|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
1-362 |
6.84e-172 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 482.31 E-value: 6.84e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 1 MRRLRIGVLFGGRSTEHEVSILSAQSIIAAMDPDRFEPVPLYIDKAGRWLVGGSLKRLVGDDAARKyvylppdptqrslv 80
Cdd:PRK01966 1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADDDNDK-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 81 aaNDRSTQELPSPARgggqggglLPLDAVFPVFHGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGL 160
Cdd:PRK01966 67 --EDLSLLILPSGGS--------EEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 161 PIVDYLPITRRQYEqdpDAFIALVEERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDRKLIVERAIDARELE 240
Cdd:PRK01966 137 PVAPYVVLTRGDWE---EASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 241 VSVLGNDqPQASVVGEVVPAHEFYDYEAKYLDEGSRLLIPAPIAQDAAETVRSMAIQAFLAVDAAGMARVDFFVErRSDR 320
Cdd:PRK01966 214 CAVLGND-PKASVPGEIVKPDDFYDYEAKYLDGSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLT-EDGE 291
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1671134683 321 IIVNELNTIPGFTRISMYPKLWEASGLSYPRLIERLVDLAIE 362
Cdd:PRK01966 292 IYLNEINTMPGFTPISMYPKLWEASGLSYPELIDRLIELALE 333
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
4-361 |
7.02e-139 |
|
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: 397.55 E-value: 7.02e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 4 LRIGVLFGGRSTEHEVSILSAQSIIAAMDPDRFEPVPLYIDKagrwlvggslkrlvgddaarkyvylppdptqrslvaan 83
Cdd:COG1181 1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDV-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 84 drstQELPSPARgggqgggLLPLDAVFPVFHGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGLPIV 163
Cdd:COG1181 43 ----EDLPAALK-------ELKPDVVFPALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 164 DYLPITRRQYeqdpdAFIALVEERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDRKLIVERAIDARELEVSV 243
Cdd:COG1181 112 PYVVLRRGEL-----ADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 244 LGNDQPQASVVGEVVPAHEFYDYEAKYLDEGSRLLIPAPIAQDAAETVRSMAIQAFLAVDAAGMARVDFFVeRRSDRIIV 323
Cdd:COG1181 187 LGNGGPRALPPIEIVPENGFYDYEAKYTDGGTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRL-DEDGEPYL 265
|
330 340 350
....*....|....*....|....*....|....*...
gi 1671134683 324 NELNTIPGFTRISMYPKLWEASGLSYPRLIERLVDLAI 361
Cdd:COG1181 266 LEVNTLPGMTPTSLLPKAAAAAGISYEELIERIIELAL 303
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
5-360 |
3.28e-123 |
|
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: 358.52 E-value: 3.28e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 5 RIGVLFGGRSTEHEVSILSAQSIIAAMDPDRFEPVPLYIDKAGRWLVggslkrlvgddaarkyvylpPDPTQRSLVAANd 84
Cdd:TIGR01205 1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSWTY--------------------KDLPQLILELGA- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 85 rstqelpspargggqggGLLPLDAVFPVFHGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGLPIVD 164
Cdd:TIGR01205 60 -----------------LLEGIDVVFPVLHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 165 YLPITRRqYEQDPDAFIALVEERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDRKLIVERAIDARELEVSVL 244
Cdd:TIGR01205 123 YIVLTQN-RASADELECEQVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSIL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 245 GNDQ--PQASVVGEVVPaheFYDYEAKYLDEGSRLLIPAPIAQDAAETVRSMAIQAFLAVDAAGMARVDFFVErRSDRII 322
Cdd:TIGR01205 202 GNEEalPIIEIVPEIEG---FYDYEAKYLDGSTEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLD-EEGEIY 277
|
330 340 350
....*....|....*....|....*....|....*...
