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Conserved domains on  [gi|688603052|ref|XP_009293161|]
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multifunctional protein CAD isoform X2 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 395-1446 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: 1714.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   395 PRKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGV 474
Cdd:TIGR01369    6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   475 LLTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPV 554
Cdd:TIGR01369   86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   555 LVRSAFALGGLGSGFANNRDEMITLVTQAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGE 632
Cdd:TIGR01369  166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGD 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   633 SIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 712
Cdd:TIGR01369  246 SIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLA 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   713 LGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG 792
Cdd:TIGR01369  326 VGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATG 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   793 FDHTIKP-----ESEEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDEsaMPPEI 867
Cdd:TIGR01369  406 FDLPDREvepdeDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTD--LDPEL 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   868 MRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVF-EQPHVMVIGSG 946
Cdd:TIGR01369  484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKKVLVLGSG 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   947 VYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN 1026
Cdd:TIGR01369  564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1027 NIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVA 1106
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1107 YSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGEVIAIAVSEHVENAGVHSGDATLVTPPQDINQKTMER 1186
Cdd:TIGR01369  724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1187 IKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVG--LMRGNGIV 1264
Cdd:TIGR01369  804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1265 GVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLPTVQTLESLG 1344
Cdd:TIGR01369  884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1345 YNLYASLGTADFYTEHGVKVMAVDWPFEeesdcpnkdKQRNIMDYLEENHFDLVINLSMRNSGgrrlssFVTKGYRTRRM 1424
Cdd:TIGR01369  964 YKLYATEGTAKFLGEAGIKPELVLKVSE---------GRPNILDLIKNGEIELVINTTSKGAG------TATDGYKIRRE 1028

                         1050      1060
                   ....*....|....*....|..
gi 688603052  1425 AIDFSVPLITDIKCTKLFVQAL 1446
Cdd:TIGR01369 1029 ALDYGVPLITTLNTAEAFAEAL 1050
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1466-1812 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: 578.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1466 KLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASS 1545
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1546 DNAALLPSIASSTAGLKMYLNDTYSTLKMDNVSLWMEHFEKWPKHLPIVAHAEKQTVAAILLVAQLYQRPVHICHVAKKE 1625
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1626 EILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPvigKDKAQVRPMLGTREDMEALWENLDIIDCFATDHAPHSAEEKISEK 1705
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLP---RGQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1706 PPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKV 1785
Cdd:cd01316   238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317

                         330       340
                  ....*....|....*....|....*..
gi 688603052 1786 KGKVMRVVLRGEVAYIDGQVLVPPGYG 1812
Cdd:cd01316   318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
4-359 1.30e-166

carbamoyl-phosphate synthase small subunit;


:

Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 515.78  E-value: 1.30e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    4 KMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESS 83
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   84 QIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIP-----FDNPD 158
Cdd:PRK12564   74 RPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  159 ARNLVKEVSMKAPKVF---NPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEY 232
Cdd:PRK12564  154 GLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEeilALNPDGVFLSNGPGDPAA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  233 CKETVENIRKVacVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDW 312
Cdd:PRK12564  234 LDYAIEMIREL--LEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANL 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 688603052  313 DVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLD 359
Cdd:PRK12564  312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1938-2243 5.03e-138

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: 432.94  E-value: 5.03e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1938 HPLVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCEST 2017
Cdd:COG0540     1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2018 SSTQKGESLVDSVNTMSCY-ADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2096
Cdd:COG0540    81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2097 VGDLKHGRTVHSLARLLTQYRITLRYVAPKNLsMPAEIidfvASKGIkqEEFNSIEEALPDTDVLYMTRIQKERFS---- 2172
Cdd:COG0540   161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEI----EELGV--EVTTDLDEALPDADVVYMLRIQKERFTdglf 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052 2173 -SEKEYnacFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR 2243
Cdd:COG0540   234 pSYREY---KRSYGLTAERLALAKPDAIVMHPGPrnRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
PHA03378 super family cl33729
EBNA-3B; Provisional
 1819-1975 7.44e-05

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.14  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1819 SATPTATTEVIMDAPKRV---IEAMTPERPRQAAPVDVVRSRAPSPRRSAGDGRFILPPRIHRSSDPGLPPAEEEVSLRA 1895
Cdd:PHA03378  677 SPTGANTMLPIQWAPGTMqppPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARP 756

