|
Name |
Accession |
Description |
Interval |
E-value |
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
8-390 |
0e+00 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 658.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 8 PKKILLLGSGELGKELVVEAKRLGLEVIAIDKYENAPAMQLADNSFVIDMSDKEILKKKIKELNPDFVVPEIEALSIEAL 87
Cdd:PRK09288 12 ATRVMLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSHVIDMLDGDALRAVIEREKPDYIVPEIEAIATDAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 88 KELEDEGINIVPNARTVEITMNRDKIRDLASKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNRK 167
Cdd:PRK09288 92 VELEKEGFNVVPTARATRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 168 EDLLLAWNDALKNSRGKIVGVILEEFLNFDYEFTLLTIRKTSGENIFCEPIGHEQYKGDYQCSWQPLDMNQSLINEARKM 247
Cdd:PRK09288 172 EDIEKAWEYAQEGGRGGAGRVIVEEFIDFDYEITLLTVRAVDGGTHFCAPIGHRQEDGDYRESWQPQPMSPAALEEAQEI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 248 TTKILNNLNGSGIYGVEFFVRGKEVIFSELSPRPHDTGMVTLVSQNINEFELHLRAFLNLPIPNISLLKPSATRVIISDK 327
Cdd:PRK09288 252 AKKVTDALGGRGLFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQNLSEFELHARAILGLPIPDIRLYSPAASAVILAEG 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81835571 328 ESNTPSYSGLNEALELENTKVLIFGKPTAKKGRRMGVVLSTDDDLNIARENADKSALKIKIVS 390
Cdd:PRK09288 332 ESANPSFDGLAEALAVPGTDVRLFGKPEIRGGRRMGVALATGEDVEEAREKAKEAASKVKVVG 394
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
8-389 |
0e+00 |
|
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: 585.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 8 PKKILLLGSGELGKELVVEAKRLGLEVIAIDKYENAPAMQLADNSFVIDMSDKEILKKKIKELNPDFVVPEIEALSIEAL 87
Cdd:COG0027 12 ATKVMLLGSGELGKEVAIELQRLGVEVIAVDRYANAPAMQVAHRSYVIDMLDGDALRALIEREKPDFIVPEIEAIATDAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 88 KELEDEGINIVPNARTVEITMNRDKIRDLASKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNRK 167
Cdd:COG0027 92 VELEAEGFRVVPTARAVRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 168 EDLLLAWNDALKNSRGKIVGVILEEFLNFDYEFTLLTIRKTSGENIFCEPIGHEQYKGDYQCSWQPLDMNQSLINEARKM 247
Cdd:COG0027 172 ADIEAAWEYAQEGGRGGAGRVIVEGFVDFDYEITLLTVRAVDGPTHFCEPIGHRQEDGDYRESWQPQPMSEAALAKAQEI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 248 TTKILNNLNGSGIYGVEFFVRGKEVIFSELSPRPHDTGMVTLVSQNINEFELHLRAFLNLPIPNISLLKPSATRVIISDK 327
Cdd:COG0027 252 AKKVTDALGGRGIFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQDLSEFALHARAILGLPVPEIRLVGPAASAVILAEG 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81835571 328 ESNTPSYSGLNEALELENTKVLIFGKPTAKKGRRMGVVLSTDDDLNIARENADKSALKIKIV 389
Cdd:COG0027 332 ESWAPAFDGLAEALAVPGTDLRLFGKPEAYGRRRMGVALATADDVEEAREKAREAAAKVKVV 393
|
|
| purT |
TIGR01142 |
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN ... |
10-388 |
9.99e-180 |
|
