|
Name |
Accession |
Description |
Interval |
E-value |
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
6-449 |
0e+00 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 605.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 6 EFQNKKVLILGLARSGEAAARLLTKLGALVTVNDGKPFEENpAAQALLEEGIKVVCGSHPLELLDeDFEYMVKNPGIPYD 85
Cdd:COG0771 1 DLKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPEL-AAAELEAPGVEVVLGEHPEELLD-GADLVVKSPGIPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 86 NPMVTRALEKQIPVLTEVELAYLVSESPIVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGYPASEVVQKASANDTLV 165
Cdd:COG0771 79 HPLLKAARAAGIPVIGEIELAYRLSPAPIIAITGTNGKTTTTTLIGHILKAAGLRVAVGGNIGTPLLDLLLEPEPPDVYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 166 MELSSFQLMGVDAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKATVIPFST 245
Cdd:COG0771 159 LELSSFQLETTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANQTPDDYAVLNADDPLTRALAEEAKARVVPFSL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 246 QEVVD-GAYLEGGMLYFK--GHPIMPAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVGKIKD 322
Cdd:COG0771 239 KEPLEgGAGLEDGKLVDRasGEELLPVDDLRLPGRHNLENALAALAAARALGVPPEAIREALRSFKGLPHRLEFVAEING 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 323 IIFYNDSKSTNILATQKALSGFDnKKLILIAGGLDRGNEFDDLVPDLRG-LKQMIILGESAERMKRAAEMANVPYLEAAD 401
Cdd:COG0771 319 VRFINDSKATNPDATLAALESFD-GPVVLIAGGLDKGADFSPLAPAVAErVKAVVLIGEDAEKIAAALAGAGVPVVIVET 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1654249257 402 VAAATELAFQEAQAGDTILLSPANASWDMYPNFEVRGDEFLATFAKLK 449
Cdd:COG0771 398 MEEAVAAAAELARPGDVVLLSPACASFDQFKNYEERGDVFKEAVRELA 445
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
6-441 |
1.47e-150 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 435.55 E-value: 1.47e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 6 EFQNKKVLILGLARSGEAAARLLTKLGALVTVNDGKpfEENPAAQALLE---EGIKVVCGSHPLELLDeDFEYMVKNPGI 82
Cdd:PRK14106 2 ELKGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEK--EEDQLKEALEElgeLGIELVLGEYPEEFLE-GVDLVVVSPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 83 PYDNPMVTRALEKQIPVLTEVELAYLVSESPIVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGYPASEVVQKASAND 162
Cdd:PRK14106 79 PLDSPPVVQAHKKGIEVIGEVELAYRFSKAPIVAITGTNGKTTTTTLLGEIFKNAGRKTLVAGNIGYPLIDAVEEYGEDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 163 TLVMELSSFQLMGVDAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKATVIP 242
Cdd:PRK14106 159 IIVAEVSSFQLETIKEFKPKVGCILNITPDHLDRHKTMENYIKAKARIFENQRPSDYTVLNYDDPRTRSLAKKAKARVIF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 243 FSTQEVVD-GAYLEGGMLY--FKGH--PIMPAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLV 317
Cdd:PRK14106 239 FSRKSLLEeGVFVKNGKIVisLGGKeeEVIDIDEIFIPGEHNLENALAATAAAYLLGISPDVIANTLKTFKGVEHRIEFV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 318 GKIKDIIFYNDSKSTNILATQKALSGFDNkKLILIAGGLDRGNEFDDLVPDLRG-LKQMIILGESAERMKRAAEMANVP- 395
Cdd:PRK14106 319 AEINGVKFINDSKGTNPDAAIKALEAYET-PIVLIAGGYDKGSDFDEFAKAFKEkVKKLILLGETAQEIAEAARKYGFDn 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1654249257 396 YLEAADVAAATELAFQEAQAGDTILLSPANASWDMYPNFEVRGDEF 441
Cdd:PRK14106 398 ILFAETLEEAVKKAYEIAKPGDVVLLSPACASWDMFKNFEERGRLF 443
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
11-441 |
6.14e-150 |
|
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273436 [Multi-domain] Cd Length: 433 Bit Score: 433.31 E-value: 6.14e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 11 KVLILGLARSGEAAARLLTKLGALVTVNDGKPFEENPAAQALLEEGIKVVCGSHPLELLDEDFEYMVKNPGIPYDNPMVT 90
Cdd:TIGR01087 1 KILILGLGKTGRAVARFLHKKGAEVTVTDLKPNEELEPSMGQLRLNEGSVLHTGLHLEDLNNADLVVKSPGIPPDHPLVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 91 RALEKQIPVLTEVELAYLVSESPIVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGYPASEVVQKASAnDTLVMELSS 170
Cdd:TIGR01087 81 AAAKRGIPVVGDIELFLRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAFLGGNIGTPALEVLDQEGA-ELYVLELSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 171 FQLMGVDAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKATVIPFSTQEVVD 250
Cdd:TIGR01087 160 FQLETTESLRPEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVAVLNADDPRFARLAQKSKAQVIWFSVEKDAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 251 -GAYLEGGMLYFKGHpimpAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVGKIKDIIFYNDS 329
Cdd:TIGR01087 240 rGLCIRDGGLYLKPN----DLEGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVGQKNGVHFYNDS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 330 KSTNILATQKALSGFDNkKLILIAGGLDRGNEFDDLVPDLRG-LKQMIILGESAERMKRAAEMANVPYLEAADVAAATEL 408
Cdd:TIGR01087 316 KATNVHATLAALSAFDN-PVILIVGGDDKGADFSPLAPAAAGkVKAVLAIGEDAAKIAPLLKEAGLSVYLVESLEEAVQA 394
|
410 420 430
....*....|....*....|....*....|...