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1896 PFDA--ELALPAEAYAHPPPLARilsPQAG-----QPQILPHPQTSPLLHPLVGQhiLSVRQFSKEQMSHLFNVAHTLRL 1968
Cdd:PHA03378  757 PAAApgRARPPAAAPGAPTPQPP---PQAPpapqqRPRGAPTPQPPPQAGPTSMQ--LMPRAAPGQQGPTKQILRQLLTG 831


                  ....*..
gi 688603052 1969 MVQKERP 1975
Cdd:PHA03378  832 GVKRGRP 838
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 395-1446 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: 1714.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   395 PRKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGV 474
Cdd:TIGR01369    6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   475 LLTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPV 554
Cdd:TIGR01369   86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   555 LVRSAFALGGLGSGFANNRDEMITLVTQAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGE 632
Cdd:TIGR01369  166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGD 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   633 SIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 712
Cdd:TIGR01369  246 SIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLA 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   713 LGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG 792
Cdd:TIGR01369  326 VGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATG 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   793 FDHTIKP-----ESEEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDEsaMPPEI 867
Cdd:TIGR01369  406 FDLPDREvepdeDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTD--LDPEL 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   868 MRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVF-EQPHVMVIGSG 946
Cdd:TIGR01369  484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKKVLVLGSG 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   947 VYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN 1026
Cdd:TIGR01369  564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1027 NIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVA 1106
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1107 YSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGEVIAIAVSEHVENAGVHSGDATLVTPPQDINQKTMER 1186
Cdd:TIGR01369  724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1187 IKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVG--LMRGNGIV 1264
Cdd:TIGR01369  804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1265 GVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLPTVQTLESLG 1344
Cdd:TIGR01369  884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1345 YNLYASLGTADFYTEHGVKVMAVDWPFEeesdcpnkdKQRNIMDYLEENHFDLVINLSMRNSGgrrlssFVTKGYRTRRM 1424
Cdd:TIGR01369  964 YKLYATEGTAKFLGEAGIKPELVLKVSE---------GRPNILDLIKNGEIELVINTTSKGAG------TATDGYKIRRE 1028

                         1050      1060
                   ....*....|....*....|..
gi 688603052  1425 AIDFSVPLITDIKCTKLFVQAL 1446
Cdd:TIGR01369 1029 ALDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
396-1447 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1451.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  396 RKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVL 475
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  476 LTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVL 555
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  556 VRSAFALGGLGSGFANNRDEMITLVTQAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGES 633
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  634 IVVAPSQTLNDYEYNMLRNTAIKVIRHLGVV-GECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 712
Cdd:PRK05294  248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  713 LGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG 792
Cdd:PRK05294  328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  793 FDHTI-----KPESEEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDesaMPPEI 867
Cdd:PRK05294  408 LDEDLfeeesLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLP---LDAEL 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  868 MRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTY-HGSESDVVfEQPHVMVIGSG 946
Cdd:PRK05294  485 LREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYeEECESNPS-DRKKVLVLGSG 563

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  947 VYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN 1026
Cdd:PRK05294  564 PNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPL 643

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1027 NIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVA 1106
Cdd:PRK05294  644 KLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIV 723

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1107 YSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVaCDGEVIAIA-VSEHVENAGVHSGDATLVTPPQDINQKTME 1185
Cdd:PRK05294  724 YDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIE 802

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1186 RIKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVGLMRGN--GI 1263
Cdd:PRK05294  803 EIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPY 882

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1264 VGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKK-NILLSIgSYKNKSELLPTVQTLES 1342
Cdd:PRK05294  883 VAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLE 961

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1343 LGYNLYASLGTADFYTEHGVKVMAVdwpfeeesdcpNKDKQR--NIMDYLEENHFDLVINlSMRNSGGRRlssfvtKGYR 1420
Cdd:PRK05294  962 LGFKILATSGTAKFLREAGIPVELV-----------NKVHEGrpHIVDLIKNGEIDLVIN-TPTGRQAIR------DGFS 1023

                        1050      1060
                  ....*....|....*....|....*..
gi 688603052 1421 TRRMAIDFSVPLITDIKCTKLFVQALK 1447
Cdd:PRK05294 1024 IRRAALEYKVPYITTLAGARAAVKAIE 1050
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 401-945 0e+00