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN (TIGR00639) [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 130212 Cd Length: 380 Bit Score: 504.66 E-value: 9.99e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 10 KILLLGSGELGKELVVEAKRLGLEVIAIDKYENAPAMQLADNSFVIDMSDKEILKKKIKELNPDFVVPEIEALSIEALKE 89
Cdd:TIGR01142 1 RVLLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSYVINMLDGDALRAVIEREKPDYIVPEIEAIATDALFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 90 LEDEGINIVPNARTVEITMNRDKIRDLASKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNRKED 169
Cdd:TIGR01142 81 LEKEGYFVVPNARATKLTMNREGIRRLAAEELGLPTSRYMFADSLDELREAVEKIGYPCVVKPVMSSSGKGQSVVRGPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 170 LLLAWNDALKNSRGKIVGVILEEFLNFDYEFTLLTIRKTSGENIFCEPIGHEQYKGDYQCSWQPLDMNQSLINEARKMTT 249
Cdd:TIGR01142 161 IEKAWEYAQEGARGGAGRVIVEEFIDFDYEITLLTVRHVDGNTTFCAPIGHRQIDGDYHESWQPQEMSEKALEEAQRIAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 250 KILNNLNGSGIYGVEFFVRGKEVIFSELSPRPHDTGMVTLVSQNINEFELHLRAFLNLPIPNISLLKPSATRVIISDKES 329
Cdd:TIGR01142 241 RITDALGGYGLFGVELFVKGDEVIFSEVSPRPHDTGMVTLISQGLSEFALHVRAILGLPIPGIPQLGPAASAVIKAKVTG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 81835571 330 NTPSYSGLNEALELENTKVLIFGKPTAKKGRRMGVVLSTDDDLNIARENADKSALKIKI 388
Cdd:TIGR01142 321 YSPAFRGLEKALSVPNTQVRLFGKPEAYVGRRLGVALATAKSVEAARERAEEVAHAVEV 379
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
19-381 |
2.37e-60 |
|
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: 198.76 E-value: 2.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 19 LGKELVVEAKRLGLEVIAIDKYENAPAMQLADNSFVIDMSDKEILKkkikelnpDF-----VVP-EIEALSIEALKELED 92
Cdd:COG0026 2 LGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALR--------EFaercdVVTfEFENVPAEALEALEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 93 EgINIVPNARTVEITmnRDKI--RDLAsKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIK-PLMSSSGKGQSLVNRKED 169
Cdd:COG0026 74 E-VPVRPGPEALEIA--QDRLleKAFL-AELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKtRRGGYDGKGQVVIKSAAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 170 LLLAWnDALKNsrgkiVGVILEEFLNFDYEFTLLTIRKTSGE-NIFcePIGHEQYKgDYQCSWQ--PLDMNQSLINEARK 246
Cdd:COG0026 150 LEAAW-AALGG-----GPCILEEFVPFERELSVIVARSPDGEvATY--PVVENVHR-NGILDESiaPARISEALAAEAEE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 247 MTTKILNNLNGSGIYGVEFFV-RGKEVIFSELSPRPHDTGMVTLVSQNINEFELHLRAFLNLPIPNISLLKPSATRVIIS 325
Cdd:COG0026 221 IAKRIAEALDYVGVLAVEFFVtKDGELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGDTELLSPAVMVNLLG 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 81835571 326 DKESNTpsysGLNEALELENTKVLIFGKPTAKKGRRMGVVLSTDDDLNIARENADK 381
Cdd:COG0026 301 DDWEDP----GWEALLALPGAHLHLYGKKEARPGRKMGHVTVLGDDLEEALERARA 352
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
8-386 |
5.77e-58 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 193.06 E-value: 5.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 8 PKKILLLGSGELGKELVVEAKRLGLEVIAIDKYENAPAMQLADNSFVIDMSDKEILKKKIKELnpDFVVPEIEALSIEAL 87
