|
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: 543.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 1 MAKMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWHINDAGNYLLNAQDPARIALRpstvtlaqip 80
Cdd:PRK01966 1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADDDNDKEDLS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 81 greaqQLINAESGQplAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK01966 71 -----LLILPSGGS--EEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 161 LTRANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDhPQ 240
Cdd:PRK01966 144 LTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 241 ASTCGEIVLNSEFYAYDTKYIDDQgAQVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTLP 320
Cdd:PRK01966 223 ASVPGEIVKPDDFYDYEAKYLDGS-AELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMP 301
|
330 340 350
....*....|....*....|....*....|..
gi 1319839448 321 GFTNISMYPKLWQASGLDYTSLITRLIELALE 352
Cdd:PRK01966 302 GFTPISMYPKLWEASGLSYPELIDRLIELALE 333
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
4-351 |
1.52e-159 |
|
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: 449.17 E-value: 1.52e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 4 MRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLwhindagnyllnaqdPARIALrpstvtlaqipgre 83
Cdd:COG1181 1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVEDL---------------PAALKE-------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 84 aqqlinaesgqplAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFITLTR 163
Cdd:COG1181 52 -------------LKPDVVFPALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 164 ANRAqfSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDHPQAST 243
Cdd:COG1181 119 GELA--DLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGPRALP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 244 CGEIVLNSEFYAYDTKYIDDqGAQVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTLPGFT 323
Cdd:COG1181 197 PIEIVPENGFYDYEAKYTDG-GTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMT 275
|
330 340
....*....|....*....|....*...
gi 1319839448 324 NISMYPKLWQASGLDYTSLITRLIELAL 351
Cdd:COG1181 276 PTSLLPKAAAAAGISYEELIERIIELAL 303
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
5-350 |
8.31e-152 |
|
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: 430.17 E-value: 8.31e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 5 RVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWhindagnyllNAQDPARIALrpstvtlaqipgrea 84
Cdd:TIGR01205 1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSW----------TYKDLPQLIL--------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 85 qqlinaESGQPLAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFITLTRa 164
Cdd:TIGR01205 56 ------ELGALLEGIDVVFPVLHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQ- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 165 NRAQFSFAD---VEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDH--P 239
Cdd:TIGR01205 129 NRASADELEceqVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEalP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 240 QASTCGEIVLnseFYAYDTKYIDDqGAQVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTL 319
Cdd:TIGR01205 209 IIEIVPEIEG---FYDYEAKYLDG-STEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTI 284
|
330 340 350
....*....|....*....|....*....|.
gi 1319839448 320 PGFTNISMYPKLWQASGLDYTSLITRLIELA 350
Cdd:TIGR01205 285 PGMTAISLFPKAAAAAGIEFSQLVERILELA 315
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
1-353 |
7.96e-110 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 323.22 E-value: 7.96e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 1 MAKMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVllGIDkqglwhindagnyllnaqdparialrpstvtlaqiP 80
Cdd:PRK01372 2 KMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAH--PID-----------------------------------P 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 81 GREAQQLINAEsgqplaAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK01372 45 GEDIAAQLKEL------GFDRVFNALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 161 LTRANraqfSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNdhpQ 240
Cdd:PRK01372 119 LTREE----DLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGG---K 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 241 ASTCGEIVLNSEFYAYDTKYIDDqGAQVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTLP 320
Cdd:PRK01372 192 ALPVIEIVPAGEFYDYEAKYLAG-GTQYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQP 270
|
330 340 350
....*....|....*....|....*....|...