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: 660.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  401 LGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVLLTFGG 480
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  481 QTALNCGVELKKQGVLEKykVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVLVRSAF 560
Cdd:COG0458    81 QTALNLAVELEEAGILEG--VKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  561 ALGGLGSGFANNRDEMITLVTQAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGESIVVAP 638
Cdd:COG0458   159 VLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  639 SQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNpeSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLP 718
Cdd:COG0458   239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  719 VLKNsvtnstTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG--FDHT 796
Cdd:COG0458   317 ELGN------DTGFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  797 IKPESEEE--LQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIadhkkLLETYKQDESAMPPEIMRKAKQL 874
Cdd:COG0458   391 VADDDKEEalLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPI-----IVDEIELEEIILVINTLLGAKSL 465

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688603052  875 GFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVFEQPHVMVIGS 945
Cdd:COG0458   466 GDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1466-1812 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: 578.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1466 KLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASS 1545
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1546 DNAALLPSIASSTAGLKMYLNDTYSTLKMDNVSLWMEHFEKWPKHLPIVAHAEKQTVAAILLVAQLYQRPVHICHVAKKE 1625
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1626 EILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPvigKDKAQVRPMLGTREDMEALWENLDIIDCFATDHAPHSAEEKISEK 1705
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLP---RGQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1706 PPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKV 1785
Cdd:cd01316   238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317

                         330       340
                  ....*....|....*....|....*..
gi 688603052 1786 KGKVMRVVLRGEVAYIDGQVLVPPGYG 1812
Cdd:cd01316   318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
4-359 1.30e-166

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 515.78  E-value: 1.30e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    4 KMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESS 83
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   84 QIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIP-----FDNPD 158
Cdd:PRK12564   74 RPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  159 ARNLVKEVSMKAPKVF---NPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEY 232
Cdd:PRK12564  154 GLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEeilALNPDGVFLSNGPGDPAA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  233 CKETVENIRKVacVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDW 312
Cdd:PRK12564  234 LDYAIEMIREL--LEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANL 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 688603052  313 DVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLD 359
Cdd:PRK12564  312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 4-362 1.19e-164

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: 510.33  E-value: 1.19e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    4 KMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPkDEDgefglskwFESS 83
Cdd:COG0505     3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVN-DED--------FESD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   84 QIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIP-----FDNPD 158
Cdd:COG0505    74 RPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLekaraAPGME 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  159 ARNLVKEVSMKAPKVF--NPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEYC 233
Cdd:COG0505   154 GLDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEeilALNPDGVFLSNGPGDPAAL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  234 KETVENIRKVacVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPK-DW 312
Cdd:COG0505   234 DYAIETIREL--LGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDL 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 688603052  313 DVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTVR 362
Cdd:COG0505   312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 6-363 1.27e-163

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: 507.16  E-value: 1.27e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052     6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESSQI 85
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADN----IPFD-NPDAR 160
Cdd:TIGR01368   72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekARVSpDITGI 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   161 NLVKEVSMKAPKVFNPEGT--VRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEYCKE 235
Cdd:TIGR01368  152 NLVAEVSTKEPYTWGQRGGkgKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeikKYNPDGIFLSNGPGDPAAVEP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   236 TVENIRKVAcveNPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPK-DWDV 314
Cdd:TIGR01368  232 AIETIRKLL---EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEV 308

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 688603052   315 LFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTVRD 363
Cdd:TIGR01368  309 THVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1938-2243 5.03e-138

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: 432.94  E-value: 5.03e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1938 HPLVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCEST 2017
Cdd:COG0540     1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2018 SSTQKGESLVDSVNTMSCY-ADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2096
Cdd:COG0540    81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2097 VGDLKHGRTVHSLARLLTQYRITLRYVAPKNLsMPAEIidfvASKGIkqEEFNSIEEALPDTDVLYMTRIQKERFS---- 2172
Cdd:COG0540   161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEI----EELGV--EVTTDLDEALPDADVVYMLRIQKERFTdglf 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052 2173 -SEKEYnacFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR 2243
Cdd:COG0540   234 pSYREY---KRSYGLTAERLALAKPDAIVMHPGPrnRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
1939-2243 2.84e-124

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 394.05  E-value: 2.84e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1939 PLVGQHILSVRQFSKEQMSHLFNVAHTLR-LMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCEST 2017
Cdd:PRK00856    2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2018 SSTQKGESLVDSVNTMSCY-ADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2096
Cdd:PRK00856   82 SSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2097 VGDLKHGRTVHSLARLLTQYRITLRYVAPKNLsMPAEIIDFvaskgikqEEFNSIEEALPDTDVLYMTRIQKERF----- 2171
Cdd:PRK00856  162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMdggll 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052 2172 SSEKEYnacFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR 2243
Cdd:PRK00856  233 PSYEEY---KRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1944-2242 3.73e-110

