|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
1-352 |
0e+00 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 544.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 1 MEKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWHVSDASNYLLNADdpahIALRPSATSLAQVP 80
Cdd:PRK01966 1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADD----DNDKEDLSLLILPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 81 GKHEHqlidaqngqplptVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFIT 160
Cdd:PRK01966 77 GGSEE-------------VDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 161 LTRANRNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDnPQ 240
Cdd:PRK01966 144 LTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 241 ASTCGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTLP 320
Cdd:PRK01966 223 ASVPGEIVKPDDFYDYEAKYLD-GSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMP 301
|
330 340 350
....*....|....*....|....*....|..
gi 446335834 321 GFTNISMYPKLWQASGLGYTDLITRLIELALE 352
Cdd:PRK01966 302 GFTPISMYPKLWEASGLSYPELIDRLIELALE 333
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
5-350 |
1.18e-156 |
|
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: 442.49 E-value: 1.18e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 5 RVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWhvsdasnyllNADDPAHIALRpsatslaqvpgkhe 84
Cdd:TIGR01205 1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSW----------TYKDLPQLILE-------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 85 hqlidaqNGQPLPTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLTRa 164
Cdd:TIGR01205 57 -------LGALLEGIDVVFPVLHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQ- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 165 NRNNISFAE---VESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDN--P 239
Cdd:TIGR01205 129 NRASADELEceqVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEalP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 240 QASTCGEIVltsDFYAYDTKYIDEDgAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTL 319
Cdd:TIGR01205 209 IIEIVPEIE---GFYDYEAKYLDGS-TEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTI 284
|
330 340 350
....*....|....*....|....*....|.
gi 446335834 320 PGFTNISMYPKLWQASGLGYTDLITRLIELA 350
Cdd:TIGR01205 285 PGMTAISLFPKAAAAAGIEFSQLVERILELA 315
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
4-351 |
1.18e-155 |
|
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: 439.16 E-value: 1.18e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 4 LRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQgqwhvsdasnyllnaDDPAHIALRPsatslaqvpgkh 83
Cdd:COG1181 1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVE---------------DLPAALKELK------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 84 ehqlidaqngqplptVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLTR 163
Cdd:COG1181 54 ---------------PDVVFPALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 164 ANRNNIsfAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDNPQAST 243
Cdd:COG1181 119 GELADL--EAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGPRALP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 244 CGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTLPGFT 323
Cdd:COG1181 197 PIEIVPENGFYDYEAKYTD-GGTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMT 275
|
330 340
....*....|....*....|....*...
gi 446335834 324 NISMYPKLWQASGLGYTDLITRLIELAL 351
Cdd:COG1181 276 PTSLLPKAAAAAGISYEELIERIIELAL 303
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
147-348 |
1.58e-109 |
|
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: 318.49 E-value: 1.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 147 LLRDAGLNIAPFITLTRANRNNI---SFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQG 223
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRADWKLNpkeWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 224 IKGREIECAVLGNDNPQASTCGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDV 303
Cdd:pfam07478 81 IEGREIECAVLGNEDPEVSPVGEIVPSGGFYDYEAKYID-DSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446335834 304 FLTPENEVVINEINTLPGFTNISMYPKLWQASGLGYTDLITRLIE 348
Cdd:pfam07478 160 FLTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
1-353 |
1.12e-106 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 315.13 E-value: 1.12e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 1 MEKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVllGIDKqgqwhvsdasnyllnADDPAHI--ALRPsatslaq 78
Cdd:PRK01372 2 KMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAH--PIDP---------------GEDIAAQlkELGF------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 79 vpgkhehqlidaqngqplptvDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPF 158
Cdd:PRK01372 58 ---------------------DRVFNALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPW 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 159 ITLTRANrnniSFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNdn 238
Cdd:PRK01372 117 IVLTREE----DLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGG-- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 239 pQASTCGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINT 318
Cdd:PRK01372 191 -KALPVIEIVPAGEFYDYEAKYLA-GGTQYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
|
