|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
1-322 |
3.10e-136 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 389.48 E-value: 3.10e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 1 MKRNIAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNLYIVEM-EGRRWEVQLPDGNKVP---VDRNDFSFTNGTEKVV-- 74
Cdd:PRK01966 2 MKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGItKDGRWYLIDADNMELAdddNDKEDLSLLILPSGGSee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 75 FDFAYITIHGTPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQ--SVSDEEVVEKI 152
Cdd:PRK01966 82 VDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTRGDweEASLAEIEAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 153 GLPCFIKPSLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKTKEKsvIFPPTEVVTHNEFFDYD 232
Cdd:PRK01966 162 GLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGNDPK--ASVPGEIVKPDDFYDYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 233 AKYN-GQVDEITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLD 311
Cdd:PRK01966 240 AKYLdGSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMPGFTPISMYPKLWEASGLS 319
|
330
....*....|.
gi 1074127292 312 IKDVMTDIIEN 322
Cdd:PRK01966 320 YPELIDRLIEL 330
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
4-322 |
1.35e-122 |
|
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: 353.64 E-value: 1.35e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 4 NIAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNLYIVEmegrrwevqlpdgnkvpVDRNDFSFTNGTEKvvFDFAYITIH 83
Cdd:COG1181 2 RVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIG-----------------IDVEDLPAALKELK--PDVVFPALH 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 84 GTPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQSVSDEEVVEKIGLPCFIKPSLG 163
Cdd:COG1181 63 GRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPARE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 164 GSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKTKEKsVIFPPTEVVTHNEFFDYDAKYN-GQVDEI 242
Cdd:COG1181 143 GSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGP-RALPPIEIVPENGFYDYEAKYTdGGTEYI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 243 TPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLDIKDVMTDIIEN 322
Cdd:COG1181 222 CPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLLPKAAAAAGISYEELIERIIEL 301
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
5-322 |
1.81e-89 |
|
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: 269.92 E-value: 1.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 5 IAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNLYIVEMEgrrwevqlPDGNKVPVDRNDFSFTNGTEKVVFDFAYITIHG 84
Cdd:TIGR01205 2 VAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDID--------KMGSWTYKDLPQLILELGALLEGIDVVFPVLHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 85 TPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQS----VSDEEVVEKIGLPCFIKP 160
Cdd:TIGR01205 74 RYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQNRAsadeLECEQVAEPLGFPVIVKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 161 SLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKTKEKSVIFPPTEVVThnEFFDYDAKYN-GQV 239
Cdd:TIGR01205 154 AREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEALPIIEIVPEIE--GFYDYEAKYLdGST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 240 DEITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLDIKDVMTDI 319
Cdd:TIGR01205 232 EYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTAISLFPKAAAAAGIEFSQLVERI 311
|
...
gi 1074127292 320 IEN 322
Cdd:TIGR01205 312 LEL 314
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
124-321 |
2.66e-51 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 168.65 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 124 LKAFGVRIAESLLLRQGQSVSD-----EEVVEKIGLPCFIKPSLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFM 198
Cdd:pfam07478 2 LKAAGLPVVPFVTFTRADWKLNpkewcAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 199 DGTELTCGCYKTkEKSVIFPPTEVVTHNEFFDYDAKY-NGQVDEITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYI 277
Cdd:pfam07478 82 EGREIECAVLGN-EDPEVSPVGEIVPSGGFYDYEAKYiDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDFF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1074127292 278 ITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLDIKDVMTDIIE 321
Cdd:pfam07478 161 LTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
1-322 |
3.10e-136 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 389.48 E-value: 3.10e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 1 MKRNIAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNLYIVEM-EGRRWEVQLPDGNKVP---VDRNDFSFTNGTEKVV-- 74
Cdd:PRK01966 2 MKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGItKDGRWYLIDADNMELAdddNDKEDLSLLILPSGGSee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 75 FDFAYITIHGTPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQ--SVSDEEVVEKI 152
Cdd:PRK01966 82 VDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTRGDweEASLAEIEAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 153 GLPCFIKPSLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKTKEKsvIFPPTEVVTHNEFFDYD 232
Cdd:PRK01966 162 GLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGNDPK--ASVPGEIVKPDDFYDYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 233 AKYN-GQVDEITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLD 311
Cdd:PRK01966 240 AKYLdGSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMPGFTPISMYPKLWEASGLS 319
|
330
....*....|.
