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Conserved domains on  [gi|807045910|ref|NP_001293008|]
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multifunctional protein CAD isoform 2 [Homo sapiens]

Protein Classification

trifunctional carbamoyl-phosphate synthase/dihydroorotase/aspartate carbamoyltransferase( domain architecture ID 12849551)

trifunctional carbamoyl-phosphate synthase (CPS)/dihydroorotase/aspartate carbamoyltransferase containing small and large subunits of CPS, is involved in pyrimidine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSaseII_lrg super family cl36884
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 391-1377 0e+00

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]


The actual alignment was detected with superfamily member TIGR01369:

Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1630.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPD 470
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   471 GVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369   84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   551 PVLVRAAFALGGLGSGFASNREELSALVAPAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYGNCVT-------------- 614
Cdd:TIGR01369  164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITvcnmenfdpmgvht 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   615 -------------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAK 645
Cdd:TIGR01369  244 gdsivvapsqtltdkeyqmlrdasikiirelgieggcnvqfalnpdsgrYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   646 LALGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 724
Cdd:TIGR01369  324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   725 VGFDHT---VKPVSD--MELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDL 799
Cdd:TIGR01369  404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   800 LQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRT-PHVLVLGSG 878
Cdd:TIGR01369  484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSG 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   879 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 958
Cdd:TIGR01369  564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   959 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVA 1038
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1039 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLER 1118
Cdd:TIGR01369  724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1119 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG--LMTGSGVV 1196
Cdd:TIGR01369  804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1197 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLG 1276
Cdd:TIGR01369  884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1277 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILEQLAEKNFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1356
Cdd:TIGR01369  964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029

                         1050      1060
                   ....*....|....*....|.
gi 807045910  1357 ADFSVPLIIDIKCTKLFVEAL 1377
Cdd:TIGR01369 1030 LDYGVPLITTLNTAEAFAEAL 1050
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1397-1743 0e+00

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


:

Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 631.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1397 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1477 ENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKE 1556
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1557 EILLIKAAKARGLPVTCEVAPHHLFLSHDDLERlgpGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSR 1636
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1637 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1716
Cdd:cd01316   238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317

                         330       340
                  ....*....|....*....|....*..
gi 807045910 1717 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1743
Cdd:cd01316   318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-355 5.26e-160

carbamoyl-phosphate synthase small subunit;


:

Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 496.52  E-value: 5.26e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    1 MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSG 80
Cdd:PRK12564    4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   81 IHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLP-----FLDPNA 155
Cdd:PRK12564   75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  156 RPLVPEVSIKTPRVFNTGGA---PRILALDCGLKYNQIRCLCQRGAEVTVVPWD---HALDSQEYEGLFLSNGPGDPASY 229
Cdd:PRK12564  155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  230 PSVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWA 309
Cdd:PRK12564  235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 807045910  310 PLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLE 355
Cdd:PRK12564  313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1856-2161 2.69e-140

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


:

Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 439.10  E-value: 2.69e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1856 HSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1935
Cdd:COG0540     1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1936 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2014
Cdd:COG0540    81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2015 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERFGSTQ- 2093
Cdd:COG0540   161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFTDGLf 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807045910 2094 -EYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2161
Cdd:COG0540   234 pSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1750-1869 8.75e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.84  E-value: 8.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1750 PQGAVPQLPPSAPATSEMTTTPerPRRGIPGLPDGRFhlPPRIHRASDPGLPAEEPKEKSSRKVAEPELMGTPDG--TCY 1827
Cdd:pfam03154  177 QSGAASPPSPPPPGTTQAATAG--PTPSAPSVPPQGS--PATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPplQPM 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 807045910  1828 PPPPVPRQASPQNLGTPgLLHPQTSPLLHSLVG-----QHILSVQQF 1869
Cdd:pfam03154  253 TQPPPPSQVSPQPLPQP-SLHGQMPPMPHSLQTgpshmQHPVPPQPF 298
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 391-1377 0e+00

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: 1630.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPD 470
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   471 GVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369   84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   551 PVLVRAAFALGGLGSGFASNREELSALVAPAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYGNCVT-------------- 614
Cdd:TIGR01369  164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITvcnmenfdpmgvht 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   615 -------------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAK 645
Cdd:TIGR01369  244 gdsivvapsqtltdkeyqmlrdasikiirelgieggcnvqfalnpdsgrYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   646 LALGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 724
Cdd:TIGR01369  324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   725 VGFDHT---VKPVSD--MELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDL 799
Cdd:TIGR01369  404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   800 LQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRT-PHVLVLGSG 878
Cdd:TIGR01369  484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSG 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   879 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 958
Cdd:TIGR01369  564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   959 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVA 1038
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1039 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLER 1118
Cdd:TIGR01369  724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1119 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG--LMTGSGVV 1196
Cdd:TIGR01369  804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1197 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLG 1276
Cdd:TIGR01369  884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1277 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILEQLAEKNFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1356
Cdd:TIGR01369  964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029

                         1050      1060
                   ....*....|....*....|.
gi 807045910  1357 ADFSVPLIIDIKCTKLFVEAL 1377
Cdd:TIGR01369 1030 LDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
394-1377 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1281.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  554 VRAAFALGGLGSGFASNREELSALVAPAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYGNCVT----------------- 614
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIvcsienidpmgvhtgds 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  615 -----------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKLA 647
Cdd:PRK05294  248 itvapaqtltdkeyqmlrdasiaiireigvetggcnvqfalnpkdgrYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  648 LGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVG 726
Cdd:PRK05294  328 VGYTLDEIKNDITGKTpASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  727 FDHTVKPVSDME-----LETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrGQPLPPDLLQ 801
Cdd:PRK05294  408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEN-GLPLDAELLR 486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  802 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYR 881
Cdd:PRK05294  487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  882 IGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMA 961
Cdd:PRK05294  567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  962 MALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTD 1041
Cdd:PRK05294  647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1042 GDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGVVAAIA-ISEHVENAGVHSGDATLVTPPQDITAKTLERIK 1120
Cdd:PRK05294  727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1121 AIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTG--SGVVGV 1198
Cdd:PRK05294  806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGliPPYVAV 885

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1199 KVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKK-NILLTIgSYKNKSELLPTVRLLESLGY 1277
Cdd:PRK05294  886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1278 SLYASLGTADFYTEHGVKVTAVDWHFEEAVDgecppqrsILEQLAEKNFELVINlSMRGAGGRRlssfvtKGYRTRRLAA 1357
Cdd:PRK05294  965 KILATSGTAKFLREAGIPVELVNKVHEGRPH--------IVDLIKNGEIDLVIN-TPTGRQAIR------DGFSIRRAAL 1029

                        1050      1060
                  ....*....|....*....|
gi 807045910 1358 DFSVPLIIDIKCTKLFVEAL 1377
Cdd:PRK05294 1030 EYKVPYITTLAGARAAVKAI 1049
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1397-1743 0e+00

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 631.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1397 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1477 ENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKE 1556
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1557 EILLIKAAKARGLPVTCEVAPHHLFLSHDDLERlgpGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSR 1636
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1637 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1716
Cdd:cd01316   238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317

                         330       340
                  ....*....|....*....|....*..
gi 807045910 1717 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1743
Cdd:cd01316   318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 875-1377 1.65e-175

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: 546.78  E-value: 1.65e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  875 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 954
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  955 QLPNNMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVL 1030
Cdd:COG0458    81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1031 SGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGV--VAAIAISEHVENAGVHSGDATLVTPP 1108
Cdd:COG0458   161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVV-RDGEdnVIIVGIMEHIEPAGVHSGDSICVAPP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1109 QDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG 1188
Cdd:COG0458   240 QTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1189 LMTG----SGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKnILLTIGSYKNKSE 1264
Cdd:COG0458   320 NDTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDKEE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1265 LLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAGGRRLSS 1344
Cdd:COG0458   399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEG--------RPIIVDEIELEEIILVINTLLGAKSLGDSDG 470

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 807045910 1345 F------VTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1377
Cdd:COG0458   471 IirralaAKVPYVTTLAAAAAAALAIKAVETEAGEFEEA 509
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-355 5.26e-160

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 496.52  E-value: 5.26e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    1 MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSG 80
Cdd:PRK12564    4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   81 IHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLP-----FLDPNA 155
Cdd:PRK12564   75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  156 RPLVPEVSIKTPRVFNTGGA---PRILALDCGLKYNQIRCLCQRGAEVTVVPWD---HALDSQEYEGLFLSNGPGDPASY 229
Cdd:PRK12564  155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  230 PSVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWA 309
Cdd:PRK12564  235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 807045910  310 PLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLE 355
Cdd:PRK12564  313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 2-359 2.23e-158

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 492.14  E-value: 2.23e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910     2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVqngTEPSSLPFL------DPNA 155
Cdd:TIGR01368   72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVIS---TEDSNDEELvekarvSPDI 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   156 RP--LVPEVSIKTPRVFN--TGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDS-QEYE--GLFLSNGPGDPAS 228
Cdd:TIGR01368  149 TGinLVAEVSTKEPYTWGqrGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEiKKYNpdGIFLSNGPGDPAA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   229 YPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-D 307
Cdd:TIGR01368  229 VEPAIETIRKLLEK---IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgD 305

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 807045910   308 WAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKE 359
Cdd:TIGR01368  306 LEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 2-358 1.38e-154

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 481.83  E-value: 1.38e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:COG0505     5 ALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---------DFESDRP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSL-------PFLDPn 154
Cdd:COG0505    76 WVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELlekaraaPGMEG- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  155 aRPLVPEVSIKTPRVF--NTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASY 229
Cdd:COG0505   155 -LDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEeilALNPDGVFLSNGPGDPAAL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  230 PSVVSTLSRVLSEpnPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-DW 308
Cdd:COG0505   234 DYAIETIRELLGK--GIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDL 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 807045910  309 APLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVK 358
Cdd:COG0505   312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1856-2161 2.69e-140

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 439.10  E-value: 2.69e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1856 HSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1935
Cdd:COG0540     1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1936 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2014
Cdd:COG0540    81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2015 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERFGSTQ- 2093
Cdd:COG0540   161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFTDGLf 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807045910 2094 -EYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2161
Cdd:COG0540   234 pSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
1857-2161 1.03e-127

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 403.68  E-value: 1.03e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1857 SLVGQHILSVQQFTKDQMSHLFNVAHTLR-MMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1935
Cdd:PRK00856    2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1936 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2014
Cdd:PRK00856   82 SSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2015 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFvasrgtkqEEFESIEEALPDTDVLYMTRIQKERFG---- 2090
Cdd:PRK00856  162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMDggll 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807045910 2091 -STQEYeacFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2161
Cdd:PRK00856  233 pSYEEY---KRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1862-2160 6.56e-111

aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273209 [Multi-domain]  Cd Length: 301  Bit Score: 355.51  E-value: 6.56e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1862 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA-TSSVQK 1940
Cdd:TIGR00670    2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVAK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1941 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2020
Cdd:TIGR00670   82 GETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  2021 GRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFG 2100
Cdd:TIGR00670  162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  2101 QFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2160
Cdd:TIGR00670  242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1374-1747 5.62e-105

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 344.00  E-value: 5.62e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1374 VEALGQIGPAPPLKVHVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPAL 1453
Cdd:COG0044    25 IAAIGPDLAAPEAAEVIDA--TGLLV-LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEAL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1454 ALAQKLAEAGARCDFALFLGASSENAGTL----GTVAGSAAGLKLYLNETFSELRLD----------------------- 1506
Cdd:COG0044   102 EFKLARAEEKALVDVGPHGALTKGLGENLaelgALAEAGAVAFKVFMGSDDGNPVLDdgllrraleyaaefgalvavhae 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1507 --SVVQWM---EHFETWPSHLPIV-AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHL 1580
Cdd:COG0044   182 dpDLIRGGvmnEGKTSPRLGLKGRpAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHL 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1581 FLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLT-AV 1655
Cdd:COG0044   262 TLTDEDLERYGT-NFKVNPPLRTEEDREALWEGLAdgTIDVIATDHAPHTLEEKELPFAeaPNGIPGLETALPLLLTeLV 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1656 SEGRLSLDDLLQRLHHNPRRIFHLPP----QEDTY---VEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRG 1727
Cdd:COG0044   341 HKGRLSLERLVELLSTNPARIFGLPRkgriAVGADadlVLFDPDAEWTVtAEDL-HSKSKNTPFEGRELTGRVVATIVRG 419

                         410       420
                  ....*....|....*....|
gi 807045910 1728 EVAYIDGQVLVPPgYGQDVR 1747
Cdd:COG0044   420 RVVYEDGEVVGEP-RGRFLR 438
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 178-354 1.43e-97

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 311.74  E-value: 1.43e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  178 ILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPnpRPVFGICLG 254
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK--IPIFGICLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  255 HQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQ 334
Cdd:cd01744    79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                         170       180
                  ....*....|....*....|
gi 807045910  335 FHPEHQAGPSDMELLFDIFL 354
Cdd:cd01744   159 FHPEASPGPHDTEYLFDEFL 178
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 1398-1733 5.24e-92

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 305.52  E-value: 5.24e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSE 1477
Cdd:TIGR00857   35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1478 NAGTLGT------VAGSAAGL----------KLYLNETfSELRLDSVVQWMEHFE---------------TWPSHLPIVA 1526
Cdd:TIGR00857  115 NQGKELTeayelkEAGAVGRMftddgsevqdILSMRRA-LEYAAIAGVPIALHAEdpdliyggvmhegpsAAQLGLPARP 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1527 -HAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQ 1605
Cdd:TIGR00857  194 pEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLD-GNGKVNPPLREKE 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1606 DVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP- 1680
Cdd:TIGR00857  273 DRLALIEGLKdgIIDIIATDHAPHTLEEKTKEFAaaPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPd 352

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 807045910  1681 --PQED----TYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1733
Cdd:TIGR00857  353 kgTLEEgnpaDITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
pyrC PRK09357
dihydroorotase; Validated
 1398-1733 9.12e-87

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 290.94  E-value: 9.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPA-----LALAQK-------------- 1458
Cdd:PRK09357   49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVI-DTPEvveyvLDRAKEaglvdvlpvgaitk 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1459 ------------LAEAGARC---DfalflGASSENAGTLGTVAGSAAGLKLYLNETFSELRL-------DSVVQWMEHFE 1516
Cdd:PRK09357  128 glageeltefgaLKEAGVVAfsdD-----GIPVQDARLMRRALEYAKALDLLIAQHCEDPSLteggvmnEGEVSARLGLP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1517 TWPshlpivAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGE 1596
Cdd:PRK09357  203 GIP------AVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDP-NYK 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1597 VRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG--SRPPPGFPGLETMLPLLLTA-VSEGRLSLDDLLQRLHH 1671
Cdd:PRK09357  276 VNPPLRTEEDREALIEGLKdgTIDAIATDHAPHAREEKECefEAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTI 355

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807045910 1672 NPRRIFHLPP------QEDTYVEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1733
Cdd:PRK09357  356 NPARILGLPAgplaegEPADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 4-138 1.78e-75

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. 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 pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.


Pssm-ID: 460017 [Multi-domain]  Cd Length: 126  Bit Score: 246.47  E-value: 1.78e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910     4 LVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMdefglckwfESSGIHV 83
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDF---------ESDKIHV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 807045910    84 AALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:pfam00988   72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 2-138 1.86e-71

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 234.96  E-value: 1.86e-71
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910      2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:smart01097    3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 807045910     82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:smart01097   74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 514-653 6.95e-58

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: 199.45  E-value: 6.95e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   514 DRRAFAARMAEIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHT------ 585
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   586 SQVLVDKSLKGWKEIEYEVVRDAYGNCVT--------------------------------------------------- 614
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITvcnrecsdqrrtqksievapsqtltdeerqmlreaavkiarhlgyvgagtv 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 807045910   615 ----------YYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 653
Cdd:pfam02786  161 efaldpfsgeYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 736-858 3.80e-56

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 190.74  E-value: 3.80e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    736 DMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIAL 815
Cdd:smart01096    2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 807045910    816 AVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTY 858
Cdd:smart01096   82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
1862-2002 3.92e-55

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 188.79  E-value: 3.92e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1862 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKG 1941
Cdd:pfam02729    1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807045910  1942 ESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGdGVGEHPTQALLDIFTIRE 2002
Cdd:pfam02729   81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1250-1375 6.05e-43

Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.