gi 1654249257 409 AFQEAQAGDTILLSPANASWDMYPNFEVRGDEF 441
Cdd:TIGR01087 395 AREVASPGDVVLLSPACASFDQFKSYEERGEKF 427
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
117-290 |
6.58e-36 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 131.27 E-value: 6.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 117 ITGSNGKTTTTTMIADVLNAGG------QSALLSGNIGYPASEVVQKASAN------DTLVMELSSFQLM---GVDAFKP 181
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGgvigtiGTYIGKSGNTTNNAIGLPLTLAEmveagaEYAVLEVSSHGLGegrLSGLLKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 182 HIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTK---ATVIPFSTQEVVD------GA 252
Cdd:pfam08245 81 DIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGIAVINADDPYGAFLIAKLKkagVRVITYGIEGEADlraaniEL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654249257 253 YLEGGMLYFKGHPIMPAA-NLGVPGSHNIENALAAIAVA 290
Cdd:pfam08245 161 SSDGTSFDLFTVPGGELEiEIPLLGRHNVYNALAAIAAA 199
|
|
| F430_CfbE |
NF033197 |
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ... |
113-422 |
3.21e-14 |
|
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in synthesizing coenzyme F430, which is used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) MurD, an enzyme of bacterial cell wall biosynthesis.
Pssm-ID: 467992 [Multi-domain] Cd Length: 419 Bit Score: 74.28 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 113 PIVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGY-------------PAS--EVVQKASAN-----DTLVMELSsfq 172
Cdd:NF033197 93 KFIEITGVKGKTTTAELLAHILSDEYVLLHTSRGTERypegelsnkgsitPASilNALELAEEIgiddyGFLIFEVS--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 173 LMGVDAFKphIAVITNLMpthldyhgsfEDYVAAKWRIQAEM-------TADDYLILNANQEISAALAKTTKATVipfst 245
Cdd:NF033197 170 LGGTGAGD--VGIITNIL----------EDYPIAGGKRSASAaklqslkNAKVGSINVADLGIYINGKNKLVITV----- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 246 qEVVDGAYLEGGMLYFKGHPImpAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQlVGKIKDIIF 325
Cdd:NF033197 233 -AGVEILSKYPLRFKYGNTEF--EFNPLLFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMA-VKKEGGVVI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 326 YNDSKS-TNILATQKALSGFDNKK--LILIAGGlDRGN---EFD---------DLVPDLRGLKqmIILGESAERMKRAAE 390
Cdd:NF033197 309 VDNINPgLNVKAIEYALDDALELLgdGTLVIGG-DFGVvceEIDidklsevlkKYRPKIDILV--GVGTELGKRLKKYLD 385
|
330 340 350
....*....|....*....|....*....|..
gi 1654249257 391 MAnvPYLEAADVAAATELAFQEAQAGDTILLS 422
Cdd:NF033197 386 KL--EGYEAGTLEEGLDDARELTGEGNTLVIY 415
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
11-39 |
7.27e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 37.10 E-value: 7.27e-03
10 20
....*....|....*....|....*....
gi 1654249257 11 KVLILGLARSGEAAARLLTKLGALVTVND 39
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLD 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
6-449 |
0e+00 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 605.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 6 EFQNKKVLILGLARSGEAAARLLTKLGALVTVNDGKPFEENpAAQALLEEGIKVVCGSHPLELLDeDFEYMVKNPGIPYD 85
Cdd:COG0771 1 DLKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPEL-AAAELEAPGVEVVLGEHPEELLD-GADLVVKSPGIPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 86 NPMVTRALEKQIPVLTEVELAYLVSESPIVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGYPASEVVQKASANDTLV 165
Cdd:COG0771 79 HPLLKAARAAGIPVIGEIELAYRLSPAPIIAITGTNGKTTTTTLIGHILKAAGLRVAVGGNIGTPLLDLLLEPEPPDVYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 166 MELSSFQLMGVDAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKATVIPFST 245
Cdd:COG0771 159 LELSSFQLETTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANQTPDDYAVLNADDPLTRALAEEAKARVVPFSL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 246 QEVVD-GAYLEGGMLYFK--GHPIMPAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVGKIKD 322
Cdd:COG0771 239 KEPLEgGAGLEDGKLVDRasGEELLPVDDLRLPGRHNLENALAALAAARALGVPPEAIREALRSFKGLPHRLEFVAEING 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 323 IIFYNDSKSTNILATQKALSGFDnKKLILIAGGLDRGNEFDDLVPDLRG-LKQMIILGESAERMKRAAEMANVPYLEAAD 401
Cdd:COG0771 319 VRFINDSKATNPDATLAALESFD-GPVVLIAGGLDKGADFSPLAPAVAErVKAVVLIGEDAEKIAAALAGAGVPVVIVET 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1654249257 402 VAAATELAFQEAQAGDTILLSPANASWDMYPNFEVRGDEFLATFAKLK 449
Cdd:COG0771 398 MEEAVAAAAELARPGDVVLLSPACASFDQFKNYEERGDVFKEAVRELA 445