gi 1671134683 323 VNELNTIPGFTRISMYPKLWEASGLSYPRLIERLVDLA 360
Cdd:TIGR01205 278 LNEINTIPGMTAISLFPKAAAAAGIEFSQLVERILELA 315
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
155-358 |
2.25e-86 |
|
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: 260.33 E-value: 2.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 155 FAAAGLPIVDYLPITRRQYEQDPDAFIALVEERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDRKLIVERAI 234
Cdd:pfam07478 2 LKAAGLPVVPFVTFTRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 235 DARELEVSVLGNDQPQASVVGEVVPAHEFYDYEAKYLDEGSRLLIPAPIAQDAAETVRSMAIQAFLAVDAAGMARVDFFV 314
Cdd:pfam07478 82 EGREIECAVLGNEDPEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDFFL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1671134683 315 ErRSDRIIVNELNTIPGFTRISMYPKLWEASGLSYPRLIERLVD 358
Cdd:pfam07478 162 T-EDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
1-363 |
1.34e-84 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 259.27 E-value: 1.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 1 MRRLRIGVLFGGRSTEHEVSILSAQSIIAAMDPDRFEPVPlyIDkagrwlvggslkrlVGDDAARKyvylppdptqrsLV 80
Cdd:PRK01372 2 KMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHP--ID--------------PGEDIAAQ------------LK 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 81 AANdrstqelpspargggqgggllpLDAVFPVFHGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGL 160
Cdd:PRK01372 54 ELG----------------------FDRVFNALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 161 PIVDYLPITRrqyeqdpDAFIALVEERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDRKLIVERAIDARELE 240
Cdd:PRK01372 112 PTPPWIVLTR-------EEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 241 VSVLGNdqpQASVVGEVVPAHEFYDYEAKYLDEGSRLLIPAPIAQDAAETVRSMAIQAFLAVDAAGMARVDFFVErRSDR 320
Cdd:PRK01372 185 VAVLGG---KALPVIEIVPAGEFYDYEAKYLAGGTQYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFMLD-EDGK 260
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1671134683 321 IIVNELNTIPGFTRISMYPKLWEASGLSYPRLIERLVDLAIER 363
Cdd:PRK01372 261 PYLLEVNTQPGMTSHSLVPMAARAAGISFSELVDRILEDALCD 303
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
8-380 |
3.76e-68 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 219.32 E-value: 3.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 8 VLFGGRSTEHEVSILSAQSIIAA-MDPDRFEPVPLYIDK-AGRWLVGGSlkrlvgddaarkyVYLPPDPTQRslvaanDR 85
Cdd:PRK14570 7 LIFGGVSFEHEISLRSAYGIYSAlLKLDKYNIYSVFIDKcTGIWYLLDS-------------VPDPPKLIKR------DV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 86 STQELPSPARGGGQGGGLLPLDAVFPVFHGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGLPIVDY 165
Cdd:PRK14570 68 LPIVSLIPGCGIFVNNKNLEIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 166 LPITRRQYEQDPDAFIALVEERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDRKLIVERAIDARELEVSVLG 245
Cdd:PRK14570 148 IGFRKYDYFLDKEGIKKDIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 246 NDQPQASVVGE-VVPAHEFYDYEAKY-LDEGSRLL--IPAPIAQDAAETVRSMAIQAFLAVDAAGMARVDFFVERRSDRI 321
Cdd:PRK14570 228 NEQIKIFTPGEiVVQDFIFYDYDAKYsTIPGNSIVfnIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDTGLI 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 322 IVNELNTIPGFTRISMYPKLWEASGLSYPRLIERLVDLAIERF-NDKQRsqtaIDSRLLE 380
Cdd:PRK14570 308 YLNEINTIPGFTDISMFAKMCEHDGLQYKSLVDNLIDLAFQSYiKRKKR----IDFERLE 363
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
2-369 |
3.41e-57 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 199.66 E-value: 3.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 2 RRLRIGVLFGGRSTEHEVSILSAQSIIAAMDPDRFEPVPLYIDKAGRWLVGGSLKrlVGDDAARKYVYLPPDPTQRslva 81
Cdd:PRK14573 450 KKLSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVSYFLINRQGLWETVSSLE--TAIEEDSGKSVLSSEIAQA---- 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 82 andrstqelpspargggqgggLLPLDAVFPVFHGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGLP 161