330 340 350
....*....|....*....|....*....|....*
gi 446335834 319 LPGFTNISMYPKLWQASGLGYTDLITRLIELALER 353
Cdd:PRK01372 269 QPGMTSHSLVPMAARAAGISFSELVDRILEDALCD 303
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
8-355 |
2.46e-67 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 216.62 E-value: 2.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 8 IVFGGKSAEHEVSLQSAKNIVDAI-DKSRFDVVLLGIDK-QGQWHVSDAsnyllnADDPAHIALRPSATSLAQVPGKHEH 85
Cdd:PRK14570 7 LIFGGVSFEHEISLRSAYGIYSALlKLDKYNIYSVFIDKcTGIWYLLDS------VPDPPKLIKRDVLPIVSLIPGCGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 86 QlidaqNGQPLpTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLTR-- 163
Cdd:PRK14570 81 V-----NNKNL-EIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIGFRKyd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 164 --ANRNNISfAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDNPQA 241
Cdd:PRK14570 155 yfLDKEGIK-KDIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGNEQIKI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 242 STCGEIVLTS-DFYAYDTKYIDEDGAKVV--VPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPE-NEVVINEIN 317
Cdd:PRK14570 234 FTPGEIVVQDfIFYDYDAKYSTIPGNSIVfnIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDtGLIYLNEIN 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 446335834 318 TLPGFTNISMYPKLWQASGLGYTDLITRLIELALERHA 355
Cdd:PRK14570 314 TIPGFTDISMFAKMCEHDGLQYKSLVDNLIDLAFQSYI 351
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
3-352 |
6.20e-56 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 186.26 E-value: 6.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 3 KLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWHVSdaSNYLLNADDPAHIALRPSATSLAQVPGK 82
Cdd:PRK14572 1 MAKIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPILLTPDGGWVVP--TVYRPSIPDESGNSEDLFLEEFQKANGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 83 HEHQLIDAQNgqplptVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLT 162
Cdd:PRK14572 79 SEPADISQLD------ADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFFELE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 163 RANRNNISFAEVES--KLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVL-----G 235
Cdd:PRK14572 153 KLKYLNSPRKTLLKleSLGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLeryrgG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 236 NDNPQASTCGEIVLTSDFYAYDTKYiDEDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDvFLTPENEVVINE 315
Cdd:PRK14572 233 KRNPIALPATEIVPGGEFFDFESKY-KQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTD-FIIVDGEPHILE 310
|
330 340 350
....*....|....*....|....*....|....*..
gi 446335834 316 INTLPGFTNISMYPKLWQASGLGYTDLITRLIELALE 352
Cdd:PRK14572 311 TNTLPGMTETSLIPQQAKAAGINMEEVFTDLIEIGLK 347
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
2-353 |
2.84e-54 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 190.80 E-value: 2.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 2 EKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWhvSDASNYLLNADDPAhialrpsatslaqvpG 81
Cdd:PRK14573 450 KKLSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVSYFLINRQGLW--ETVSSLETAIEEDS---------------G 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 82 KHehqLIDAQNGQPLPTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITL 161
Cdd:PRK14573 513 KS---VLSSEIAQALAKVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPL 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 162 TRA--NRN-NISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKG-REIECAVLGND 237
Cdd:PRK14573 590 TLAgwKREpELCLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESRLGsREIEVSCLGDG 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 238 N-------PQaSTCGEivltSDFYAYDTKY--IDEDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPE 308
Cdd:PRK14573 670 SsayviagPH-ERRGS----GGFIDYQEKYglSGKSSAQIVFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEE 744
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446335834 309 NEVVINEINTLPGFTNISMYPKLWQASGLGYTDLITRLIELALER 353
Cdd:PRK14573 745 GNFWLSEMNPIPGMTEASPFLTAFVRKGWTYEQIVHQLIIDGLHK 789
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
4-350 |
1.38e-49 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 168.46 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 4 LRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKqgqwhvsdasNYLLNADDpahialrpsatslaqvpgkh 83
Cdd:PRK14571 1 MRVALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDVDE----------DFLKKVDQ-------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 84 ehqlidaqngqpLPTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAgLNIAPFITltr 163
Cdd:PRK14571 51 ------------LKSFDVVFNVLHGTFGEDGTLQAILDFLGIRYTGSDAFSSMICFDKLLTYRFLKGT-VEIPDFVE--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 164 anrnnISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLG-NDNPQAS 242
Cdd:PRK14571 115 -----IKEFMKTSPLGYPCVVKPRREGSSIGVFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILEtEKGFEVL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 243 TCGEIVLTSDFYAYDTKYIDEDgAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTpENEVVINEINTLPGF 322
Cdd:PRK14571 190 PILELRPKRRFYDYVAKYTKGE-TEFILPAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIFS-DGRFYFLEINTVPGL 267
|
330 340
....*....|....*....|....*...