Pssm-ID: 238711 [Multi-domain]  Cd Length: 116  Bit Score: 152.84  E-value: 6.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1250 KNILLTIGSYkNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGEcppqRSILEQLAEKNFELV 1329
Cdd:cd01423     1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK----PSLRELLAEGKIDLV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 807045910 1330 INLSMRGAGGRRLSsfvtkGYRTRRLAADFSVPLIIDIKCTKLFVE 1375
Cdd:cd01423    76 INLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1401-1729 1.01e-07

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 56.36  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1401 LPGLIDVHVHLR--------EPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDApalalaqkLAEAGARCDFALFL 1472
Cdd:pfam01979    3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA--------LLEAAEELPLGLRF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1473 GASSENAGTLGTVAGSAA-GLKLYLNETFSELRLDSVVQ-WMEHFETWpshlpivaHAEQQTVAAVLMVAQLTQRSVHIc 1550
Cdd:pfam01979   75 LGPGCSLDTDGELEGRKAlREKLKAGAEFIKGMADGVVFvGLAPHGAP--------TFSDDELKAALEEAKKYGLPVAI- 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1551 HVAR-KEEILLIKAAKARG---------------LPVTCEVAPHHLFLSHDDLERLGPGKGEVR------PELGSRQDVE 1608
Cdd:pfam01979  146 HALEtKGEVEDAIAAFGGGiehgthlevaesgglLDIIKLILAHGVHLSPTEANLLAEHLKGAGvahcpfSNSKLRSGRI 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1609 ALWE--NMAVIDCFASDHAPHTleekcgsRPPPGFPGLETMlpLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTy 1686
Cdd:pfam01979  226 ALRKalEDGVKVGLGTDGAGSG-------NSLNMLEELRLA--LELQFDPEGGLSPLEALRMATINPAKALGLDDKVGS- 295

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 807045910  1687 VEV----DLehewtipshMPFSKAHWTPFEGQKVKGTVRRVVLRGEV 1729
Cdd:pfam01979  296 IEVgkdaDL---------VVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1750-1869 8.75e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.84  E-value: 8.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1750 PQGAVPQLPPSAPATSEMTTTPerPRRGIPGLPDGRFhlPPRIHRASDPGLPAEEPKEKSSRKVAEPELMGTPDG--TCY 1827
Cdd:pfam03154  177 QSGAASPPSPPPPGTTQAATAG--PTPSAPSVPPQGS--PATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPplQPM 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 807045910  1828 PPPPVPRQASPQNLGTPgLLHPQTSPLLHSLVG-----QHILSVQQF 1869
Cdd:pfam03154  253 TQPPPPSQVSPQPLPQP-SLHGQMPPMPHSLQTgpshmQHPVPPQPF 298
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 391-1377 0e+00

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: 1630.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPD 470
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   471 GVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369   84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   551 PVLVRAAFALGGLGSGFASNREELSALVAPAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYGNCVT-------------- 614
Cdd:TIGR01369  164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITvcnmenfdpmgvht 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   615 -------------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAK 645
Cdd:TIGR01369  244 gdsivvapsqtltdkeyqmlrdasikiirelgieggcnvqfalnpdsgrYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   646 LALGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 724
Cdd:TIGR01369  324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   725 VGFDHT---VKPVSD--MELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDL 799
Cdd:TIGR01369  404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   800 LQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRT-PHVLVLGSG 878
Cdd:TIGR01369  484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSG 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   879 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 958
Cdd:TIGR01369  564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   959 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVA 1038
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1039 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLER 1118
Cdd:TIGR01369  724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1119 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG--LMTGSGVV 1196
Cdd:TIGR01369  804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1197 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLG 1276
Cdd:TIGR01369  884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1277 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILEQLAEKNFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1356
Cdd:TIGR01369  964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029

                         1050      1060
                   ....*....|....*....|.
gi 807045910  1357 ADFSVPLIIDIKCTKLFVEAL 1377
Cdd:TIGR01369 1030 LDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
394-1377 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1281.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  554 VRAAFALGGLGSGFASNREELSALVAPAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYGNCVT----------------- 614
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIvcsienidpmgvhtgds 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  615 -----------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKLA 647
Cdd:PRK05294  248 itvapaqtltdkeyqmlrdasiaiireigvetggcnvqfalnpkdgrYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  648 LGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVG 726
Cdd:PRK05294  328 VGYTLDEIKNDITGKTpASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  727 FDHTVKPVSDME-----LETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrGQPLPPDLLQ 801
Cdd:PRK05294  408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEN-GLPLDAELLR 486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  802 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYR 881
Cdd:PRK05294  487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  882 IGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMA 961
Cdd:PRK05294  567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  962 MALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTD 1041
Cdd:PRK05294  647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1042 GDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGVVAAIA-ISEHVENAGVHSGDATLVTPPQDITAKTLERIK 1120
Cdd:PRK05294  727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1121 AIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTG--SGVVGV 1198
Cdd:PRK05294  806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGliPPYVAV 885

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1199 KVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKK-NILLTIgSYKNKSELLPTVRLLESLGY 1277
Cdd:PRK05294  886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1278 SLYASLGTADFYTEHGVKVTAVDWHFEEAVDgecppqrsILEQLAEKNFELVINlSMRGAGGRRlssfvtKGYRTRRLAA 1357
Cdd:PRK05294  965 KILATSGTAKFLREAGIPVELVNKVHEGRPH--------IVDLIKNGEIDLVIN-TPTGRQAIR------DGFSIRRAAL 1029

                        1050      1060
                  ....*....|....*....|
gi 807045910 1358 DFSVPLIIDIKCTKLFVEAL 1377
Cdd:PRK05294 1030 EYKVPYITTLAGARAAVKAI 1049
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 394-1385 0e+00

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 940.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PRK12815    8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK12815   88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  554 VRAAFALGGLGSGFASNREELSALVAPAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYGNCVT----------------- 614
Cdd:PRK12815  168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITvcnmenidpvgihtgds 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  615 ----------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 648
Cdd:PRK12815  248 ivvapsqtltddeyqmlrsaslkiisalgvvggcniqfaldpkskqYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  649 GIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALR--MVDENCV 725
Cdd:PRK12815  328 GYTLNELKNPVTGLTyASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRslEIKRNGL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  726 GFDHTVKPVSDMEL----ETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQpLPPDLLQ 801
Cdd:PRK12815  408 SLPIELSGKSDEELlqdlRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLD-LSADLLR 486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  802 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTH-DLTFRTPHVLVLGSGVY 880
Cdd:PRK12815  487 KVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEaEPSSEKKKVLILGSGPI 566

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  881 RIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNM 960
Cdd:PRK12815  567 RIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAINL 646

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  961 AMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYT 1040
Cdd:PRK12815  647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1041 DGDLERFLssAAAVSKEHPVVISKFIqEAKEIDVDAVaSDGVVAAIA-ISEHVENAGVHSGDATLVTPPQDITAKTLERI 1119
Cdd:PRK12815  727 EPALEAYL--AENASQLYPILIDQFI-DGKEYEVDAI-SDGEDVTIPgIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEKI 802

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1120 KAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMG----EEVEPVGLMTGSGV 1195
Cdd:PRK12815  803 RDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGkslaELGYPNGLWPGSPF 882

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1196 VGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESL 1275
Cdd:PRK12815  883 IHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQL 962

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1276 GYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAGGRrlssfvtKGYRTRRL 1355
Cdd:PRK12815  963 GFKLLATEGTANWLAEEGITTGVVEKVQEG--------SPSLLERIKQHRIVLVVNTSLSDSASE-------DAIKIRDE 1027

                        1050      1060      1070
                  ....*....|....*....|....*....|
gi 807045910 1356 AADFSVPLIIDIKCTKLFVEALGQIGPAPP 1385
Cdd:PRK12815 1028 ALSTHIPVFTELETAQAFLQVLESLALTTQ 1057
PLN02735 PLN02735
carbamoyl-phosphate synthase
 394-1377 0e+00

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 772.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PLN02735   24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLG-YPV 552
Cdd:PLN02735  104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  553 LVRAAFALGGLGSGFASNREELSALVAPAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYGNCVT---------------- 614
Cdd:PLN02735  184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRDLADNVVIicsienidpmgvhtgd 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  615 ------------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKL 646
Cdd:PLN02735  264 sitvapaqtltdkeyqrlrdysvaiireigvecggsnvqfavnpvdgeVMIIEMNPRVSRSSALASKATGFPIAKMAAKL 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  647 ALGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCV 725
Cdd:PLN02735  344 SVGYTLDQIPNDITLKTpASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETGFS 423

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  726 GFDhtVKPVSDME---------LETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLP 796
Cdd:PLN02735  424 GWG--CAKVKELDwdweqlkykLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSELS 501

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  797 PDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLG 876
Cdd:PLN02735  502 KDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLILG 581

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  877 SGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQL 956
Cdd:PLN02735  582 GGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGGQT 661

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  957 PNNMAMALHRQ-------------QCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCV 1023
Cdd:PLN02735  662 PLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVV 741

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1024 VRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVA-SDGVVAAIAISEHVENAGVHSGDA 1102
Cdd:PLN02735  742 VRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSGDS 821

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1103 TLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMG 1181
Cdd:PLN02735  822 ACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSG 901

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1182 ---------EEVEPVGlmtgsgvVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNI 1252
Cdd:PLN02735  902 kslkdlgftEEVIPAH-------VSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGT 974

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1253 LLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAV-DWHfeeavdgECPPQrsILEQLAEKNFELVIN 1331
Cdd:PLN02735  975 VFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVlKLH-------EGRPH--AGDMLANGQIQLMVI 1045

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*.
gi 807045910 1332 LSMRGAGGRRlssfvtKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1377
Cdd:PLN02735 1046 TSSGDALDQK------DGRQLRRMALAYKVPIITTVAGALATAQAV 1085
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1397-1743 0e+00

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 631.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1397 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1477 ENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKE 1556
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1557 EILLIKAAKARGLPVTCEVAPHHLFLSHDDLERlgpGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSR 1636
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1637 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1716
Cdd:cd01316   238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317

                         330       340
                  ....*....|....*....|....*..
gi 807045910 1717 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1743
Cdd:cd01316   318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 875-1377 1.65e-175

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: 546.78  E-value: 1.65e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  875 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 954
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  955 QLPNNMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVL 1030
Cdd:COG0458    81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1031 SGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGV--VAAIAISEHVENAGVHSGDATLVTPP 1108
Cdd:COG0458   161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVV-RDGEdnVIIVGIMEHIEPAGVHSGDSICVAPP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1109 QDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG 1188
Cdd:COG0458   240 QTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1189 LMTG----SGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKnILLTIGSYKNKSE 1264
Cdd:COG0458   320 NDTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDKEE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1265 LLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAGGRRLSS 1344
Cdd:COG0458   399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEG--------RPIIVDEIELEEIILVINTLLGAKSLGDSDG 470

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 807045910 1345 F------VTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1377
Cdd:COG0458   471 IirralaAKVPYVTTLAAAAAAALAIKAVETEAGEFEEA 509
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 399-877 5.66e-166

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: 520.59  E-value: 5.66e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  399 LGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGG 478
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  479 QTALNCGVELTKAGVLAryGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAF 558
Cdd:COG0458    81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  559 ALGGLGSGFASNREELSALVAPAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYGNCVT---------------------- 614
Cdd:COG0458   159 VLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLGAKEIEVDVVRDGEDNVIIvgimehiepagvhsgdsicvap 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  615 ---------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPEL 655
Cdd:COG0458   239 pqtlsdkeyqrlrdatlkiaralgvvglcniqfavddgrVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDEL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  656 RNSvTGgtaaFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDencVGFDHTV--KP 733
Cdd:COG0458   319 GND-TG----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLE---IGLPGTVllSL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  734 VSD-----MELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrgqPLPPDLLQQAKCLGF 808
Cdd:COG0458   391 VADddkeeALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEI---ILVINTLLGAKSLGD 467

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807045910  809 SDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGS 877
Cdd:COG0458   468 SDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-355 5.26e-160

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 496.52  E-value: 5.26e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    1 MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSG 80
Cdd:PRK12564    4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   81 IHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLP-----FLDPNA 155
Cdd:PRK12564   75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  156 RPLVPEVSIKTPRVFNTGGA---PRILALDCGLKYNQIRCLCQRGAEVTVVPWD---HALDSQEYEGLFLSNGPGDPASY 229
Cdd:PRK12564  155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  230 PSVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWA 309
Cdd:PRK12564  235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 807045910  310 PLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLE 355
Cdd:PRK12564  313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 2-359 2.23e-158

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 492.14  E-value: 2.23e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910     2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVqngTEPSSLPFL------DPNA 155
Cdd:TIGR01368   72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVIS---TEDSNDEELvekarvSPDI 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   156 RP--LVPEVSIKTPRVFN--TGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDS-QEYE--GLFLSNGPGDPAS 228
Cdd:TIGR01368  149 TGinLVAEVSTKEPYTWGqrGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEiKKYNpdGIFLSNGPGDPAA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   229 YPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-D 307
Cdd:TIGR01368  229 VEPAIETIRKLLEK---IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgD 305

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 807045910   308 WAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKE 359
Cdd:TIGR01368  306 LEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 2-358 1.38e-154

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 481.83  E-value: 1.38e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:COG0505     5 ALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---------DFESDRP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSL-------PFLDPn 154
Cdd:COG0505    76 WVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELlekaraaPGMEG- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  155 aRPLVPEVSIKTPRVF--NTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASY 229
Cdd:COG0505   155 -LDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEeilALNPDGVFLSNGPGDPAAL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  230 PSVVSTLSRVLSEpnPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-DW 308
Cdd:COG0505   234 DYAIETIRELLGK--GIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDL 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 807045910  309 APLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVK 358
Cdd:COG0505   312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1856-2161 2.69e-140

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 439.10  E-value: 2.69e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1856 HSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1935
Cdd:COG0540     1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1936 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2014
Cdd:COG0540    81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2015 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERFGSTQ- 2093
Cdd:COG0540   161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFTDGLf 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807045910 2094 -EYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2161
Cdd:COG0540   234 pSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 1398-1723 1.36e-128

Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.


Pssm-ID: 238627 [Multi-domain]  Cd Length: 337  Bit Score: 407.55  E-value: 1.36e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1398 LVRLPGLIDVHVHLREPGGT-HKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:cd01302     1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1477 EnaGTLGTVAGS----AAGLKLYLNETFSELRLDSVVQWMEHFETWPS-HLPIVAHAEqqtvaavlMVAQLTQ---RSVH 1548
Cdd:cd01302    81 G--DVTDELKKLfdagINSLKVFMNYYFGELFDVDDGTLMRTFLEIASrGGPVMVHAE--------RAAQLAEeagANVH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1549 ICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAP 1626
Cdd:cd01302   151 IAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGA-WGKVNPPLRSKEDREALWEGVKngKIDTIASDHAP 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1627 HTLEEKC----GSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQED---------TYVEVDLEH 1693
Cdd:cd01302   230 HSKEEKEsgkdIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKGTiavgydadlVIVDPKKEW 309

                         330       340       350
                  ....*....|....*....|....*....|
gi 807045910 1694 EWTIPSHMpfSKAHWTPFEGQKVKGTVRRV 1723
Cdd:cd01302   310 KVTAEEIE--SKADWTPFEGMEVTGKPVST 337
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
1857-2161 1.03e-127

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 403.68  E-value: 1.03e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1857 SLVGQHILSVQQFTKDQMSHLFNVAHTLR-MMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1935
Cdd:PRK00856    2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1936 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2014
Cdd:PRK00856   82 SSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2015 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFvasrgtkqEEFESIEEALPDTDVLYMTRIQKERFG---- 2090
Cdd:PRK00856  162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMDggll 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807045910 2091 -STQEYeacFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2161
Cdd:PRK00856  233 pSYEEY---KRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
PLN02527 PLN02527
aspartate carbamoyltransferase
 1861-2160 7.20e-127

aspartate carbamoyltransferase


Pssm-ID: 178142 [Multi-domain]  Cd Length: 306  Bit Score: 401.43  E-value: 7.20e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1861 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA--TSSV 1938
Cdd:PLN02527    1 SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAgeFSSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1939 QKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2018
Cdd:PLN02527   81 AKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2019 KHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFG-STQEYE 2096
Cdd:PLN02527  161 ANGRTVRSLAYLLAKYEdVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDLMEVASKCDVLYQTRIQRERFGeRIDLYE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807045910 2097 ACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2160
Cdd:PLN02527  241 AARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLG 304
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 4-360 1.89e-126

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 401.96  E-value: 1.89e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    4 LVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEmdefglckwFESSGIHV 83
Cdd:PRK12838    5 LILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADD---------YESKQPQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   84 AALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLPF----LDPNarpLV 159
Cdd:PRK12838   76 KGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFDQIkalvLPKN---VV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  160 PEVSIKTPRVFNTGGaPRILALDCGLKYNQIRCLCQRGAEVTVVPWD---HALDSQEYEGLFLSNGPGDPASYPSVVSTL 236
Cdd:PRK12838  153 AQVSTKEPYTYGNGG-KHVALIDFGYKKSILRSLSKRGCKVTVLPYDtslEEIKNLNPDGIVLSNGPGDPKELQPYLPEI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  237 SRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSL-PADWAPLFTNA 315
Cdd:PRK12838  232 KKLISS---YPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNV 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 807045910  316 NDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEA 360
Cdd:PRK12838  309 NDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKA 353
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1862-2160 6.56e-111

aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273209 [Multi-domain]  Cd Length: 301  Bit Score: 355.51  E-value: 6.56e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1862 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA-TSSVQK 1940
Cdd:TIGR00670    2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVAK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1941 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2020
Cdd:TIGR00670   82 GETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  2021 GRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFG 2100
Cdd:TIGR00670  162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  2101 QFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2160
Cdd:TIGR00670  242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1374-1747 5.62e-105

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 344.00  E-value: 5.62e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1374 VEALGQIGPAPPLKVHVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPAL 1453
Cdd:COG0044    25 IAAIGPDLAAPEAAEVIDA--TGLLV-LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEAL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1454 ALAQKLAEAGARCDFALFLGASSENAGTL----GTVAGSAAGLKLYLNETFSELRLD----------------------- 1506
Cdd:COG0044   102 EFKLARAEEKALVDVGPHGALTKGLGENLaelgALAEAGAVAFKVFMGSDDGNPVLDdgllrraleyaaefgalvavhae 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1507 --SVVQWM---EHFETWPSHLPIV-AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHL 1580
Cdd:COG0044   182 dpDLIRGGvmnEGKTSPRLGLKGRpAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHL 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1581 FLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLT-AV 1655
Cdd:COG0044   262 TLTDEDLERYGT-NFKVNPPLRTEEDREALWEGLAdgTIDVIATDHAPHTLEEKELPFAeaPNGIPGLETALPLLLTeLV 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1656 SEGRLSLDDLLQRLHHNPRRIFHLPP----QEDTY---VEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRG 1727
Cdd:COG0044   341 HKGRLSLERLVELLSTNPARIFGLPRkgriAVGADadlVLFDPDAEWTVtAEDL-HSKSKNTPFEGRELTGRVVATIVRG 419

                         410       420
                  ....*....|....*....|
gi 807045910 1728 EVAYIDGQVLVPPgYGQDVR 1747
Cdd:COG0044   420 RVVYEDGEVVGEP-RGRFLR 438
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 178-354 1.43e-97

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 311.74  E-value: 1.43e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  178 ILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPnpRPVFGICLG 254
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK--IPIFGICLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  255 HQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQ 334
Cdd:cd01744    79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                         170       180
                  ....*....|....*....|
gi 807045910  335 FHPEHQAGPSDMELLFDIFL 354
Cdd:cd01744   159 FHPEASPGPHDTEYLFDEFL 178
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 1401-1727 6.87e-93

Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.