Cdd:PRK06019 2 MKTIGIIGGGQLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEQC--DVITYEFENVPAEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 88 KELEDEgINIVPNARTVEITmnRDKI--RDLAsKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKplmSSS----GKGQ 161
Cdd:PRK06019 80 DALAAR-VPVPPGPDALAIA--QDRLteKQFL-DKLGIPVAPFAVVDSAEDLEAALADLGLPAVLK---TRRggydGKGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 162 SLVNRKEDLLLAWnDALKNsrgkiVGVILEEFLNFDYEFTLLTIRKTSGEnIFCEPIGH-EQYKGdyQCSWQ--PLDMNQ 238
Cdd:PRK06019 153 WVIRSAEDLEAAW-ALLGS-----VPCILEEFVPFEREVSVIVARGRDGE-VVFYPLVEnVHRNG--ILRTSiaPARISA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 239 SLINEARKMTTKILNNLNGSGIYGVEFFVRG-KEVIFSELSPRPHDTGMVTL----VSQnineFELHLRAFLNLPIPNIS 313
Cdd:PRK06019 224 ELQAQAEEIASRIAEELDYVGVLAVEFFVTGdGELLVNEIAPRPHNSGHWTIeacsTSQ----FEQHLRAILGLPLGTTR 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81835571 314 LLKPSATRVIISDKesntPSYSGLNEALELENTKVLIFGKPTAKKGRRMGVVLSTDDDLNIARENADKSALKI 386
Cdd:PRK06019 300 LLSPAVMVNLLGDD----WLEPRWDALLALPGAHLHLYGKAEARPGRKMGHVTVLGDDVEALLAKLEALAPDW 368
|
|
| purK |
TIGR01161 |
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole ... |
14-371 |
7.74e-55 |
|
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, N5-carboxyaminoimidazole ribonucleotide synthetase, which hydrolyzes ATP and converts AIR to N5-CAIR. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273473 [Multi-domain] Cd Length: 352 Bit Score: 184.46 E-value: 7.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 14 LGSGELGKELVVEAKRLGLEVIAIDKYENAPAMQLADNsfVIDMSDKEILKKKIKELNPDFVVPEIEALSIEALKELEDE 93
Cdd:TIGR01161 5 LGGGQLGRMLALAARPLGIKVHVLDPDANSPAVQVADH--VVLAPFFDPAAIRELAESCDVITFEFEHVDVEALEKLEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 94 GINIVPNARTVEITMNRDKIRdLASKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKplmSSS----GKGQSLVNRKED 169
Cdd:TIGR01161 83 GVKLFPSPDALAIIQDRLTQK-QFLQKLGLPVPPFLVIKDEEELDAALQELGFPVVLK---ARTggydGRGQYRIRNEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 170 LllawNDALKNSRGKivGVILEEFLNFDYEFTLLTIRKTSGEnIFCEPIGHE-QYKGDYQCSWQPLDMNQSLINEARKMT 248
Cdd:TIGR01161 159 L----PQAAKELGDR--ECIVEEFVPFERELSVIVARSADGE-TAFYPVVENiHQDGILRYVVAPAAVPDAIQARAEEIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 249 TKILNNLNGSGIYGVEFFVRG-KEVIFSELSPRPHDTGMVTLVSQNINEFELHLRAFLNLPIPNISLLKPSATRVIISDK 327
Cdd:TIGR01161 232 RRLMEELGYVGVLAVEMFVLPdGRLLINELAPRVHNSGHYTLDGCSTSQFEQHLRAILGLPLGSTELLLPSVMVNLLGTE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 81835571 328 ESNTPsysGLNEALELENTKVLIFGKPTAKKGRRMGVVLSTDDD 371
Cdd:TIGR01161 312 DDVIP---LWEEILALPGAKLHWYGKAEVRPGRKVGHVNLVGSD 352
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
119-291 |
1.23e-51 |
|