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
6-441 |
1.47e-150 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 435.55 E-value: 1.47e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 6 EFQNKKVLILGLARSGEAAARLLTKLGALVTVNDGKpfEENPAAQALLE---EGIKVVCGSHPLELLDeDFEYMVKNPGI 82
Cdd:PRK14106 2 ELKGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEK--EEDQLKEALEElgeLGIELVLGEYPEEFLE-GVDLVVVSPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 83 PYDNPMVTRALEKQIPVLTEVELAYLVSESPIVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGYPASEVVQKASAND 162
Cdd:PRK14106 79 PLDSPPVVQAHKKGIEVIGEVELAYRFSKAPIVAITGTNGKTTTTTLLGEIFKNAGRKTLVAGNIGYPLIDAVEEYGEDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 163 TLVMELSSFQLMGVDAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKATVIP 242
Cdd:PRK14106 159 IIVAEVSSFQLETIKEFKPKVGCILNITPDHLDRHKTMENYIKAKARIFENQRPSDYTVLNYDDPRTRSLAKKAKARVIF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 243 FSTQEVVD-GAYLEGGMLY--FKGH--PIMPAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLV 317
Cdd:PRK14106 239 FSRKSLLEeGVFVKNGKIVisLGGKeeEVIDIDEIFIPGEHNLENALAATAAAYLLGISPDVIANTLKTFKGVEHRIEFV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 318 GKIKDIIFYNDSKSTNILATQKALSGFDNkKLILIAGGLDRGNEFDDLVPDLRG-LKQMIILGESAERMKRAAEMANVP- 395
Cdd:PRK14106 319 AEINGVKFINDSKGTNPDAAIKALEAYET-PIVLIAGGYDKGSDFDEFAKAFKEkVKKLILLGETAQEIAEAARKYGFDn 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1654249257 396 YLEAADVAAATELAFQEAQAGDTILLSPANASWDMYPNFEVRGDEF 441
Cdd:PRK14106 398 ILFAETLEEAVKKAYEIAKPGDVVLLSPACASWDMFKNFEERGRLF 443
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
11-441 |
6.14e-150 |
|
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273436 [Multi-domain] Cd Length: 433 Bit Score: 433.31 E-value: 6.14e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 11 KVLILGLARSGEAAARLLTKLGALVTVNDGKPFEENPAAQALLEEGIKVVCGSHPLELLDEDFEYMVKNPGIPYDNPMVT 90
Cdd:TIGR01087 1 KILILGLGKTGRAVARFLHKKGAEVTVTDLKPNEELEPSMGQLRLNEGSVLHTGLHLEDLNNADLVVKSPGIPPDHPLVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 91 RALEKQIPVLTEVELAYLVSESPIVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGYPASEVVQKASAnDTLVMELSS 170
Cdd:TIGR01087 81 AAAKRGIPVVGDIELFLRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAFLGGNIGTPALEVLDQEGA-ELYVLELSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 171 FQLMGVDAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKATVIPFSTQEVVD 250
Cdd:TIGR01087 160 FQLETTESLRPEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVAVLNADDPRFARLAQKSKAQVIWFSVEKDAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 251 -GAYLEGGMLYFKGHpimpAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVGKIKDIIFYNDS 329
Cdd:TIGR01087 240 rGLCIRDGGLYLKPN----DLEGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVGQKNGVHFYNDS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 330 KSTNILATQKALSGFDNkKLILIAGGLDRGNEFDDLVPDLRG-LKQMIILGESAERMKRAAEMANVPYLEAADVAAATEL 408
Cdd:TIGR01087 316 KATNVHATLAALSAFDN-PVILIVGGDDKGADFSPLAPAAAGkVKAVLAIGEDAAKIAPLLKEAGLSVYLVESLEEAVQA 394
|
410 420 430
....*....|....*....|....*....|...
gi 1654249257 409 AFQEAQAGDTILLSPANASWDMYPNFEVRGDEF 441
Cdd:TIGR01087 395 AREVASPGDVVLLSPACASFDQFKSYEERGEKF 427
|
|
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
25-352 |
1.06e-48 |
|
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 172.56 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 25 ARLLTKLGALVTVNDGKpfeENPAAQALLEEGIKVVCGSHPLELLDEDFeyMVKNPGIPYDNPMVTRALEKQIPVLT--E 102
Cdd:COG0773 21 AEILLALGYKVSGSDLA---ESPMTERLEALGIPVFIGHDAENIDDADL--VVVSSAIPRDNPELVAARERGIPVLSraE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 103 VeLAYLVSESPIVGITGSNGKTTTTTMIADVLNAGGQ--SALLSG---NIGYPAsevvqKASANDTLVME----LSSFQL 173
Cdd:COG0773 96 M-LAELMRGKRSIAVAGTHGKTTTTSMLAHILEEAGLdpTFLIGGilnNFGTNA-----RLGDGDYFVAEadesDGSFLH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 174 mgvdaFKPHIAVITNLMPTHLDYHGSFEDYVAAkWRIQAEMTADD-YLILNANQEISAALAKTTKATVIPFSTQE----- 247
Cdd:COG0773 170 -----YSPDIAVVTNIEADHLDIYGDLEAIKEA-FHEFARNVPFYgLLVLCADDPGLRELLPRCGRPVITYGFSEdadyr 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 248 VVDGAYLEGGM---LYFKGHPIMPAaNLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVGKIKDII 324
Cdd:COG0773 244 AENIRIDGGGStfdVLRRGEELGEV-ELNLPGRHNVLNALAAIAVALELGVDPEAIAEALASFKGVKRRFELKGEVGGVT 322
|
330 340 350
....*....|....*....|....*....|....
