDVSTIEEVIELPTEIKERVNKASLACYKA 238
Cdd:PRK01372 163 ELAFKYDDEVLVEKYIKGRELTVAVLGGKALPVIEIVPAGEFYDYEAKYlAGGTQYICPAGLPAEIEAELQELALKAYRA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487965615 239 LKCSVYARVDMMVKD-GIPYVMEVNTLPGMTQSSLLPKSADAAGINYSKLLDMIIETSLRVR 299
Cdd:PRK01372 243 LGCRGWGRVDFMLDEdGKPYLLEVNTQPGMTSHSLVPMAARAAGISFSELVDRILEDALCDR 304
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
1-296 |
5.86e-128 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 366.74 E-value: 5.86e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 1 MRIGVIMGGVSSEKQVSIMTGNEMIAHLDKNKYEIVPITLNEKmDLIE--KAKDIDFALLALHGKYGEDGTVQGTLESLG 78
Cdd:COG1181 1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVE-DLPAalKELKPDVVFPALHGRGGEDGTIQGLLELLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 79 IPYSGSNMLSSGICMDKNISKKILRYEGVETPDWIELTKMADLKLDDLDKL-GFPLVVKPNSGGSSVGVKIVNDKNELIS 157
Cdd:COG1181 80 IPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEElGLPLFVKPAREGSSVGVSKVKNAEELAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 158 MLETVFEWDSEVVIEKYIKGDEITCSIFDGKH---LPIVSIRHAAEFFDYNAKYDDVSTIEEVI-ELPTEIKERVNKASL 233
Cdd:COG1181 160 ALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGpraLPPIEIVPENGFYDYEAKYTDGGTEYICPaRLPEELEERIQELAL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487965615 234 ACYKALKCSVYARVDMMV-KDGIPYVMEVNTLPGMTQSSLLPKSADAAGINYSKLLDMIIETSL 296
Cdd:COG1181 240 KAFRALGCRGYARVDFRLdEDGEPYLLEVNTLPGMTPTSLLPKAAAAAGISYEELIERIIELAL 303
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
1-297 |
3.25e-94 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 282.01 E-value: 3.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 1 MRIGVIMGGVSSEKQVSIMTGNEMIAHLDKNKYEIVPI--------------------------TLNEKMDLIEKAKDID 54
Cdd:PRK01966 4 MRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIgitkdgrwylidadnmeladddndkeDLSLLILPSGGSEEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 55 FALLALHGKYGEDGTVQGTLESLGIPYSGSNMLSSGICMDKNISKKILRYEGVETPDWIELTKMADLKLDDLDKL---GF 131
Cdd:PRK01966 84 VVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTRGDWEEASLAEIEaklGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 132 PLVVKPNSGGSSVGVKIVNDKNELISMLETVFEWDSEVVIEKYIKGDEITCSI--FDGKHLPIVSIRHAAEFFDYNAKYD 209
Cdd:PRK01966 164 PVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVlgNDPKASVPGEIVKPDDFYDYEAKYL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 210 DVSTiEEVIE--LPTEIKERVNKASLACYKALKCSVYARVDMMV-KDGIPYVMEVNTLPGMTQSSLLPKSADAAGINYSK 286
Cdd:PRK01966 244 DGSA-ELIIPadLSEELTEKIRELAIKAFKALGCSGLARVDFFLtEDGEIYLNEINTMPGFTPISMYPKLWEASGLSYPE 322
|
330
....*....|.