gi 1074127292 312 IKDVMTDIIEN 322
Cdd:PRK01966 320 YPELIDRLIEL 330
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
4-322 |
1.35e-122 |
|
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: 353.64 E-value: 1.35e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 4 NIAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNLYIVEmegrrwevqlpdgnkvpVDRNDFSFTNGTEKvvFDFAYITIH 83
Cdd:COG1181 2 RVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIG-----------------IDVEDLPAALKELK--PDVVFPALH 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 84 GTPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQSVSDEEVVEKIGLPCFIKPSLG 163
Cdd:COG1181 63 GRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPARE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 164 GSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKTKEKsVIFPPTEVVTHNEFFDYDAKYN-GQVDEI 242
Cdd:COG1181 143 GSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGP-RALPPIEIVPENGFYDYEAKYTdGGTEYI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 243 TPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLDIKDVMTDIIEN 322
Cdd:COG1181 222 CPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLLPKAAAAAGISYEELIERIIEL 301
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
1-321 |
6.35e-93 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 278.53 E-value: 6.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 1 MKRNIAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNLYIVEMeGRRWEVQLpdgnkvpvdrndfsftngtEKVVFDFAYI 80
Cdd:PRK01372 3 MFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPIDP-GEDIAAQL-------------------KELGFDRVFN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 81 TIHGTPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQSvsDEEVVEKIGLPCFIKP 160
Cdd:PRK01372 63 ALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREED--LLAAIDKLGLPLVVKP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 161 SLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKTKeksvIFPPTEVVTHNEFFDYDAKY-NGQV 239
Cdd:PRK01372 141 AREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGGK----ALPVIEIVPAGEFYDYEAKYlAGGT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 240 DEITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLDIKDVMTDI 319
Cdd:PRK01372 217 QYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSHSLVPMAARAAGISFSELVDRI 296
|
..
gi 1074127292 320 IE 321
Cdd:PRK01372 297 LE 298
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
5-322 |
1.81e-89 |
|
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: 269.92 E-value: 1.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 5 IAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNLYIVEMEgrrwevqlPDGNKVPVDRNDFSFTNGTEKVVFDFAYITIHG 84
Cdd:TIGR01205 2 VAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDID--------KMGSWTYKDLPQLILELGALLEGIDVVFPVLHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 85 TPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQS----VSDEEVVEKIGLPCFIKP 160
Cdd:TIGR01205 74 RYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQNRAsadeLECEQVAEPLGFPVIVKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 161 SLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKTKEKSVIFPPTEVVThnEFFDYDAKYN-GQV 239
Cdd:TIGR01205 154 AREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEALPIIEIVPEIE--GFYDYEAKYLdGST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 240 DEITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLDIKDVMTDI 319
Cdd:TIGR01205 232 EYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTAISLFPKAAAAAGIEFSQLVERI 311
|
...