gi 1654249257 325 FYND-----SKstnILATQKAL-SGFDNKKLILI 352
Cdd:COG0773 323 VIDDyahhpTE---IAATLAAArEKYPDRRLVAV 353
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
114-421 |
8.09e-43 |
|
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440532 [Multi-domain] Cd Length: 459 Bit Score: 156.78 E-value: 8.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 114 IVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGYPASEVVQKAS------------------AN-DTLVMELSSFQL- 173
Cdd:COG0769 82 LIGVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGGELIPSSlttpealdlqrllaemvdAGvTHVVMEVSSHALd 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 174 MG-VDAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKATVIPFSTQEVVD-- 250
Cdd:COG0769 162 QGrVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDQLGPGGAAVINADDPYGRRLAAAAPARVITYGLKADADlr 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 251 ----GAYLEGGMLYFKGHPIMPAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVGKIKDIIFY 326
Cdd:COG0769 242 atdiELSADGTRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRMERVDGGQGPTVI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 327 NDSKST-----NILatqKALSGFDNKKLILI--AGGlDRGnefddlvPDLRglKQMiilGESAER--------------- 384
Cdd:COG0769 322 VDYAHTpdaleNVL---EALRPHTKGRLIVVfgCGG-DRD-------RGKR--PLM---GEIAARladvvivtsdnprse 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1654249257 385 --------MKRAAEMANvPYLEAADVAAATELAFQEAQAGDTILL 421
Cdd:COG0769 386 dpaaiiadILAGIPGAG-KVLVIPDRAEAIRYAIALAKPGDVVLI 429
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
23-352 |
1.11e-42 |
|
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273433 [Multi-domain] Cd Length: 448 Bit Score: 156.31 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 23 AAARLLTKLGALVTvndGKPFEENPAAQALLEEGIKVVCGsHPLELLDeDFEYMVKNPGIPYDNPMVTRALEKQIPVLTE 102
Cdd:TIGR01082 14 GIAEILLNRGYQVS---GSDIAENATTKRLEALGIPIYIG-HSAENLD-DADVVVVSAAIKDDNPEIVEAKERGIPVIRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 103 VE-LAYLVSESPIVGITGSNGKTTTTTMIADVLNAGG--QSALLSGNIGypASEVVQKASANDTLVMEL----SSFQLmg 175
Cdd:TIGR01082 89 AEmLAELMRFRHSIAVAGTHGKTTTTAMIAVILKEAGldPTVVVGGLVK--EAGTNARLGSGEYLVAEAdesdASFLH-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 176 vdaFKPHIAVITNLMPTHLD-YHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAAL-AKTTKATVIPFSTQEVVDgAY 253
Cdd:TIGR01082 165 ---LQPNVAIVTNIEPDHLDtYGSSFERLKAAFEKFIHNLPFYGLAVICADDPVLRELvPKATEQVITYGGSGEDAD-YR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 254 LE-----GGMLYF---KGHPIMPAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVGKIKDIIF 325
Cdd:TIGR01082 241 AEniqqsGAEGKFsvrGKGKLYLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQGVKRRFEILGEFGGVLL 320
|
330 340 350
....*....|....*....|....*....|
gi 1654249257 326 YND--SKSTNILATQKAL-SGFDNKKLILI 352
Cdd:TIGR01082 321 IDDyaHHPTEIKATLKAArQGYPDKRIVVV 350
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
88-421 |
2.96e-40 |
|
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440533 [Multi-domain] Cd Length: 451 Bit Score: 149.87 E-value: 2.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 88 MVTRALEKQIPVLtEVE--------LA-YLVSES--PIVGITGSNGKTTTTTMIADVLNAGGQ---SAllsGN----IGY 149
Cdd:COG0770 66 LVSRPLPADLPLI-VVDdtlkalqqLAaAHRARFniPVIAITGSNGKTTTKEMLAAVLSTKGKvlaTP---GNfnneIGV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 150 PASevVQKASAN-DTLVMElssfqlMGVDAF----------KPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADD 218
Cdd:COG0770 142 PLT--LLRLPEDhEFAVLE------MGMNHPgeiaylariaRPDIAVITNIGPAHLEGFGSLEGIARAKGEIFEGLPPGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 219 YLILNANQEISAALAKTTKATVIPFSTQE-----VVDGAYLEGGM---LYFKGHPImpAANLGVPGSHNIENALAAIAVA 290
Cdd:COG0770 214 VAVLNADDPLLAALAERAKARVLTFGLSEdadvrAEDIELDEDGTrftLHTPGGEL--EVTLPLPGRHNVSNALAAAAVA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 291 KLSGIADDVIVEVLSHFGGVKHRLQLVGKIKDIIFYNDSKSTNILATQKALSGF----DNKKLILIAG-----GLDRGNE 361
Cdd:COG0770 292 LALGLDLEEIAAGLAAFQPVKGRLEVIEGAGGVTLIDDSYNANPDSMKAALDVLaqlpGGGRRIAVLGdmlelGEESEEL 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654249257 362 FDDLVPDLR--GLKQMIILGESAERMKRAAEMANVPYleAADVAAATELAFQEAQAGDTILL 421
Cdd:COG0770 372 HREVGELAAelGIDRLFTVGELARAIAEAAGGERAEH--FEDKEELLAALKALLRPGDVVLV 431
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
117-290 |