gi 487965615 287 LLDMIIETSLR 297
Cdd:PRK01966 323 LIDRLIELALE 333
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
2-295 |
1.90e-88 |
|
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273498 [Multi-domain] Cd Length: 315 Bit Score: 266.84 E-value: 1.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 2 RIGVIMGGVSSEKQVSIMTGNEMIAHLDKNKYEIVPITLNEK------------MDLIEKAKDIDFALLALHGKYGEDGT 69
Cdd:TIGR01205 1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMgswtykdlpqliLELGALLEGIDVVFPVLHGRYGEDGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 70 VQGTLESLGIPYSGSNMLSSGICMDKNISKKILRYEGVETPDWIELTKM-----ADLKLDDLDKLGFPLVVKPNSGGSSV 144
Cdd:TIGR01205 81 IQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQNrasadELECEQVAEPLGFPVIVKPAREGSSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 145 GVKIVNDKNELISMLETVFEWDSEVVIEKYIKGDEITCSIFD-GKHLPIVSIRHAAEFF-DYNAKYDDVSTiEEVIE--L 220
Cdd:TIGR01205 161 GVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGnEEALPIIEIVPEIEGFyDYEAKYLDGST-EYVIPapL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487965615 221 PTEIKERVNKASLACYKALKCSVYARVDMMV-KDGIPYVMEVNTLPGMTQSSLLPKSADAAGINYSKLLDMIIETS 295
Cdd:TIGR01205 240 DEELEEKIKELALKAYKALGCRGLARVDFFLdEEGEIYLNEINTIPGMTAISLFPKAAAAAGIEFSQLVERILELA 315
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
1-297 |
8.03e-74 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 228.94 E-value: 8.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 1 MRIGVIMGGVSSEKQVSIMTGNEMIAHLDKNKYEIVPITLNEkmDLIEKA---KDIDFALLALHGKYGEDGTVQGTLESL 77
Cdd:PRK14571 1 MRVALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDVDE--DFLKKVdqlKSFDVVFNVLHGTFGEDGTLQAILDFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 78 GIPYSGSNMLSSGICMDKNISKKILRyEGVETPDWIELTKmadlkLDDLDKLGFPLVVKPNSGGSSVGVKIVNDKNELIS 157
Cdd:PRK14571 79 GIRYTGSDAFSSMICFDKLLTYRFLK-GTVEIPDFVEIKE-----FMKTSPLGYPCVVKPRREGSSIGVFICESDEEFQH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 158 MLETVFEWDSEVVIEKYIKGDEITCSIFDG----KHLPIVSIRHAAEFFDYNAKYDDVSTieEVI---ELPTEIKERVNK 230
Cdd:PRK14571 153 ALKEDLPRYGSVIVQEYIPGREMTVSILETekgfEVLPILELRPKRRFYDYVAKYTKGET--EFIlpaPLNPEEERLVKE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487965615 231 ASLACYKALKCSVYARVDMMVKDGIPYVMEVNTLPGMTQSSLLPKSADAAGINYSKLLDMIIETSLR 297
Cdd:PRK14571 231 TALKAFVEAGCRGFGRVDGIFSDGRFYFLEINTVPGLTELSDLPASAKAGGIEFEELVDIIIKSAFL 297
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
2-297 |
2.32e-63 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 203.60 E-value: 2.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 2 RIGVIMGGVSSEKQVSIMTGNEMIAHLDKNKYEIVPITLN------------------------------EKMDLIEKAK 51
Cdd:PRK14572 3 KIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPILLTpdggwvvptvyrpsipdesgnsedlfleefQKANGVSEPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 52 DI-----DFALLALHGKYGEDGTVQGTLESLGIPYSGSNMLSSGICMDKNISKKILRYEGVETPDWIELTKMADLKLDDL 126
Cdd:PRK14572 83 DIsqldaDIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFFELEKLKYLNSPRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 127 -----DKLGFPLVVKPNSGGSSVGVKIVNDKNELISMLETVFEWDSEVVIEKYIKGDEITCSIF----DGKH----LPIV 193
Cdd:PRK14572 163 tllklESLGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLeryrGGKRnpiaLPAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 194 SIRHAAEFFDYNAKYDDVSTiEEVIELPT--EIKERVNKASLACYKALKCSVYARVDMMVKDGIPYVMEVNTLPGMTQSS 271
Cdd:PRK14572 243 EIVPGGEFFDFESKYKQGGS-EEITPARIsdQEMKRVQELAIRAHESLGCKGYSRTDFIIVDGEPHILETNTLPGMTETS 321
|
330 340
....*....|....*....|....*.