gi 1319839448 321 GFTNISMYPKLWQASGLDYTSLITRLIELALER 353
Cdd:PRK01372 271 GMTSHSLVPMAARAAGISFSELVDRILEDALCD 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 |
3.80e-107 |
|
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: 312.33 E-value: 3.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 147 LLRDAGLAVAPFITLTRANRAQ---FSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQG 223
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRADWKLnpkEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 224 IKGREIECAVLGNDHPQASTCGEIVLNSEFYAYDTKYIDDqGAQVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDV 303
Cdd:pfam07478 81 IEGREIECAVLGNEDPEVSPVGEIVPSGGFYDYEAKYIDD-SAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1319839448 304 FLTADNEVVINEINTLPGFTNISMYPKLWQASGLDYTSLITRLIE 348
Cdd:pfam07478 160 FLTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
3-355 |
6.77e-75 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 235.88 E-value: 6.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 3 KMRVGIVFGGKSAEHEVSLQSAKNIVEAI-DKSRFDVVLLGIDK-QGLWHINDAgnyllnAQDPARIALRPSTVTLAQIP 80
Cdd:PRK14570 2 KKNLMLIFGGVSFEHEISLRSAYGIYSALlKLDKYNIYSVFIDKcTGIWYLLDS------VPDPPKLIKRDVLPIVSLIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 81 GreAQQLINAESGQplaaIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK14570 76 G--CGIFVNNKNLE----IDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 161 LTR----ANRAQFSfADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGN 236
Cdd:PRK14570 150 FRKydyfLDKEGIK-KDIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 237 DHPQASTCGEIVLNS-EFYAYDTKYIDDQGAQVV--VPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTAD-NEVV 312
Cdd:PRK14570 229 EQIKIFTPGEIVVQDfIFYDYDAKYSTIPGNSIVfnIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDtGLIY 308
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1319839448 313 INEINTLPGFTNISMYPKLWQASGLDYTSLITRLIELALERHA 355
Cdd:PRK14570 309 LNEINTIPGFTDISMFAKMCEHDGLQYKSLVDNLIDLAFQSYI 351
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
3-353 |
4.08e-56 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 196.19 E-value: 4.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 3 KMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWhindagnyllnaqdparialrpSTVTL--AQIP 80
Cdd:PRK14573 451 KLSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVSYFLINRQGLW----------------------ETVSSleTAIE 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 81 GREAQQLINAESGQPLAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK14573 509 EDSGKSVLSSEIAQALAKVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQP 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 161 LTRANRAQ---FSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKG-REIECAVLGN 236
Cdd:PRK14573 589 LTLAGWKRepeLCLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESRLGsREIEVSCLGD 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 237 dhpqASTCGEIVLNSE------FYAYDTKYIDD--QGAQVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTAD 308
Cdd:PRK14573 669 ----GSSAYVIAGPHErrgsggFIDYQEKYGLSgkSSAQIVFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEE 744
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1319839448 309 NEVVINEINTLPGFTNISMYPKLWQASGLDYTSLITRLIELALER 353
Cdd:PRK14573 745 GNFWLSEMNPIPGMTEASPFLTAFVRKGWTYEQIVHQLIIDGLHK 789
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
3-352 |
1.95e-55 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 185.11 E-value: 1.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 3 KMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWHINDAgnyllnaqdpARIALrPSTVTLAQIPGR 82
Cdd:PRK14572 1 MAKIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPILLTPDGGWVVPTV----------YRPSI-PDESGNSEDLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 83 EAQQLINAESGQPLAA---IDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFI 159
Cdd:PRK14572 70 EEFQKANGVSEPADISqldADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 160 TLTR---ANRAQFSFADVEAkLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVL-- 234
Cdd:PRK14572 150 ELEKlkyLNSPRKTLLKLES-LGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLer 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 235 ---GNDHPQASTCGEIVLNSEFYAYDTKYiDDQGAQVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDvFLTADNEV 311
Cdd:PRK14572 229 yrgGKRNPIALPATEIVPGGEFFDFESKY-KQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTD-FIIVDGEP 306
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1319839448 312 VINEINTLPGFTNISMYPKLWQASGLDYTSLITRLIELALE 352
Cdd:PRK14572 307 HILETNTLPGMTETSLIPQQAKAAGINMEEVFTDLIEIGLK 347
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
4-350 |
1.09e-49 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 168.85 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 4 MRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKqglwhindagNYLlnaqdparialrpstvtlaqipgRE 83
Cdd:PRK14571 1 MRVALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDVDE----------DFL-----------------------KK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 84 AQQLinaesgqplAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDaglavapfiTLTR 163
Cdd:PRK14571 48 VDQL---------KSFDVVFNVLHGTFGEDGTLQAILDFLGIRYTGSDAFSSMICFDKLLTYRFLKG---------TVEI 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 164 ANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLG-NDHPQAS 242
Cdd:PRK14571 110 PDFVEIKEFMKTSPLGYPCVVKPRREGSSIGVFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILEtEKGFEVL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 243 TCGEIVLNSEFYAYDTKYIDDQgAQVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTaDNEVVINEINTLPGF 322
Cdd:PRK14571 190 PILELRPKRRFYDYVAKYTKGE-TEFILPAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIFS-DGRFYFLEINTVPGL 267
|
330 340
....*....|....*....|....*...