6.58e-36 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 131.27 E-value: 6.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 117 ITGSNGKTTTTTMIADVLNAGG------QSALLSGNIGYPASEVVQKASAN------DTLVMELSSFQLM---GVDAFKP 181
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGgvigtiGTYIGKSGNTTNNAIGLPLTLAEmveagaEYAVLEVSSHGLGegrLSGLLKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 182 HIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTK---ATVIPFSTQEVVD------GA 252
Cdd:pfam08245 81 DIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGIAVINADDPYGAFLIAKLKkagVRVITYGIEGEADlraaniEL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654249257 253 YLEGGMLYFKGHPIMPAA-NLGVPGSHNIENALAAIAVA 290
Cdd:pfam08245 161 SSDGTSFDLFTVPGGELEiEIPLLGRHNVYNALAAIAAA 199
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
114-421 |
4.30e-35 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 135.64 E-value: 4.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 114 IVGITGSNGKTTTTTMIADVLN-AGGQSALLS--GNIGYPASEV----------VQKASAN------DTLVMELSS---- 170
Cdd:PRK00139 97 LIGVTGTNGKTTTAYLLAQILRlLGEKTALIGtlGNGIGGELIPsglttpdaldLQRLLAElvdagvTYAAMEVSShald 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 171 -FQLMGVDaFKphIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEmtADDYLILNANQEISAALAKTTKATVIPFSTQEV- 248
Cdd:PRK00139 177 qGRVDGLK-FD--VAVFTNLSRDHLDYHGTMEDYLAAKARLFSE--LGLAAVINADDEVGRRLLALPDAYAVSMAGADLr 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 249 -VDGAYLEGGMLYFKGHPImpaaNLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVGKIKDIIFYN 327
Cdd:PRK00139 252 aTDVEYTDSGQTFTLVTEV----ESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRMERVDAGQGPLVIV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 328 DSKST-----NILatqKALSGFDNKKLILI--AGGlDRGnefddlvpdlRGlK--QMiilGESAER-------------- 384
Cdd:PRK00139 328 DYAHTpdaleKVL---EALRPHAKGRLICVfgCGG-DRD----------KG-KrpLM---GAIAERladvvivtsdnprs 389
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1654249257 385 ---MKRAAEMANVPYLEAADVAAATELAFQEAQAGDTILL 421
Cdd:PRK00139 390 edpAAIIADILAGIYDVIEDRAEAIRYAIAQAKPGDVVLI 429
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
114-421 |
3.59e-30 |
|
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273435 [Multi-domain] Cd Length: 464 Bit Score: 122.04 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 114 IVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGY----------------PASEVVQKASAN------DTLVMELSSF 171
Cdd:TIGR01085 87 VIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYrlggndliknpaalttPEALTLQSTLAEmveagaQYAVMEVSSH 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 172 QL-----MGVDAFkphIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTT-KATVIPFST 245
Cdd:TIGR01085 167 ALaqgrvRGVRFD---AAVFTNLSRDHLDFHGTMENYFAAKASLFTELGLKRFAVINLDDEYGAQFVKRLpKDITVSAIT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 246 QEVV----------DGAYLEGGMLYFkghpIMPA--ANLGVP--GSHNIENALAAIAVAKLSGIAD-DVIVEVLSHFGGV 310
Cdd:TIGR01085 244 QPADgraqdikitdSGYSFEGQQFTF----ETPAgeGHLHTPliGRFNVYNLLAALATLLHLGGIDlEDIVAALEKFRGV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 311 KHRLQLVGKIKDIIFYNDSKST-----NILATQKALSGfdnKKLILI--AGG-LDRGN---------EFDDLV----PDL 369
Cdd:TIGR01085 320 PGRMELVDGGQKFLVIVDYAHTpdaleKALRTLRKHKD---GRLIVVfgCGGdRDRGKrplmgaiaeQLADLViltsDNP 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1654249257 370 RGLKQMIILGEsaerMKRAAEMAnVPYLEAADVAAATELAFQEAQAGDTILL 421
Cdd:TIGR01085 397 RGEDPEQIIAD----ILAGISEK-EKVVIIADRRQAIRYAISNAKAGDVVLI 443
|
|
| murF |
TIGR01143 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ... |
113-354 |
4.27e-26 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273468 [Multi-domain] Cd Length: 417 Bit Score: 109.66 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 113 PIVGITGSNGKTTTTTMIADVLNAGGQSALLSGN----IGYPASeVVQKASANDTLVMElssfqlMGVDAF--------- 179
Cdd:TIGR01143 75 KVIGITGSSGKTTTKEMLAAILSHKYKVFATPGNfnneIGLPLT-LLRAPGDHDYAVLE------MGASHPgeiaylaei 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 180 -KPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKAT-VIPFSTQ------EVVDG 251
Cdd:TIGR01143 148 aKPDIAVITNIGPAHLEGFGSLEGIAEAKGEILQGLKENGIAVINADDPAFADLAKRLPNRnILSFGFEggdfvaKDISY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 252 AYLEGGMLYFKGHPIMPAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVGKiKDIIFYNDSKS 331
Cdd:TIGR01143 228 SALGSTSFTLVAPGGEFEVSLPLLGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRFEVQTK-NGLTLIDDTYN 306
|
250 260
....*....|....*....|....*.