gi 487965615 272 LLPKSADAAGINYSKLLDMIIETSLR 297
Cdd:PRK14572 322 LIPQQAKAAGINMEEVFTDLIEIGLK 347
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
104-293 |
1.01e-51 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 169.03 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 104 YEGVETPDWIELTKmaDLKLDDLDKLGFPLVVKPNSGGSSVGVKIVNDKNELISMLETVFEWDSEVVIEKYIKGDEITCS 183
Cdd:pfam07478 12 FVTFTRADWKLNPK--EWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGIEGREIECA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 184 IF---DGKHLPIVSIRHAAEFFDYNAKYDDVSTIEEV-IELPTEIKERVNKASLACYKALKCSVYARVDMMV-KDGIPYV 258
Cdd:pfam07478 90 VLgneDPEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVpADLEEEQEEQIQELALKAYKALGCRGLARVDFFLtEDGEIVL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 487965615 259 MEVNTLPGMTQSSLLPKSADAAGINYSKLLDMIIE 293
Cdd:pfam07478 170 NEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
2-295 |
1.80e-47 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 161.00 E-value: 1.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 2 RIGVIMGGVSSEKQVSIMTGNEMIAHLDKNKYEIVPITLNEKmDLIEKAKDI--DFALLALHGKYGEDGTVQGTLESLGI 79
Cdd:PRK14569 5 KIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAVGVDASGK-ELVAKLLELkpDKCFVALHGEDGENGRVSALLEMLEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 80 PYSGSNMLSSGICMDKNISKKILRYEGVETPdwieLTKMADLKLDDLDKLGFPLVVKPNSGGSSVGVKIVNDKNELISML 159
Cdd:PRK14569 84 KHTSSSMKSSVITMDKMISKEILMHHRMPTP----MAKFLTDKLVAEDEISFPVAVKPSSGGSSIATFKVKSIQELKHAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 160 ETVFEWdSEVVIEKYIKGDEITCSIFDGKHLPIVSIRHAAEFFDYNAKYDDVSTIEEVIELPTEIKERVNKASLACYKAL 239
Cdd:PRK14569 160 EEASKY-GEVMIEQWVTGKEITVAIVNDEVYSSVWIEPQNEFYDYESKYSGKSIYHSPSGLCEQKELEVRQLAKKAYDLL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 487965615 240 KCSVYARVDMMVKD-GIPYVMEVNTLPGMTQSSLLPKSADAAGINYSKLLDMIIETS 295
Cdd:PRK14569 239 GCSGHARVDFIYDDrGNFYIMEINSSPGMTDNSLSPKSAAAEGVDFDSFVKRIIEQA 295
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
1-292 |
1.41e-34 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 133.02 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 1 MRIGVIMGGVSSEKQVSIMTGNEMIAHLDKNKYEI----------------VPITLNEKM-------DLIEKAKDIDFAL 57
Cdd:PRK14573 452 LSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVsyflinrqglwetvssLETAIEEDSgksvlssEIAQALAKVDVVL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 58 LALHGKYGEDGTVQGTLESLGIPYSGSNMLSSGICMDKNISKKILRYEGVETPDWIELTKMA------DLKLDDLDKLGF 131
Cdd:PRK14573 532 PILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPLTLAGwkrepeLCLAHIVEAFSF 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 132 PLVVKPNSGGSSVGVKIVNDKNELISMLETVFEWDSEVVIEKYIKGD---EITCsIFDGKHLPIVSIRH----AAEFFDY 204
Cdd:PRK14573 612 PMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESRLGSreiEVSC-LGDGSSAYVIAGPHerrgSGGFIDY 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 205 NAKYD----DVSTIEEVIELPTEIKERVNKASLACYKALKCSVYARVDMMVKD-GIPYVMEVNTLPGMTQSSLLPKSADA 279
Cdd:PRK14573 691 QEKYGlsgkSSAQIVFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEeGNFWLSEMNPIPGMTEASPFLTAFVR 770
|
330
....*....|...