gi 1319839448 323 TNISMYPKLWQASGLDYTSLITRLIELA 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 |
6.50e-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: 152.76 E-value: 6.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 5 RVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWHinDAGNYLLNAQDPARIALRpstvtlAQIPGREA 84
Cdd:pfam01820 1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIGITKDGRLG--EAALRELASDDGLLLEVD------DAPDGGPA 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1319839448 85 QQLINAESGQPLAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGS 130
Cdd:pfam01820 73 GLLFGPNVLELLIEVDVVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
1-350 |
3.58e-35 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 130.57 E-value: 3.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 1 MAKMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVllGIDKQGlwhiNDAGNYLLNaqdpariaLRPstvtlaqip 80
Cdd:PRK14569 1 MKNEKIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAV--GVDASG----KELVAKLLE--------LKP--------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 81 greaqqlinaesgqplaaiDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLA--VAPF 158
Cdd:PRK14569 58 -------------------DKCFVALHGEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPtpMAKF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 159 ITLTRANRAQFSFadveaklglPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDhKVVVEQGIKGREIECAVLGNDh 238
Cdd:PRK14569 119 LTDKLVAEDEISF---------PVAVKPSSGGSSIATFKVKSIQELKHAYEEASKYG-EVMIEQWVTGKEITVAIVNDE- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 239 pqASTCGEIVLNSEFYAYDTKYiddQGAQVV-VPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEIN 317
Cdd:PRK14569 188 --VYSSVWIEPQNEFYDYESKY---SGKSIYhSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEIN 262
|
330 340 350
....*....|....*....|....*....|...
gi 1319839448 318 TLPGFTNISMYPKLWQASGLDYTSLITRLIELA 350
Cdd:PRK14569 263 SSPGMTDNSLSPKSAAAEGVDFDSFVKRIIEQA 295
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
124-351 |
8.55e-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: 104.18 E-value: 8.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 124 NLPFVGSDVlgSAACMDKDVTKRLLRDAGLAVAPFITLTRANRAqfsfADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQ 203
Cdd:COG0439 40 GLPGPSPEA--IRAMRDKVLMREALAAAGVPVPGFALVDSPEEA----LAFAEEIGYPVVVKPADGAGSRGVRVVRDEEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 204 YHQAVALA------FEFDHKVVVEQGIKGREIECAVLGNDhpqastcGEIVLNSEF-YAYDTKYIDDQGAqvVVPAAIAP 276
Cdd:COG0439 114 LEAALAEAraeakaGSPNGEVLVEEFLEGREYSVEGLVRD-------GEVVVCSITrKHQKPPYFVELGH--EAPSPLPE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319839448 277 EINDKIRAIAVQAYQTLG-CSGMARVDVFLTADNEVVINEINT-LPGftniSMYPKLWQ-ASGLDytsLITRLIELAL 351
Cdd:COG0439 185 ELRAEIGELVARALRALGyRRGAFHTEFLLTPDGEPYLIEINArLGG----EHIPPLTElATGVD---LVREQIRLAL 255
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
91-356 |
3.41e-16 |
|
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: 78.06 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 91 ESGQPLAAIDVIF----PIVHGTlgedgSLQGMLRMANLPFVgSDVLGSAACMDKDVTKRLLRDAGLAVAPFITLTRANR 166
Cdd:COG0189 49 YRGEDLSEFDAVLpridPPFYGL-----ALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 167 AqfsfADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQ----GIKGREIECAVLGndhpqas 242
Cdd:COG0189 123 L----RAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSEPVLVQefipEEDGRDIRVLVVG------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 243 tcGEIVlnsefYAYdtKYIDDQGAQVVVPA----AIAPEINDKIRAIAVQAYQTLGCsGMARVDVFLTADNEVVInEINT 318
Cdd:COG0189 192 --GEPV-----AAI--RRIPAEGEFRTNLArggrAEPVELTDEERELALRAAPALGL-DFAGVDLIEDDDGPLVL-EVNV 260
|
250 260 270
....*....|....*....|....*....|....*...