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: 170.13 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 119 KELNIKTAKFSYVFNVDELEIKSSEIGFPLLIK-PLMSSSGKGQSLVNRKEDLLLAWnDALKNSRgkivgVILEEFLNFD 197
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKaRRGGYDGKGQYVVRSEADLPQAW-EELGDGP-----VIVEEFVPFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 198 YEFTLLTIRKTSGENIFCEPIGHEQYKGDYQCSWQPLDMNQSLINEARKMTTKILNNLNGSGIYGVEFFV-RGKEVIFSE 276
Cdd:pfam02222 75 RELSVLVVRSVDGETAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVtEDGDLLINE 154
|
170
....*....|....*
gi 81835571 277 LSPRPHDTGMVTLVS 291
Cdd:pfam02222 155 LAPRPHNSGHYTLDG 169
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
14-385 |
9.83e-39 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 145.97 E-value: 9.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 14 LGSGELGKELVVEAKRLGLEVIAIDKYENAPAMQLADNSFVIDMSDKEILKKKIKELnpDFVVPEIEALSIEALKELEDE 93
Cdd:PLN02948 28 LGGGQLGRMLCQAASQMGIKVKVLDPLEDCPASSVAARHVVGSFDDRAAVREFAKRC--DVLTVEIEHVDVDTLEALEKQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 94 GINIVPNARTVEITmnRDKIRdlaSKE----LNIKTAKFSYVFNVDELEIKSSEIGFPLLIKP-LMSSSGKGQSLVNRKE 168
Cdd:PLN02948 106 GVDVQPKSSTIRII--QDKYA---QKVhfskHGIPLPEFMEIDDLESAEKAGDLFGYPLMLKSrRLAYDGRGNAVAKTEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 169 DLLlawnDALKNSRGKIVGVILEEFLNFDYEFTLLTIRKTSGEnIFCEPIGHEQYKgDYQC--SWQPLDMNQSLINEARK 246
Cdd:PLN02948 181 DLS----SAVAALGGFERGLYAEKWAPFVKELAVMVARSRDGS-TRCYPVVETIHK-DNIChvVEAPANVPWKVAKLATD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 247 MTTKILNNLNGSGIYGVEFFVRGKE-VIFSELSPRPHDTGMVTLVSQNINEFELHLRAFLNLPIPNISLLKPSATRVIIS 325
Cdd:PLN02948 255 VAEKAVGSLEGAGVFGVELFLLKDGqILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPLGDTSMKVPAAIMYNIL 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81835571 326 DKESNTPSYS----GLNEALELENTKVLIFGKPTAKKGRRMG---VVLST----DDDLN--IARENADKSALK 385
Cdd:PLN02948 335 GEDEGEAGFRlahqLMGRALNIPGASVHWYGKPEMRKQRKMGhitVVGPSaaevEARLDqlLAEESADPDALP 407
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
71-309 |
5.27e-17 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 79.92 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 71 NPDFVVPEIEALSIEALKELEDEGINiVPNARTVEITmnRDKI--RDLAsKELNIKTAKFSYVFNVDELEIKSSEIGFPL 148
Cdd:COG0439 17 GIDAVLSESEFAVETAAELAEELGLP-GPSPEAIRAM--RDKVlmREAL-AAAGVPVPGFALVDSPEEALAFAEEIGYPV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 149 LIKPLMSSSGKGQSLVNRKEDLLLAWNDALKNSRGKIVG--VILEEFLN----------FDYEFTLLTI-RKTSGENIFC 215
Cdd:COG0439 93 VVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNgeVLVEEFLEgreysveglvRDGEVVVCSItRKHQKPPYFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 216 EpIGHEqykgdyqcswQPLDMNQSLINEARKMTTKILNNLN-GSGIYGVEFFV-RGKEVIFSELSPRPHDTGMVTLV--S 291
Cdd:COG0439 173 E-LGHE----------APSPLPEELRAEIGELVARALRALGyRRGAFHTEFLLtPDGEPYLIEINARLGGEHIPPLTelA 241
|
250
....*....|....*...