Pssm-ID: 238643 [Multi-domain]  Cd Length: 361  Bit Score: 306.18  E-value: 6.87e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGAS-SENA 1479
Cdd:cd01318     5 LPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTgSEDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1480 GTLgtVAGSAAGLKLYLNETFSELRLDsvvqwMEHFETWPSH--LPIVAHAEQQT------------------------- 1532
Cdd:cd01318    85 EEL--DKAPPAGYKIFMGDSTGDLLDD-----EETLERIFAEgsVLVTFHAEDEDrlrenrkelkgesahprirdaeaaa 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1533 --VAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARglpVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQDVEAL 1610
Cdd:cd01318   158 vaTARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLG-TLGKVNPPLRSREDRKAL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1611 WENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP---PQE 1683
Cdd:cd01318   234 LQALAdgRIDVIASDHAPHTLEEKRKGYPaaPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIKnkgRIA 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 807045910 1684 DTY----VEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRG 1727
Cdd:cd01318   314 EGYdadlTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
PRK08192 PRK08192
aspartate carbamoyltransferase; Provisional
 1860-2160 3.65e-92

aspartate carbamoyltransferase; Provisional


Pssm-ID: 169269 [Multi-domain]  Cd Length: 338  Bit Score: 303.19  E-value: 3.65e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1860 GQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVL-SFSEATSSV 1938
Cdd:PRK08192    5 GSHILSVNQLDRDAIQRIFNVADRMEPYALREKRTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVReTTGMASSSL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1939 QKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREEL----GTVNGMTITM 2014
Cdd:PRK08192   85 SKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGIDGMHIAM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2015 VGDLKHGRTVHSLACLLTQY-RVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQ 2093
Cdd:PRK08192  165 VGDLKFGRTVHSLSRLLCMYkNVSFTLVSPKELAMPDYVISDIENAGHKITITDQLEGNLDKADILYLTRIQEERFPSQE 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807045910 2094 EYEACFGQFILTPHIMTR-AKKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2160
Cdd:PRK08192  245 EANKYRGKFRLNQSIYTQhCKSNTVIMHPLPRdsraqANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLG 317
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 1398-1733 5.24e-92

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 305.52  E-value: 5.24e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSE 1477
Cdd:TIGR00857   35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1478 NAGTLGT------VAGSAAGL----------KLYLNETfSELRLDSVVQWMEHFE---------------TWPSHLPIVA 1526
Cdd:TIGR00857  115 NQGKELTeayelkEAGAVGRMftddgsevqdILSMRRA-LEYAAIAGVPIALHAEdpdliyggvmhegpsAAQLGLPARP 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1527 -HAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQ 1605
Cdd:TIGR00857  194 pEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLD-GNGKVNPPLREKE 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1606 DVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP- 1680
Cdd:TIGR00857  273 DRLALIEGLKdgIIDIIATDHAPHTLEEKTKEFAaaPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPd 352

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 807045910  1681 --PQED----TYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1733
Cdd:TIGR00857  353 kgTLEEgnpaDITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
PRK11891 PRK11891
aspartate carbamoyltransferase; Provisional
 1861-2160 7.47e-87

aspartate carbamoyltransferase; Provisional


Pssm-ID: 183362 [Multi-domain]  Cd Length: 429  Bit Score: 291.38  E-value: 7.47e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1861 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT-SSVQ 1939
Cdd:PRK11891   88 PQLLSVDQFSRDSVEALFRVADVMQPIARRQKISRVLEGAVLGNLFFEASTRTRVSFGAAFCRLGGSVCDTTGFTfSSMA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1940 KGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREE---LG-TVNGMTITMV 2015
Cdd:PRK11891  168 KGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVINGGDGPGEHPSQALLDLYTIQREfsrLGkIVDGAHIALV 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2016 GDLKHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGStQE 2094
Cdd:PRK11891  248 GDLKYGRTVHSLVKLLALYRgLKFTLVSPPTLEMPAYIVEQISRNGHVIEQTDDLAAGLRGADVVYATRIQKERFAD-ES 326

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807045910 2095 YEACFGQFILTPHIMTRA-KKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2160
Cdd:PRK11891  327 FEGYTPDFQINQALVDAVcKPDTLIMHPLPRdsrpgANDLSTDLNRDPRLAIFRQTDNGIPVRMAIFAVLLG 398
pyrC PRK09357
dihydroorotase; Validated
 1398-1733 9.12e-87

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 290.94  E-value: 9.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPA-----LALAQK-------------- 1458
Cdd:PRK09357   49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVI-DTPEvveyvLDRAKEaglvdvlpvgaitk 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1459 ------------LAEAGARC---DfalflGASSENAGTLGTVAGSAAGLKLYLNETFSELRL-------DSVVQWMEHFE 1516
Cdd:PRK09357  128 glageeltefgaLKEAGVVAfsdD-----GIPVQDARLMRRALEYAKALDLLIAQHCEDPSLteggvmnEGEVSARLGLP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1517 TWPshlpivAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGE 1596
Cdd:PRK09357  203 GIP------AVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDP-NYK 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1597 VRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG--SRPPPGFPGLETMLPLLLTA-VSEGRLSLDDLLQRLHH 1671
Cdd:PRK09357  276 VNPPLRTEEDREALIEGLKdgTIDAIATDHAPHAREEKECefEAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTI 355

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807045910 1672 NPRRIFHLPP------QEDTYVEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1733
Cdd:PRK09357  356 NPARILGLPAgplaegEPADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-358 2.85e-85

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 285.15  E-value: 2.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEmdefglckwFESSGI 81
Cdd:CHL00197    7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLED---------IESVKI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLG-------------KLVQNGTEPSSL 148
Cdd:CHL00197   78 QVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGcisnqnlnlsylrAKIKESPHMPSS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  149 PFLDPNARPLVPEVSIKTPRVFN--------TGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGL 217
Cdd:CHL00197  158 DLIPRVTTSSYYEWDEKSHPSFYladnkrphSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQdilSYQPDGI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  218 FLSNGPGDPASYPSVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLvgSGRCFLTSQNHGF 297
Cdd:CHL00197  238 LLSNGPGDPSAIHYGIKTVKKLLKYN--IPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSGL--NQQVEITSQNHGF 313

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807045910  298 AVETDSLPADWAPL-FTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVK 358
Cdd:CHL00197  314 AVNLESLAKNKFYItHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIK 375
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 2-350 4.01e-76

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 259.91  E-value: 4.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemDEfglckwfESSGI 81
Cdd:PLN02771   57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFD--DE-------ESRQC 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLV--QNGTEPSSLPF---LDPNAR 156
Cdd:PLN02771  128 FLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSteDSKTDEELLKMsrsWDIVGI 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  157 PLVPEVSIKTPRV----------FNTGGAP----RILALDCGLKYNQIRCLCQRGAEVTVVP--WDhALDSQEY--EGLF 218
Cdd:PLN02771  208 DLISGVSCKSPYEwvdktnpewdFNTNSRDgesyHVIAYDFGIKHNILRRLASYGCKITVVPstWP-ASEALKMkpDGVL 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  219 LSNGPGDPASYPSVVSTLSRVLSEPnprPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFA 298
Cdd:PLN02771  287 FSNGPGDPSAVPYAVETVKELLGKV---PVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYA 363

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 807045910  299 VETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLF 350
Cdd:PLN02771  364 VDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
PRK04250 PRK04250
dihydroorotase; Provisional
 1401-1740 6.24e-76

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 258.54  E-value: 6.24e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFAL-FLGASseNA 1479
Cdd:PRK04250   46 LPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALnFLIAG--NC 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1480 GTLGTVagSAAGLKLYLNETFSELRLDSvvqWMEHFETWPSHLPIVAH--------------AEQQTVAAVLMVAQLTQR 1545
Cdd:PRK04250  124 EKAEEI--KADFYKIFMGASTGGIFSEN---FEVDYACAPGIVSVHAEdpelirefperppeAEVVAIERALEAGKKLKK 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1546 SVHICHVARKEEILLIKaaKARGLPVTCEVAPHHLFLSHDDLERlGPgKGEVRPELGSRQDVEALWENMAVIDCFASDHA 1625
Cdd:PRK04250  199 PLHICHISTKDGLKLIL--KSNLPWVSFEVTPHHLFLTRKDYER-NP-LLKVYPPLRSEEDRKALWENFSKIPIIASDHA 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1626 PHTLEEKcgSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPP------QEDTYVEVDLEHEWTIPS 1699
Cdd:PRK04250  275 PHTLEDK--EAGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNygieegNYANFAVFDMKKEWTIKA 352

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 807045910 1700 HMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1740
Cdd:PRK04250  353 EELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 4-138 1.78e-75

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. 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 pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.


Pssm-ID: 460017 [Multi-domain]  Cd Length: 126  Bit Score: 246.47  E-value: 1.78e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910     4 LVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMdefglckwfESSGIHV 83
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDF---------ESDKIHV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 807045910    84 AALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:pfam00988   72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
PRK02382 PRK02382
dihydroorotase; Provisional
 1401-1747 1.35e-72

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 250.72  E-value: 1.35e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGAS----- 1475
Cdd:PRK02382   53 LPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgnwdp 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1476 -----SENAGTLGTV--AGSAAGLKLYLnETFSEL-----RLDSVV--------------QWMEHFETWPSHLPI-VAHA 1528
Cdd:PRK02382  133 leslwERGVFALGEIfmADSTGGMGIDE-ELFEEAlaeaaRLGVLAtvhaededlfdelaKLLKGDADADAWSAYrPAAA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1529 EQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKarglpVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSRQDVE 1608
Cdd:PRK02382  212 EAAAVERALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGT-FGKMNPPLRSEKRRE 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1609 ALWE--NMAVIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQ-- 1682
Cdd:PRK02382  286 ALWErlNDGTIDVVASDHAPHTREEKDADiwDAPSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLDGKgr 365

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807045910 1683 -EDTY----VEVDLEHEWTIPSHMPFSKAHWTPFEGqkVKGTVRRVVL-RGEVAYIDGQVLVPPGYGQDVR 1747
Cdd:PRK02382  366 iAEGYdadlVLVDPDAAREIRGDDLHSKAGWTPFEG--MEGVFPELTMvRGTVVWDGDDINAKRGRGEFLR 434
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 2-138 1.86e-71

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 234.96  E-value: 1.86e-71
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910      2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:smart01097    3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 807045910     82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:smart01097   74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
PRK07575 PRK07575
dihydroorotase; Provisional
 1379-1736 4.55e-71

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 246.12  E-value: 4.55e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1379 QIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPalALAQK 1458
Cdd:PRK07575   33 AIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQA--ALDDK 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1459 LAEAGARC--DFALFLGASSENAGTLGTVAGsAAGLKLYLNETFSELRLDSVVQWMEHF-ETwpsHLPIVAHAEQQTV-- 1533
Cdd:PRK07575  111 LARAAEKCvvNYGFFIGATPDNLPELLTANP-TCGIKIFMGSSHGPLLVDEEAALERIFaEG---TRLIAVHAEDQARir 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1534 ---------------------AAVLMVAQLT-------QRSVHICHVARKEEILLIKAAKarGLPVTCEVAPHHLFLSHD 1585
Cdd:PRK07575  187 arraefagisdpadhsqiqdeEAALLATRLAlklskkyQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTD 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1586 DLERLGPgKGEVRPELGSRQDVEALWENM--AVIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLS 1661
Cdd:PRK07575  265 AYERIGT-LAQMNPPLRSPEDNEALWQALrdGVIDFIATDHAPHTLEEKAQPYPnsPSGMPGVETSLPLMLTAAMRGKCT 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1662 LDDLLQRLHHNPRRIFHLP------PQEDT-YVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDG 1734
Cdd:PRK07575  344 VAQVVRWMSTAVARAYGIPnkgriaPGYDAdLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423


                  ..
gi 807045910 1735 QV 1736
Cdd:PRK07575  424 QV 425
PRK09060 PRK09060
dihydroorotase; Validated
 1366-1747 4.62e-70

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 243.29  E-value: 4.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1366 DIKCTKLFVEALGQIGPAPPLKVhVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRP 1445
Cdd:PRK09060   24 DIGIRDGRIAAIGDLSGASAGEV-IDC---RGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1446 PIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTV--AGSAAGLKLYLNETFSELRLD---SVVQWME------- 1513
Cdd:PRK09060  100 LTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELerLPGCAGIKVFMGSSTGDLLVEddeGLRRILRngrrraa 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1514 -HFE---------------TWPSHlPIVAHAEqqtvAAVLM------VAQLTQRSVHICHVARKEEILLIKAAKARglpV 1571
Cdd:PRK09060  180 fHSEdeyrlrerkglrvegDPSSH-PVWRDEE----AALLAtrrlvrLARETGRRIHVLHVSTAEEIDFLADHKDV---A 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1572 TCEVAPHHLFLSHDDL-ERLGpGKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKcgSRP----PPGFPGL 1644
Cdd:PRK09060  252 TVEVTPHHLTLAAPECyERLG-TLAQMNPPIRDARHRDGLWRGVRqgVVDVLGSDHAPHTLEEK--AKPypasPSGMTGV 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1645 ETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQ--------EDTYVeVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1716
Cdd:PRK09060  329 QTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAGKgriavgydADFTI-VDLKRRETITNEWIASRCGWTPYDGKEV 407

                         410       420       430
                  ....*....|....*....|....*....|.
gi 807045910 1717 KGTVRRVVLRGEVAYIDGQVLVPPGyGQDVR 1747
Cdd:PRK09060  408 TGWPVGTIVRGQRVMWDGELVGPPT-GEPVR 437
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 1390-1723 7.90e-70

Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.


Pssm-ID: 238642 [Multi-domain]  Cd Length: 374  Bit Score: 240.22  E-value: 7.90e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1390 VDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPAL--ALAQKLAEAGARCD 1467
Cdd:cd01317     5 IDA---EGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVI-DNPAVveLLKNRAKDVGIVRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1468 FAL------FLGASSENAGTL---GTVAGSAAGLKLYLNETfselrLDSVVQWMEHFEtwpshLPIVAH----------- 1527
Cdd:cd01317    81 LPIgaltkgLKGEELTEIGELleaGAVGFSDDGKPIQDAEL-----LRRALEYAAMLD-----LPIIVHpedpslagggv 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1528 ------------------AEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLER 1589
Cdd:cd01317   151 mnegkvasrlglpgippeAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALES 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1590 LGPGkGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCgsRP----PPGFPGLETMLPLLLT-AVSEGRLSL 1662
Cdd:cd01317   231 YDTN-AKVNPPLRSEEDREALIEALKdgTIDAIASDHAPHTDEEKD--LPfaeaPPGIIGLETALPLLWTlLVKGGLLTL 307

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807045910 1663 DDLLQRLHHNPRRIFHLPPQEDTYVE------VDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRV 1723
Cdd:cd01317   308 PDLIRALSTNPAKILGLPPGRLEVGApadlvlFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 1398-1740 6.42e-64

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 225.63  E-value: 6.42e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:cd01315    48 LVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVP 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1477 EN---------AGTLG---TVAGSAAGL-----KLYLNETFSEL-RLDSVVqwMEHFE------------------TWPS 1520
Cdd:cd01315   128 GNldqlrpldeAGVVGfkcFLCPSGVDEfpavdDEQLEEAMKELaKTGSVL--AVHAEnpeitealqeqakakgkrDYRD 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1521 HL---PIVAhaEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEV 1597
Cdd:cd01315   206 YLasrPVFT--EVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGT-EFKC 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1598 RPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRPP-----PGFPGLETMLPLLLT-AVSEGRLSLDDLLQRL 1669
Cdd:cd01315   283 APPIRDAANQEQLWEALEngDIDMVVSDHSPCTPELKLLGKGDffkawGGISGLQLGLPVMLTeAVNKRGLSLEDIARLM 362

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807045910 1670 HHNPRRIFHLPPQEDT--------YVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1740
Cdd:cd01315   363 CENPAKLFGLSHQKGRiavgydadFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP 441
GATase pfam00117
Glutamine amidotransferase class-I;
179-355 7.08e-61

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 207.09  E-value: 7.08e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   179 LALDCGL--KYNQIRCLCQRGAEVTVVPWDH---ALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVLsePNPRPVFGICL 253
Cdd:pfam00117    1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREAR--ELKIPILGICL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   254 GHQLLALAIGAKTYKM-RYGNRGHNQPC------LLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHN 326
Cdd:pfam00117   79 GHQLLALAFGGKVVKAkKFGHHGKNSPVgddgcgLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHK 158

                          170       180
                   ....*....|....*....|....*....
gi 807045910   327 SLPFFSVQFHPEHQAGPSDMELLFDIFLE 355
Cdd:pfam00117  159 KLPIFGVQFHPESILTPHGPEILFNFFIK 187
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 514-653 6.95e-58

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: 199.45  E-value: 6.95e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   514 DRRAFAARMAEIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHT------ 585
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   586 SQVLVDKSLKGWKEIEYEVVRDAYGNCVT--------------------------------------------------- 614
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITvcnrecsdqrrtqksievapsqtltdeerqmlreaavkiarhlgyvgagtv 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 807045910   615 ----------YYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 653
Cdd:pfam02786  161 efaldpfsgeYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
ArgF COG0078
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ...
 1857-2161 1.46e-56

Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine carbamoyltransferase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439848 [Multi-domain]  Cd Length: 310  Bit Score: 199.51  E-value: 1.46e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1857 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1936
Cdd:COG0078     2 NLKGRHFLSLLDLTPEELRALLDLAAELKAKRKAGIPHRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYLDPGDS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1937 SVQKGESLADSVQTMSCYADVVVLR-HPQPGAVELaAKHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMTITM 2014
Cdd:COG0078    82 QLGRGESIKDTARVLSRYVDGIMIRtFGHETLEEL-AKYAGVPVINGlTD--LFHPCQALADLLTIREHFGKLKGLKVAY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2015 VGDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLY------MTR 2083
Cdd:COG0078   159 VGD---GNNVaNSLLLAAAKLGMDVRIATPEGYEPDPEIvakaKEIAAESGGSITITHDPAEAVKGADVVYtdvwvsMGQ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2084 iQKERfgstQEYEACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEV-DSdPRAAYFRQAENGMYIRMALLATVLG 2160
Cdd:COG0078   236 -EEEA----EERIKAFKPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEViDG-PQSVVFDEAENRLHAQKALLAWLLG 309


                  .
gi 807045910 2161 R 2161
Cdd:COG0078   310 G 310
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 736-858 3.80e-56

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 190.74  E-value: 3.80e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910    736 DMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIAL 815
Cdd:smart01096    2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 807045910    816 AVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTY 858
Cdd:smart01096   82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
1862-2002 3.92e-55

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 188.79  E-value: 3.92e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1862 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKG 1941
Cdd:pfam02729    1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807045910  1942 ESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGdGVGEHPTQALLDIFTIRE 2002
Cdd:pfam02729   81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
PRK09236 PRK09236
dihydroorotase; Reviewed
 1401-1736 1.56e-54

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 198.17  E-value: 1.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAG 1480
Cdd:PRK09236   53 LPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLD 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1481 TLGTV-AGSAAGLKLY---------------LNETFSELRL---------DSVVQWMEHF-ETWPSHLPIVAHAEQQTVA 1534
Cdd:PRK09236  133 EIKRLdPKRVCGVKVFmgastgnmlvdnpetLERIFRDAPTliathcedtPTIKANLAKYkEKYGDDIPAEMHPLIRSAE 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1535 AVL----MVAQLTQRS---VHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQDV 1607
Cdd:PRK09236  213 ACYksssLAVSLAKKHgtrLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLG-NLIKCNPAIKTASDR 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1608 EALWENMA--VIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLppQE 1683
Cdd:PRK09236  292 EALRQALAddRIDVIATDHAPHTWEEKQGPyfQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDI--KE 369

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807045910 1684 DTY---------VEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQV 1736
Cdd:PRK09236  370 RGFiregywadlVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQL 431
PRK06189 PRK06189
allantoinase; Provisional
 1401-1748 9.72e-53

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 192.99  E-value: 9.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENA 1479
Cdd:PRK06189   53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1480 GTLGTVA-GSAAGLKLYLNETFSE-----------------LRLDSVVQWMEHFETWPSHLPIVAHAEQQT--------- 1532
Cdd:PRK06189  133 EHLRELAeAGVIGFKAFMSNSGTDefrssddltlyegmkeiAALGKILALHAESDALTRHLTTQARQQGKTdvrdylesr 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1533 -----VAAV---LMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSR 1604
Cdd:PRK06189  213 pvvaeLEAVqraLLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGA-VAKCAPPLRSR 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1605 QDVEALWENMAV--IDCFASDHAPHTLEEKCGS---RPPPGFPGLETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFH 1678
Cdd:PRK06189  292 SQKEELWRGLLAgeIDMISSDHSPCPPELKEGDdffLVWGGISGGQSTLLVMLTeGYIERGIPLETIARLLATNPAKRFG 371

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807045910 1679 LPP-------QEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVlVPPGYGQDVRK 1748
Cdd:PRK06189  372 LPQkgrlevgADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV-FPPPRGQLLRP 447
allantoinase TIGR03178
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ...
 1398-1740 5.77e-48

allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.