gi 1654249257 332 TN---ILATQKALSGFDNKKlILIAG 354
Cdd:TIGR01143 307 ANpdsMRAALDALARFPGKK-ILVLG 331
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
114-318 |
1.33e-23 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 104.02 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 114 IVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGYPASEVVQKASAN-------------------DTLVMELSSFQL- 173
Cdd:PRK11929 114 LVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGTLGARLDGRLIPGSLTtpdaiilhrilarmraagaDAVAMEASSHGLe 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 174 MG-VDAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKATVIPFSTQEVVDG- 251
Cdd:PRK11929 194 QGrLDGLRIAVAGFTNLTRDHLDYHGTMQDYEEAKAALFSKLPGLGAAVINADDPAAARLLAALPRGLKVGYSPQNAGAd 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654249257 252 -------AYLEGGMLYFKGHPIMPAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVG 318
Cdd:PRK11929 274 vqardlrATAHGQVFTLATPDGSYQLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVSPVPGRMERVG 347
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
113-307 |
8.66e-20 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 92.14 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 113 PIVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIG-YPASEVVQK------ASANDTL--------VMELSSFQLM--- 174
Cdd:PRK14016 481 PIVAVTGTNGKTTTTRLIAHILKLSGKRVGMTTTDGvYIDGRLIDKgdctgpKSARRVLmnpdveaaVLETARGGILreg 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 175 -GVDafKPHIAVITNLMPTHLDYHG--SFEDYVAAKwRIQAEMTADD-YLILNANQEISAALAKTTKATVIPFSTQ---E 247
Cdd:PRK14016 561 lAYD--RCDVGVVTNIGEDHLGLGGinTLEDLAKVK-RVVVEAVKPDgYAVLNADDPMVAAMAERCKGKVIFFSMDpdnP 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654249257 248 VV-----DG---AYLEGGMLY-FKG---HPIMPAANL-----GVPGsHNIENALAAIAVAKLSGIADDVIVEVLSHF 307
Cdd:PRK14016 638 VIaehraQGgraVYVEGDYIVlAEGgweIRIISLADIpltlgGKAG-FNIENALAAIAAAWALGIDIELIRAGLRTF 713
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
112-420 |
1.41e-19 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 91.69 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 112 SPIVGITGSNGKTTTTTMIADVLNAG-GQSALLsgnigypASEvvqkASANDTLVMELSSFQLMGVDAF----------- 179
Cdd:PRK11929 603 LPVVAITGSNGKTTTKEMIAAILAAWqGEDRVL-------ATE----GNFNNEIGVPLTLLRLRAQHRAavfelgmnhpg 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 180 ---------KPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKATVIP-------- 242
Cdd:PRK11929 672 eiaylaaiaAPTVALVTNAQREHQEFMHSVEAVARAKGEIIAALPEDGVAVVNGDDPYTAIWAKLAGARRVLrfglqpga 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 243 --FSTQEVVDGAYLEGGMLYFKGHPIMPAANLGVP--GSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLVG 318
Cdd:PRK11929 752 dvYAEKIAKDISVGEAGGTRCQVVTPAGSAEVYLPliGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRR 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 319 KIKDIIFYNDSKSTNILATQKALSGFDN----KKLILIAGGLDRGNEFDDLVPDL------RGLKQMIILGESAERMKRA 388
Cdd:PRK11929 832 LSCGTRIIDDTYNANPDSMRAAIDVLAElpngPRALVLGDMLELGDNGPAMHREVgkyarqLGIDALITLGEAARDAAAA 911
|
330 340 350
....*....|....*....|....*....|..
gi 1654249257 389 AEmaNVPYLEAADVAAATELAFQEAQAGDTIL 420
Cdd:PRK11929 912 FG--AGARGVCASVDEIIAALRGALPEGDSVL 941
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
23-315 |
2.08e-14 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 75.62 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 23 AAARLLTKLGALVTvndGKPFEENPAAQALLEEGIKVVCGsHPLELLDEDfEYMVKNPGIPYDNPMVTRALEKQIPVLTE 102
Cdd:PRK14573 19 ALAHILLDRGYSVS---GSDLSEGKTVEKLKAKGARFFLG-HQEEHVPED-AVVVYSSSISKDNVEYLSAKSRGNRLVHR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 103 VEL-AYLVSESPIVGITGSNGKTTTTTMIADVLNAGGQSAllSGNIGYPASEVVQKASANDTLVMELSSFQLMGVDAFKP 181
Cdd:PRK14573 94 AELlAELMQEQISILVSGSHGKTTVSSLITAIFQEAKKDP--SYAIGGLNQEGLNGYSGSSEYFVAEADESDGSLKHYTP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 182 HIAVITNLMPTHL-DYHGSFEDYVAAKWRIQAEMTADDYLILNAN-QEISAALAKTTKAtvipFST--QEVVDGAYLEGG 257
Cdd:PRK14573 172 EFSVITNIDNEHLsNFEGDRELLLASIQDFARKVQQINKCFYNGDcPRLKGCLQGHSYG----FSSscDLHILSYYQEGW 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654249257 258 MLYFKGH---PIMPAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQ 315
Cdd:PRK14573 248 RSYFSAKflgVVYQDIELNLVGMHNVANAAAAMGIALTLGIDEGAIRNALKGFSGVQRRLE 308
|
|
| F430_CfbE |
NF033197 |
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ... |
113-422 |
3.21e-14 |
|
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in synthesizing coenzyme F430, which is used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) MurD, an enzyme of bacterial cell wall biosynthesis.