gi 81835571 292 QNINEFELHLRAFLNLPI 309
Cdd:COG0439 242 TGVDLVREQIRLALGEPR 259
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
10-280 |
4.55e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 69.53 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 10 KILLLGSGELGKelVVEAKRLGLE---VIAIDKYENAPAMQLADNSFVI-DMSDKE---ILKKKIKELNPDFVVPEIEA- 81
Cdd:PRK12767 3 NILVTSAGRRVQ--LVKALKKSLLkgrVIGADISELAPALYFADKFYVVpKVTDPNyidRLLDICKKEKIDLLIPLIDPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 82 LSI--EALKELEDEGIN-IVPNARTVEITMNRDKIRDLAsKELNIKTAKFSYVFNVDELE--IKSSEIGFPLLIKPLMSS 156
Cdd:PRK12767 81 LPLlaQNRDRFEEIGVKvLVSSKEVIEICNDKWLTYEFL-KENGIPTPKSYLPESLEDFKaaLAKGELQFPLFVKPRDGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 157 SGKGQSLVNRKEDLLLAWNdalknsrgKIVGVILEEFLNfDYEFTLLTIRKTSGE--NIF----CEPIGHEQYKGDyqcs 230
Cdd:PRK12767 160 ASIGVFKVNDKEELEFLLE--------YVPNLIIQEFIE-GQEYTVDVLCDLNGEviSIVprkrIEVRAGETSKGV---- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 81835571 231 wqpldmnqSLINEA-RKMTTKILNNLNGSGIYGVEFFVRGKEVIFSELSPR 280
Cdd:PRK12767 227 --------TVKDPElFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPR 269
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
88-317 |
9.47e-13 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 70.03 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 88 KELEDEGINIV-PNARTVEITMNRDKIRDLAsKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNR 166
Cdd:TIGR01369 647 KALEEAGVPILgTSPESIDRAEDREKFSELL-DELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYN 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 167 KEDLLLAWNDALKNSRGKivGVILEEFLNFDYEFTLLTIrkTSGENIFCEPIG-H-EQ---YKGDYQCSWQPLDMNQSLI 241
Cdd:TIGR01369 726 EEELRRYLEEAVAVSPEH--PVLIDKYLEDAVEVDVDAV--SDGEEVLIPGIMeHiEEagvHSGDSTCVLPPQTLSAEIV 801
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81835571 242 NEARKMTTKILNNLNGSGIYGVEFFVRGKEVIFSELSPRPHDTgmVTLVSQ--NINEFELHLRAFLNLPIPNISLLKP 317
Cdd:TIGR01369 802 DRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRT--VPFVSKatGVPLAKLAVRVMLGKKLEELGVGKE 877
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
88-280 |
5.10e-09 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 57.97 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 88 KELEDEGINI-VP----NARTVEITMNRDKIRDLAsKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQS 162
Cdd:COG0458 88 VELEEAGILEgVKilgtSPDAIDLAEDRELFKELL-DKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 163 LVNRKEDLLLAWNDALKNSRGKivGVILEEFLN----------FDYEFTLLTIrkTSGENIfcEPIG-HeqyKGDYQCSW 231
Cdd:COG0458 167 IVYNEEELEEYLERALKVSPDH--PVLIDESLLgakeievdvvRDGEDNVIIV--GIMEHI--EPAGvH---SGDSICVA 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 81835571 232 QPLDMNQSLINEARKMTTKILNNLNGSGIYGVEFFVRGKEVIFSELSPR 280