gi 446335834 323 TNISMYPKLWQASGLGYTDLITRLIELA 350
Cdd:PRK14571 268 TELSDLPASAKAGGIEFEELVDIIIKSA 295
|
|
| Dala_Dala_lig_N |
pfam01820 |
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ... |
5-130 |
1.05e-44 |
|
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: 149.68 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 5 RVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWHvsDASNYLLNADDPAHIALRPSAtslaqvPGKHE 84
Cdd:pfam01820 1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIGITKDGRLG--EAALRELASDDGLLLEVDDAP------DGGPA 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446335834 85 HQLIDAQNGQPLPTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGS 130
Cdd:pfam01820 73 GLLFGPNVLELLIEVDVVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
1-350 |
8.30e-34 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 126.71 E-value: 8.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 1 MEKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVllGIDKQGQWHVSDAsnyllnaddpahIALRPsatslaqvp 80
Cdd:PRK14569 1 MKNEKIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAV--GVDASGKELVAKL------------LELKP--------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 81 gkhehqlidaqngqplptvDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLN--IAPF 158
Cdd:PRK14569 58 -------------------DKCFVALHGEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPtpMAKF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 159 ITLTRANRNNISFaevesklglPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDhKVIVEQGIKGREIECAVLGNDn 238
Cdd:PRK14569 119 LTDKLVAEDEISF---------PVAVKPSSGGSSIATFKVKSIQELKHAYEEASKYG-EVMIEQWVTGKEITVAIVNDE- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 239 pqASTCGEIVLTSDFYAYDTKYideDGAKVV-VPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEIN 317
Cdd:PRK14569 188 --VYSSVWIEPQNEFYDYESKY---SGKSIYhSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEIN 262
|
330 340 350
....*....|....*....|....*....|...
gi 446335834 318 TLPGFTNISMYPKLWQASGLGYTDLITRLIELA 350
Cdd:PRK14569 263 SSPGMTDNSLSPKSAAAEGVDFDSFVKRIIEQA 295
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
124-351 |
3.77e-26 |
|
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: 105.34 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 124 NLPFVGSDvlASAACMDKDVTKRLLRDAGLNIAPFITLTRANRNnISFAEvesKLGLPLFVKPANQGSSVGVSKVTSEEQ 203
Cdd:COG0439 40 GLPGPSPE--AIRAMRDKVLMREALAAAGVPVPGFALVDSPEEA-LAFAE---EIGYPVVVKPADGAGSRGVRVVRDEEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 204 YAIAVDLA------FEFDHKVIVEQGIKGREIECAVLGNDnpqastcGEIVLTSDF-YAYDTKYIDEDGAkvVVPAAIAP 276
Cdd:COG0439 114 LEAALAEAraeakaGSPNGEVLVEEFLEGREYSVEGLVRD-------GEVVVCSITrKHQKPPYFVELGH--EAPSPLPE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446335834 277 EINDKIRAIAVQAYQTLG-CAGMARVDVFLTPENEVVINEINT-LPGftniSMYPKLWQ-ASGLgytDLITRLIELAL 351
Cdd:COG0439 185 ELRAEIGELVARALRALGyRRGAFHTEFLLTPDGEPYLIEINArLGG----EHIPPLTElATGV---DLVREQIRLAL 255
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
93-356 |
5.57e-15 |
|
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: 74.21 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 93 GQPLPTVDVIF----PIVHGTlgedgslqGMLRVA---NLPFVgSDVLASAACMDKDVTKRLLRDAGLNIAPfitlTRAN 165
Cdd:COG0189 51 GEDLSEFDAVLpridPPFYGL--------ALLRQLeaaGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPP----TLVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 166 RNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQ----GIKGREIECAVLGndnpqa 241
Cdd:COG0189 118 RDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSEPVLVQefipEEDGRDIRVLVVG------ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 242 stcGEIVltsdfYAYDtKYIDEDGAKVVVPA---AIAPEINDKIRAIAVQAYQTLGcAGMARVDVFLTPENEVVInEINT 318
Cdd:COG0189 192 ---GEPV-----AAIR-RIPAEGEFRTNLARggrAEPVELTDEERELALRAAPALG-LDFAGVDLIEDDDGPLVL-EVNV 260
|
250 260 270
....*....|....*....|....*....|....*...
gi 446335834 319 LPGFTNISmypklwQASGLgytDLITRLIElALERHAA 356
Cdd:COG0189 261 TPGFRGLE------RATGV---DIAEAIAD-YLEARAA 288
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
149-316 |
5.35e-13 |
|
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: 66.51 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 149 RDAGLNIAPFITLTRANrnniSFAEVESKLGLPLFVKPANQGSS-VGVSKVTSEEQYAIAVDLAFefDHKVIVEQGIKgR 227
Cdd:pfam02222 1 QKLGLPTPRFMAAESLE----ELIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELG--DGPVIVEEFVP-F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 228 EIECAVLGNDNPQASTcgeivltsdfYAYD---TKYIDEDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVF 304
Cdd:pfam02222 74 DRELSVLVVRSVDGET----------AFYPvveTIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELF 143
|
170
....*....|..