Pssm-ID: 163175 [Multi-domain]  Cd Length: 443  Bit Score: 179.12  E-value: 5.77e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:TIGR03178   47 LVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVP 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1477 ENAGTLGTVAGSAA-GLKLYLN----ETFSELRLDSVVQWME-----------HFETwPSHL-----------PIVAH-- 1527
Cdd:TIGR03178  127 YNLDDLRELDEAGVvGFKAFLSpsgdDEFPHVDDWQLYKGMRelarlgqlllvHAEN-PAITsalgeeappqgGVGADay 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1528 -------AEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPE 1600
Cdd:TIGR03178  206 lasrpvfAEVEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGT-LAKCAPP 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1601 LGSRQDVEALWENMA--VIDCFASDHAPHTLEEKC--------GsrpppGFPGLETMLPLLLTAVSEGR-LSLDDLLQRL 1669
Cdd:TIGR03178  285 IRDLANQEGLWEALLngLIDCVVSDHSPCTPDLKRagdffkawG-----GIAGLQSTLDVMFDEAVQKRgLPLEDIARLM 359

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807045910  1670 HHNPRRIFHLP------PQEDT-YVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1740
Cdd:TIGR03178  360 ATNPAKRFGLAqkgriaPGKDAdFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP 437
pyrC PRK00369
dihydroorotase; Provisional
 1401-1741 2.49e-47

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 175.72  E-value: 2.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPAlALAQKLAE--AGARCDFALFLGA--SS 1476
Cdd:PRK00369   46 LPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPL-NTPE-AITEKLAEleYYSRVDYFVYSGVtkDP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1477 ENAGTLGTvagsaAGLKLYLNETfseLRLDSVVQWMEhfetwpSHLPIVAHAEQQTV--------------AAVLMVAQL 1542
Cdd:PRK00369  124 EKVDKLPI-----AGYKIFPEDL---EREETFRVLLK------SRKLKILHPEVPLAlksnrklrrncwyeIAALYYVKD 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1543 TQRsVHICHVARKEEILLikaAKARGLpvTCEVAPHHLFLshddlERLGPGKGEVRPELGSRQDVEALWENMAVIDCFAS 1622
Cdd:PRK00369  190 YQN-VHITHASNPRTVRL---AKELGF--TVDITPHHLLV-----NGEKDCLTKVNPPIRDINERLWLLQALSEVDAIAS 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1623 DHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPpqeDTYVEVDLEHEWTIPS- 1699
Cdd:PRK00369  259 DHAPHSSFEKLQPYEvcPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIP---YGEIKEGYRANFTVIQf 335

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 807045910 1700 -----HMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPG 1741
Cdd:PRK00369  336 edwrySTKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKG 382
pyrB PRK13814
aspartate carbamoyltransferase;
1862-2161 3.49e-46

aspartate carbamoyltransferase;


Pssm-ID: 139876 [Multi-domain]  Cd Length: 310  Bit Score: 169.51  E-value: 3.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1862 HILSVQQFTKDQMSHLFNVA-HTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 1940
Cdd:PRK13814    7 HLLNMRSLTRDHIEKLIQRAnYFLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1941 GESLADSVQTMSCYA-DVVVLRHPQPGAVELAAKHCRRPV-INAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2018
Cdd:PRK13814   87 GETLFDTIKTLEAMGvYFFIVRHSENETPEQIAKQLSSGVvINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2019 KHGRTVHSLA-CLLTQYRVSLRYVAPPSLrMPPTVrafvasRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEA 2097
Cdd:PRK13814  167 RHSRVANSLMdGLVTMGVPEIRLVGPSSL-LPDKV------GNDSIKKFTELKPSLLNSDVIVTLRLQKERHDNSVDIDA 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807045910 2098 CFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2161
Cdd:PRK13814  240 FRGSFRLTPEKLYSAKPDAIVMHPGPvnREVEINSDVADNQQSVILQQVRNGVAMRMAVLELFLLR 305
PRK01211 PRK01211
dihydroorotase; Provisional
 1401-1748 5.60e-46

dihydroorotase; Provisional


Pssm-ID: 179247 [Multi-domain]  Cd Length: 409  Bit Score: 171.96  E-value: 5.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAG 1480
Cdd:PRK01211   45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1481 TLGTVagsAAGLKLYLNETFSELRLDSVVQWMEHFETwpSHLPIVAHAEQQ------------------------TVAAV 1536
Cdd:PRK01211  125 ILDER---SIGLKVYMGGTTNTNGTDIEGGEIKKINE--ANIPVFFHAELSeclrkhqfesknlrdhdlarpiecEIKAV 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1537 LMVAQLTQRSVHICHVARKEEIllikaakargLPVTCEVAPHHLFLsHDDLErLGpGKGEVRPELGSRQDVEALWENM-- 1614
Cdd:PRK01211  200 KYVKNLDLKTKIIAHVSSIDVI----------GRFLREVTPHHLLL-NDDMP-LG-SYGKVNPPLRDRWTQERLLEEYis 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1615 AVIDCFASDHAPHTLEEKCG-SRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQ--EDTY----V 1687
Cdd:PRK01211  267 GRFDILSSDHAPHTEEDKQEfEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKGkiEEGYdadfM 346

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807045910 1688 EVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTvRRVVLRGEVAyIDGQVLVPPGYGQDVRK 1748
Cdd:PRK01211  347 AFDFTNIKKINDKRLHSKCPVSPFNGFDAIFP-SHVIMRGEVV-IDNYELISERTGKFVPK 405
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 1376-1743 1.52e-44

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 168.94  E-value: 1.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1376 ALGQ-IGPAPPLKVhVDCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPA 1452
Cdd:cd01314    28 AIGPnLEAPGGVEV-IDA--TGKYV-LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1453 LALAQKLAEAGARCDFALFLGASSENAGT---LGTVAgsAAGL---KLYLneTFSELRLDSVVQWMEHFETWPSH--LPI 1524
Cdd:cd01314   104 VEKWRGKADGKSVIDYGFHMIITDWTDSVieeLPELV--KKGIssfKVFM--AYKGLLMVDDEELLDVLKRAKELgaLVM 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1525 VaHAEQQTVAAVL--------------------------------MVAQLTQRSVHICHVARKEEILLIKAAKARGLPVT 1572
Cdd:cd01314   180 V-HAENGDVIAELqkkllaqgktgpeyhalsrppeveaeataraiRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVY 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1573 CEVAPHHLFLSHDDLERLGP-GKGEV-RPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP-----PPGFPG 1643
Cdd:cd01314   259 GETCPQYLLLDDSDYWKDWFeGAKYVcSPPLRPKEDQEALWDGLSsgTLQTVGSDHCPFNFAQKARGKDdftkiPNGVPG 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1644 LETMLPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVE--------VDLEHEWTIPSHMPFSKAHWTPFEGQ 1714
Cdd:cd01314   339 VETRMPLLWSEgVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVgsdadlviWDPNAEKTISADTHHHNVDYNIFEGM 418

                         410       420
                  ....*....|....*....|....*....
gi 807045910 1715 KVKGTVRRVVLRGEVAYIDGQVLVPPGYG 1743
Cdd:cd01314   419 KVKGWPVVTISRGKVVVEDGELVGEKGSG 447
PRK00779 PRK00779
ornithine carbamoyltransferase; Provisional
 1857-2159 1.57e-43

ornithine carbamoyltransferase; Provisional


Pssm-ID: 234835 [Multi-domain]  Cd Length: 304  Bit Score: 161.80  E-value: 1.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1857 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1936
Cdd:PRK00779    1 MLMGRHFLSLDDLSPEELEELLDLAAELKKKRKAGEPHPPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIFLSPRDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1937 SVQKGESLADSVQTMSCYADVVVLR-HPQPGAVELaAKHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMTITM 2014
Cdd:PRK00779   81 QLGRGEPIEDTARVLSRYVDAIMIRtFEHETLEEL-AEYSTVPVINGlTD--LSHPCQILADLLTIYEHRGSLKGLKVAW 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2015 VGDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVA-SRGTKQEEFESIEEALPDTDVLY------Mtriqk 2086
Cdd:PRK00779  158 VGD---GNNVaNSLLLAAALLGFDLRVATPKGYEPDPEIVEKIAkETGASIEVTHDPKEAVKGADVVYtdvwvsM----- 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807045910 2087 erfGSTQEYE---ACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2159
Cdd:PRK00779  230 ---GQEAEAEerlKAFAPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEVIDGPQSVVWDEAENRLHAQKALLAWLL 304
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1250-1375 6.05e-43

Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.


Pssm-ID: 238711 [Multi-domain]  Cd Length: 116  Bit Score: 152.84  E-value: 6.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1250 KNILLTIGSYkNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGEcppqRSILEQLAEKNFELV 1329
Cdd:cd01423     1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK----PSLRELLAEGKIDLV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 807045910 1330 INLSMRGAGGRRLSsfvtkGYRTRRLAADFSVPLIIDIKCTKLFVE 1375
Cdd:cd01423    76 INLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
 1379-1748 2.52e-42

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


Pssm-ID: 273937 [Multi-domain]  Cd Length: 454  Bit Score: 162.56  E-value: 2.52e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1379 QIGP--APPLKVHV-DCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPAL 1453
Cdd:TIGR02033   28 AVGDnlIPPDAVEViDA--TGKYV-LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEAL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1454 ALAQKLAEAGARCDFALFLGASSENAGTLG-----TVAGSAAGLKLY-------------LNETFSELR----------- 1504
Cdd:TIGR02033  105 ETWHEKAEGKSVIDYGFHMDITHWNDSVLEehipeVKEEGINSFKVFmayknllmvddeeLFEILKRLKelgallqvhae 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1505 ----LDSVVQWM-EHFETWPSHLPIV--AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAP 1577
Cdd:TIGR02033  185 ngdiIAELQARMlAQGITGPEYHALSrpPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCP 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1578 HHLFLSHDDLERLG--PGKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG------SRPPPGFPGLETM 1647
Cdd:TIGR02033  265 QYLVLDDTHYDKPGfeGAKYVCSPPLREPEDQDALWSALSsgALQTVGSDHCTFNFAQKKAigkddfTKIPNGGPGVEER 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1648 LPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVE--------VDLEHEWTIPSHMPFSKAHWTPFEGQKVKG 1718
Cdd:TIGR02033  345 MSLLFDEgVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVgsdadiviWDPNRTTVISAETHHSNADYNPFEGFKVRG 424

                          410       420       430
                   ....*....|....*....|....*....|
gi 807045910  1719 TVRRVVLRGEVAYIDGQVLVPPGYGQDVRK 1748
Cdd:TIGR02033  425 APVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
PRK07369 PRK07369
dihydroorotase; Provisional
 1379-1720 4.08e-41

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 158.23  E-value: 4.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1379 QIGPAPPLKVHVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPAL--ALA 1456
Cdd:PRK07369   37 HIDPIPPDTQIIDA---SGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPL-DNPATlaRLQ 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1457 QKLAE-AGARCDF--ALFLGASSENAGTLGT-----VAGSAAGLKLylnETFSELR--LDSVVQWMEHFETWPSHL---- 1522
Cdd:PRK07369  113 QQAQQiPPVQLHFwgALTLGGQGKQLTELAElaaagVVGFTDGQPL---ENLALLRrlLEYLKPLGKPVALWPCDRslag 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1523 ----------------PIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDD 1586
Cdd:PRK07369  190 ngvmregllalrlglpGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEA 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1587 LERLGPgkgEVR--PELGSRQDVEALWENM--AVIDCFASDHAPHTLEEKCG--SRPPPGFPGLETMLPLLL-TAVSEGR 1659
Cdd:PRK07369  270 LASYDP---NLRldPPLGNPSDRQALIEGVrtGVIDAIAIDHAPYTYEEKTVafAEAPPGAIGLELALPLLWqNLVETGE 346

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807045910 1660 LSLDDLLQRLHHNPRRIFHLPP------QEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTV 1720
Cdd:PRK07369  347 LSALQLWQALSTNPARCLGQEPpslapgQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
PRK08323 PRK08323
phenylhydantoinase; Validated
 1397-1754 7.89e-41

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 158.41  E-value: 7.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1397 KLVrLPGLIDVHVHLREP-GGTH-KEDFASGTAAALAGGITMVC--AMPNTRPPIIDApaLALAQKLAEAGARCD--FAL 1470
Cdd:PRK08323   45 KYV-MPGGIDPHTHMEMPfGGTVsSDDFETGTRAAACGGTTTIIdfALQPKGQSLREA--LEAWHGKAAGKAVIDygFHM 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1471 FLGASSENAGT-LGTVAgsAAG---LKLYLN-------------ETFSELR-LDSVVqwMEHFE---------------- 1516
Cdd:PRK08323  122 IITDWNEVVLDeMPELV--EEGitsFKLFMAykgalmldddellRALQRAAeLGALP--MVHAEngdaiaylqakllaeg 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1517 -TWPSHLPIV--AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPG 1593
Cdd:PRK08323  198 kTGPEYHALSrpPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWF 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1594 KGEVR---PELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG------SRPPPGFPGLETMLPLLLTA-VSEGRLS 1661
Cdd:PRK08323  278 EGAKYvmsPPLRDKEHQDALWRGLQdgDLQVVATDHCPFCFEQKKQlgrgdfTKIPNGTPGVEDRMPLLFSEgVMTGRIT 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1662 LDDLLQRLHHNPRRIFHLPPQEDTyVEV---------DLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYI 1732
Cdd:PRK08323  358 LNRFVELTSTNPAKIFGLYPRKGT-IAVgadadiviwDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVE 436

                         410       420
                  ....*....|....*....|..
gi 807045910 1733 DGQVLVPPGYGQDVRKWPQGAV 1754
Cdd:PRK08323  437 DGEFRGKAGHGRFLKRKPFQAV 458
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 1397-1783 2.25e-38

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 151.39  E-value: 2.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1397 KLVrLPGLIDVHVHLREPGGT---HKEDFASGTAAALAGGITMVC--AMPNTRPPIIDApaLALAQKLAEAGARCDFALF 1471
Cdd:PRK13404   50 RLV-LPGGVDSHCHIDQPSGDgimMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSLREA--VEDYHRRAAGKAVIDYAFH 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1472 LGASSENAGTLG-----TVAGSAAGLKLYLneTFSELRLDS-------------------------VVQWM-----EHFE 1516
Cdd:PRK13404  127 LIVADPTEEVLTeelpaLIAQGYTSFKVFM--TYDDLKLDDrqildvlavarrhgamvmvhaenhdMIAWLtkrllAAGL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1517 TWPSH----LPIVAHAEQQTVAAVLmvAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERlgP 1592
Cdd:PRK13404  205 TAPKYhaisRPMLAEREATHRAIAL--AELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDR--P 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1593 G----KGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP----------PPGFPGLETMLPLLLTA-V 1655
Cdd:PRK13404  281 GmegaKYICSPPPRDKANQEAIWNGLAdgTFEVFSSDHAPFRFDDTDGKLAaganpsfkaiANGIPGIETRLPLLFSEgV 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1656 SEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYV---EVDL-----EHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRG 1727
Cdd:PRK13404  361 VKGRISLNRFVALTSTNPAKLYGLYPRKGAIAigaDADIaiwdpDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRG 440

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 807045910 1728 EVAYIDGQVLVPPGYGQDVRKwpqgavpqlppsapatsemtTTPERPRRGIPGLPD 1783
Cdd:PRK13404  441 RVVVEDGELVAERGSGQFLAR--------------------SLPDRARPNGRLEPE 476
OTCace pfam00185
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
2011-2158 2.99e-38

Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;


Pssm-ID: 425511 [Multi-domain]  Cd Length: 154  Bit Score: 140.82  E-value: 2.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  2011 TITMVGDlKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLYMTRIQ- 2085
Cdd:pfam00185    1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVldkaKKIAEKSGGSIEITDDPAEAVKGADVVYTDVWQs 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807045910  2086 ----KERFgstQEYEAcFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATV 2158
Cdd:pfam00185   80 mgqeKERE---ERLKA-FKPYQVNEELMKLAKKDAIFMHCLPahRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLALL 154
pyrB PRK13376
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ...
 1857-2160 7.60e-35

bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional


Pssm-ID: 237369 [Multi-domain]  Cd Length: 525  Bit Score: 141.82  E-value: 7.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1857 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLD---ILKGKV-MASMFYEVSTRTSSSFA-AAMARLGGAVLSF 1931
Cdd:PRK13376    4 DFLGRTLAVIEDLSVEEQLFLYEKTRELKQRWYEGEDVSefrIKKRDVgIYIVFVEPSTRTKESFInAAKFHKNVKVNIF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1932 SEATSSVQKGESLADSVQTMSCYAD--VVVLRHPQPG--------AVELAAKH-CRRPV-INAGDGVGEHPTQALLDIFT 1999
Cdd:PRK13376   84 DSEHSSFNKQESYTDTFNMLTGYSDysIFIVRTRLEGvcrlleekVSEFASRNgIEVPAfINAGDGKHEHPTQELLDEFT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2000 IREELGTVNG-MTITMVGDLKHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTD 2077
Cdd:PRK13376  164 FLEQNNFDNSfIHIALVGDLLHGRTVHSKVNGLKIFKnVKVDLIAPEELAMPEHYVEKMKKNGFEVRIFSSIEEYLSQKD 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2078 VL---YMTRIQKERFGStqeyeacfgQFILTPHIMTRA---KKKMV--------VMHPMPRVN---EISVEVDSDPRAAY 2140
Cdd:PRK13376  244 VAkiwYFTRLQLERMGE---------DILEKEHILRKAvtfRKEFLdklpegvkFYHPLPRHKvypTIPTFLDTLPLNGW 314