Pssm-ID: 467992 [Multi-domain] Cd Length: 419 Bit Score: 74.28 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 113 PIVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGY-------------PAS--EVVQKASAN-----DTLVMELSsfq 172
Cdd:NF033197 93 KFIEITGVKGKTTTAELLAHILSDEYVLLHTSRGTERypegelsnkgsitPASilNALELAEEIgiddyGFLIFEVS--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 173 LMGVDAFKphIAVITNLMpthldyhgsfEDYVAAKWRIQAEM-------TADDYLILNANQEISAALAKTTKATVipfst 245
Cdd:NF033197 170 LGGTGAGD--VGIITNIL----------EDYPIAGGKRSASAaklqslkNAKVGSINVADLGIYINGKNKLVITV----- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 246 qEVVDGAYLEGGMLYFKGHPImpAANLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQlVGKIKDIIF 325
Cdd:NF033197 233 -AGVEILSKYPLRFKYGNTEF--EFNPLLFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMA-VKKEGGVVI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 326 YNDSKS-TNILATQKALSGFDNKK--LILIAGGlDRGN---EFD---------DLVPDLRGLKqmIILGESAERMKRAAE 390
Cdd:NF033197 309 VDNINPgLNVKAIEYALDDALELLgdGTLVIGG-DFGVvceEIDidklsevlkKYRPKIDILV--GVGTELGKRLKKYLD 385
|
330 340 350
....*....|....*....|....*....|..
gi 1654249257 391 MAnvPYLEAADVAAATELAFQEAQAGDTILLS 422
Cdd:NF033197 386 KL--EGYEAGTLEEGLDDARELTGEGNTLVIY 415
|
|
| PRK14093 |
PRK14093 |
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; ... |
110-318 |
9.32e-11 |
|
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; Provisional
Pssm-ID: 184501 [Multi-domain] Cd Length: 479 Bit Score: 63.64 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 110 SESPIVGITGSNGKTTTTTMIADVLNAGGQS----ALLSGNIGYPASEVVQKASANDTlVMELSsfqlMG--------VD 177
Cdd:PRK14093 106 LEAKVIAVTGSVGKTSTKEALRGVLGAQGEThasvASFNNHWGVPLSLARCPADARFA-VFEIG----MNhageieplVK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 178 AFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNANQEISAALAKTTKAT----VIPFSTQEVVDGAY 253
Cdd:PRK14093 181 MVRPHVAIITTVEPVHLEFFSGIEAIADAKAEIFTGLEPGGAAVLNRDNPQFDRLAASARAAgiarIVSFGADEKADARL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 254 LEGGMlyfkgHPIMPAAN-----------LGVPGSHNIENALAAIAVAKLSGiADDVIVEV-LSHFG-----GVKHRLQL 316
Cdd:PRK14093 261 LDVAL-----HADCSAVHadilghdvtykLGMPGRHIAMNSLAVLAAAELAG-ADLALAALaLSQVQpaagrGVRHTLEV 334
|
..
gi 1654249257 317 VG 318
Cdd:PRK14093 335 GG 336
|
|
| PRK14022 |
PRK14022 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; |
114-305 |
2.32e-10 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
Pssm-ID: 237588 [Multi-domain] Cd Length: 481 Bit Score: 62.36 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 114 IVGITGSNGKTTTTTMIADVLNAGGQSALLSGNIGYPASEVVQKaSANDT--------------------LVMELSS--F 171
Cdd:PRK14022 112 LLAFTGTKGKTTAAYFAYHILKQLHKPAMLSTMNTTLDGETFFK-SALTTpesldlfkmmaeavdngmthLIMEVSSqaY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 172 QLMGVDAFKPHIAVITNLMPTHLDY--HGSFEDYVAAKWRIqaeMTADDYLILN-------------ANQEI------SA 230
Cdd:PRK14022 191 LVGRVYGLTFDVGVFLNITPDHIGPieHPTFEDYFYHKRLL---MENSKAVVVNsdmdhfselleqvTPQEHdfygidSE 267
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654249257 231 ALAKTTKAtvIPFSTQEVVDGAYleggmlyfkghpimpaaNLGVPGSHNIENALAA-IAVAKLsGIADDVIVEVLS 305
Cdd:PRK14022 268 NQIMASNA--FSFEATGKLAGTY-----------------DIQLIGKFNQENAMAAgLACLRL-GASLEDIQKGIA 323
|
|
| murF |
PRK10773 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed |
104-314 |
4.86e-10 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
Pssm-ID: 182718 [Multi-domain] Cd Length: 453 Bit Score: 61.20 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 104 ELAYLV---SESPIVGITGSNGKTTTTTMIADVLNAGGQSALLSGN----IGYPASeVVQKASANDTLVMELSSFQL--- 173
Cdd:PRK10773 89 QLAAWVrqqVPARVVALTGSSGKTSVKEMTAAILRQCGNTLYTAGNlnndIGVPLT-LLRLTPEHDYAVIELGANHQgei 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 174 -MGVDAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIQAEMTADDYLILNAN-------QEISAAlakttkATVIPFST 245
Cdd:PRK10773 168 aYTVSLTRPEAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLPENGIAIMNADsndwlnwQSVIGS------KTVWRFSP 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654249257 246 QEVVDGAYLEGGM------LYFKGH-PIMPAA-NLGVPGSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRL 314
Cdd:PRK10773 242 NAANSVDFTATNIhvtshgTEFTLHtPTGSVDvLLPLPGRHNIANALAAAALAMSVGATLDAVKAGLANLKAVPGRL 318
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
310-369 |
6.71e-10 |
|