gi 487965615 280 AGINYSKLLDMII 292
Cdd:PRK14573 771 KGWTYEQIVHQLI 783
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
5-292 |
2.66e-32 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 122.63 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 5 VIMGGVSSEKQVSIMTGNEM-IAHLDKNKYEIVPITLNE------------------KMDLI--------------EKAK 51
Cdd:PRK14570 7 LIFGGVSFEHEISLRSAYGIySALLKLDKYNIYSVFIDKctgiwylldsvpdppkliKRDVLpivslipgcgifvnNKNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 52 DIDFALLALHGKYGEDGTVQGTLESLGIPYSGSNMLSSGICMDKNISKKILRYEGVETPDWIELTK------MADLKLDD 125
Cdd:PRK14570 87 EIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIGFRKydyfldKEGIKKDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 126 LDKLGFPLVVKPNSGGSSVGVKIVNDKNELISMLETVFEWDSEVVIEKYIKGDEITCSIFDGKHLPIVS----IRHAAEF 201
Cdd:PRK14570 167 KEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGNEQIKIFTpgeiVVQDFIF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 202 FDYNAKYDDVSTIEEVIELPTEIKER----VNKASLACYKALKCSVYARVDMMV--KDGIPYVMEVNTLPGMTQSSLLPK 275
Cdd:PRK14570 247 YDYDAKYSTIPGNSIVFNIPAHLDTKhlldIKEYAFLTYKNLELRGMARIDFLIekDTGLIYLNEINTIPGFTDISMFAK 326
|
330
....*....|....*..
gi 487965615 276 SADAAGINYSKLLDMII 292
Cdd:PRK14570 327 MCEHDGLQYKSLVDNLI 343
|
|
| Dala_Dala_lig_N |
pfam01820 |
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ... |
2-84 |
1.38e-28 |
|
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4 which is thought to be involved in substrate binding. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF). This domain is structurally related to the PreATP-grasp domain.
Pssm-ID: 460346 [Multi-domain] Cd Length: 118 Bit Score: 106.15 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 2 RIGVIMGGVSSEKQVSIMTGNEMIAHLDKNKYEIVPI-----------------------------------TLNEKMDL 46
Cdd:pfam01820 1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIgitkdgrlgeaalrelasddglllevddapdggpaGLLFGPNV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 487965615 47 IEKAKDIDFALLALHGKYGEDGTVQGTLESLGIPYSGS 84
Cdd:pfam01820 81 LELLIEVDVVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
75-288 |
2.94e-22 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 93.40 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 75 ESLGIPYSGSNmlSSGICMDKNISKKILRYEGVETPDWIELTKMADLKLDDLDKlGFPLVVKPNSGGSSVGVKIVNDKNE 154
Cdd:COG0439 37 EELGLPGPSPE--AIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEI-GYPVVVKPADGAGSRGVRVVRDEEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 155 LISMLETV------FEWDSEVVIEKYIKGDEITCSIF--DGKHLPIvsirhaaEFFDYNAKYDDVSTIEEVI--ELPTEI 224
Cdd:COG0439 114 LEAALAEAraeakaGSPNGEVLVEEFLEGREYSVEGLvrDGEVVVC-------SITRKHQKPPYFVELGHEApsPLPEEL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 225 KERVNKASLACYKALKcsvYAR----VDMMV-KDGIPYVMEVNT-LPGMTQSSLLPksaDAAGINYSKLL 288
Cdd:COG0439 187 RAEIGELVARALRALG---YRRgafhTEFLLtPDGEPYLIEINArLGGEHIPPLTE---LATGVDLVREQ 250
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
91-293 |
1.06e-17 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 81.14 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 91 ICMDKNISKKILRYEGVETPDWIeLTKMADLKLDDLDKLGFPLVVKPNSGGSSVGVKIVNDKNELISMLETVFEWDSEVV 170
Cdd:COG0189 93 RARDKLFTLQLLARAGIPVPPTL-VTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSEPV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 171 I-EKYI---KGDEITCSIFDGKHLPIVSIRHAAEFFDYNAKYDDVStieEVIELPTEIKERVNKASlacyKALKCsVYAR 246