                         330       340
                  ....*....|....*....|
gi 807045910 2141 FRQAENGMYIRMALLATVLG 2160
Cdd:PRK13376  315 ETQAINGYWVRIVLLSMLGG 334
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 738-814 2.74e-33

Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 460695  Cd Length: 79  Bit Score: 124.03  E-value: 2.74e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807045910   738 ELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrGQPLPPDLLQQAKCLGFSDKQIA 814
Cdd:pfam02787    2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEA-GLDLDAELLREAKRLGFSDRQIA 77
PRK07627 PRK07627
dihydroorotase; Provisional
 1380-1731 6.08e-33

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 134.03  E-value: 6.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1380 IGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPALA----- 1454
Cdd:PRK07627   33 IGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPVL-DEPGLVemlkf 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1455 LAQKLAEAGARCDFALFLGASSENAGTL------GTVAGSAAGLKLylnetfselrLDSVVQW--MEH-----FETWPSH 1521
Cdd:PRK07627  112 RARNLNQAHVYPLGALTVGLKGEVLTEMvelteaGCVGFSQANVPV----------VDTQVLLraLQYastfgFTVWLRP 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1522 LPI------VAH----------------AEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHH 1579
Cdd:PRK07627  182 LDAflgrggVAAsgavasrlglsgvpvaAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNH 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1580 LFLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKC--GSRPPPGFPGLETMLPLLLTAV 1655
Cdd:PRK07627  262 VHLIDVDIGYFDS-QFRLDPPLRSQRDREAIRAALAdgTIDAICSDHTPVDDDEKLlpFAEATPGATGLELLLPLTLKWA 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1656 SEGRLSLDDLLQRLHHNPRRIFHLPPQE-------DTYVeVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGE 1728
Cdd:PRK07627  341 DEAKVPLARALARITSAPARVLGLPAGRlaegapaDLCV-FDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQ 419


                  ...
gi 807045910 1729 VAY 1731
Cdd:PRK07627  420 VAF 422
PLN02342 PLN02342
ornithine carbamoyltransferase
 1819-2160 1.64e-32

ornithine carbamoyltransferase


Pssm-ID: 177976 [Multi-domain]  Cd Length: 348  Bit Score: 131.07  E-value: 1.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1819 MGTPDGTCYPPPPVPRQASPQNlGTPGLLHPQTSPLLHSLVG----QHILSVQQFTKDQMSHLFNVAHTLRMMVQK-ERS 1893
Cdd:PLN02342    1 MFFSLRRARSPSAVSSSSRARR-GLVVCAASSSAAAPSPIKGkskpKHFLHIDDFDKEEILGLLDRAKEVKALLKSgDRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1894 LDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLR---HPQpgAVEL 1970
Cdd:PLN02342   80 FQPFKGKSMAMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQLGKREETRDIARVLSRYNDIIMARvfaHQD--VLDL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1971 aAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkHGRTVHSLACLLTQYRVSLRYVAPPSLRMPP 2050
Cdd:PLN02342  158 -AEYSSVPVINGLTDY-NHPCQIMADALTIIEHIGRLEGTKVVYVGD--GNNIVHSWLLLAAVLPFHFVCACPKGYEPDA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2051 TVrafvaSRGTKQEEFESIE------EALPDTDVLY------MTriQKErfgstqEYE---ACFGQFILTPHIMTRAKKK 2115
Cdd:PLN02342  234 KT-----VEKARAAGISKIEitndpaEAVKGADVVYtdvwasMG--QKE------EAEkrkKAFQGFQVNEALMKLAGPQ 300

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 807045910 2116 MVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2160
Cdd:PLN02342  301 AYFMHCLPaeRGVEVTDGVMEAPNSIVFPQAENRMHAQNAIMLHQLG 347
PLN02795 PLN02795
allantoinase
 1399-1734 6.66e-31

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 129.51  E-value: 6.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1399 VRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASSE 1477
Cdd:PLN02795   96 VVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPE 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1478 NA------------GTLG----------------TVAGSAAGLK---------LYLNETFSELRLDSVVQ-----WMEHF 1515
Cdd:PLN02795  176 NAhnasvleelldaGALGlksfmcpsgindfpmtTATHIKAALPvlakygrplLVHAEVVSPVESDSRLDadprsYSTYL 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1516 ETWPshlpivAHAEQQTVAAVLMVAQLTQR-------SVHICHVARKEEIL-LIKAAKARGLPVTCEVAPHHLFLSHDDL 1587
Cdd:PLN02795  256 KSRP------PSWEQEAIRQLLEVAKDTRPggvaegaHVHIVHLSDAESSLeLIKEAKAKGDSVTVETCPHYLAFSAEEI 329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1588 erlgpGKGEVR----PELGSRQDVEALWENMA--VIDCFASDHAPHT-----LEEKCGSRPPPGFPGLETMLPLLLTAVS 1656
Cdd:PLN02795  330 -----PDGDTRykcaPPIRDAANRELLWKALLdgDIDMLSSDHSPSPpdlklLEEGNFLRAWGGISSLQFVLPATWTAGR 404

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1657 EGRLSLDDLLQRLHHNPRRIFHLP------PQEDTYVEV-DLEHEWTIPSHMPFSKAH--WTPFEGQKVKGTVRRVVLRG 1727
Cdd:PLN02795  405 AYGLTLEQLARWWSERPAKLAGLDskgaiaPGKDADIVVwDPEAEFVLDESYPIYHKHksLSPYLGTKLSGKVIATFVRG 484


                  ....*..
gi 807045910 1728 EVAYIDG 1734
Cdd:PLN02795  485 NLVFLEG 491
PRK09059 PRK09059
dihydroorotase; Validated
 1390-1731 6.00e-30

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 125.15  E-value: 6.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1390 VDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPpIIDAPAL---------------- 1453
Cdd:PRK09059   51 VDC---AGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDP-VIDDVALvefvkrtardtaivni 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1454 ----ALAQKLA-----------EAGARC----------------------DFALFLGASSENAgTLGtvagsAAGLklyL 1496
Cdd:PRK09059  127 hpaaAITKGLAgeemtefgllrAAGAVAftdgrrsvantqvmrraltyarDFDAVIVHETRDP-DLG-----GNGV---M 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1497 NETFselrldsvvqwmehFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVA 1576
Cdd:PRK09059  198 NEGL--------------FASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVS 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1577 PHHLFLSHDDLerlgpgkGEVR------PELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKcgsRPP-----PGFPG 1643
Cdd:PRK09059  264 INHLSLNENDI-------GEYRtffklsPPLRTEDDRVAMVEAVAsgTIDIIVSSHDPQDVDTK---RLPfseaaAGAIG 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1644 LETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP-------PQEDTYVeVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1716
Cdd:PRK09059  334 LETLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGLPagtlkpgAPADIIV-IDLDEPWVVDPEDLKSRSKNTPFEEARF 412

                         410
                  ....*....|....*
gi 807045910 1717 KGTVRRVVLRGEVAY 1731
Cdd:PRK09059  413 QGRVVRTIVAGKTVY 427
PRK08044 PRK08044
allantoinase AllB;
1391-1731 1.91e-29

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 124.20  E-value: 1.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1391 DCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFA 1469
Cdd:PRK08044   42 EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1470 LFLGASSENAGTLGTV-AGSAAGLKLYL--------NETFSELRLDSVVQWME-----------HFETWP--SHLPIVAH 1527
Cdd:PRK08044  122 QLGGLVSYNLDRLHELdEVGVVGFKCFVatcgdrgiDNDFRDVNDWQFYKGAQklgelgqpvlvHCENALicDELGEEAK 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1528 AEQQTVAA-----------------VLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERL 1590
Cdd:PRK08044  202 REGRVTAHdyvasrpvfteveairrVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEI 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1591 GPgKGEVRPELGSRQDVEALWENM--AVIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLL-TAVSEGRLSLDDL 1665
Cdd:PRK08044  282 GT-LAKCSPPIRDLENQKGMWEKLfnGEIDCLVSDHSPCPPEMKAGNimEAWGGIAGLQNCMDVMFdEAVQKRGMSLPMF 360

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807045910 1666 LQRLHHNPRRIFHL-------PPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAY 1731
Cdd:PRK08044  361 GKLMATNAADIFGLqqkgriaPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
PRK14805 PRK14805
ornithine carbamoyltransferase; Provisional
 1861-2160 3.39e-26

ornithine carbamoyltransferase; Provisional


Pssm-ID: 237819 [Multi-domain]  Cd Length: 302  Bit Score: 111.32  E-value: 3.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1861 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSldILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 1940
Cdd:PRK14805    2 KHLLSIKELTQQQLLDLLALAKTIKANPAEYRQ--ALAGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGALGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1941 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkh 2020
Cdd:PRK14805   80 RESVADFAANLSCWADAIVARVFSHSTIEQLAEHGSVPVINALCDL-YHPCQALADFLTLAEQFGDVSKVKLAYVGD--- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2021 GRTV-HSL----ACLLTQYRVslryVAPPSLRMPPTV----RAFVASRGTKQEEFESIeEALPDTDVLYM-TRIQKERFG 2090
Cdd:PRK14805  156 GNNVtHSLmygaAILGATMTV----ICPPGHFPDGQIvaeaQELAAKSGGKLVLTSDI-EAIEGHDAIYTdTWISMGDDT 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807045910 2091 STQEYEACFGQFILTPHIMTRAKKKMvVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2160
Cdd:PRK14805  231 PLAEIKAKFAPYQVNKALMEKAGATF-VMHCQPahRGVEITSEVMDGEGSLILQQAENRMHAQNAVLVTLLS 301
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 966-1184 9.49e-24

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: 103.03  E-value: 9.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  966 RQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLE 1045
Cdd:COG0439    36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1046 RFL----SSAAAVSKEHPVVISKFIqEAKEIDVDAVASDGVVAAIAISEHvENAGVHSGDATLVTPPqDITAKTLERIKA 1121
Cdd:COG0439   116 AALaearAEAKAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGE 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807045910 1122 IVHAVGQELQV-TGPFNLQ-LIAKDDQLKVIECNVRVS--RSFPFVSKTLGVDLVALATRVIMGEEV 1184
Cdd:COG0439   193 LVARALRALGYrRGAFHTEfLLTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
PRK02102 PRK02102
ornithine carbamoyltransferase; Validated
 1858-2160 1.62e-23

ornithine carbamoyltransferase; Validated


Pssm-ID: 179366 [Multi-domain]  Cd Length: 331  Bit Score: 104.20  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1858 LVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSS 1937
Cdd:PRK02102    5 LKGRSFLKLLDFTPEEIEYLIDLSIELKAAKKAGIEHQYLEGKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLGPNDSQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1938 VQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGD 2017
Cdd:PRK02102   85 LGKKESIEDTARVLGRMYDGIEYRGFKQEIVEELAKYSGVPVWNGLTDE-WHPTQMLADFMTMKEHFGPLKGLKLAYVGD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2018 lkhGR--TVHSL---ACLLTqyrVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLYmTRI---- 2084
Cdd:PRK02102  164 ---GRnnMANSLmvgGAKLG---MDVRICAPKELWPEEELvalaREIAKETGAKITITEDPEEAVKGADVIY-TDVwvsm 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2085 --QKERfgstQEYEACFGQFILTPHIMTR-AKKKMVVMHPMP-----------------RVNEISV--EVDSDPRAAYFR 2142
Cdd:PRK02102  237 geEDEW----EERIKLLKPYQVNMDLMKAtGNPDVIFMHCLPafhdtetkvgkeiaekyGLKGLEVtdEVFESKYSIVFD 312

                         330
                  ....*....|....*...
gi 807045910 2143 QAENGMYIRMALLATVLG 2160
Cdd:PRK02102  313 EAENRMHTIKAVMVATLG 330
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 187-338 7.72e-23

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 97.99  E-value: 7.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  187 YNQIRCLCQRGAEVTVVPWDHALDSQE----YEGLFLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAI 262
Cdd:cd01743    12 YNLVQYLRELGAEVVVVRNDEITLEELellnPDAIVISPGPGHPEDAGISLEIIRALAGK---VPILGVCLGHQAIAEAF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  263 GAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWapLFTNANDgsnEGIV----HNSLPFFS 332
Cdd:cd01743    89 GGKVVRAPEPMHGktseihHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLL--EVTASTE---DGVImalrHRDLPIYG 163


                  ....*.
gi 807045910  333 VQFHPE 338
Cdd:cd01743   164 VQFHPE 169
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 1404-1676 5.65e-22

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 98.17  E-value: 5.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1404 LIDVHVHLREPGGTH------------------KEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGAR 1465
Cdd:cd01292     1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1466 CDFALFLGASSENAGTLGTV------------AGSAAGLKLYLNETFSELRLDSVvqwMEHFETWPSH-LPIVAHAEQQT 1532
Cdd:cd01292    81 IRVVLGLGIPGVPAAVDEDAealllellrrglELGAVGLKLAGPYTATGLSDESL---RRVLEEARKLgLPVVIHAGELP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1533 VA--AVLMVAQLTQR--SVHICHVARKEEILLIKAAKArglPVTCEVAPHHLFLSHDDlerlgpgkgevrpelgsRQDVE 1608
Cdd:cd01292   158 DPtrALEDLVALLRLggRVVIGHVSHLDPELLELLKEA---GVSLEVCPLSNYLLGRD-----------------GEGAE 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807045910 1609 ALWENMA--VIDCFASDHAPHTLEekcgsrpppgfpglETMLPLLLTAVSEGRL--SLDDLLQRLHHNPRRI 1676
Cdd:cd01292   218 ALRRLLElgIRVTLGTDGPPHPLG--------------TDLLALLRLLLKVLRLglSLEEALRLATINPARA 275
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 985-1182 2.19e-21

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: 94.68  E-value: 2.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   985 RFKFSRLLDTIGISQPQW--RELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKE----H 1058
Cdd:pfam02786    2 KVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1059 PVVISKFIQEAKEIDVDAVAsDGVVAAIAISEhVENA-GVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFN 1137
Cdd:pfam02786   82 QVLVEKSLKGPKHIEYQVLR-DAHGNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 807045910  1138 LQLI--AKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGE 1182
Cdd:pfam02786  160 VEFAldPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGY 206
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1264-1364 8.63e-19

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 460462 [Multi-domain]  Cd Length: 93  Bit Score: 82.92  E-value: 8.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1264 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEA-VDGECppqrSILEQLAEKNFELVINLSMRGAGGRRl 1342
Cdd:pfam02142    1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGrPGGRV----QIGDLIKNGEIDLVINTLYPFKATVH- 75

                           90       100
                   ....*....|....*....|..
gi 807045910  1343 ssfvtKGYRTRRLAADFSVPLI 1364
Cdd:pfam02142   76 -----DGYAIRRAAENIDIPGP 92
PRK04284 PRK04284
ornithine carbamoyltransferase; Provisional
 1857-2161 9.29e-19

ornithine carbamoyltransferase; Provisional


Pssm-ID: 235269 [Multi-domain]  Cd Length: 332  Bit Score: 89.80  E-value: 9.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1857 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1936
Cdd:PRK04284    3 NLRNRSFLTLLDFTPKEIEYLLDLSEDLKRAKYAGIEVQKLKGKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGPTGS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1937 SVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINaGDGVGEHPTQALLDIFTIREEL-GTVNGMTITMV 2015
Cdd:PRK04284   83 QMGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSGVPVWN-GLTDEDHPTQVLADFLTAKEHLkKPYKDIKFTYV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2016 GDlkhGRTVHSLACLLTQYRVSLRY--VAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLYM-------- 2081
Cdd:PRK04284  162 GD---GRNNVANALMQGAAIMGMDFhlVCPKELNPDDELlnkcKEIAAETGGKITITDDIDEGVKGSDVIYTdvwvsmge 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2082 -TRIQKERFGSTQEYEacfgqfiLTPHIMTRAKKKMVV-MHPMPRVN-------------------EISVEVDSDPRAAY 2140
Cdd:PRK04284  239 pDEVWEERIKLLKPYQ-------VNKEMMKKTGNPNAIfEHCLPSFHdldtkvgkeifekyglkemEVTDEVFESKASVV 311

                         330       340
                  ....*....|....*....|.
gi 807045910 2141 FRQAENGMYIRMALLATVLGR 2161
Cdd:PRK04284  312 FDEAENRMHTIKAVMVATLGE 332
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 177-351 8.56e-17

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 81.53  E-value: 8.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  177 RILALDCGLKYNQI-----RCLCQRGAEVTVV--------PWDHALDsqEYEGLFLSNGPG---DPASYPSVVSTLSRVL 240
Cdd:COG0518     1 KILILDHDPFGGQYpgliaRRLREAGIELDVLrvyageilPYDPDLE--DPDGLILSGGPMsvyDEDPWLEDEPALIREA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  241 SEPNpRPVFGICLGHQLLALAIGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVetDSLPADWAPLFTN 314
Cdd:COG0518    79 FELG-KPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelTEADPLFAGLPDEFTVWMSHGDTV--TELPEGAEVLASS 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 807045910  315 ANDgSNEGIVHNSlPFFSVQFHPEhqAGPSDMELLFD 351
Cdd:COG0518   156 DNC-PNQAFRYGR-RVYGVQFHPE--VTHTMMEAWLE 188
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 963-1186 3.78e-16

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 81.85  E-value: 3.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  963 ALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT--VGYPCVVRPSYVLSGAAMNVAYT 1040
Cdd:PRK12767   90 RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKgeLQFPLFVKPRDGSASIGVFKVND 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1041 DGDLERFLSSAAavskehPVVISKFIQEaKEIDVDA-VASDGVVAAIAISEHVEnagVHSGDATlvtppQDITAKTLERI 1119
Cdd:PRK12767  170 KEELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETS-----KGVTVKDPELF 234