gi 446335834 305 LTPENEVVINEI 316
Cdd:pfam02222 144 VTEDGDLLINEL 155
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
138-317 |
3.61e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 66.45 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 138 CMDKDVTKRLLRDAGLNIApfITLTRANRNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQyaiaVDLAFEFDHK 217
Cdd:PRK12767 109 CNDKWLTYEFLKENGIPTP--KSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEE----LEFLLEYVPN 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 218 VIVEQGIKGREIECAVL--GNDNPQASTCGE-IVLTSDfyAYDTKYIDEDgakvvvpaaiaPEINDKIRAIAvqayQTLG 294
Cdd:PRK12767 183 LIIQEFIEGQEYTVDVLcdLNGEVISIVPRKrIEVRAG--ETSKGVTVKD-----------PELFKLAERLA----EALG 245
|
170 180
....*....|....*....|...
gi 446335834 295 CAGMARVDVFLTpENEVVINEIN 317
Cdd:PRK12767 246 ARGPLNIQCFVT-DGEPYLFEIN 267
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
129-316 |
7.68e-10 |
|
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: 59.70 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 129 GSDVLAsaACMDKDVTKRLLRDAGLNIAPFITLTranrnniSFAEVES---KLGLPLFVKPANQGSS-VGVSKVTSEEQY 204
Cdd:COG0026 80 GPEALE--IAQDRLLEKAFLAELGIPVAPFAAVD-------SLEDLEAaiaELGLPAVLKTRRGGYDgKGQVVIKSAADL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 205 AIAVDlafEFDHK-VIVEQGIK-GREIecAVLGNDNPQastcGEIVltsdfyAYD-TKYIDEDG--AKVVVPAAIAPEIN 279
Cdd:COG0026 151 EAAWA---ALGGGpCILEEFVPfEREL--SVIVARSPD----GEVA------TYPvVENVHRNGilDESIAPARISEALA 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 446335834 280 DKIRAIAVQAYQTLGCAG-MArVDVFLTPENEVVINEI 316
Cdd:COG0026 216 AEAEEIAKRIAEALDYVGvLA-VEFFVTKDGELLVNEI 252
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
127-316 |
2.09e-09 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 58.24 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 127 FVGSDVLASAAcmDKDVTKRLLRDAGLNIAPFITLTRANrnniSFAEVESKLGLPLFVKPANQGss-vGVSKVTSEEQYA 205
Cdd:PRK06019 89 PPGPDALAIAQ--DRLTEKQFLDKLGIPVAPFAVVDSAE----DLEAALADLGLPAVLKTRRGGydgkGQWVIRSAEDLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 206 IAVDlafEFDHK-VIVEQGIKGREiECAVLGNDNPQastcGEIVltsdfyAYD-TKYIDEDG--AKVVVPAAIAPEINDK 281
Cdd:PRK06019 163 AAWA---LLGSVpCILEEFVPFER-EVSVIVARGRD----GEVV------FYPlVENVHRNGilRTSIAPARISAELQAQ 228
|
170 180 190
....*....|....*....|....*....|....*.
gi 446335834 282 IRAIAVQAYQTLGCAG-MArVDVFLTPENEVVINEI 316
Cdd:PRK06019 229 AEEIASRIAEELDYVGvLA-VEFFVTGDGELLVNEI 263
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
137-228 |
2.94e-08 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 55.55 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 137 ACmDKDVTKRLLRDAGLNIApfitLTRANRNNISFAEVESKLGLPLFVKP--ANQGSsvGVS-KVTSEEQYAIAVDLAFE 213
Cdd:PRK14016 212 AC-DKELTKRLLAAAGVPVP----EGRVVTSAEDAWEAAEEIGYPVVVKPldGNHGR--GVTvNITTREEIEAAYAVASK 284
|
90
....*....|....*
gi 446335834 214 FDHKVIVEQGIKGRE 228
Cdd:PRK14016 285 ESSDVIVERYIPGKD 299
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
131-237 |
5.64e-07 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 51.47 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 131 DVLASAACMD-KDVTKRLLRDAGLNI---APFITLTRANRnniSFAEVESKlglPLFVKPANQGSSVGVS---KVTSEEQ 203
Cdd:PRK02471 478 DNYISPLIMEnKVVTKKILAEAGFPVpagDEFTSLEEALA---DYSLFADK---AIVVKPKSTNFGLGISifkEPASLED 551
|
90 100 110
....*....|....*....|....*....|....