Cdd:PRK14573 524 ---------------------LAKVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVP 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 162 IVDYLPITRRQYEQDPDAFIALVEERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDRKLIVERA-IDARELE 240
Cdd:PRK14573 583 VVPYQPLTLAGWKREPELCLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESrLGSREIE 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 241 VSVLGNdqpqASVVGEVVPAHE------FYDYEAKYLDEG---SRLLIPAPIAQDAAETVRSMAIQAFLAVDAAGMARVD 311
Cdd:PRK14573 663 VSCLGD----GSSAYVIAGPHErrgsggFIDYQEKYGLSGkssAQIVFDLDLSKESQEQVLELAERIYRLLQGKGSCRID 738
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1671134683 312 FFVERRSDrIIVNELNTIPGFTRISMYPKLWEASGLSYPRLIERLVDLAIERFNDKQR 369
Cdd:PRK14573 739 FFLDEEGN-FWLSEMNPIPGMTEASPFLTAFVRKGWTYEQIVHQLIIDGLHKFDQRQR 795
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
5-362 |
1.71e-56 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 188.58 E-value: 1.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 5 RIGVLFGGRSTEHEVSILSAQSIIAAMDPDRFEPVPLYIDKAGRWLVGGSLKRLVGDDAARKyvylpPDPTQRSLVAAND 84
Cdd:PRK14572 3 KIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPILLTPDGGWVVPTVYRPSIPDESGNS-----EDLFLEEFQKANG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 85 RSTQELPSPargggqggglLPLDAVFPVFHGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGLPIVD 164
Cdd:PRK14572 78 VSEPADISQ----------LDADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 165 YLPITRRQYEQDPDAFIALVEErIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDRKLIVERAIDARELEVSVL 244
Cdd:PRK14572 148 FFELEKLKYLNSPRKTLLKLES-LGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 245 -----GNDQPQASVVGEVVPAHEFYDYEAKYLDEGSRLLIPAPIAQDAAETVRSMAIQAFLAVDAAGMARVDFFVERRSD 319
Cdd:PRK14572 227 eryrgGKRNPIALPATEIVPGGEFFDFESKYKQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTDFIIVDGEP 306
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1671134683 320 RIIvnELNTIPGFTRISMYPKLWEASGLSYPRLIERLVDLAIE 362
Cdd:PRK14572 307 HIL--ETNTLPGMTETSLIPQQAKAAGINMEEVFTDLIEIGLK 347
|
|
| Dala_Dala_lig_N |
pfam01820 |
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ... |
5-137 |
4.72e-46 |
|
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: 153.91 E-value: 4.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 5 RIGVLFGGRSTEHEVSILSAQSIIAAMDPDRFEPVPLYIDKAGRWlvggslkrlvGDDAARKYVYLPPDptqrsLVAAND 84
Cdd:pfam01820 1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIGITKDGRL----------GEAALRELASDDGL-----LLEVDD 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1671134683 85 RSTQELPSPARGGGQGGGLLPLDAVFPVFHGLNGEDGTVQGVLELANIPYVGA 137
Cdd:pfam01820 66 APDGGPAGLLFGPNVLELLIEVDVVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
4-362 |
3.13e-42 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 149.59 E-value: 3.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 4 LRIGVLFGGRSTEHEVSILSAQSIIAAmdpdrfepvplyidkagrwlvggsLKRLvgddaarKYVYLPPDptqrslvaAN 83
Cdd:PRK14571 1 MRVALLMGGVSREREISLRSGERVKKA------------------------LEKL-------GYEVTVFD--------VD 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 84 DRSTQELPSpargggqgggLLPLDAVFPVFHGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRaFAAAGLPIV 163
Cdd:PRK14571 42 EDFLKKVDQ----------LKSFDVVFNVLHGTFGEDGTLQAILDFLGIRYTGSDAFSSMICFDKLLTYR-FLKGTVEIP 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 164 DYLPITrrqyeqdpdafIALVEERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDRKLIVERAIDARELEVSV 243
Cdd:PRK14571 111 DFVEIK-----------EFMKTSPLGYPCVVKPRREGSSIGVFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 244 LG-NDQPQASVVGEVVPAHEFYDYEAKYLDEGSRLLIPAPIAQDAAETVRSMAIQAFLAVDAAGMARVDFFVerRSDRII 322
Cdd:PRK14571 180 LEtEKGFEVLPILELRPKRRFYDYVAKYTKGETEFILPAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIF--SDGRFY 257
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1671134683 323 VNELNTIPGFTRISMYPKLWEASGLSYprliERLVDLAIE 362