gi 1074127292 320 IEN 322
Cdd:TIGR01205 312 LEL 314
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
2-321 |
2.40e-78 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 242.89 E-value: 2.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 2 KRNIAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNL--YIVEMEGRRW-----EVQLPD--GNKVPVDRNDFSFTNGTEK 72
Cdd:PRK14572 1 MAKIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVkpILLTPDGGWVvptvyRPSIPDesGNSEDLFLEEFQKANGVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 73 VV------FDFAYITIHGTPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQSVSDE 146
Cdd:PRK14572 81 PAdisqldADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFFELEKLKYLNSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 147 EVV----EKIGLPCFIKPSLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKT----KEKSVIFP 218
Cdd:PRK14572 161 RKTllklESLGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLERyrggKRNPIALP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 219 PTEVVTHNEFFDYDAKY-NGQVDEITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKlNLLEVNTTPGMTT 297
Cdd:PRK14572 241 ATEIVPGGEFFDFESKYkQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTDFIIVDGEP-HILETNTLPGMTE 319
|
330 340
....*....|....*....|....
gi 1074127292 298 TSFIPQQVRAAGLDIKDVMTDIIE 321
Cdd:PRK14572 320 TSLIPQQAKAAGINMEEVFTDLIE 343
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
124-321 |
2.66e-51 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 168.65 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 124 LKAFGVRIAESLLLRQGQSVSD-----EEVVEKIGLPCFIKPSLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFM 198
Cdd:pfam07478 2 LKAAGLPVVPFVTFTRADWKLNpkewcAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 199 DGTELTCGCYKTkEKSVIFPPTEVVTHNEFFDYDAKY-NGQVDEITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYI 277
Cdd:pfam07478 82 EGREIECAVLGN-EDPEVSPVGEIVPSGGFYDYEAKYiDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDFF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1074127292 278 ITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLDIKDVMTDIIE 321
Cdd:pfam07478 161 LTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
5-324 |
6.53e-47 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 160.37 E-value: 6.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 5 IAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNLyivemegrrwevqlpdgnkVPVDRNDFSFTNGTEKVVFDFAYITIHG 84
Cdd:PRK14571 3 VALLMGGVSREREISLRSGERVKKALEKLGYEV-------------------TVFDVDEDFLKKVDQLKSFDVVFNVLHG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 85 TPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFgVRIAESLLLRQGQSVSdeevveKIGLPCFIKPSLGG 164
Cdd:PRK14571 64 TFGEDGTLQAILDFLGIRYTGSDAFSSMICFDKLLTYRFLKGT-VEIPDFVEIKEFMKTS------PLGYPCVVKPRREG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 165 SSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKTKEKSVIFPPTEVVTHNEFFDYDAKY-NGQVDEIT 243
Cdd:PRK14571 137 SSIGVFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILETEKGFEVLPILELRPKRRFYDYVAKYtKGETEFIL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 244 PARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEkLNLLEVNTTPGMTTTSFIPQQVRAAGLDIKDVMTDIIENK 323
Cdd:PRK14571 217 PAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIFSDGR-FYFLEINTVPGLTELSDLPASAKAGGIEFEELVDIIIKSA 295
|
.
gi 1074127292 324 F 324
Cdd:PRK14571 296 F 296
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1-324 |