Cdd:COG0189 172 LvQEFIpeeDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRA---EPVELTDEERELALRAA----PALGL-DFAG 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 487965615 247 VDMMVKDGIPYVMEVNTLPGmtqsslLPKSADAAGIN-YSKLLDMIIE 293
Cdd:COG0189 244 VDLIEDDDGPLVLEVNVTPG------FRGLERATGVDiAEAIADYLEA 285
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
35-262 |
2.28e-15 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 75.31 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 35 IVPITLNEKMDLIEKAKDIDFALLALHGKygedgtvqgTLESLGIPYSGSNMLSSGICMDKNISKKILRYEGVETPD-WI 113
Cdd:PRK12767 61 LLDICKKEKIDLLIPLIDPELPLLAQNRD---------RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKsYL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 114 ELTKMADLKLDDLDKLGFPLVVKPNSGGSSVGVKIVNDKNELismlETVFEWDSEVVIEKYIKGDEITCSIF---DGKHL 190
Cdd:PRK12767 132 PESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEEL----EFLLEYVPNLIIQEFIEGQEYTVDVLcdlNGEVI 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487965615 191 PIVSIRhaaeffdynaKYDDVSTieEVIELPTEIKERVNKASLACYKALKCSVYARVDMMVKDGIPYVMEVN 262
Cdd:PRK12767 208 SIVPRK----------RIEVRAG--ETSKGVTVKDPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEIN 267
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
92-262 |
2.66e-10 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 58.17 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 92 CMDKNISKKILRYEGVETPDWIELTKmadlklddLDKLGFPLVVKPNSGGSSVGVKIVNDKNELismletvFEWDSEVVI 171
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPETLQAEE--------LLREEKKYVVKPRDGCGGEGVRKVENGRED-------EAFIENVLV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 172 EKYIKGDEITCS-IFDGKHLPIVS-----IRHAAEFFDYNAkyddvstieEVIELPTEIKERV-NKASLACYKALKCSVY 244
Cdd:pfam02655 66 QEFIEGEPLSVSlLSDGEKALPLSvnrqyIDNGGSGFVYAG---------NVTPSRTELKEEIiELAEEVVECLPGLRGY 136
|
170
....*....|....*...
gi 487965615 245 ARVDMMVKDGIPYVMEVN 262
Cdd:pfam02655 137 VGVDLVLKDNEPYVIEVN 154
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
95-220 |
4.78e-08 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 54.16 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 95 KNISKKILRYEGVETPDWIELTKMADLKLDDLDKLGFPLVVKPNSGGSSVGV---KIVNDKNELISMLETVFEWDSEVVI 171
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLFADKAIVVKPKSTNFGLGIsifKEPASLEDYEKALEIAFREDSSVLV 568
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 487965615 172 EKYIKGDEITCSIFDGKHLPIVsIRHAAeffdyNAKYDDVSTIEEVIEL 220
Cdd:PRK02471 569 EEFIVGTEYRFFVLDGKVEAVL-LRVPA-----NVVGDGIHTVRELVAQ 611
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
37-262 |
1.36e-07 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 52.69 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 37 PITLNEKMDLIEKAKdIDFALLALHGKYGEDGTVQgtLESLGIPYSGSNMLSSGICMDKNISKKILRYEGVETPDWIELT 116
Cdd:TIGR01369 615 PLTFEDVMNIIELEK-PEGVIVQFGGQTPLNLAKA--LEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTAT 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 117 KMAdLKLDDLDKLGFPLVVKPNS--GGSSvgVKIVNDKNELISMLETVFEWDSE--VVIEKYIKgdeitcsifDGKHLPI 192
Cdd:TIGR01369 692 SVE-EAVEFASEIGYPVLVRPSYvlGGRA--MEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLE---------DAVEVDV 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 193 VSIRHAAEFFdynakyddVSTIEEVIE-----------------LPTEIKERVNKASLACYKALKCSVYARVDMMVKDGI 255
Cdd:TIGR01369 760 DAVSDGEEVL--------IPGIMEHIEeagvhsgdstcvlppqtLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGE 831
|
....*..