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807045910 1120 KAIVHaVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFvSKTLGVDLVALATRVIMGEEVEP 1186
Cdd:PRK12767  235 KLAER-LAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL-SYMAGANEPDWIIRNLLGGENEP 299
PRK12562 PRK12562
ornithine carbamoyltransferase subunit F; Provisional
 1855-2161 4.67e-16

ornithine carbamoyltransferase subunit F; Provisional


Pssm-ID: 105755  Cd Length: 334  Bit Score: 82.03  E-value: 4.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1855 LHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA 1934
Cdd:PRK12562    1 MSGFYKKHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1935 TSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINaGDGVGEHPTQALLDIFTIREEL--GTVNGMTI 2012
Cdd:PRK12562   81 GSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWN-GLTNEFHPTQLLADLLTMQEHLpgKAFNEMTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2013 TMVGDLKH--GRTVHSLACLLTqyrVSLRYVAP----PSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLY------ 2080
Cdd:PRK12562  160 VYAGDARNnmGNSMLEAAALTG---LDLRLVAPqacwPEASLVAECSALAQKHGGKITLTEDIAAGVKGADFIYtdvwvs 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2081 MTRIQK---ERFGSTQEYEACFGQFILT--PHI------------MTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQ 2143
Cdd:PRK12562  237 MGEPKEkwaERIALLRGYQVNSKMMALTgnPQVkflhclpafhddQTTLGKKMAKEFGLHGGMEVTDEVFESPASIVFDQ 316

                         330
                  ....*....|....*...
gi 807045910 2144 AENGMYIRMALLATVLGR 2161
Cdd:PRK12562  317 AENRMHTIKAVMVATLAK 334
PRK03515 PRK03515
ornithine carbamoyltransferase subunit I; Provisional
 1861-2159 2.00e-15

ornithine carbamoyltransferase subunit I; Provisional


Pssm-ID: 179587 [Multi-domain]  Cd Length: 336  Bit Score: 79.76  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1861 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 1940
Cdd:PRK03515    7 RHFLRLLDFTPAELNSLLQLAAKLKADKKNGKEEQKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1941 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINagdGVGE--HPTQALLDIFTIREEL--GTVNGMTITMVG 2016
Cdd:PRK03515   87 KESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYAGVPVWN---GLTNefHPTQLLADLLTMQEHLpgKAFNEMTLAYAG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2017 DLKH--GRTVHSLACLLTqyrVSLRYVAP----PSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYM--------- 2081
Cdd:PRK03515  164 DARNnmGNSLLEAAALTG---LDLRLVAPkacwPEAALVTECRALAQKNGGNITLTEDIAEGVKGADFIYTdvwvsmgep 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2082 TRIQKERFGSTQEYEACFGQFILT--PHI------------MTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENG 2147
Cdd:PRK03515  241 KEVWAERIALLRPYQVNSKMMQLTgnPQVkflhclpafhddQTTLGKKMAEEYGLHGGMEVTDEVFESAHSIVFDQAENR 320

                         330
                  ....*....|...
gi 807045910 2148 MY-IRMALLATVL 2159
Cdd:PRK03515  321 LHtIKAVMVATLS 333
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 187-338 2.06e-15

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 76.62  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  187 YNQIRCLCQRGAEVTVVPWDH----ALDSQEYEGLFLSNGPGDPASYP---SVVSTLSRVLsepnprPVFGICLGHQLLA 259
Cdd:COG0512    12 YNLVQYLGELGAEVVVVRNDEitleEIEALAPDGIVLSPGPGTPEEAGislEVIRAFAGKI------PILGVCLGHQAIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  260 LAIGAKTYKMRY------------GN---RGHNQPcLLVgsGRcfltsqNHGFAVETDSLPAD-----WAPlftnanDGS 319
Cdd:COG0512    86 EAFGGKVVRAPEpmhgktspithdGSglfAGLPNP-FTA--TR------YHSLVVDRETLPDElevtaWTE------DGE 150

                         170
                  ....*....|....*....
gi 807045910  320 NEGIVHNSLPFFSVQFHPE 338
Cdd:COG0512   151 IMGIRHRELPIEGVQFHPE 169
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 187-338 3.51e-14

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 72.90  E-value: 3.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   187 YNQIRCLCQRGAEVtVVPWDHALDSQEYEGL---FLSNGPGdpASYPSVVSTLSRVLSEPNPR-PVFGICLGHQLLALAI 262
Cdd:TIGR00566   13 YNLVQYFCELGAEV-VVKRNDSLTLQEIEALlplLIVISPG--PCTPNEAGISLEAIRHFAGKlPILGVCLGHQAMGQAF 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   263 GAKTYKMRYGNRGHNQPCLLVGSGRC------FLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFH 336
Cdd:TIGR00566   90 GGDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFH 169


                   ..
gi 807045910   337 PE 338
Cdd:TIGR00566  170 PE 171
PRK01713 PRK01713
ornithine carbamoyltransferase; Provisional
 1857-2159 3.70e-14

ornithine carbamoyltransferase; Provisional


Pssm-ID: 167263 [Multi-domain]  Cd Length: 334  Bit Score: 76.18  E-value: 3.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1857 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1936
Cdd:PRK01713    4 NLKNRHLLSLVNHTEREIKYLLDLSRDLKRAKYAGTEQQRLKGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYIDPNSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1937 SVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINagdGVGE--HPTQALLDIFTIREELGT-VNGMTIT 2013
Cdd:PRK01713   84 QIGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFN---GLTDefHPTQMLADVLTMIENCDKpLSEISYV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2014 MVGDLKHGRTvHSLACLLTQYRVSLRYVAPPSL----RMPPTVRAFVASRGTKQEEFESIEEALPDTDVlymtrIQKERF 2089
Cdd:PRK01713  161 YIGDARNNMG-NSLLLIGAKLGMDVRICAPKALlpeaSLVEMCEKFAKESGARITVTDDIDKAVKGVDF-----VHTDVW 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2090 GSTQEYEACFGQFI-------LTPHIMTR-AKKKMVVMHPMPRVN---------------------EISVEVDSDPRAAY 2140
Cdd:PRK01713  235 VSMGEPLETWGERIkllmpyqVTPELMKRtGNPKVKFMHCLPAFHnsetkvgrqiaekypelangiEVTEDVFESPMNIA 314

                         330
                  ....*....|....*....
gi 807045910 2141 FRQAENGMYIRMALLATVL 2159
Cdd:PRK01713  315 FEQAENRMHTIKAVMVASL 333
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
866-1187 4.87e-14

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 76.51  E-value: 4.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  866 TFRTPHVLVLGSgvyrigssvefDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLY------FDEISF-EVVMD 938
Cdd:COG3919     2 MTMRFRVVVLGG-----------DINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVvvpdpgDDPEAFvDALLE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  939 IYELENPEGVILSMGGQLpnnMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQF 1014
Cdd:COG3919    71 LAERHGPDVLIPTGDEYV---ELLSRHRDEleehYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDAL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1015 CQTVGYPCVVRPSYvlSGAAMNV----------AYTDGDLERFLSSAAAVskEHPVVISKFI--QEAKEIDVDA-VASDG 1081
Cdd:COG3919   148 AEDLGFPVVVKPAD--SVGYDELsfpgkkkvfyVDDREELLALLRRIAAA--GYELIVQEYIpgDDGEMRGLTAyVDRDG 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1082 VVAAIAISEHV----ENAGVHSgdATLVTPPQDItaktLERIKAIVHAVGqelqVTGPFNLQLI--AKDDQLKVIECNVR 1155
Cdd:COG3919   224 EVVATFTGRKLrhypPAGGNSA--ARESVDDPEL----EEAARRLLEALG----YHGFANVEFKrdPRDGEYKLIEINPR 293

                         330       340       350
                  ....*....|....*....|....*....|..
gi 807045910 1156 VSRSFPFVSKTlGVDLVALATRVIMGEEVEPV 1187
Cdd:COG3919   294 FWRSLYLATAA-GVNFPYLLYDDAVGRPLEPV 324
PRK04523 PRK04523
N-acetylornithine carbamoyltransferase; Reviewed
 1861-2161 7.76e-14

N-acetylornithine carbamoyltransferase; Reviewed


Pssm-ID: 235304 [Multi-domain]  Cd Length: 335  Bit Score: 75.17  E-value: 7.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1861 QHILSVQQFTKDQMSHLFNVAHTLRmmvQKERSlDILKGKVMASMFYEVSTRTSSSFAAAMARLGG-AV----------L 1929
Cdd:PRK04523    4 KHFLNTQDWSRAELDALLTQAAAFK---RNKLG-SALKGKSIALVFFNPSLRTRTSFELGAFQLGGhAVvlqpgkdawpI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1930 SFSEATssVQKG---ESLADSVQTMSCYADVVVLR----------HPQPGAVELAAKHCRRPVINAGDGVgeHPTQALLD 1996
Cdd:PRK04523   80 EFELGA--VMDGeteEHIREVARVLSRYVDLIGVRafpkfvdwskDRQDQVLNSFAKYSTVPVINMETIT--HPCQELAH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1997 IFTIREELG-TVNGMTI------------TMVGD------LKHGRTVhSLACLLTQYRVSLRYVAppslrmppTVRAFVA 2057
Cdd:PRK04523  156 ALALQEHFGtTLRGKKYvltwtyhpkplnTAVANsalliaTRLGMDV-TLLCPTPDYILDERYMD--------WAEQNAA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2058 SRGTKQEEFESIEEALPDTDVLYM----TRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKmVVMH--PMPRVNEISVE 2131
Cdd:PRK04523  227 ESGGSLTVSHDIDSAYAGADVVYAkswgALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNG-VFSHclPLRRNVKVTDA 305

                         330       340       350
                  ....*....|....*....|....*....|
gi 807045910 2132 VDSDPRAAYFRQAENGMYIRMALLATVLGR 2161
Cdd:PRK04523  306 VMDSPNCIAIDEAENRLHVQKAIMAALASQ 335
PRK14804 PRK14804
ornithine carbamoyltransferase; Provisional
 1861-2159 8.38e-14

ornithine carbamoyltransferase; Provisional


Pssm-ID: 173265 [Multi-domain]  Cd Length: 311  Bit Score: 74.68  E-value: 8.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1861 QHILSVQQFTKDQMSHLFNVAhtlrMMVQKERS--LDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSV 1938
Cdd:PRK14804    7 KHLISWEDWSDSEILDLLDFA----VHVKKNRVnyAGHMSGRSLAMLFQKTSTRTRVSFEVAMTEMGGHGIYLDWMASNF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1939 QkgesLAD---SVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGeHPTQALLDIFTIREELGTV--NGMTIT 2013
Cdd:PRK14804   83 Q----LSDidlEARYLSRNVSVIMARLKKHEDLLVMKNGSQVPVINGCDNMF-HPCQSLADIMTIALDSPEIplNQKQLT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 2014 MVGdlKHGRTVHSLACLLTQYRVSLRYVAPPSLR---MPPTV-RAfvASRGTKQEEfESIEEALPDTDVLYMTRIQKERF 2089
Cdd:PRK14804  158 YIG--VHNNVVNSLIGITAALGIHLTLVTPIAAKeniHAQTVeRA--KKKGTLSWE-MNLHKAVSHADYVYTDTWLDMEF 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807045910 2090 GSTQEYEACFGQFI--LTPH-----IMTRAKKKmvVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2159
Cdd:PRK14804  233 FNDPSYADKKKQRMelMMPYqinssLMEKTNAK--VMHDMPihAGYEITREVVLSDRSIIFQQAENRLDAQKAVILKLL 309
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
177-338 1.00e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 69.31  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  177 RILALDC--GLKYNQIRCLCQRGAEVTVV------PWDHALDSQEYEGLFLSNGPGDP----ASYPSVVSTLSRVLsepn 244
Cdd:PRK07765    2 RILVVDNydSFVFNLVQYLGQLGVEAEVWrnddprLADEAAVAAQFDGVLLSPGPGTPeragASIDMVRACAAAGT---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  245 prPVFGICLGHQLLALAIGA-----------KTYKMRYGNRGhnqpcLLVGSGRCFLTSQNHGFAVETDSLPADwapLFT 313
Cdd:PRK07765   78 --PLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG-----VLAGLPDPFTATRYHSLTILPETLPAE---LEV 147

                         170       180
                  ....*....|....*....|....*....
gi 807045910  314 NANDGSneGIV----HNSLPFFSVQFHPE 338
Cdd:PRK07765  148 TARTDS--GVImavrHRELPIHGVQFHPE 174
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 187-338 1.27e-12

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 68.62  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  187 YN---QIRCLcqrGAEVTVVPWDhALDSQEYE-----GLFLSNGPGDPA---SYPSVVSTLSRVLsepnprPVFGICLGH 255
Cdd:PRK05670   13 YNlvqYLGEL---GAEVVVYRND-EITLEEIEalnpdAIVLSPGPGTPAeagISLELIREFAGKV------PILGVCLGH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  256 QLLALAIGA-----------KTYKMRygnrgHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADwapLFTNA--NDGSNEG 322
Cdd:PRK05670   83 QAIGEAFGGkvvrakeimhgKTSPIE-----HDGSGIFAGLPNPFTVTRYHSLVVDRESLPDC---LEVTAwtDDGEIMG 154

                         170
                  ....*....|....*.
gi 807045910  323 IVHNSLPFFSVQFHPE 338
Cdd:PRK05670  155 VRHKELPIYGVQFHPE 170
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
187-355 1.35e-12

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 68.35  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  187 YNQIRCLCQRGAEVtVVPWDHALDSQEYEGL-----FLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALA 261
Cdd:PRK06774   13 YNLYQYFCELGTEV-MVKRNDELQLTDIEQLapshlVISPGPCTPNEAGISLAVIRHFADK---LPILGVCLGHQALGQA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  262 IGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNE---GIVHNSLPFFS 332
Cdd:PRK06774   89 FGARVVRARQVMHGktsaicHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERGGEMDeimGIRHRTLPLEG 168

                         170       180
                  ....*....|....*....|...
gi 807045910  333 VQFHPEHQAGPSDMELLfDIFLE 355
Cdd:PRK06774  169 VQFHPESILSEQGHQLL-DNFLK 190
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1264-1364 1.44e-12

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 214855 [Multi-domain]  Cd Length: 91  Bit Score: 65.19  E-value: 1.44e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   1264 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKV--TAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAggrr 1341
Cdd:smart00851    1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHGG--------IPQILDLIKNGEIDLVINTLYPFE---- 68

                            90       100
                    ....*....|....*....|...
gi 807045910   1342 lSSFVTKGYRTRRLAADFSVPLI 1364
Cdd:smart00851   69 -AQAHEDGYSIRRAAENIDIPGP 90
DHOase cd01294
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ...
 1401-1715 1.48e-12

Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.


Pssm-ID: 238619  Cd Length: 335  Bit Score: 71.16  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1401 LPGLIDVHVHLREpgGTHKEDFASGTAAALAGGITMvcamPNTRPPIIDAP-ALALAQKLAEAGARCDF----ALFLGAS 1475
Cdd:cd01294     3 IPRPDDMHLHLRD--GAMLKLVLPYTARGFSRAIVM----PNLKPPVTTTAdALAYRERILAADPGPNFtplmTLYLTEN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1476 -SENAGTLGTVAGSAAGLKLYLN--ETFSELRLDSVVQWMEHFETWPSH-LPIVAHAEQQTVAAVLM---------VAQL 1542
Cdd:cd01294    77 tTPEELREAKKKGGIRGVKLYPAgaTTNSQGGVTDLEKIYPVLEAMQKLgMPLLVHGEVPDFKIDVLdreakfipvLEPL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1543 TQR----SVHICHVARKEEILLIKAAKARglpVTCEVAPHHLFLSHDDLerLGPGKGEV---RPELGSRQDVEALwENMA 1615
Cdd:cd01294   157 AQRfpklKIVLEHITTADAVEYVKSCNEN---VAATITPHHLLLTRDDL--LGGGLNPHlycKPVAKRPEDREAL-RKAA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1616 VIDC----FASDHAPHTLEEKcgsRPPPGFPGLET---MLPLLLTAVSEGRlSLDDLLQRLHHNPRRIFHLPPQEDTYVE 1688
Cdd:cd01294   231 TSGHpkffLGSDSAPHPKSNK---ESSCGCAGIFSapiALPYLAEVFEEHN-ALDKLEAFASDNGPNFYGLPPNKKTITL 306

                         330       340
                  ....*....|....*....|....*..
gi 807045910 1689 VdlEHEWTIPSHMPFSKAHWTPFEGQK 1715
Cdd:cd01294   307 V--KEPWKVPEKIPFGNNGVVPFRAGE 331
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 178-338 1.68e-12

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 68.11  E-value: 1.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   178 ILALDCGLKYNQI--RCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGdpasypsvvSTLSRVLSEPNPR------ 246
Cdd:TIGR00888    1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTTPLEeirEKNPKGIILSGGPS---------SVYAENAPRADEKifelgv 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   247 PVFGICLGHQLLALAIG---AKTYKMRYGN---RGHNQPCLLVGSGRCFLTSQNHGFAVEtdSLPADWAPLFTNANdGSN 320
Cdd:TIGR00888   72 PVLGICYGMQLMAKQLGgevGRAEKREYGKaelEILDEDDLFRGLPDESTVWMSHGDKVK--ELPEGFKVLATSDN-CPV 148

                          170
                   ....*....|....*...
gi 807045910   321 EGIVHNSLPFFSVQFHPE 338
Cdd:TIGR00888  149 AAMAHEEKPIYGVQFHPE 166
PRK13566 PRK13566
anthranilate synthase component I;
172-338 2.72e-12

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 72.26  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  172 TGGAPRILALDCGLKY-----NQIRclcQRGAEVTVVPWDHA---LDSQEYEGLFLSNGPGDPASY--PSVVST-LSRVL 240
Cdd:PRK13566  523 VGEGKRVLLVDHEDSFvhtlaNYFR---QTGAEVTTVRYGFAeemLDRVNPDLVVLSPGPGRPSDFdcKATIDAaLARNL 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  241 sepnprPVFGICLGHQLLALAIGAKTYKMRYGNRG------HNQPC-LLVGSGRCFLTSQNHGFAVETDSLPADwaplFT 313
Cdd:PRK13566  600 ------PIFGVCLGLQAIVEAFGGELGQLAYPMHGkpsrirVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDE----LL 669

                         170       180
                  ....*....|....*....|....*...
gi 807045910  314 N---ANDGSNEGIVHNSLPFFSVQFHPE 338
Cdd:PRK13566  670 VtaeTEDGVIMAIEHKTLPVAAVQFHPE 697
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 996-1156 7.26e-12