Cdd:PRK14571 258 FLEINTVPGLTELSDLPASAKAGGIEF----EELVDIIIK 293
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
1-360 |
1.87e-28 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 112.85 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 1 MRRLRIGVLFGGRSTEHEVSILSAQSIIAAMDPDRFEPVPLyiDKAGRWLVGgslkrlvgddaarKYVYLPPDptqrslv 80
Cdd:PRK14569 1 MKNEKIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAVGV--DASGKELVA-------------KLLELKPD------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 81 aandrstqelpspargggqgggllpldAVFPVFHGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGL 160
Cdd:PRK14569 59 ---------------------------KCFVALHGEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRM 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 161 PIVDYLPITRRQYEQDpdafialveeRIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASSFDrKLIVERAIDARELE 240
Cdd:PRK14569 112 PTPMAKFLTDKLVAED----------EISFPVAVKPSSGGSSIATFKVKSIQELKHAYEEASKYG-EVMIEQWVTGKEIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 241 VSVLgNDQPQASVVGEvvPAHEFYDYEAKYLDEgSRLLIPAPIAQDAAETVRSMAIQAFLAVDAAGMARVDFFVERRSDR 320
Cdd:PRK14569 181 VAIV-NDEVYSSVWIE--PQNEFYDYESKYSGK-SIYHSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNF 256
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1671134683 321 IIVnELNTIPGFTRISMYPKLWEASGLSYPRLIERLVDLA 360
Cdd:PRK14569 257 YIM-EINSSPGMTDNSLSPKSAAAEGVDFDSFVKRIIEQA 295
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
147-361 |
6.02e-17 |
|
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: 79.92 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 147 DKIFMKRAFAAAGLPIVDYLPITrrqyeqDPDAFIALVEErIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLA----- 221
Cdd:COG0439 54 DKVLMREALAAAGVPVPGFALVD------SPEEALAFAEE-IGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAraeak 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 222 -SSFDRKLIVERAIDARELEVSVLGNDqpqasvvGEVVPA--HEFYDYEAKYLDEGsrLLIPAPIAQDAAETVRSMAIQa 298
Cdd:COG0439 127 aGSPNGEVLVEEFLEGREYSVEGLVRD-------GEVVVCsiTRKHQKPPYFVELG--HEAPSPLPEELRAEIGELVAR- 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1671134683 299 flAVDAAGMAR----VDFFVERRsDRIIVNELNT-IPGftriSMYPKLWE-ASGLSyprLIERLVDLAI 361
Cdd:COG0439 197 --ALRALGYRRgafhTEFLLTPD-GEPYLIEINArLGG----EHIPPLTElATGVD---LVREQIRLAL 255
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
147-328 |
2.24e-08 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 53.85 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 147 DKIFMKRAFAAAGLPIVdylPITRRQYEQDPDAFIAlvEERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLA----- 221
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTV---PGTAGPVETEEEALAA--AKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALAlaeap 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 222 SSFDRK-LIVERAIDA-RELEVSVLGNDQPQASVVGE---VVPAHefydyEAKYLDEGsrlliPAPIAQDAA-ETVRSMA 295
Cdd:pfam02786 76 AAFGNPqVLVEKSLKGpKHIEYQVLRDAHGNCITVCNrecSDQRR-----TQKSIEVA-----PSQTLTDEErQMLREAA 145
|
170 180 190
....*....|....*....|....*....|...
gi 1671134683 296 IQAFLAVDAAGMARVDFFVERRSDRIIVNELNT 328
Cdd:pfam02786 146 VKIARHLGYVGAGTVEFALDPFSGEYYFIEMNT 178
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
156-326 |
8.39e-08 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 51.49 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 156 AAAGLPIVDYLPITrrqyeqDPDAFIALVEeRIGYPCFTKFANSGSS-VGTTKAHHRAELLEGLRLAssFDRKLIVERAI 234
Cdd:pfam02222 1 QKLGLPTPRFMAAE------SLEELIEAGQ-ELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEEL--GDGPVIVEEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 235 DArELEVSVLGNDQPQasvvGEVVpaheFYD-YEAKYLDEGSRLLI-PAPIAQDAAETVRSMAIQAFLAVDAAGMARVDF 312
Cdd:pfam02222 72 PF-DRELSVLVVRSVD----GETA----FYPvVETIQEDGICRLSVaPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
170
....*....|....