gi 487965615 256 PYVMEVN 262
Cdd:TIGR01369 832 VYVIEVN 838
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
94-263 |
2.18e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 51.91 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 94 DKNISKKILRYEGVE----TPDWIELTKMADLKLDDLdklGFPLVVKPNSGGSSVGVKIVNDKNELISMLETV------- 162
Cdd:PRK08654 115 SKINAKKLMKKAGVPvlpgTEEGIEDIEEAKEIAEEI---GYPVIIKASAGGGGIGMRVVYSEEELEDAIESTqsiaqsa 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 163 FEwDSEVVIEKYI-KGDEITCSIFDGKHLPIV-------SI--RHAaeffdynakyddvSTIEEV---IELPtEIKERVN 229
Cdd:PRK08654 192 FG-DSTVFIEKYLeKPRHIEIQILADKHGNVIhlgdrecSIqrRHQ-------------KLIEEApspIMTP-ELRERMG 256
|
170 180 190
....*....|....*....|....*....|....*..
gi 487965615 230 KASLacyKALKCSVYAR---VDMMVKDGIPYVMEVNT 263
Cdd:PRK08654 257 EAAV---KAAKAINYENagtVEFLYSNGNFYFLEMNT 290
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
74-291 |
2.29e-06 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 48.11 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 74 LESLGIPYSGSnmlSSGI--CMDKNISKKILRYEGVETPDWIeLTKMADLKLDDLDKLGFPLVVKPNSGGSSVGVKIVND 151
Cdd:TIGR00768 69 LESLGVPVINS---SDAIlnAGDKFLSHQLLAKAGIPLPRTG-LAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 152 KNELISMLEtVFEWDSEV----VIEKYIK---GDEITCSIFDGKHLPIVSIRHAAEFFDYNAKYDDVstieEVIELPTEI 224
Cdd:TIGR00768 145 RQAAESLLE-HFEQLNGPqnlfLVQEYIKkpgGRDIRVFVVGDEVVAAIYRITSGHWRSNLARGGKA----EPCSLTEEI 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487965615 225 KERVNKASlacyKALKCSvYARVDMMVKDGIPYVMEVNTLPGMTQSSLlpksadAAGINYS-KLLDMI 291
Cdd:TIGR00768 220 EELAIKAA----KALGLD-VAGVDLLESEDGLLVNEVNANPEFKNSVK------TTGVNIAgKLLDYI 276
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
77-189 |
4.02e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 48.30 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 77 LGIPysGSNMLSSGICMDKNISKKILRYEGVETPDwIELTKMADLKLDDLDKLGFPLVVKPNSGGSSVGVKIVNDKNELI 156
Cdd:PRK02186 92 LGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPR-THALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAA 168
|
90 100 110
....*....|....*....|....*....|....*.
gi 487965615 157 SMLETVFEWDS-EVVIEKYIKGDEITCSIF--DGKH 189
Cdd:PRK02186 169 AHCAALRRAGTrAALVQAYVEGDEYSVETLtvARGH 204
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
130-182 |
1.72e-05 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 44.20 E-value: 1.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487965615 130 GFPLVVKPNSGGSSVGVKIVNDKNELI----SMLETVFEW----------DSEVVIEKYIKGDEITC 182
Cdd:pfam13535 2 PYPCVIKPSVGFFSVGVYKINNREEWKaafaAIREEIEQWkemypeavvdGGSFLVEEYIEGEEFAV 68
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
130-283 |
3.63e-05 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 44.92 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 130 GFPLVVKPNSGGS--------SVGVKIVNDKNELISMLETVFEWDSEVVIEKYIKGD---EITCSIF---DGKHLPIVS- 194
Cdd:COG3919 152 GFPVVVKPADSVGydelsfpgKKKVFYVDDREELLALLRRIAAAGYELIVQEYIPGDdgeMRGLTAYvdrDGEVVATFTg 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 195 --IRHAAEFFdynakydDVSTIEEVIELPtEIKERVnKASLacyKALKCSVYARVDMMV--KDGIPYVMEVNTLPGmtQS 270
Cdd:COG3919 232 rkLRHYPPAG-------GNSAARESVDDP-ELEEAA-RRLL---EALGYHGFANVEFKRdpRDGEYKLIEINPRFW--RS 297
|
170
....*....|...