6.67e-40 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 143.43 E-value: 6.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 1 MKRNIAIVAGGDTSEIVVSLRSAQGIYS-FIDKEKYNLYIVEMEGRR--WEV--QLPDGNKvPVDRNDFSFTN------- 68
Cdd:PRK14570 1 MKKNLMLIFGGVSFEHEISLRSAYGIYSaLLKLDKYNIYSVFIDKCTgiWYLldSVPDPPK-LIKRDVLPIVSlipgcgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 69 --GTEKVVFDFAYITIHGTPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQSVSDE 146
Cdd:PRK14570 80 fvNNKNLEIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIGFRKYDYFLDK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 147 E-----VVEKIGLPCFIKPSLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGTELTCGCYKTkEKSVIFPPTE 221
Cdd:PRK14570 160 EgikkdIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGN-EQIKIFTPGE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 222 VVTHN-EFFDYDAKY-----NGQVDEItPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITA-GEKLNLLEVNTTPG 294
Cdd:PRK14570 239 IVVQDfIFYDYDAKYstipgNSIVFNI-PAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKdTGLIYLNEINTIPG 317
|
330 340 350
....*....|....*....|....*....|
gi 1074127292 295 MTTTSFIPQQVRAAGLDIKDVMTDIIENKF 324
Cdd:PRK14570 318 FTDISMFAKMCEHDGLQYKSLVDNLIDLAF 347
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
2-321 |
8.01e-38 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 136.34 E-value: 8.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 2 KRNIAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNLYIVEMEGRRWEVQLPDGNKvpvdrndfsftngtekvvfDFAYIT 81
Cdd:PRK14569 3 NEKIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAVGVDASGKELVAKLLELKP-------------------DKCFVA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 82 IHGTPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLLRQGQSVSDEevvekIGLPCFIKPS 161
Cdd:PRK14569 64 LHGEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPTPMAKFLTDKLVAEDE-----ISFPVAVKPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 162 LGGSSFGVTKVKTKEQIQPAIVKAfGEAEEVIVEAFMDGTELTCGCYKTKEKSVIFppteVVTHNEFFDYDAKYNGQVDE 241
Cdd:PRK14569 139 SGGSSIATFKVKSIQELKHAYEEA-SKYGEVMIEQWVTGKEITVAIVNDEVYSSVW----IEPQNEFYDYESKYSGKSIY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 242 ITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKLNLLEVNTTPGMTTTSFIPQQVRAAGLDIKDVMTDIIE 321
Cdd:PRK14569 214 HSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEINSSPGMTDNSLSPKSAAAEGVDFDSFVKRIIE 293
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
2-307 |
7.09e-29 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 116.84 E-value: 7.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 2 KRNIAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYNL--YIVEMEGRrWEvqlpdgnkvPVDRNDFSFTNGTEKVVF---- 75
Cdd:PRK14573 451 KLSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVsyFLINRQGL-WE---------TVSSLETAIEEDSGKSVLssei 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 76 -------DFAYITIHGTPGEDGRLQGYFDMMRIPYSCCGVLAAAITYDKFTCNQYLKAFGVRIAESLLL-----RQGQSV 143
Cdd:PRK14573 521 aqalakvDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPLtlagwKREPEL 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 144 SDEEVVEKIGLPCFIKPSLGGSSFGVTKVKTKEQIQPAIVKAFGEAEEVIVEAFMDGT---ELTC-----GCYktkeksV 215
Cdd:PRK14573 601 CLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESRLGSreiEVSClgdgsSAY------V 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 216 IFPPTEVVTHNEFFDYDAKYNgqVDEITPARI------SDELTKRVQMLTSAIYDILGCSGIIRVDYIITAGEKLNLLEV 289
Cdd:PRK14573 675 IAGPHERRGSGGFIDYQEKYG--LSGKSSAQIvfdldlSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEM 752
|
330
....*....|....*....