Cdd:COG0458 238 PPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPR 286
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
10-281 |
6.60e-09 |
|
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: 56.49 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 10 KILLLGSGELG---KELVVEAKRLGLEVIAIDKyenapamqladNSFVIDMSDKEILKKKIKELNPDFVVPEIEAL--SI 84
Cdd:COG0189 3 KIAILTDPPDKdstKALIEAAQRRGHEVEVIDP-----------DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPPfyGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 85 EALKELEDEGINIVPNARTVEItmNRDKIR--DLASKeLNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQS 162
Cdd:COG0189 72 ALLRQLEAAGVPVVNDPEAIRR--ARDKLFtlQLLAR-AGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 163 LVNRKEDLLLAWnDALKNSRGKIvgVILEEFLNFDYEFtllTIRktsgenIFC---EPIGHEQY---KGDYQC------S 230
Cdd:COG0189 149 LVEDEDALESIL-EALTELGSEP--VLVQEFIPEEDGR---DIR------VLVvggEPVAAIRRipaEGEFRTnlarggR 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 81835571 231 WQPLDMNQSLINEARKMTTKIlnnlnGSGIYGVEFFVRGKEVIFSELSPRP 281
Cdd:COG0189 217 AEPVELTDEERELALRAAPAL-----GLDFAGVDLIEDDDGPLVLEVNVTP 262
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
71-296 |
3.94e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 52.28 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 71 NPDFVVPEIEALSIEAL-KELEDEGINIV-PNARTVEITMNRDKIRDLAsKELNIKTAKFSYVFNVDELEIKSSEIGFPL 148
Cdd:PRK12815 630 NIKGVIVQFGGQTAINLaKGLEEAGLTILgTSPDTIDRLEDRDRFYQLL-DELGLPHVPGLTATDEEEAFAFAKRIGYPV 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 149 LIKPLMSSSGKGQSLVNRKEDL--LLAWNDALKNSrgkivgVILEEFLN-FDYEFTLLtirkTSGENIFCEPI-GH-EQ- 222
Cdd:PRK12815 709 LIRPSYVIGGQGMAVVYDEPALeaYLAENASQLYP------ILIDQFIDgKEYEVDAI----SDGEDVTIPGIiEHiEQa 778
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81835571 223 --YKGDYQCSWQPLDMNQSLINEARKMTTKILNNLNGSGIYGVEFFVRGKEVIFSELSPRPHDTgmVTLVSQNINE 296
Cdd:PRK12815 779 gvHSGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRT--VPFVSKATGV 852
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
106-289 |
1.40e-06 |
|
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: 49.59 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 106 ITMNRDKIRDLAsKELNIKTAKFSYV----FNVDELEIKSSE--IGFPLLIKPLMSSSGKGQSLVNRKEDLLLAWNDALK 179
Cdd:TIGR01205 102 LSMDKLLTKLLW-KALGLPTPDYIVLtqnrASADELECEQVAepLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 180 NSRgkivGVILEEFLNfDYEFTLLTIRKTSGENIfCEPIGHEQYKGDYQCSWQ--------PLDMNQSLINEARKMTTKI 251
Cdd:TIGR01205 181 YDE----EVLVEQFIK-GRELEVSILGNEEALPI-IEIVPEIEGFYDYEAKYLdgsteyviPAPLDEELEEKIKELALKA 254
|
170 180 190
....*....|....*....|....*....|....*....