gi 1319839448 319 LPGFTNISmypklwQASGLDytslITRLIELALERHAA 356
Cdd:COG0189 261 TPGFRGLE------RATGVD----IAEAIADYLEARAA 288
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
149-316 |
4.99e-15 |
|
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: 72.29 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 149 RDAGLAVAPFITLTRANraqfSFADVEAKLGLPLFVKPANQGSS-VGVSKVKNEEQYHQAVALAFefDHKVVVEQGIKgR 227
Cdd:pfam02222 1 QKLGLPTPRFMAAESLE----ELIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELG--DGPVIVEEFVP-F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 228 EIECAVLGndhpqASTcgeivLNSEFYAYD---TKYIDDQGAQVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVF 304
Cdd:pfam02222 74 DRELSVLV-----VRS-----VDGETAFYPvveTIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELF 143
|
170
....*....|..
gi 1319839448 305 LTADNEVVINEI 316
Cdd:pfam02222 144 VTEDGDLLINEL 155
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
138-317 |
4.24e-14 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 72.22 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 138 CMDKDVTKRLLRDAGLAVApfITLTRANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQyhqaVALAFEFDHK 217
Cdd:PRK12767 109 CNDKWLTYEFLKENGIPTP--KSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEE----LEFLLEYVPN 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 218 VVVEQGIKGREIECAVLgNDhpqastcgeivLNSEFYAYDT-KYID------DQGaqVVVPaaiAPEINDKIRAIAvqay 290
Cdd:PRK12767 183 LIIQEFIEGQEYTVDVL-CD-----------LNGEVISIVPrKRIEvragetSKG--VTVK---DPELFKLAERLA---- 241
|
170 180
....*....|....*....|....*..