gi 1074127292 290 NTTPGMTTTS-FIPQQVRA 307
Cdd:PRK14573 753 NPIPGMTEASpFLTAFVRK 771
|
|
| Dala_Dala_lig_N |
pfam01820 |
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ... |
4-103 |
3.88e-22 |
|
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: 89.59 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 4 NIAIVAGGDTSEIVVSLRSAQGIYSFIDKEKYN---LYI------------VEMEGRRWEVQLPDGNKVPVDRNDFSFTN 68
Cdd:pfam01820 1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEvipIGItkdgrlgeaalrELASDDGLLLEVDDAPDGGPAGLLFGPNV 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1074127292 69 GTEKVVFDFAYITIHGTPGEDGRLQGYFDMMRIPY 103
Cdd:pfam01820 81 LELLIEVDVVFPVLHGPNGEDGTLQGLLELAGIPY 115
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
110-312 |
1.28e-18 |
|
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: 83.77 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 110 AAAITYDKFTCNQYLKAFGVRIAESLLLRqgqSVSD-EEVVEKIGLPCFIKPSLGGSSFGVTKVKTKEQIQPAIVKAFGE 188
Cdd:COG0439 48 AIRAMRDKVLMREALAAAGVPVPGFALVD---SPEEaLAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 189 A------EEVIVEAFMDGTELTCGCYKTKEKSVIFPPTEVVTHNEFFdydakynGQVDEITPARISDELTKRVQMLTSAI 262
Cdd:COG0439 125 AkagspnGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQKPPYF-------VELGHEAPSPLPEELRAEIGELVARA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1074127292 263 YDILG-CSGIIRVDYIITAGEKLNLLEVNT-TPGmtttSFIPQQVRAA-GLDI 312
Cdd:COG0439 198 LRALGyRRGAFHTEFLLTPDGEPYLIEINArLGG----EHIPPLTELAtGVDL 246
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
113-216 |
5.19e-15 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 74.54 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 113 ITYDKFTCNQYLKAFGVRIAESLLLRQGQSVSDEEVVEKIGLPCFIKPSLGGSSFGVTKVKTKEQIQPaivkAFGEAEEV 192
Cdd:PRK12767 108 ICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEF----LLEYVPNL 183
|
90 100
....*....|....*....|....
gi 1074127292 193 IVEAFMDGTELTCGCYKTKEKSVI 216
Cdd:PRK12767 184 IIQEFIEGQEYTVDVLCDLNGEVI 207
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
112-284 |
1.05e-08 |
|
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: 55.85 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 112 AITYDKFTCNQYLKAFGVRIAESLLLRqgqSVSD-EEVVEKIGLPCFIKPSLGGss-fGVTKVKTKEQIQPAiVKAFGEA 189
Cdd:COG0026 85 EIAQDRLLEKAFLAELGIPVAPFAAVD---SLEDlEAAIAELGLPAVLKTRRGGydgkGQVVIKSAADLEAA-WAALGGG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 190 EeVIVEAFMDgteltcgcYKtKEKSVI-----------FPPTEvvthNEFfdydakYNGQVDE-ITPARISDELTKRVQM 257
Cdd:COG0026 161 P-CILEEFVP--------FE-RELSVIvarspdgevatYPVVE----NVH------RNGILDEsIAPARISEALAAEAEE 220
|
170 180
....*....|....*....|....*..
gi 1074127292 258 LTSAIYDILGCSGIIRVDYIITAGEKL 284
Cdd:COG0026 221 IAKRIAEALDYVGVLAVEFFVTKDGEL 247
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
146-204 |
2.47e-08 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 54.75 E-value: 2.47e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1074127292 146 EEVVEKIGLPCFIKPSLGGSSFGVTKVKTKEQIQP----AIVKAFGEAEEVIVEAFMD-GTELT 204
Cdd:COG0027 142 RAAVEEIGYPCVVKPVMSSSGKGQSVVRSPADIEAaweyAQEGGRGGAGRVIVEGFVDfDYEIT 205
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
146-316 |
2.51e-08 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 54.76 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 146 EEVVEKIGLPCFIKPSLGGSSFGVTKVKTKEQIQP----AIVKAFGEAEEVIVEAFMDG----TELTcgcYKTKEKSVIF 217
Cdd:PRK09288 142 RAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDIEKaweyAQEGGRGGAGRVIVEEFIDFdyeiTLLT---VRAVDGGTHF 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 218 -PPtevVTHnefFDYDAKYngqVDEITPARISDELTKRVQMLTSAIYDILGCSGIIRVDYIITaGEKLNLLEVNTTP--- 293
Cdd:PRK09288 219 cAP---IGH---RQEDGDY---RESWQPQPMSPAALEEAQEIAKKVTDALGGRGLFGVELFVK-GDEVYFSEVSPRPhdt 288
|
170 180 190
....*....|....*....|....*....|.