gi 81835571 252 LNNLNGSGIYGVEFFV-RGKEVIFSELSPRPhdtGMVTL 289
Cdd:TIGR01205 255 YKALGCRGLARVDFFLdEEGEIYLNEINTIP---GMTAI 290
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
88-280 |
1.09e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 47.78 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 88 KELEDEGINIV-PNARTVEITMNRDKIRDLAsKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPlmsS---SGKGQSL 163
Cdd:PRK05294 647 KALEAAGVPILgTSPDAIDLAEDRERFSKLL-EKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRP---SyvlGGRAMEI 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 164 VNRKEDLLLAWNDALKNSRGKivGVILEEFLN----------FDyeftlltirktsGENIFcepIG----H-EQ---YKG 225
Cdd:PRK05294 723 VYDEEELERYMREAVKVSPDH--PVLIDKFLEgaievdvdaiCD------------GEDVL---IGgimeHiEEagvHSG 785
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 81835571 226 DYQCSWQPLDMNQSLINEARKMTTKILNNLNGSGIYGVEFFVRGKEVIFSELSPR 280
Cdd:PRK05294 786 DSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPR 840
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
106-194 |
1.68e-05 |
|
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: 46.25 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 106 ITMnrDKIRdlaSKEL----NIKTAKFSYVF--NVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNRKEDLLLAWNDALK 179
Cdd:COG1181 92 LAM--DKAL---TKRVlaaaGLPTPPYVVLRrgELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFK 166
|
90
....*....|....*
gi 81835571 180 NSRgkivGVILEEFL 194
Cdd:COG1181 167 YDD----KVLVEEFI 177
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
131-198 |
3.38e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.92 E-value: 3.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 131 VFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSL-VNRKEDLLLAWNDALKNSRgkivGVILEEFLN-FDY 198
Cdd:PRK14016 235 VTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESS----DVIVERYIPgKDH 300
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
119-222 |
5.46e-05 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 43.81 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 119 KELNIKTAKFSYVFNVDELEIKSSEIGFPLL-IKPLMSSSGKGQSLVNRKEDLLLAWNDALKNSRGKIVG--VILEEFLN 195
Cdd:pfam01071 11 KRYGIPTAEYETFTDPEEAKSYIQEAGFPAIvVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAGetVVIEEFLE 90
|
90 100
....*....|....*....|....*..
gi 81835571 196 fDYEFTLLTIrkTSGENIFcePIGHEQ 222
Cdd:pfam01071 91 -GEEVSVLAF--VDGKTVK--PLPPAQ 112
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
103-194 |
2.01e-04 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 43.45 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 103 TVEITMNRDKIRDlASKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNRKEDLLLAWNDALKNSr 182
Cdd:TIGR01369 121 AIKKAEDRELFRE-AMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSAS- 198
|
90
....*....|..
gi 81835571 183 gKIVGVILEEFL 194
Cdd:TIGR01369 199 -PINQVLVEKSL 209
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
29-211 |
2.47e-04 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 42.99 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 29 RLGLEVIAIDKYENAPAMQ--LADNSFVI-DMSDKEIL-----KKKIKELNPDFVVP----EIEALSiEALKELEDEGIN 96
Cdd:COG3919 26 EAGVRVIVVDRDPLGPAARsrYVDEVVVVpDPGDDPEAfvdalLELAERHGPDVLIPtgdeYVELLS-RHRDELEEHYRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 97 IVPNARTVEITMNRDKIRDLAsKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSS--------GKGQSLVNRKE 168
Cdd:COG3919 105 PYPDADLLDRLLDKERFYELA-EELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPADSVGydelsfpgKKKVFYVDDRE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 81835571 169 DLLlawnDALKNSRGKIVGVILEEFL--NFDYEFTLLTIRKTSGE 211
Cdd:COG3919 184 ELL----ALLRRIAAAGYELIVQEYIpgDDGEMRGLTAYVDRDGE 224
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
106-194 |
3.80e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 42.02 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 106 ITMnrDKIRdlaSKEL----NIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNRKEDLLLAWNDALKNs 181
Cdd:PRK01372 95 LAM--DKLR---TKLVwqaaGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKY- 168
|
90
....*....|...
gi 81835571 182 rGKIvgVILEEFL 194
Cdd:PRK01372 169 -DDE--VLVEKYI 178
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
100-280 |
8.10e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 41.49 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 100 NARTVEITMNRDKIRDLAsKELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNRKEDLLLAWNDALK 179
Cdd:PRK12815 119 NIEAIQKGEDRERFRALM-KELGEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 180 NSrgKIVGVILEE-FLNF-DYEF--------TLLTIrkTSGENIfcEPIG-HeqyKGDYQCSWQPLDMNQSLINEARKMT 248
Cdd:PRK12815 198 AS--PIHQCLLEEsIAGWkEIEYevmrdrngNCITV--CNMENI--DPVGiH---TGDSIVVAPSQTLTDDEYQMLRSAS 268
|
170 180 190
....*....|....*....|....*....|....