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460731 [Multi-domain] Cd Length: 87 Bit Score: 55.43 E-value: 6.71e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654249257 310 VKHRLQLVGKIKDIIFYNDsKSTNILATQKALSGF---DNKKLILIAGG-LDRGNEFDDLVPDL 369
Cdd:pfam02875 1 VPGRLEVVGENNGVLVIDD-YAHNPDAMEAALRALrnlFPGRLILVFGGmGDRDAEFHALLGRL 63
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
113-355 |
7.42e-09 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 58.05 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 113 PIVGITGSNGKttttTMIADVLNaggqsALLS-------------GNIGYPASevVQKASANDTL-VME--LSSFQLMGV 176
Cdd:PRK11930 108 PVIGITGSNGK----TIVKEWLY-----QLLSpdynivrsprsynSQIGVPLS--VWQLNEEHELgIFEagISQPGEMEA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 177 --DAFKPHIAVITNLMPTHLDYHGSFEDYVAAKWRIqaeMTADDYLILNA-NQEISAALA-------------KTTKATV 240
Cdd:PRK11930 177 lqKIIKPTIGILTNIGGAHQENFRSIKQKIMEKLKL---FKDCDVIIYNGdNELISSCITksnltlkliswsrKDPEAPL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 241 -IPFSTQEVVDGAYleggMLYFKGHPImpaaNLGVP--GSHNIENALAAIAVAKLSGIADDVIVEVLSHFGGVKHRLQLV 317
Cdd:PRK11930 254 yIPFVEKKEDHTVI----SYTYKGEDF----HFEIPfiDDASIENLIHCIAVLLYLGYSADQIQERMARLEPVAMRLEVK 325
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1654249257 318 GKIKDIIFYNDSKSTNILATQKALSGFD----NKKLILIAGG 355
Cdd:PRK11930 326 EGINNCTLINDSYNSDLQSLDIALDFLNrrsqSKKKTLILSD 367
|
|
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
272-420 |
3.76e-05 |
|
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 45.87 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 272 LGVPGSHNIENALAAIAVAKLS-----GIADDVIVEVLSHfggVKH--RLQLVGKIKDIIF---YNDSKSTNILATQKAL 341
Cdd:COG0285 247 LPLLGAHQAENAALALAALEALrelglPISEEAIREGLAN---ARWpgRLEVLSRGPLVILdgaHNPAGARALAETLKEL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 342 sgFDNKKLILIAGGLdRGNEFDDLVPDLRGLKQMIIL-------GESAERMKRAAEMANVPYLEAADVAAATELAFQEAQ 414
Cdd:COG0285 324 --FPFRKLHLVFGML-ADKDIEGMLAALAPLADEVIVttppsprALDAEELAEAARELGLRVEVAPDVEEALEAALELAD 400
|
....*.
gi 1654249257 415 AGDTIL 420
Cdd:COG0285 401 PDDLIL 406
|
|
| poly_gGlu_PgsB |
TIGR04012 |
poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in ... |
114-395 |
2.22e-04 |
|
poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in biosynthesis and export of poly-gamma-glutamate, pgsB(capB) and pgsC(capC) are found to be involved in the synthesis per se. Members of this family are designated PgsB, a nomeclature that covers both cases in which the poly-gamma-glutamate is secreted and those in which it is retained to form capsular material.PgsB has been shown to have poly-gamma-glutamate activity by itself but is bound tightly by PgsC (TIGR04011). [Cell envelope, Other]
Pssm-ID: 188527 [Multi-domain] Cd Length: 366 Bit Score: 43.08 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 114 IVGITGSNGKTTTTTMIADVLNAGGQSAL-----LSGNIGYPASE-----------------VVQKASAN--DTLVMEL- 168
Cdd:TIGR04012 17 RIHVNGTRGKSTVTRLITAGLREGGYKVVgkttgTDARMIYPDGSefpifrpgganigeqkrVVKKAVKLkaDALVLECm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 169 -------SSFQLMGVDAfkpHIAVITNLMPTHLDYHGSFEDYVA----AKWRIQAEM-TADDYLIlnanqEISAALAKTT 236
Cdd:TIGR04012 97 avqpdyqIVFELKLVKA---NIGVITNVREDHMDVMGPTLDDVAeaftATIPYNGDLfTAEDDYL-----DFFKEAAKDR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 237 KATVIPFSTQEVVDGAYLEGGMLYFKghpimpaanlgvpgshniENALAAIAVAKLSGIADDV----IVEVLSHFGGVKh 312
Cdd:TIGR04012 169 NTKLIVADAEEISDDILRKFGYIVFP------------------ENVALALAVAEALGVDREIalrgMLNAPPDPGAMK- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654249257 313 RLQLVGKIKDIIFY-----NDSKST-NILATQKALSGFDNKKLILI---AGGLDRGNEFDDLVPDLRGLKQMIILGESAE 383
Cdd:TIGR04012 230 ILYLNDKNKRIFFVnafaaNDPVSTeRIWDRVCAKGYPTDKPVLIMncrADRVDRTKQFAEDVLPWSPADKLVLIGEGTE 309
|
330
....*....|..
gi 1654249257 384 RMKRAAEMANVP 395
Cdd:TIGR04012 310 LFTSVYKKGKIP 321
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
11-39 |
7.27e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 37.10 E-value: 7.27e-03
10 20
....*....|....*....|....*....
gi 1654249257 11 KVLILGLARSGEAAARLLTKLGALVTVND 39
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLD 50
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
1-62 |
7.41e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 38.12 E-value: 7.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654249257 1 MKKIREFQNKKVLILGLARSGEAAARLLTKLGALVTVndgkpFEENP-AAQALLEEGIKVVCG 62
Cdd:COG0569 87 MERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVV-----IDKDPeRVERLAEEDVLVIVG 144
|
|
| |