gi 487965615 271 SLLPKsadAAGIN 283
Cdd:COG3919 298 LYLAT---AAGVN 307
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
90-179 |
9.01e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 43.99 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 90 GICMDKNISKKILRYEGVETP------DWIELTKMADLKlddldklGFPLVVKPNSGGSSVGVKI-VNDKNELISMLETV 162
Cdd:PRK14016 210 DIACDKELTKRLLAAAGVPVPegrvvtSAEDAWEAAEEI-------GYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVA 282
|
90
....*....|....*..
gi 487965615 163 FEWDSEVVIEKYIKGDE 179
Cdd:PRK14016 283 SKESSDVIVERYIPGKD 299
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
130-271 |
1.65e-04 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 41.72 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 130 GFPLVVKPNSGGSSVGVKIVNDKNELISMLETVFEwdsEVVIEKYIK---GDEITCSIFDGKhlPIVSIRHAAEFFDYNA 206
Cdd:pfam08443 40 QFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATNE---QILVQEFIAeanNEDIRCLVVGDQ--VVGALHRQSNEGDFRS 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487965615 207 KYDDVSTIEevielPTEIKERVNKASLACYKALKcSVYARVDMMVKDGIPYVMEVNTLPGMTQSS 271
Cdd:pfam08443 115 NLHRGGVGE-----KYQLSQEETELAIKAAQAMQ-LDVAGVDLLRQKRGLLVCEVNSSPGLEGIE 173
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
94-189 |
4.06e-04 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 40.73 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 94 DKNISKKILRYEGVETPDWIELTKMADLKLDDLDKlGFP-LVVKPNSGGSSVGVKIVNDKNELISMLETVFE------WD 166
Cdd:pfam01071 2 SKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEA-GFPaIVVKADGLAAGKGVIVASSNEEAIKAVDEILEqkkfgeAG 80
|
90 100
....*....|....*....|....
gi 487965615 167 SEVVIEKYIKGDEITCSIF-DGKH 189
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFvDGKT 104
|
|
| PRK10446 |
PRK10446 |
30S ribosomal protein S6--L-glutamate ligase; |
94-267 |
6.41e-04 |
|
30S ribosomal protein S6--L-glutamate ligase;
Pssm-ID: 182468 [Multi-domain] Cd Length: 300 Bit Score: 40.66 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 94 DKNISKKILRYEGVETP---------DWIELTKMADlklddldklGFPLVVKPNSGGSSVGVKIVNDKNELISMLETVFE 164
Cdd:PRK10446 99 DKLRSMQLLARQGIDLPvtgiahspdDTSDLIDMVG---------GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 165 WDSEVVIEKYI---KGDEITCSIFDGKHLPIVSiRHAAEF-FDYNAKYDDVSTIeevielpTEIKERVNKASLACYKALK 240
Cdd:PRK10446 170 LNAHILVQEYIkeaQGCDIRCLVVGDEVVAAIE-RRAKEGdFRSNLHRGGAASV-------ASITPQEREIAIKAARTMA 241
|
170 180
....*....|....*....|....*..