gi 1671134683 313 FVERRSDrIIVNEL 326
Cdd:pfam02222 143 FVTEDGD-LLINEL 155
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
147-326 |
1.19e-07 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 53.15 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 147 DKIFMKRAFAAAGLPIVDYLPITrrqyeqDPDAFIALVEErIGYPCFTKFANSGS-SVGTTKAHHRAELLEGLRLASsfD 225
Cdd:COG0026 89 DRLLEKAFLAELGIPVAPFAAVD------SLEDLEAAIAE-LGLPAVLKTRRGGYdGKGQVVIKSAADLEAAWAALG--G 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 226 RKLIVERAID-ARELevSVLGndqpqA-SVVGEVVpaheFYD-----YEAKYLDEgsrLLIPAPIAQDAAETVRSMAIQA 298
Cdd:COG0026 160 GPCILEEFVPfEREL--SVIV-----ArSPDGEVA----TYPvvenvHRNGILDE---SIAPARISEALAAEAEEIAKRI 225
|
170 180
....*....|....*....|....*....
gi 1671134683 299 FLAVDAAG-MArVDFFVeRRSDRIIVNEL 326
Cdd:COG0026 226 AEALDYVGvLA-VEFFV-TKDGELLVNEI 252
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
94-344 |
2.27e-06 |
|
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: 48.78 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 94 ARGGGQGGGLLPLDAVF----PVFHGLngedgtvqGVLELANIPyvGAGVLGSALGL----DKIFMKRAFAAAGLPIVDY 165
Cdd:COG0189 45 APELYRGEDLSEFDAVLpridPPFYGL--------ALLRQLEAA--GVPVVNDPEAIrrarDKLFTLQLLARAGIPVPPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 166 LpITRrqyeqDPDAFIALVEErIGYPCFTKFANSGSSVGTTKAHHRAELLEGLR-LASSFDRKLIVER---AIDARELEV 241
Cdd:COG0189 115 L-VTR-----DPDDLRAFLEE-LGGPVVLKPLDGSGGRGVFLVEDEDALESILEaLTELGSEPVLVQEfipEEDGRDIRV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 242 SVLGndqpqasvvGEVVPAHEFY--DYEAK-YLDEGSRllipaPIAQDAAETVRSMAIQAFLAVDaAGMARVDFFVERrs 318
Cdd:COG0189 188 LVVG---------GEPVAAIRRIpaEGEFRtNLARGGR-----AEPVELTDEERELALRAAPALG-LDFAGVDLIEDD-- 250
|
250 260 270
....*....|....*....|....*....|..
gi 1671134683 319 DRIIVNELNTIPGF------TRISMYPKLWEA 344
Cdd:COG0189 251 DGPLVLEVNVTPGFrgleraTGVDIAEAIADY 282
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
134-326 |
2.17e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 45.91 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 134 YVGAGVLgsALGLDKIFMKRAFAAAGLPIVDYLPITRRqyeQDPDAFIAlveeRIGYPCFTKfansgSSV------GTTK 207
Cdd:PRK06019 89 PPGPDAL--AIAQDRLTEKQFLDKLGIPVAPFAVVDSA---EDLEAALA----DLGLPAVLK-----TRRggydgkGQWV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 208 AHHRAELLEGLRLASSFDrkLIVERAIDArELEVSVLGndqpqA-SVVGEVVpaheFYDYEAKYLDEG--SRLLIPAPIA 284
Cdd:PRK06019 155 IRSAEDLEAAWALLGSVP--CILEEFVPF-EREVSVIV-----ArGRDGEVV----FYPLVENVHRNGilRTSIAPARIS 222
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1671134683 285 QDAAETVRSMAIQAFLAVDAAG-MArVDFFVeRRSDRIIVNEL 326
Cdd:PRK06019 223 AELQAQAEEIASRIAEELDYVGvLA-VEFFV-TGDGELLVNEI 263
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
144-362 |
2.94e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 45.65 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 144 LGLDKIFMKRAFAAAGLPIVD-YLPitrrqyEQDPDAFIALVEERIGYPCFTKFANSGSSVGTTKAHHRAEllegLRLAS 222
Cdd:PRK12767 108 ICNDKWLTYEFLKENGIPTPKsYLP------ESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEE----LEFLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 223 SFDRKLIVERAIDARELEVSVL--GNDQPQASVV--------GEVVPAHEFYDYEakyldegsrllipapiaqdaaetVR 292
Cdd:PRK12767 178 EYVPNLIIQEFIEGQEYTVDVLcdLNGEVISIVPrkrievraGETSKGVTVKDPE-----------------------LF 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 293 SMAIQAFLAVDAAGMARVDFFVerRSDRIIVNELNtiPGFTriSMYPKLWEAsGLSYPRLIERLVDLAIE 362
Cdd:PRK12767 235 KLAERLAEALGARGPLNIQCFV--TDGEPYLFEIN--PRFG--GGYPLSYMA-GANEPDWIIRNLLGGEN 297
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
147-315 |
3.59e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 45.40 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 147 DKIFMKRAFAAAGLPIVdylPITRRQYEqDPDAFIALVEErIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRL----AS 222
Cdd:PRK06111 115 SKIEARRAMQAAGVPVV---PGITTNLE-DAEEAIAIARQ-IGYPVMLKASAGGGGIGMQLVETEQELTKAFESnkkrAA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 223 SF--DRKLIVERAI-DARELEVSVLGNDQPQASVVGE----VVPAHEfydyeaKYLDEGsrlliPAPIAQDAA-ETVRSM 294
Cdd:PRK06111 190 NFfgNGEMYIEKYIeDPRHIEIQLLADTHGNTVYLWErecsVQRRHQ------KVIEEA-----PSPFLDEETrKAMGER 258
|
170 180
....*....|....*....|.