gi 81835571 249 TKILNNLNGSGIYGVEFFV--RGKEVIFSELSPR 280
Cdd:PRK12815 269 LKIISALGVVGGCNIQFALdpKSKQYYLIEVNPR 302
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
119-294 |
1.94e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.53 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 119 KELNIKTAKFSYVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNRKEDLLLAWNDALKNSRGKivGVILEEFLNFDY 198
Cdd:PLN02735 711 NELKIEQPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPER--PVLVDKYLSDAT 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 199 EFTLLTIRKTSGENIFCEPIGH-EQ---YKGDYQCSWQPLDMNQSLINEARKMTTKILNNLNGSGIYGVEFFV-RGKEVI 273
Cdd:PLN02735 789 EIDVDALADSEGNVVIGGIMEHiEQagvHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVY 868
|
170 180
....*....|....*....|.
gi 81835571 274 FSELSPRPHDTgmVTLVSQNI 294
Cdd:PLN02735 869 IIEANPRASRT--VPFVSKAI 887
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
97-244 |
3.22e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 39.31 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 97 IVPNARTVEITMNRDKIRDLASK---------ELNIKTAKFSyvfnvdeLEIkSSEIGFPLLIKPLMSSSGKGQSLVNRK 167
Cdd:PRK05586 103 IGPDSETIELMGNKSNAREIMIKagvpvvpgsEGEIENEEEA-------LEI-AKEIGYPVMVKASAGGGGRGIRIVRSE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 168 EDLLLAWNDALKNSRGKIV--GVILEEFLNF--DYEFTLLtirktsgenifCEPIGHEQYKGDYQCSWQplDMNQSLINE 243
Cdd:PRK05586 175 EELIKAFNTAKSEAKAAFGddSMYIEKFIENpkHIEFQIL-----------GDNYGNVVHLGERDCSLQ--RRNQKVLEE 241
|
.
gi 81835571 244 A 244
Cdd:PRK05586 242 A 242
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
142-281 |
4.82e-03 |
|
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: 38.07 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 142 SEIGFPLLIKPLMSSSGKGQSLVNRKEDLLLAWNDALKNSRgkivGVILEEFLNFDyEFTLLTIRKTSGEnifCEPIGHE 221
Cdd:pfam07478 33 EALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDE----KVLVEEGIEGR-EIECAVLGNEDPE---VSPVGEI 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81835571 222 QYKG---DYQCSWQ--------PLDMNQSLINEARKMTTKILNNLNGSGIYGVEFFVRGK-EVIFSELSPRP 281
Cdd:pfam07478 105 VPSGgfyDYEAKYIddsaqivvPADLEEEQEEQIQELALKAYKALGCRGLARVDFFLTEDgEIVLNEVNTIP 176
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
111-194 |
5.37e-03 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 38.05 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 111 DKIR-DLASKELNIKTAKFS--YVFNVDELEIKSSEIGFPLLIKPLMSSSGKGQSLVNRKEDLLLAWNDALKNSRGKIV- 186
Cdd:pfam02786 1 DKVLfKAAMKEAGVPTVPGTagPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGn 80
|
....*....
gi 81835571 187 -GVILEEFL 194
Cdd:pfam02786 81 pQVLVEKSL 89
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
233-324 |
8.73e-03 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 37.98 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81835571 233 PLDMNQSLINEARKMTTKILNNLNGSGIYGVEFFVRGKEVIFSELSPRPhdTGMVTLV--SQNINEFELHLRAFLN-LPI 309
Cdd:COG2232 215 PLALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRP--QASLDLYedATGGNLFDAHLRACRGeLPE 292
|
90
....*....|....*
gi 81835571 310 PNISLLKPSATRVII 324
Cdd:COG2232 293 VPRPKPRRVAAKAIL 307
|
|
| |