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: 65.74  E-value: 7.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   996 GISQPQWRELSDLESARQFCQTVGYPCVV---RPSYvlSGAAMNVAYTDGDLERFLSSAAAVskehPVVISKFIQEAKEI 1072
Cdd:pfam02222    4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEELGDG----PVIVEEFVPFDREL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1073 DVDAVAS-DGVVAAIAISEHVEnagvHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVI 1150
Cdd:pfam02222   78 SVLVVRSvDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELfVTEDGDLLIN 153


                   ....*.
gi 807045910  1151 ECNVRV 1156
Cdd:pfam02222  154 ELAPRP 159
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 460-651 1.73e-11

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: 66.82  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  460 VTQVIRNERPDGVLltfggqtALNCGVELTKAGVLARYGVRvlGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLE 539
Cdd:COG0439     9 AAELARETGIDAVL-------SESEFAVETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  540 QAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVA------PAFAHTSQVLVDKSLKGwKEIEYEV--------- 604
Cdd:COG0439    80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAearaeaKAGSPNGEVLVEEFLEG-REYSVEGlvrdgevvv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  605 -----------------------------------VRDA-----YGNCVTY-----------YIIEVNARLS--RSSALA 631
Cdd:COG0439   159 csitrkhqkppyfvelgheapsplpeelraeigelVARAlralgYRRGAFHteflltpdgepYLIEINARLGgeHIPPLT 238

                         250       260
                  ....*....|....*....|
gi 807045910  632 SKATGYPLAYVAAKLALGIP 651
Cdd:COG0439   239 ELATGVDLVREQIRLALGEP 258
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 190-340 3.33e-11

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 64.19  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  190 IRCLCQRGAEVTVVPW---DHALDSQEYEGLFLSNGPGDP--ASYPSVVST---LSRVLSEPnpRPVFGICLGHQLLALA 261
Cdd:cd01741    20 LREAGAETIEIDVVDVyagELLPDLDDYDGLVILGGPMSVdeDDYPWLKKLkelIRQALAAG--KPVLGICLGHQLLARA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  262 IGAKTYKMRYG----------NRGHNQPCLLVGSGRCFLTSQNHGFAVEtdSLPADWAPLFTNAnDGSNEGIVHNSLpFF 331
Cdd:cd01741    98 LGGKVGRNPKGweigwfpvtlTEAGKADPLFAGLPDEFPVFHWHGDTVV--ELPPGAVLLASSE-ACPNQAFRYGDR-AL 173


                  ....*....
gi 807045910  332 SVQFHPEHQ 340
Cdd:cd01741   174 GLQFHPEER 182
PRK06895 PRK06895
anthranilate synthase component II;
209-338 4.22e-11

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 63.99  E-value: 4.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  209 LDSQE-YEGLFLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGR 287
Cdd:PRK06895   38 LDEVEnFSHILISPGPDVPRAYPQLFAMLERYHQH---KSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSP 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807045910  288 CF--LTSQ-----NHGFAVETDSLPAdwaPLFTNANdgSNEGIV----HNSLPFFSVQFHPE 338
Cdd:PRK06895  115 LFdgLPEEfniglYHSWAVSEENFPT---PLEITAV--CDENVVmamqHKTLPIYGVQFHPE 171
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
187-338 5.20e-11

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 64.13  E-value: 5.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  187 YNQIRCLCQRGAEVTVVPWDHaLDSQEYEGL-----FLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALA 261
Cdd:PRK08857   13 YNLYQYFCELGAQVKVVRNDE-IDIDGIEALnpthlVISPGPCTPNEAGISLQAIEHFAGK---LPILGVCLGHQAIAQV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  262 IGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWA-PLFTNANDGSNE---GIVHNSLPFF 331
Cdd:PRK08857   89 FGGQVVRARQVMHGktspirHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFElTAWTELEDGSMDeimGFQHKTLPIE 168


                  ....*..
gi 807045910  332 SVQFHPE 338
Cdd:PRK08857  169 AVQFHPE 175
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 178-338 6.85e-11

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 63.32  E-value: 6.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  178 ILALDCGLKYNQ-----IRCLcqrGAEVTVVPWDHALDS---QEYEGLFLSNGPgdpasypsvvstlSRVLSEPNPR--- 246
Cdd:cd01742     1 ILILDFGSQYTHliarrVREL---GVYSEILPNTTPLEEiklKNPKGIILSGGP-------------SSVYEEDAPRvdp 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  247 -------PVFGICLGHQLLALAIGAKTYKMRYGNRGHNQpCLLVGSGRCF--LTSQ-----NHGFAVETdsLPADWAPLF 312
Cdd:cd01742    65 eifelgvPVLGICYGMQLIAKALGGKVERGDKREYGKAE-IEIDDSSPLFegLPDEqtvwmSHGDEVVK--LPEGFKVIA 141

                         170       180
                  ....*....|....*....|....*.
gi 807045910  313 TNANDGsNEGIVHNSLPFFSVQFHPE 338
Cdd:cd01742   142 SSDNCP-VAAIANEEKKIYGVQFHPE 166
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 924-1174 1.35e-10

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: 64.58  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  924 DRLYFDEISFEVVMDIYELENPEGVILsmgGQLPNNMAMA----LHRQQCRVLGtSPEAIDSAENRFKFSRLLDTIGISQ 999
Cdd:COG0189    36 DDLTLDLGRAPELYRGEDLSEFDAVLP---RIDPPFYGLAllrqLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1000 PQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEhPVVISKFIQEAKEIDVDAVAS 1079
Cdd:COG0189   112 PPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSE-PVLVQEFIPEEDGRDIRVLVV 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1080 DG-VVAAIA-ISEHVENAG-VHSGDATLvtpPQDITAKTLERIKAIVHAVGqeLQVTGpfnLQLIAKDDQLKVIECNVRV 1156
Cdd:COG0189   191 GGePVAAIRrIPAEGEFRTnLARGGRAE---PVELTDEERELALRAAPALG--LDFAG---VDLIEDDDGPLVLEVNVTP 262

                         250
                  ....*....|....*...
gi 807045910 1157 srSFPFVSKTLGVDLVAL 1174
Cdd:COG0189   263 --GFRGLERATGVDIAEA 278
PRK08417 PRK08417
metal-dependent hydrolase;
1401-1731 9.25e-10

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 63.18  E-value: 9.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1401 LPGLIDVHVHLREPGGTHKeDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQK---------------LAEAGAR 1465
Cdd:PRK08417   29 LPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDNEIALELINSaqrelpmqifpsiraLDEDGKL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1466 CDFALFL--GA------SSENAGTLGTVAGSAAGLK--LYLNETFSELRlDSVVqwMEHFETWPS-HLP-IVAHAEQQTV 1533
Cdd:PRK08417  108 SNIATLLkkGAkalelsSDLDANLLKVIAQYAKMLDvpIFCRCEDSSFD-DSGV--MNDGELSFElGLPgIPSIAETKEV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1534 AAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSRQDVEALWEN 1613
Cdd:PRK08417  185 AKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNT-AAKLNPPLRSKEDRLALLEA 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1614 M--AVIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDT--- 1685
Cdd:PRK08417  264 LkeGKIDFLTSLHSAKSNSKKDLAfdEAAFGIDSICEYFSLCYTyLVKEGIITWSELSRFTSYNPAQFLGLNSGEIEvgk 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 807045910 1686 ---YVEVDLEHEWTIPSHMPfskahwtPFEGQKVKGTVRRVVLRGEVAY 1731
Cdd:PRK08417  344 eadLVLFDPNESTIIDDNFS-------LYSGDELYGKIEAVIIKGKLYL 385
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
247-338 1.50e-09

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 62.81  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  247 PVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSG------RCFLTSQNHGFAVETDSLPADWAPLfTNANDGSN 320
Cdd:PRK14607   75 PILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGlfrgipNPTVATRYHSLVVEEASLPECLEVT-AKSDDGEI 153

                          90
                  ....*....|....*...
gi 807045910  321 EGIVHNSLPFFSVQFHPE 338
Cdd:PRK14607  154 MGIRHKEHPIFGVQFHPE 171
MGS_CPS_II cd01424
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ...
 1251-1364 2.95e-09

Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.


Pssm-ID: 238712 [Multi-domain]  Cd Length: 110  Bit Score: 56.33  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1251 NILLTIgSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVI 1330
Cdd:cd01424     2 TVFISV-ADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEG--------RPNIVDLIKNGEIQLVI 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 807045910 1331 NlsmrGAGGRRlssFVTKGYRTRRLAADFSVPLI 1364
Cdd:cd01424    73 N----TPSGKR---AIRDGFSIRRAALEYKVPYF 99
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 395-654 7.02e-09

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 59.90  E-value: 7.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  395 KVLILGSGGlsigqagefdysGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLP-IT-PHYVTQVI---RNERP 469
Cdd:PRK12767    3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkVTdPNYIDRLLdicKKEKI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  470 DGVLLTFGgqtalncgVELtkaGVLARY-------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQ 542
Cdd:PRK12767   71 DLLIPLID--------PEL---PLLAQNrdrfeeiGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFK 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  543 AA--AERLGYPVLVRAAFALGGLGSGFASNREELSalvaPAFAHTSQVLVDKSLKGwKEIEYEVVRDAYGNCV------- 613
Cdd:PRK12767  140 AAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVIsivprkr 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  614 ---------------------------------------------TYYIIEVNARLSrssalaskaTGYPLAYVA----- 643
Cdd:PRK12767  215 ievragetskgvtvkdpelfklaerlaealgargplniqcfvtdgEPYLFEINPRFG---------GGYPLSYMAganep 285

                         330
                  ....*....|....*
gi 807045910  644 ----AKLALGIPLPE 654
Cdd:PRK12767  286 dwiiRNLLGGENEPI 300
PLN02942 PLN02942
dihydropyrimidinase
 1383-1750 7.10e-09

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 60.63  E-value: 7.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1383 APPLKVHVDCMT---SQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGITMvcampntrppIID-------- 1449
Cdd:PLN02942   36 APNLKVPDDVRVidaTGKFV-MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTM----------HIDfvipvngn 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1450 -APALALAQKLAEAGArCDFALFLGAS------SENAGTLGTVAGSAAgLKLYLNETFSELRLDSVVqwMEHFETWPS-- 1520
Cdd:PLN02942  105 lLAGYEAYEKKAEKSC-MDYGFHMAITkwddtvSRDMETLVKEKGINS-FKFFMAYKGSLMVTDELL--LEGFKRCKSlg 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1521 HLPIVaHAEQ--------------------------------QTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARG 1568
Cdd:PLN02942  181 ALAMV-HAENgdavfegqkrmielgitgpeghalsrppllegEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSG 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1569 LPVTCEVAPHHLFLshDDLERLGP-----GKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP---- 1637
Cdd:PLN02942  260 QRVIGEPVVSGLVL--DDSKLWDPdftiaSKYVMSPPIRPAGHGKALQAALSsgILQLVGTDHCPFNSTQKAFGKDdfrk 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1638 -PPGFPGLETMLPLLL-TAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVE--------VDLEHEWTIPSHMPFSKAH 1707
Cdd:PLN02942  338 iPNGVNGIEERMHLVWdTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAgsdadiiiLNPNSTFTISAKTHHSRID 417

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 807045910 1708 WTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWP 1750
Cdd:PLN02942  418 TNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPP 460
PRK07200 PRK07200
aspartate/ornithine carbamoyltransferase family protein; Validated
 1870-2080 8.15e-09

aspartate/ornithine carbamoyltransferase family protein; Validated


Pssm-ID: 235961 [Multi-domain]  Cd Length: 395  Bit Score: 60.14  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1870 TKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQ 1949
Cdd:PRK07200   30 TPDELKAVLDVADALRALREENISTKVFNSGLGISVFRDNSTRTRFSYASACNLLGLEVQDLDEGKSQIAHGETVRETAN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1950 TMSCYADVVVLR------------HPQPGAVELAAKHC---RRP-VINAGDGVgEHPTQALLDIFTIREELGTVN---GM 2010
Cdd:PRK07200  110 MISFMADVIGIRddmyigkgnaymREVGAAVDDGYKQGvlpQRPtLVNLQCDI-DHPTQSMADLLHLIEHFGGLEnlkGK 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807045910 2011 TITMVGDL--KHGRTV---HSLACLLTQYRVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLY 2080
Cdd:PRK07200  189 KIAMTWAYspSYGKPLsvpQGIIGLMTRFGMDVTLAHPEGYDLMPEVvevaKKNAKASGGSFRQVNSMEEAFKDADIVY 267
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
187-362 1.29e-08

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 57.12  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  187 YNQIRCLCQRGAEVtVVPWDHALDSQEYEGL---FLSNGPGdPASYPSVVSTLSRVLSEPNPRPVFGICLGHQLLALAIG 263
Cdd:PRK07649   13 FNLVQFLGELGQEL-VVKRNDEVTISDIENMkpdFLMISPG-PCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  264 A---KTYKMRYGNRG---HNQPCLLVGSGRCFLTSQNHGFAVETDSLPaDWAPLFTNANDGSNEGIVHNSLPFFSVQFHP 337
Cdd:PRK07649   91 GevvRAERLMHGKTSlmhHDGKTIFSDIPNPFTATRYHSLIVKKETLP-DCLEVTSWTEEGEIMAIRHKTLPIEGVQFHP 169

                         170       180
                  ....*....|....*....|....*
gi 807045910  338 EHQAGPSDMELLFDiFLETVKEATA 362
Cdd:PRK07649  170 ESIMTSHGKELLQN-FIRKYSPSVT 193
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 498-613 1.87e-08

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 59.27  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  498 GVRVLGTPVETIELTEDRraFAAR--MAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREE 573
Cdd:PRK06111   99 GIVFIGPSADIIAKMGSK--IEARraMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQE 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 807045910  574 LSAlvapAFAHTSQ----------VLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK06111  177 LTK----AFESNKKraanffgngeMYIEKYIEDPRHIEIQLLADTHGNTV 222
PRK00758 PRK00758
GMP synthase subunit A; Validated
 247-338 2.02e-08

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 56.01  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  247 PVFGICLGHQLLALAIGAKTYKMRYGNRG--------HNQPclLVGSGRCFLTSQNHgfAVETDSLPADWAPLFTNANDG 318
Cdd:PRK00758   69 PILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDDI--LKGLPPEIRVWASH--ADEVKELPDGFEILARSDICE 144

                          90       100
                  ....*....|....*....|
gi 807045910  319 sNEGIVHNSLPFFSVQFHPE 338
Cdd:PRK00758  145 -VEAMKHKEKPIYGVQFHPE 163
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
498-613 2.56e-08

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 58.84  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL- 574
Cdd:PRK08654   99 GIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELe 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 807045910  575 ------SALVAPAFAhTSQVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK08654  179 daiestQSIAQSAFG-DSTVFIEKYLEKPRHIEIQILADKHGNVI 222
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
491-616 3.90e-08

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 58.19  E-value: 3.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  491 AGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLGSGFA 568
Cdd:PRK07178   91 AEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNlaDLDEALAEAERIGYPVMLKATSGGGGRGIRRC 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 807045910  569 SNREELS-------ALVAPAFAhTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTYY 616
Cdd:PRK07178  171 NSREELEqnfprviSEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLF 224
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1401-1729 1.01e-07

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 56.36  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1401 LPGLIDVHVHLR--------EPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDApalalaqkLAEAGARCDFALFL 1472
Cdd:pfam01979    3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA--------LLEAAEELPLGLRF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1473 GASSENAGTLGTVAGSAA-GLKLYLNETFSELRLDSVVQ-WMEHFETWpshlpivaHAEQQTVAAVLMVAQLTQRSVHIc 1550
Cdd:pfam01979   75 LGPGCSLDTDGELEGRKAlREKLKAGAEFIKGMADGVVFvGLAPHGAP--------TFSDDELKAALEEAKKYGLPVAI- 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1551 HVAR-KEEILLIKAAKARG---------------LPVTCEVAPHHLFLSHDDLERLGPGKGEVR------PELGSRQDVE 1608
Cdd:pfam01979  146 HALEtKGEVEDAIAAFGGGiehgthlevaesgglLDIIKLILAHGVHLSPTEANLLAEHLKGAGvahcpfSNSKLRSGRI 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1609 ALWE--NMAVIDCFASDHAPHTleekcgsRPPPGFPGLETMlpLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTy 1686
Cdd:pfam01979  226 ALRKalEDGVKVGLGTDGAGSG-------NSLNMLEELRLA--LELQFDPEGGLSPLEALRMATINPAKALGLDDKVGS- 295

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 807045910  1687 VEV----DLehewtipshMPFSKAHWTPFEGQKVKGTVRRVVLRGEV 1729
Cdd:pfam01979  296 IEVgkdaDL---------VVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
trpG CHL00101
anthranilate synthase component 2
 187-338 1.23e-07

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 53.97  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  187 YNQIRCLCQRGAEVTVVPWDH----ALDSQEYEGLFLSNGPGDPASypsvvSTLSR-VLSEPNPR-PVFGICLGHQLLAL 260
Cdd:CHL00101   13 YNLVQSLGELNSDVLVCRNDEidlsKIKNLNIRHIIISPGPGHPRD-----SGISLdVISSYAPYiPILGVCLGHQSIGY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  261 AIGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPadwAPLFTNA--NDGSNEGIVHNSLPF-F 331
Cdd:CHL00101   88 LFGGKIIKAPKPMHGktskiyHNHDDLFQGLPNPFTATRYHSLIIDPLNLP---SPLEITAwtEDGLIMACRHKKYKMlR 164


                  ....*..
gi 807045910  332 SVQFHPE 338
Cdd:CHL00101  165 GIQFHPE 171
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
391-661 1.77e-07

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 55.70  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  391 PPPRKVLILGS--GGLSIgqagefdysgsqaIKALKEENIQTLLInpniATVQTSQGL----ADKVYFLPITPH------ 458
Cdd:COG3919     3 TMRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVV----DRDPLGPAArsryVDEVVVVPDPGDdpeafv 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  459 -YVTQVIRNERPDgVLLTFGGQTALncgveltkagVLARY------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP 531
Cdd:COG3919    66 dALLELAERHGPD-VLIPTGDEYVE----------LLSRHrdeleeHYRLPYPDADLLDRLLDKERFYELAEELGVPVPK 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  532 SEAANSLEQAQAAAERLGYPVLVRAA--------FALGGLGSGFASNREELSALVAPAFA------------------HT 585
Cdd:COG3919   135 TVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAagyelivqeyipgddgemRG 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  586 SQVLVDKS-----------LKGW--------------------------KEIEY------EVVRDAYGNcvTYYIIEVNA 622
Cdd:COG3919   215 LTAYVDRDgevvatftgrkLRHYppaggnsaaresvddpeleeaarrllEALGYhgfanvEFKRDPRDG--EYKLIEINP 292