gi 1319839448 291 QTLGCSGMARVDVFLTaDNEVVINEIN 317
Cdd:PRK12767 242 EALGARGPLNIQCFVT-DGEPYLFEIN 267
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
129-316 |
7.57e-12 |
|
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: 65.87 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 129 GSDVLgsAACMDKDVTKRLLRDAGLAVAPFITLTranraqfSFADVEA---KLGLPLFVKPANQGS-SVGVSKVKNEEQY 204
Cdd:COG0026 80 GPEAL--EIAQDRLLEKAFLAELGIPVAPFAAVD-------SLEDLEAaiaELGLPAVLKTRRGGYdGKGQVVIKSAADL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 205 HQAVALAFEFDhkVVVEQGIK-GREIecAVLGndhpqA-STCGEIVlnsefyAYD---TKYIDDQGAQVVVPAAIAPEIN 279
Cdd:COG0026 151 EAAWAALGGGP--CILEEFVPfEREL--SVIV-----ArSPDGEVA------TYPvveNVHRNGILDESIAPARISEALA 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 1319839448 280 DKIRAIAVQAYQTLGCSG-MArVDVFLTADNEVVINEI 316
Cdd:COG0026 216 AEAEEIAKRIAEALDYVGvLA-VEFFVTKDGELLVNEI 252
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
127-316 |
1.01e-09 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 59.40 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 127 FVGSDVLGSAAcmDKDVTKRLLRDAGLAVAPFITLTRANraqfSFADVEAKLGLPLFVKPANQGss-vGVSKVKNEEQYH 205
Cdd:PRK06019 89 PPGPDALAIAQ--DRLTEKQFLDKLGIPVAPFAVVDSAE----DLEAALADLGLPAVLKTRRGGydgkGQWVIRSAEDLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 206 QAVAlafEFDHK-VVVEQGIKGREiECAVLGndhpqA-STCGEIVlnsefyAYD-TKYIDDQG--AQVVVPAAIAPEIND 280
Cdd:PRK06019 163 AAWA---LLGSVpCILEEFVPFER-EVSVIV-----ArGRDGEVV------FYPlVENVHRNGilRTSIAPARISAELQA 227
|
170 180 190
....*....|....*....|....*....|....*..
gi 1319839448 281 KIRAIAVQAYQTLGCSG-MArVDVFLTADNEVVINEI 316
Cdd:PRK06019 228 QAEEIASRIAEELDYVGvLA-VEFFVTGDGELLVNEI 263
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
137-228 |
8.67e-09 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 57.09 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 137 ACmDKDVTKRLLRDAGLAVAPFITLTRANRAqfsfadVEA--KLGLPLFVKP--ANQGSsvGVS-KVKNEEQYHQAVALA 211
Cdd:PRK14016 212 AC-DKELTKRLLAAAGVPVPEGRVVTSAEDA------WEAaeEIGYPVVVKPldGNHGR--GVTvNITTREEIEAAYAVA 282
|
90
....*....|....*..
gi 1319839448 212 FEFDHKVVVEQGIKGRE 228
Cdd:PRK14016 283 SKESSDVIVERYIPGKD 299
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
141-237 |
7.00e-07 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 51.08 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 141 KDVTKRLLRDAGLAVAPFITLTRANRAQFSFADVEAKlglPLFVKPANQGSSVGVS---KVKNEEQYHQAVALAFEFDHK 217
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLFADK---AIVVKPKSTNFGLGISifkEPASLEDYEKALEIAFREDSS 565
|
90 100
....*....|....*....|
gi 1319839448 218 VVVEQGIKGREIECAVLGND 237
Cdd:PRK02471 566 VLVEEFIVGTEYRFFVLDGK 585
|
|
| PRK10446 |
PRK10446 |
30S ribosomal protein S6--L-glutamate ligase; |
179-363 |
1.18e-06 |
|
30S ribosomal protein S6--L-glutamate ligase;
Pssm-ID: 182468 [Multi-domain] Cd Length: 300 Bit Score: 49.51 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 179 GLPLFVKPANQGSSVGVSkVKNEEQYHQAVALAFE-FDHKVVVEQGI---KGREIECAVLGNdhpqastcgEIVLNSEFY 254
Cdd:PRK10446 135 GAPLVVKLVEGTQGIGVV-LAETRQAAESVIDAFRgLNAHILVQEYIkeaQGCDIRCLVVGD---------EVVAAIERR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 255 AYDTKYIDD--QGAqvvvpAAIAPEINDKIRAIAVQAYQTLGCSgMARVDVfLTADNEVVINEINTLPGFTNISmypklw 332
Cdd:PRK10446 205 AKEGDFRSNlhRGG-----AASVASITPQEREIAIKAARTMALD-VAGVDI-LRANRGPLVMEVNASPGLEGIE------ 271
|
170 180 190
....*....|....*....|....*....|..