gi 487965615 241 CSVyARVDMMVKDGIPYVMEVNTLPGM 267
Cdd:PRK10446 242 LDV-AGVDILRANRGPLVMEVNASPGL 267
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
130-262 |
8.70e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 40.85 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 130 GFPLVVKPnS---GGSsvGVKIVNDKNELISMLETVFEW--DSEVVIEKYIKGD---EITCsIFDGKHLPIVSI-RHaae 200
Cdd:PRK05294 704 GYPVLVRP-SyvlGGR--AMEIVYDEEELERYMREAVKVspDHPVLIDKFLEGAievDVDA-ICDGEDVLIGGImEH--- 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 201 ffdynakyddvstIEE-------------VIELPTEIKERVNKASLACYKALKCsvyarVDMM-----VKDGIPYVMEVN 262
Cdd:PRK05294 777 -------------IEEagvhsgdsacslpPQTLSEEIIEEIREYTKKLALELNV-----VGLMnvqfaVKDDEVYVIEVN 838
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
130-263 |
1.06e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 40.47 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 130 GFPLVVKPNSGGSSVGVKIVNDKNELISMLET------VFEWDSEVVIEKYI-KGDEITCSIFDGKHLPIVsirHAAEfF 202
Cdd:PRK05586 152 GYPVMVKASAGGGGRGIRIVRSEEELIKAFNTakseakAAFGDDSMYIEKFIeNPKHIEFQILGDNYGNVV---HLGE-R 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487965615 203 DYNAKYDDVSTIEEVIE--LPTEIKERVNKASLACYKALKCSVYARVDMMV-KDGIPYVMEVNT 263
Cdd:PRK05586 228 DCSLQRRNQKVLEEAPSpvMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNT 291
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
130-177 |
1.46e-03 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 39.86 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 487965615 130 GFPLVVKPnS---GGSsvGVKIVNDKNELISMLETVFEW--DSEVVIEKYIKG 177
Cdd:COG0458 149 GYPVIVRP-SyvlGGR--GMGIVYNEEELEEYLERALKVspDHPVLIDESLLG 198
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
59-175 |
2.08e-03 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 39.41 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 59 ALHGKYG---EDGTVQGTLESLGIPYSGSNMLSSGICMDKNISKKILRYEGVE-TPDWIELTKMADLKLDD-LDKLGFPL 133
Cdd:PRK08463 76 AIHPGYGflsENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPiVPGTEKLNSESMEEIKIfARKIGYPV 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 487965615 134 VVKPNSGGSSVGVKIVNDKNELISMLET------VFEWDSEVVIEKYI 175
Cdd:PRK08463 156 ILKASGGGGGRGIRVVHKEEDLENAFESckrealAYFNNDEVFMEKYV 203
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
130-194 |
2.87e-03 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 38.84 E-value: 2.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487965615 130 GFPLVVKPN--SGGSsvGVKIVNDKNELISMLETVFEW------DSEVVIEKYIKGDEITCSIF-DGKH-LPIVS 194
Cdd:COG0151 137 GAPIVVKADglAAGK--GVVVAETLEEALAAVDDMLADgkfgdaGARVVIEEFLEGEEASLFALtDGKTvLPLPT 209
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
26-262 |
3.22e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 38.86 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 26 AHLDKNKYEIVpITLNEKMDLIEKAKDIDF-ALLAlhgkygedGTVQGTL------ESLGIPYSGSNMLSSGIcMDKNIS 98
Cdd:PRK07206 43 ASFDTSDFIEV-IINGDIDDLVEFLRKLGPeAIIA--------GAESGVEladrlaEILTPQYSNDPALSSAR-RNKAEM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 99 KKILRYEGVETP------DWIEltkmADLKLDDLDKLGFPLVVKP-NSGGSSvGVKIVNDKNELISMLETVFE------- 164
Cdd:PRK07206 113 INALAEAGLPAArqintaDWEE----AEAWLRENGLIDRPVVIKPlESAGSD-GVFICPAKGDWKHAFNAILGkanklgl 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487965615 165 WDSEVVIEKYIKGDEITCSIF--DGKHLPIVSIR-HAAEFFDYNAKYDDVSTIEEVIELPTEIKERVNKASLACYKALKC 241
Cdd:PRK07206 188 VNETVLVQEYLIGTEYVVNFVslDGNHLVTEIVRyHKTSLNSGSTVYDYDEFLDYSEPEYQELVDYTKQALDALGIKNGP 267
|
250 260
....*....|....*....|.
gi 487965615 242 SvYARVdMMVKDGiPYVMEVN 262
Cdd:PRK07206 268 A-HAEV-MLTADG-PRLIEIG 285
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
130-175 |
6.57e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 37.70 E-value: 6.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 487965615 130 GFPLVVKPNSGGSSVGVKIVNDKNELISMLE------TVFEWDSEVVIEKYI 175
Cdd:PRK06111 152 GYPVMLKASAGGGGIGMQLVETEQELTKAFEsnkkraANFFGNGEMYIEKYI 203
|
|
| |