gi 1671134683 295 AIQAFLAVDAAGMARVDFFVE 315
Cdd:PRK06111 259 AVQAAKAIGYTNAGTIEFLVD 279
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
107-246 |
2.38e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 42.82 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 107 DAVFPVFhGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGLPIVDYLPitrrQYEQDPDAFIAlVEE 186
Cdd:PRK12833 79 DAIHPGY-GFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSD----GVVASLDAALE-VAA 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1671134683 187 RIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASS-----F-DRKLIVERAID-ARELEVSVLGN 246
Cdd:PRK12833 153 RIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQReaqaaFgDGGVYLERFIArARHIEVQILGD 219
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
143-245 |
3.56e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.82 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 143 ALGlDKIFMKRAFAAAGLPIVD--YLPITrrqyeqDPDAFIALVEErIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRL 220
Cdd:PRK12999 116 LLG-DKVAARNAAIKAGVPVIPgsEGPID------DIEEALEFAEE-IGYPIMLKASAGGGGRGMRIVRSEEELEEAFER 187
|
90 100 110
....*....|....*....|....*....|..
gi 1671134683 221 ASS-----F-DRKLIVERAI-DARELEVSVLG 245
Cdd:PRK12999 188 AKReakaaFgNDEVYLEKYVeNPRHIEVQILG 219
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
147-338 |
1.40e-03 |
|
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: 40.02 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 147 DKIFMKRAFAAAGLPIVDYLPITrrqyeqDPDAFIALVEErIGYPCFTK--FANSGSSVGTTKAHHRAE-LLEGLRLASS 223
Cdd:TIGR00768 88 DKFLSHQLLAKAGIPLPRTGLAG------SPEEALKLIEE-IGFPVVLKpvFGSWGRGVSLARDRQAAEsLLEHFEQLNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 224 FDRKLIVERAIDARelevsvlGNDQPQASVVGEVVPAHEFYDYEAKYLDEGSRLLIPAPIaqDAAETVRSMAIQA--FLA 301
Cdd:TIGR00768 161 PQNLFLVQEYIKKP-------GGRDIRVFVVGDEVVAAIYRITSGHWRSNLARGGKAEPC--SLTEEIEELAIKAakALG 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 1671134683 302 VDAAGmarVDFFveRRSDRIIVNELNTIPGFTRISMY 338
Cdd:TIGR00768 232 LDVAG---VDLL--ESEDGLLVNEVNANPEFKNSVKT 263
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
143-245 |
1.87e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 40.45 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 143 ALGlDKIFMKRAFAAAGLPIVD--YLPITrrqyeqDPDAFIALVEErIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRL 220
Cdd:COG1038 115 MLG-DKVAARAAAIEAGVPVIPgtEGPVD------DLEEALAFAEE-IGYPVMLKAAAGGGGRGMRVVRSEEELEEAFES 186
|
90 100 110
....*....|....*....|....*....|..