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 807045910  623 RLSRSSALASKAtGYPLAYVAAKLALGIPLPELRNSVTG 661
Cdd:COG3919   293 RFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREG 330
PLN02335 PLN02335
anthranilate synthase
 216-338 2.76e-07

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 53.65  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  216 GLFLSNGPGDPASypSVVStLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYG-NRGHNQPC---------LLVGS 285
Cdd:PLN02335   65 GVLISPGPGTPQD--SGIS-LQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVhydekgeegLFSGL 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 807045910  286 GRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFS-VQFHPE 338
Cdd:PLN02335  142 PNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 190-263 4.47e-07

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 50.29  E-value: 4.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  190 IRCLCQRGAEVTVVPWDH-----ALDSQEYEGLFLSNGPGDP---ASYPSVVSTLSRVLSepNPRPVFGICLGHQLLALA 261
Cdd:cd01653    18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlARDEALLALLREAAA--AGKPILGICLGAQLLVLG 95


                  ..
gi 807045910  262 IG 263
Cdd:cd01653    96 VQ 97
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 247-353 7.60e-07

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 51.81  E-value: 7.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  247 PVFGICLGHQLLALAIGAKTYkmrygnrghnqPCLLVGSgrcfltsqNHGFAVetDSLPADWAPLFTnANDGSNEGIVHN 326
Cdd:cd01745   102 PILGICRGMQLLNVALGGTLY-----------QDIRVNS--------LHHQAI--KRLADGLRVEAR-APDGVIEAIESP 159

                          90       100
                  ....*....|....*....|....*....
gi 807045910  327 SLPF-FSVQFHPE-HQAGPSDMELLFDIF 353
Cdd:cd01745   160 DRPFvLGVQWHPEwLADTDPDSLKLFEAF 188
PRK06849 PRK06849
hypothetical protein; Provisional
 969-1156 2.53e-06

hypothetical protein; Provisional


Pssm-ID: 235876 [Multi-domain]  Cd Length: 389  Bit Score: 51.97  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  969 CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQF-CQTVGYPCVVRPSYVLSGAAMNVAYTdgdlERF 1047
Cdd:PRK06849  101 CEVLHFDFELLLLLHNKWEFAEQARSLGLSVPKTYLITDPEAIRNFmFKTPHTPYVLKPIYSRFVRRVDLLPK----EAA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1048 LSSaAAVSKEHPVVISKFIQeAKEIDVDAVASDGVVAAIA--ISEHVENAGVHSGDATLVTPpqditaktleRIKAIVHA 1125
Cdd:PRK06849  177 LKE-LPISKDNPWVMQEFIQ-GKEYCSYSIVRSGELRAHScyKPEYCAGSGAQIAFQPINHP----------RIEEFVTH 244

                         170       180       190
                  ....*....|....*....|....*....|..
gi 807045910 1126 VGQELQVTGPFNLQLI-AKDDQLKVIECNVRV 1156
Cdd:PRK06849  245 FVKELNYTGQISFDFIeTENGDAYPIECNPRT 276
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 190-258 3.39e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 47.20  E-value: 3.39e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807045910  190 IRCLCQRGAEVTVVPWDH-----ALDSQEYEGLFLSNGPGDP---ASYPSVVSTLSRVLSepNPRPVFGICLGHQLL 258
Cdd:cd03128    18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlAWDEALLALLREAAA--AGKPVLGICLGAQLL 92
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
493-613 4.15e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 51.67  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  493 VLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASN 570
Cdd:PRK08462   96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGAlKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 807045910  571 REEL--SALVAPAFAHTS----QVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK08462  176 ESDLenLYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVI 224
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
187-338 1.31e-05

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 47.99  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  187 YNQIRCLCQRGAEVTVVPWDH----ALDSQEYEGLFLSNGPGDPASypSVVStLSRVLSEPNPRPVFGICLGHQLLALAI 262
Cdd:PRK08007   13 WNLYQYFCELGADVLVKRNDAltlaDIDALKPQKIVISPGPCTPDE--AGIS-LDVIRHYAGRLPILGVCLGHQAMAQAF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  263 GA---KTYKMRYGNRG---HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAplfTNANDGSNE--GIVHNSLPFFSVQ 334
Cdd:PRK08007   90 GGkvvRAAKVMHGKTSpitHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQ 166


                  ....
gi 807045910  335 FHPE 338
Cdd:PRK08007  167 FHPE 170
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 247-338 1.34e-05

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 48.41  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   247 PVFGICLGHQLLALAIGAKTY---KMRYGNRGHNQPC----------LLVGSGRCF--LTSQN-------HGFAVetDSL 304
Cdd:pfam07722  107 PILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAI--DRL 184

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 807045910   305 PADWAPLFTnANDGSNEGIVHNSLPFF--SVQFHPE 338
Cdd:pfam07722  185 APGLRVEAV-APDGTIEAIESPNAKGFalGVQWHPE 219
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 498-613 1.97e-05

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 50.14  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  498 GVRVLGTPVETIELTEDRraFAARMA--EIGEHVAPS--EAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREE 573
Cdd:PRK12999  103 GITFIGPTAEVLRLLGDK--VAARNAaiKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEE 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 807045910  574 LSALVAPA-------FAhTSQVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK12999  181 LEEAFERAkreakaaFG-NDEVYLEKYVENPRHIEVQILGDKHGNVV 226
guaA PRK00074
GMP synthase; Reviewed
 177-338 2.88e-05

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 48.89  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  177 RILALDCGLKYNQ-----IRCL---CQrgaevtVVPWDHALDS-QEYE--GLFLSNGPgdpASypsvvstlsrVLSEPNP 245
Cdd:PRK00074    5 KILILDFGSQYTQliarrVRELgvySE------IVPYDISAEEiRAFNpkGIILSGGP---AS----------VYEEGAP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  246 R----------PVFGICLGHQLLALAIGAK---TYKMRYGN---RGHNQPCLLVGSGRCFLTSQNHGFAVETdsLPADWA 309
Cdd:PRK00074   66 RadpeifelgvPVLGICYGMQLMAHQLGGKverAGKREYGRaelEVDNDSPLFKGLPEEQDVWMSHGDKVTE--LPEGFK 143

                         170       180
                  ....*....|....*....|....*....
gi 807045910  310 PLFTNANdGSNEGIVHNSLPFFSVQFHPE 338
Cdd:PRK00074  144 VIASTEN-CPIAAIANEERKFYGVQFHPE 171
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 247-341 3.41e-05

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 47.70  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  247 PVFGICLGHQLLAL----------AIGAKTYKMRYGNRGHNQPCLLVGS----------GRCFlTSQNHGFAVETDSLP- 305
Cdd:cd01747    94 PVWGTCLGFELLTYltsgetllleATEATNSALPLNFTEDALQSRLFKRfppdllkslaTEPL-TMNNHRYGISPENFTe 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 807045910  306 ----ADWAP-LFTNANDGSNEGIV---HNSLPFFSVQFHPEHQA 341
Cdd:cd01747   173 ngllSDFFNvLTTNDDWNGVEFIStveAYKYPIYGVQWHPEKNA 216
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 990-1122 4.40e-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: 47.79  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  990 RLLDTIGISQPQWRELS--DLESARQFCQTVGYPCVVRPsyVLSGAA--MNVAYTDGDLERFLSSAAAVSkeHPVVISKF 1065
Cdd:COG1181   101 RVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKP--AREGSSvgVSKVKNAEELAAALEEAFKYD--DKVLVEEF 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807045910 1066 IqEAKEIDVdAVASDGVVAAIAISEHVENAGV-------HSGDATLVTPPqDITAKTLERIKAI 1122
Cdd:COG1181   177 I-DGREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLPEELEERIQEL 237
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 991-1179 7.78e-05

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: 45.77  E-value: 7.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   991 LLDTIGISQPQW-------RELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLssAAAVSKEHPVVIS 1063
Cdd:pfam07478    1 LLKAAGLPVVPFvtftradWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAI--EEAFQYDEKVLVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1064 KFIqEAKEIDVdAVASDGVVAAIAISEHVENAGV------HSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTG--- 1134
Cdd:pfam07478   79 EGI-EGREIEC-AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGlar 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 807045910  1135 -PFNLQliaKDDQLKVIECN-----VRVSRsFPFVSKTLGVDLVALATRVI 1179
Cdd:pfam07478  157 vDFFLT---EDGEIVLNEVNtipgfTSISM-FPKLAAAAGVSFPDLVDQLI 203
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1750-1869 8.75e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.84  E-value: 8.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  1750 PQGAVPQLPPSAPATSEMTTTPerPRRGIPGLPDGRFhlPPRIHRASDPGLPAEEPKEKSSRKVAEPELMGTPDG--TCY 1827
Cdd:pfam03154  177 QSGAASPPSPPPPGTTQAATAG--PTPSAPSVPPQGS--PATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPplQPM 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 807045910  1828 PPPPVPRQASPQNLGTPgLLHPQTSPLLHSLVG-----QHILSVQQF 1869
Cdd:pfam03154  253 TQPPPPSQVSPQPLPQP-SLHGQMPPMPHSLQTgpshmQHPVPPQPF 298
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
502-613 8.98e-05

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 47.40  E-value: 8.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  502 LGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL----- 574
Cdd:PRK05586  103 IGPDSETIELMGNKSNAREIMIKAGVPVVPgSEGEiENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELikafn 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 807045910  575 --SALVAPAFAHTSqVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK05586  183 taKSEAKAAFGDDS-MYIEKFIENPKHIEFQILGDNYGNVV 222
ddl PRK01966
D-alanine--D-alanine ligase;
522-601 1.20e-04

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 46.65  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  522 MAEIGEHVAPSEAANSLEQA----QAAAERLGYPVLVRAAfalgGLGSGF----ASNREELSALVAPAFAHTSQVLVDKS 593
Cdd:PRK01966  131 LAAAGIPVAPYVVLTRGDWEeaslAEIEAKLGLPVFVKPA----NLGSSVgiskVKNEEELAAALDLAFEYDRKVLVEQG 206


                  ....*...
gi 807045910  594 LKGwKEIE 601
Cdd:PRK01966  207 IKG-REIE 213
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 498-576 2.10e-04

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 46.29  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  498 GVRVLGTPVETIELTEDRrAFAARMA-EIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL 574
Cdd:PRK12833  102 GLIFVGPDAQTIRTMGDK-ARARRTArRAGVPTVPGSDGvvASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQL 180


                  ..
gi 807045910  575 SA 576
Cdd:PRK12833  181 AA 182
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 395-601 2.22e-04

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: 45.48  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  395 KVLILgSGGLSigqaGEFD---YSGSQAIKALKEENIQtllinpniatvqtsqgladkVYFLPITPHYVTQVIRNERPDG 471
Cdd:COG1181     2 RVAVL-FGGRS----AEREvslKSGRAVAAALDKAGYD--------------------VVPIGIDVEDLPAALKELKPDV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  472 VLLtfggqtALNC--GVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANS--LEQAQAAAER 547
Cdd:COG1181    57 VFP------ALHGrgGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRgeLADLEAIEEE 130

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 807045910  548 LGYPVLVRAAFAlgglGSGF----ASNREELSALVAPAFAHTSQVLVDKSLKGwKEIE 601
Cdd:COG1181   131 LGLPLFVKPARE----GSSVgvskVKNAEELAAALEEAFKYDDKVLVEEFIDG-REVT 183
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 536-601 2.89e-04

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: 44.23  E-value: 2.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910   536 NSLEQAQAAAERLGYPVLVRAAfalgGLGSGF----ASNREELSALVAPAFAHTSQVLVDKSLKGwKEIE 601
Cdd:pfam07478   23 NPKEWCAQVEEALGYPVFVKPA----RLGSSVgvskVESREELQAAIEEAFQYDEKVLVEEGIEG-REIE 87
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 498-613 2.96e-04

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 45.57  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL 574
Cdd:PRK08463   98 GIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPgTEKLNseSMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDL 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 807045910  575 SALV------APAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK08463  178 ENAFesckreALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNII 222
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
 1016-1080 4.73e-04

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 44.82  E-value: 4.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807045910 1016 QTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVskEHPVVISKFIqEAKEIDVDAVASD 1080
Cdd:PRK14570  168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFI-EAREIECSVIGNE 229
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
972-1078 5.49e-04

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 44.97  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  972 LGTSPEAIDSAENRFKFSRLLDTIGISQPQWRE--LSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLS 1049
Cdd:PRK08654  103 IGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEegIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182

                          90       100       110
                  ....*....|....*....|....*....|...
gi 807045910 1050 S----AAAVSKEHPVVISKFIQEAKEIDVDAVA 1078
Cdd:PRK08654  183 StqsiAQSAFGDSTVFIEKYLEKPRHIEIQILA 215
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 529-596 7.71e-04

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 43.95  E-value: 7.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  529 VAPSEAANSLEQAQAAAERLGYPVLVRAafALGG--LGSGFASNREELSALVAPAFAHTSQVLVDKSLKG 596
Cdd:PRK01372  113 TPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGssVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKG 180
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 973-1212 1.29e-03

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 44.07  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  973 GTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPsyVLSGAAMNVAYTDGDLERFLSSAA 1052
Cdd:PRK02186   96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKP--RMGSGSVGVRLCASVAEAAAHCAA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1053 AVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISE-------HVENAGvHSGDATLVTPPQDITAKTLERikaIVHA 1125
Cdd:PRK02186  174 LRRAGTRAALVQAYVEGDEYSVETLTVARGHQVLGITRkhlgpppHFVEIG-HDFPAPLSAPQRERIVRTVLR---ALDA 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1126 VGQELqvtGPFNLQLIAKDDQLKVIECNVRVSRSF-P-FVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQF 1203
Cdd:PRK02186  250 VGYAF---GPAHTELRVRGDTVVIIEINPRLAGGMiPvLLEEAFGVDLLDHVIDLHLGVAAFADPTAKRYGAIRFVLPAR 326


                  ....*....
gi 807045910 1204 SfSRLAGAD 1212
Cdd:PRK02186  327 S-GVLRGLL 334
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 975-1149 1.39e-03

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 43.22  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  975 SPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVV---RPSY------VLSGAAmnvaytdgDLE 1045
Cdd:PRK06019   91 GPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLktrRGGYdgkgqwVIRSAE--------DLE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1046 RFLSSAAAVskehPVVISKFIQEAKEIDVDAVAS-DGVVAAIAIsehVENagVHSG---DATLVtpPQDITAKTLERIKA 1121
Cdd:PRK06019  163 AAWALLGSV----PCILEEFVPFEREVSVIVARGrDGEVVFYPL---VEN--VHRNgilRTSIA--PARISAELQAQAEE 231

                         170       180
                  ....*....|....*....|....*....
gi 807045910 1122 IVHAVGQELQVTGPFNLQL-IAKDDQLKV 1149
Cdd:PRK06019  232 IASRIAEELDYVGVLAVEFfVTGDGELLV 260
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 507-613 1.62e-03

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 43.25  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  507 ETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELsalvAPAFAH 584
Cdd:PRK08591  108 ETIRLMGDKVTAKATMKKAGVPVVPgSDGPvDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAEL----EKAFSM 183

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 807045910  585 TSQ----------VLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK08591  184 ARAeakaafgnpgVYMEKYLENPRHIEIQVLADGHGNAI 222
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 507-647 1.64e-03

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: 43.14  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFalGGL-GSG--FASNREELSALVApAFA 583
Cdd:COG0026    82 EALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRR--GGYdGKGqvVIKSAADLEAAWA-ALG 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  584 HTSQVL---VDkslkgwkeIEYE----VVRDAYGNCVTYYIIE------------VNARLsrSSALASKATGYplayvAA 644
Cdd:COG0026   159 GGPCILeefVP--------FERElsviVARSPDGEVATYPVVEnvhrngildesiAPARI--SEALAAEAEEI-----AK 223


                  ...
gi 807045910  645 KLA 647
Cdd:COG0026   224 RIA 226
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 507-615 1.94e-03

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 42.83  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910  507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFaLG--GLGSGFASNREELSALVApAFAH 584
Cdd:PRK06019   93 DALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRR-GGydGKGQWVIRSAEDLEAAWA-LLGS 170

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 807045910  585 TSQVlvdksLKGWKEIEYE----VVRDAYGNCVTY 615
Cdd:PRK06019  171 VPCI-----LEEFVPFEREvsviVARGRDGEVVFY 200
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
1005-1186 5.04e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 41.65  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1005 LSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLER-FL---SSAAAVSKEHPVVISKFIQEAKEIDVDAVAsD 1080
Cdd:PRK08462  140 LKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENlYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILG-D 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1081 GVVAAIAISEhvENAGVHSGDATLV--TPPQDITAKTLER-----IKAiVHAVGQELQVTGPFnlqLIAKDDQLKVIECN 1153
Cdd:PRK08462  219 KHGNVIHVGE--RDCSLQRRHQKLIeeSPAVVLDEKTRERlhetaIKA-AKAIGYEGAGTFEF---LLDSNLDFYFMEMN 292

                         170       180       190
                  ....*....|....*....|....*....|...
gi 807045910 1154 VRVSRSFPFVSKTLGVDLVALATRVIMGEEVEP 1186
Cdd:PRK08462  293 TRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1380-1568 7.59e-03

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 41.10  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1380 IGPAPPLKV-----HVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGT---------------AAALAGGITMVCA 1439
Cdd:COG1228    41 VGPAADLAVpagaeVIDA--TGKTV-LPGLIDAHTHLGLGGGRAVEFEAGGGitptvdlvnpadkrlRRALAAGVTTVRD 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045910 1440 MPNTRPPIIDAPA------LALAQKLAEAGArcdFALFLGASSENAGTLG-----TVAGSAAGLKLYLNETFSELRLDSV 1508
Cdd:COG1228   118 LPGGPLGLRDAIIagesklLPGPRVLAAGPA---LSLTGGAHARGPEEARaalreLLAEGADYIKVFAEGGAPDFSLEEL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807045910 1509 VQWMEhfETWPSHLPIVAHAEQQtvAAVLMVAQLTQRSV-HICHVArkEEIllIKAAKARG 1568
Cdd:COG1228   195 RAILE--AAHALGLPVAAHAHQA--DDIRLAVEAGVDSIeHGTYLD--DEV--ADLLAEAG 247
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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