gi 1074127292 294 GMTTtsFIPQ-------QVRAA-GLDIKDVM 316
Cdd:PRK09288 289 GMVT--LISQnlsefelHARAIlGLPIPDIR 317
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
109-202 |
1.24e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 53.24 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 109 LAAAITYDKFTCNQYLKAFGVRIAEslllrqGQSVSDEE----VVEKIGLPCFIKPSLGGSSFGVT-KVKTKEQIQPAIV 183
Cdd:PRK14016 207 IAVDIACDKELTKRLLAAAGVPVPE------GRVVTSAEdaweAAEEIGYPVVVKPLDGNHGRGVTvNITTREEIEAAYA 280
|
90
....*....|....*....
gi 1074127292 184 KAFGEAEEVIVEAFMDGTE 202
Cdd:PRK14016 281 VASKESSDVIVERYIPGKD 299
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
152-267 |
2.87e-07 |
|
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: 49.59 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 152 IGLPCFIKPSLGGSSFGVTKVKTKEQIQPAIV--------------KAFGEAEEVIVEAFMDGTELTCGCYKTKE-KSVI 216
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAaireeieqwkemypEAVVDGGSFLVEEYIEGEEFAVDAYFDENgEPVI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1074127292 217 FppteVVTHNEFfdYDAKYNGQVDEITPARISDELTKRVQMLTSAIYDILG 267
Cdd:pfam13535 81 L----NILKHDF--ASSEDVSDRIYVTSASIIRETQAAFTEFLKRINALLG 125
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
116-298 |
4.12e-06 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 46.22 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 116 DKFTCNQYLKAFGVRIAESLllrqgqsvSDEEVVEkIGLPCFIKPSLGGSSFGVTKVKTKEQIQPAIvkafgeaEEVIVE 195
Cdd:pfam02655 3 DKLKTYKALKNAGVPTPETL--------QAEELLR-EEKKYVVKPRDGCGGEGVRKVENGREDEAFI-------ENVLVQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 196 AFMDGTELTCGCYKTKEKSVIFPPTEVVTHNEFFDYdaKYNGqvdEITPARisDELTKRVQMLTS-AIYDILGCSGIIRV 274
Cdd:pfam02655 67 EFIEGEPLSVSLLSDGEKALPLSVNRQYIDNGGSGF--VYAG---NVTPSR--TELKEEIIELAEeVVECLPGLRGYVGV 139
|
170 180
....*....|....*....|....
gi 1074127292 275 DYIITAGEkLNLLEVNttPGMTTT 298
Cdd:pfam02655 140 DLVLKDNE-PYVIEVN--PRITTS 160
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
112-284 |
3.25e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 45.14 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 112 AITYDKFTCNQYLKAFGVRIAESLLLrqgQSVSD-EEVVEKIGLPCFIKPSLGGssF---GVTKVKTKEQIQpAIVKAFG 187
Cdd:PRK06019 96 AIAQDRLTEKQFLDKLGIPVAPFAVV---DSAEDlEAALADLGLPAVLKTRRGG--YdgkGQWVIRSAEDLE-AAWALLG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074127292 188 eAEEVIVEAFMDgteltcgcYKtKEKSVI-----------FPPTEvvTHNEffdydakyNGQVDE-ITPARISDELTKRV 255
Cdd:PRK06019 170 -SVPCILEEFVP--------FE-REVSVIvargrdgevvfYPLVE--NVHR--------NGILRTsIAPARISAELQAQA 229
|
170 180
....*....|....*....|....*....
gi 1074127292 256 QMLTSAIYDILGCSGIIRVDYIITAGEKL 284
Cdd:PRK06019 230 EEIASRIAEELDYVGVLAVEFFVTGDGEL 258
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
147-201 |
5.52e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 38.43 E-value: 5.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1074127292 147 EVVEKIGLPCFIKPSLGGSSFGVTKVKTKEQIQPAIVKAFGEAEevivEAFMDGT 201
Cdd:PRK08654 146 EIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQSIAQ----SAFGDST 196
|
|
|