gi 1671134683 221 ASS-----F-DRKLIVERAID-ARELEVSVLG 245
Cdd:COG1038 187 ARReakaaFgDDEVFLEKYIErPKHIEVQILG 218
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
107-328 |
1.90e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 40.08 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 107 DAVFPVFhGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGLPIVdylPITRRQYEQDPDAF-IAlve 185
Cdd:PRK05586 76 QAIHPGF-GFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVV---PGSEGEIENEEEALeIA--- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 186 ERIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLA-----SSF-DRKLIVERAIDA-RELEVSVLGNDqpqasvVGEVV 258
Cdd:PRK05586 149 KEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAkseakAAFgDDSMYIEKFIENpKHIEFQILGDN------YGNVV 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1671134683 259 PAHE----FYDYEAKYLDEGsrlliPAPIAQDaaETVRSM---AIQAFLAVDAAGMARVDFFVERRSDRIIVnELNT 328
Cdd:PRK05586 223 HLGErdcsLQRRNQKVLEEA-----PSPVMTE--ELRKKMgeiAVKAAKAVNYKNAGTIEFLLDKDGNFYFM-EMNT 291
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
107-328 |
2.56e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 39.73 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 107 DAVFPVFhGLNGEDGTVQGVLELANIPYVGAGVLGSALGLDKIFMKRAFAAAGLPIVDYLPITRRQYEQDPDafialVEE 186
Cdd:PRK08462 78 DAIFPGY-GFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKK-----IAK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 187 RIGYPCFTKFANSGSSVGtTKAHHRAELLEGLRLA------SSF-DRKLIVERAID-ARELEVSVLGNDQPQASVVGE-- 256
Cdd:PRK08462 152 EIGYPVILKAAAGGGGRG-MRVVEDESDLENLYLAaesealSAFgDGTMYMEKFINnPRHIEVQILGDKHGNVIHVGErd 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1671134683 257 --VVPAHEfydyeaKYLDEGsrlliPAPIAQDAA-ETVRSMAIQAFLAVDAAGMARVDFFVERRSDrIIVNELNT 328
Cdd:PRK08462 231 csLQRRHQ------KLIEES-----PAVVLDEKTrERLHETAIKAAKAIGYEGAGTFEFLLDSNLD-FYFMEMNT 293
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
147-256 |
4.00e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 39.01 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 147 DKIFMKRAFAAAGLPIVdylPITRRQYEqDPDAFIALVEErIGYPCFTKFANSGSSVGTTKAHHRAELLEGLRLASS--- 223
Cdd:PRK08591 115 DKVTAKATMKKAGVPVV---PGSDGPVD-DEEEALAIAKE-IGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAeak 189
|
90 100 110
....*....|....*....|....*....|....*..
gi 1671134683 224 --F-DRKLIVERAI-DARELEVSVLGNDQPQASVVGE 256
Cdd:PRK08591 190 aaFgNPGVYMEKYLeNPRHIEIQVLADGHGNAIHLGE 226
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
147-261 |
5.31e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 38.98 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 147 DKIFMKRAFAAAGLPIvdylPITRRQYEQDpDAFIALveERIGYPCFTK--FANSGSSVgTTKAHHRAELLEGLRLASSF 224
Cdd:PRK14016 214 DKELTKRLLAAAGVPV----PEGRVVTSAE-DAWEAA--EEIGYPVVVKplDGNHGRGV-TVNITTREEIEAAYAVASKE 285
|
90 100 110
....*....|....*....|....*....|....*..
gi 1671134683 225 DRKLIVERAIDARELEVSVLGNdqpQASVVGEVVPAH 261
Cdd:PRK14016 286 SSDVIVERYIPGKDHRLLVVGG---KLVAAARREPPH 319
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
143-248 |
8.33e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 38.04 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671134683 143 ALGlDKIFMKRAFAAAGLPIvdyLPITRRQYEqDPDAFIALVEErIGYPCFTKFANSGSSVGTTKAHHRAELLEGL---- 218
Cdd:PRK08654 112 AMG-SKINAKKLMKKAGVPV---LPGTEEGIE-DIEEAKEIAEE-IGYPVIIKASAGGGGIGMRVVYSEEELEDAIestq 185
|
90 100 110
....*....|....*....|....*....|...
gi 1671134683 219 RLASSF--DRKLIVERAID-ARELEVSVLGNDQ 248
Cdd:PRK08654 186 SIAQSAfgDSTVFIEKYLEkPRHIEIQILADKH 218
|
|
| |