gi 446335834 204 YAIAVDLAFEFDHKVIVEQGIKGREIECAVLGND 237
Cdd:PRK02471 552 YEKALEIAFREDSSVLVEEFIVGTEYRFFVLDGK 585
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
134-328 |
3.07e-05 |
|
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: 45.03 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 134 ASAACMDKDVTKRLLRDAGLNIApfITLTRANRNN-ISFAEvesKLGLPLFVKPANQGSSVGVSKVTsEEQYAIAVDLAF 212
Cdd:TIGR00768 82 AILNAGDKFLSHQLLAKAGIPLP--RTGLAGSPEEaLKLIE---EIGFPVVLKPVFGSWGRGVSLAR-DRQAAESLLEHF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 213 E----FDHKVIVEQGIK---GREIECAVLGNDNPQA-STCGEivltSDFYAYDTKyidedGAKvvvpaAIAPEINDKIRA 284
Cdd:TIGR00768 156 EqlngPQNLFLVQEYIKkpgGRDIRVFVVGDEVVAAiYRITS----GHWRSNLAR-----GGK-----AEPCSLTEEIEE 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446335834 285 IAVQAYQTLGcAGMARVDvFLTPENEVVINEINTLPGFTNISMY 328
Cdd:TIGR00768 222 LAIKAAKALG-LDVAGVD-LLESEDGLLVNEVNANPEFKNSVKT 263
|
|
| PRK10446 |
PRK10446 |
30S ribosomal protein S6--L-glutamate ligase; |
179-362 |
1.58e-04 |
|
30S ribosomal protein S6--L-glutamate ligase;
Pssm-ID: 182468 [Multi-domain] Cd Length: 300 Bit Score: 42.97 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 179 GLPLFVKPANQGSSVGVskVTSE-EQYAIAVDLAFE-FDHKVIVEQGI---KGREIECAVLGNdnpqastcgEIVLTSDF 253
Cdd:PRK10446 135 GAPLVVKLVEGTQGIGV--VLAEtRQAAESVIDAFRgLNAHILVQEYIkeaQGCDIRCLVVGD---------EVVAAIER 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 254 YAYDTKY---IDEDGAKVVVpaaiapEINDKIRAIAVQAYQTLGCaGMARVDVFLTPENEVVInEINTLPGFTNISmypk 330
Cdd:PRK10446 204 RAKEGDFrsnLHRGGAASVA------SITPQEREIAIKAARTMAL-DVAGVDILRANRGPLVM-EVNASPGLEGIE---- 271
|
170 180 190
....*....|....*....|....*....|...
gi 446335834 331 lwQASGLgytDLITRLIELaLERHAADN-ALKT 362
Cdd:PRK10446 272 --KTTGI---DIAGKMIRW-IERHATTEyCLKT 298
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
268-316 |
6.13e-04 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 41.58 E-value: 6.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446335834 268 VVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEI 316
Cdd:PLN02948 238 VEAPANVPWKVAKLATDVAEKAVGSLEGAGVFGVELFLLKDGQILLNEV 286
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
125-346 |
6.51e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 41.76 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 125 LPfvGSDVLASAACMDKDVTKRLLRDAGLNIAPfitlTRANRNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQY 204
Cdd:PRK02186 94 LP--AANTEAIRTCRDKKRLARTLRDHGIDVPR----THALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 205 -AIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDNPQAStcgeIVLTSDFYAYDTKYIDedgAKVVVPAAIAPEINDKIR 283
Cdd:PRK02186 168 aAHCAALRRAGTRAALVQAYVEGDEYSVETLTVARGHQV----LGITRKHLGPPPHFVE---IGHDFPAPLSAPQRERIV 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446335834 284 AIAVQAYQTLGCA-GMARVDVFLTpENEVVINEINT-LPGftniSMYPKLW-QASGLGYTDLITRL 346
Cdd:PRK02186 241 RTVLRALDAVGYAfGPAHTELRVR-GDTVVIIEINPrLAG----GMIPVLLeEAFGVDLLDHVIDL 301
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
108-318 |
4.72e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 38.92 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 108 GTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPfiTLTRANRNNISFAEVESKLGLPLFVKPA 187
Cdd:PRK05586 83 GFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVP--GSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 188 NQGSSVGVSKVTSEEQYAIAVD------LAFEFDHKVIVEQGI-KGREIECAVLGNDnpqastCGEIVLTSD----FYAY 256
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNtakseaKAAFGDDSMYIEKFIeNPKHIEFQILGDN------YGNVVHLGErdcsLQRR 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446335834 257 DTKYIDEDGAKVvvpaaIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINT 318
Cdd:PRK05586 235 NQKVLEEAPSPV-----MTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNT 291
|
|
|