gi 1319839448 333 QASGLDYTSLITRLIelalERHAADR-ALKTS 363
Cdd:PRK10446 272 KTTGIDIAGKMIRWI----ERHATTEyCLKTG 299
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
140-316 |
1.57e-05 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 46.59 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 140 DKDVTKRLLRDAGLAVAPFITLTRANRAQfsfaDVEAKLGLPLFVKP---ANQGSsvGVSKVKNEEQYHQAVALAFEFDH 216
Cdd:PLN02948 121 DKYAQKVHFSKHGIPLPEFMEIDDLESAE----KAGDLFGYPLMLKSrrlAYDGR--GNAVAKTEEDLSSAVAALGGFER 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 217 KVVVEQGIKGREiECAVL---GNDhpqastcGEIVLnseFYAYDTKYIDDQGAQVVVPAAIAPEINDKIRAIAVQAYQTL 293
Cdd:PLN02948 195 GLYAEKWAPFVK-ELAVMvarSRD-------GSTRC---YPVVETIHKDNICHVVEAPANVPWKVAKLATDVAEKAVGSL 263
|
170 180
....*....|....*....|...
gi 1319839448 294 GCSGMARVDVFLTADNEVVINEI 316
Cdd:PLN02948 264 EGAGVFGVELFLLKDGQILLNEV 286
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
92-318 |
2.40e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 45.89 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 92 SGQPLAAIDVIFPiVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPfitltranRAQFSF 171
Cdd:PRK08462 70 SAAEIFEADAIFP-GYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIP--------GSDGAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 172 ADVEA------KLGLPLFVKPANQGSSVGVSKVKNEEQYHQAV------ALAFEFDHKVVVEQGI-KGREIECAVLGNDH 238
Cdd:PRK08462 141 KSYEEakkiakEIGYPVILKAAAGGGGRGMRVVEDESDLENLYlaaeseALSAFGDGTMYMEKFInNPRHIEVQILGDKH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 239 PQASTCGEivLNSEFYAYDTKYIDDQGAQVvvpaaIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINT 318
Cdd:PRK08462 221 GNVIHVGE--RDCSLQRRHQKLIEESPAVV-----LDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNT 293
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
97-318 |
3.04e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 45.79 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 97 AAIDVIFPiVHGTLGEDGSLQGMLRMANLPFVGSdvlgSAACM----DKDVTKRLLRDAGLAVAPFITltranraqFSFA 172
Cdd:PRK06111 73 TGAEAIHP-GYGLLSENASFAERCKEEGIVFIGP----SADIIakmgSKIEARRAMQAAGVPVVPGIT--------TNLE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 173 DVE------AKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVAL----AFEF--DHKVVVEQGI-KGREIECAVLGNDHp 239
Cdd:PRK06111 140 DAEeaiaiaRQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESnkkrAANFfgNGEMYIEKYIeDPRHIEIQLLADTH- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 240 qastcGEIVlnsefYAYDTKYIDDQGAQVVVPAAIAPEINDKIRA----IAVQAYQTLGCSGMARVDVFLTADNEVVINE 315
Cdd:PRK06111 219 -----GNTV-----YLWERECSVQRRHQKVIEEAPSPFLDEETRKamgeRAVQAAKAIGYTNAGTIEFLVDEQKNFYFLE 288
|
...
gi 1319839448 316 INT 318
Cdd:PRK06111 289 MNT 291
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
136-347 |
5.60e-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: 44.26 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 136 AACMDKDVTKRLLRDAGLAVApfITLTRANRAQFS-FADveaKLGLPLFVKPANQGSSVGVSKVkNEEQYHQAVALAFE- 213
Cdd:TIGR00768 84 LNAGDKFLSHQLLAKAGIPLP--RTGLAGSPEEALkLIE---EIGFPVVLKPVFGSWGRGVSLA-RDRQAAESLLEHFEq 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 214 ---FDHKVVVEQGIK---GREIECAVLGndhpqastcGEIVLnsefyAYDTKYIDDQGAQVVVPAAIAP-EINDKIRAIA 286
Cdd:TIGR00768 158 lngPQNLFLVQEYIKkpgGRDIRVFVVG---------DEVVA-----AIYRITSGHWRSNLARGGKAEPcSLTEEIEELA 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319839448 287 VQAYQTLGcSGMARVDvFLTADNEVVINEINTLPGFTNISMYpklwqaSGLDYTSLITRLI 347
Cdd:TIGR00768 224 IKAAKALG-LDVAGVD-LLESEDGLLVNEVNANPEFKNSVKT------TGVNIAGKLLDYI 276
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
108-318 |
5.72e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 41.62 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 108 GTLGEDGSLQGMLRMANLPFVGSDvlgsAACMD----KDVTKRLLRDAGLAVAP-FITLTRANRAQFSFADveaKLGLPL 182
Cdd:PRK05586 83 GFLSENSKFAKMCKECNIVFIGPD----SETIElmgnKSNAREIMIKAGVPVVPgSEGEIENEEEALEIAK---EIGYPV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 183 FVKPANQGSSVGVSKVKNEEQYHQAV------ALAFEFDHKVVVEQGI-KGREIECAVLGNDHPQASTCGEIVLNSEfya 255
Cdd:PRK05586 156 MVKASAGGGGRGIRIVRSEEELIKAFntakseAKAAFGDDSMYIEKFIeNPKHIEFQILGDNYGNVVHLGERDCSLQ--- 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319839448 256 ydtkyiddQGAQVVVPAAIAPEINDKIRA----IAVQAYQTLGCSGMARVDVFLTADNEVVINEINT 318
Cdd:PRK05586 233 --------RRNQKVLEEAPSPVMTEELRKkmgeIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNT 291
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
178-209 |
7.66e-04 |
|
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: 39.57 E-value: 7.66e-04
10 20 30
....*....|....*....|....*....|..
gi 1319839448 178 LGLPLFVKPANQGSSVGVSKVKNEEQYHQAVA 209
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFA 32
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
125-346 |
2.02e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 40.22 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 125 LPfvGSDVLGSAACMDKDVTKRLLRDAGLAVAPfitlTRANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQY 204
Cdd:PRK02186 94 LP--AANTEAIRTCRDKKRLARTLRDHGIDVPR----THALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 205 --HQAVALAfEFDHKVVVEQGIKGREIECAVLGNDHPQAstCGEIVlnSEFYAYDTKYIDdqgAQVVVPAAIAPEINDKI 282
Cdd:PRK02186 168 aaHCAALRR-AGTRAALVQAYVEGDEYSVETLTVARGHQ--VLGIT--RKHLGPPPHFVE---IGHDFPAPLSAPQRERI 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319839448 283 RAIAVQAYQTLGCS-GMARVDVFLTADNEVVInEINT-LPGftniSMYPKLW-QASGLDYTSLITRL 346
Cdd:PRK02186 240 VRTVLRALDAVGYAfGPAHTELRVRGDTVVII-EINPrLAG----GMIPVLLeEAFGVDLLDHVIDL 301
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
177-331 |
6.52e-03 |
|
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: 37.48 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319839448 177 KLGLPLFVKPANQGSSVGVSKVKNEEQyhqAVALAFEFDHKVVVEQGIK---GREIECAVLGNDhpQASTCGEIVLNSEF 253
Cdd:pfam08443 38 KRQFPVIVKSIYGSQGIGVFLAEDEQK---LRQTLSATNEQILVQEFIAeanNEDIRCLVVGDQ--VVGALHRQSNEGDF 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319839448 254 YAYDTKyiddqGAqVVVPAAIAPEIndkiRAIAVQAYQTLGCSgMARVDVFLTADNEVVInEINTLPGFTNISMYPKL 331
Cdd:pfam08443 113 RSNLHR-----GG-VGEKYQLSQEE----TELAIKAAQAMQLD-VAGVDLLRQKRGLLVC-EVNSSPGLEGIEKTLGI 178
|
|
|