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: 353.20  E-value: 3.73e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1944 HILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCES-TSSTQK 2022
Cdd:TIGR00670    2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVAK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  2023 GESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2102
Cdd:TIGR00670   82 GETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  2103 GRTVHSLARLLTQYRITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFSSEKEYNACFG 2182
Cdd:TIGR00670  162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  2183 QFILTPHIMTGAKRKMVVMHPLPRVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2242
Cdd:TIGR00670  242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 182-358 6.31e-103

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: 327.15  E-value: 6.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  182 ITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEYCKETVENIRKVAcvENPKPIFGICLG 258
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLL--GKKIPIFGICLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  259 HQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHKPLFSVQ 338
Cdd:cd01744    79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                         170       180
                  ....*....|....*....|
gi 688603052  339 FHPEHMAGPTDLVGLFDVFL 358
Cdd:cd01744   159 FHPEASPGPHDTEYLFDEFL 178
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 516-718 2.33e-100

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: 321.18  E-value: 2.33e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   516 DRKIFVEKMEEINEHVAPSEAAM--SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAFAHT------ 587
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   588 SQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLgiHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGEC 667
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 688603052   668 NIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLP 718
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1470-1816 2.42e-100

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: 330.90  E-value: 2.42e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSD--- 1546
Cdd:COG0044    49 LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGlge 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1547 NAALLPSIASSTA-GLKMYLndTYSTLK-MDNVSLWMEHFEKWPKH-LPIVAHAEKQT---------------------- 1601
Cdd:COG0044   129 NLAELGALAEAGAvAFKVFM--GSDDGNpVLDDGLLRRALEYAAEFgALVAVHAEDPDlirggvmnegktsprlglkgrp 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1602 -------VAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPviGKD-KAQVRPMLGTR 1673
Cdd:COG0044   207 aeaeeeaVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLE--RYGtNFKVNPPLRTE 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1674 EDMEALWENL--DIIDCFATDHAPHSAEEKisEKP----PPGYPGLETMLPLLFT-AVSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:COG0044   285 EDREALWEGLadGTIDVIATDHAPHTLEEK--ELPfaeaPNGIPGLETALPLLLTeLVHKGRLSLERLVELLSTNPARIF 362

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052 1747 SLPA----QEDTY---VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPgYGQDVK 1816
Cdd:COG0044   363 GLPRkgriAVGADadlVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP-RGRFLR 438
pyrC PRK09357
dihydroorotase; Validated
 1467-1802 4.15e-89

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 297.88  E-value: 4.15e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1467 LIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDY----ALFVG 1542
Cdd:PRK09357   49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVlpvgAITKG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1543 ASSDNAALLPSIASstAGLKMYLNDTystLKMDNVSLWMEHFEKWPKH-LPIVAHAE-----------KQTVAAIL---- 1606
Cdd:PRK09357  129 LAGEELTEFGALKE--AGVVAFSDDG---IPVQDARLMRRALEYAKALdLLIAQHCEdpslteggvmnEGEVSARLglpg 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1607 --------------LVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPviGKD-KAQVRPMLG 1671
Cdd:PRK09357  204 ipavaeevmiardvLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLL--TYDpNYKVNPPLR 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1672 TREDMEALWENL--DIIDCFATDHAPHSAEEKISE--KPPPGYPGLETMLPLLFTA-VSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:PRK09357  282 TEEDREALIEGLkdGTIDAIATDHAPHAREEKECEfeAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTINPARIL 361

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688603052 1747 SLPA------QEDTYVEVDLEQEWII-PKHMqFTKSKWTPFEGMKVKGKVMRVVLRGEVAYID 1802
Cdd:PRK09357  362 GLPAgplaegEPADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 1467-1802 2.76e-88

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: 294.74  E-value: 2.76e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1467 LIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSD 1546
Cdd:TIGR00857   35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1547 N--AALLPSIASSTAGL--KMYLNDTYSTLKMDNVSLWME-----------HFE---------------KWPKHLPIVA- 1595
Cdd:TIGR00857  115 NqgKELTEAYELKEAGAvgRMFTDDGSEVQDILSMRRALEyaaiagvpialHAEdpdliyggvmhegpsAAQLGLPARPp 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1596 HAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKDkAQVRPMLGTRED 1675
Cdd:TIGR00857  195 EAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLDGN-GKVNPPLREKED 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1676 MEALWENL--DIIDCFATDHAPHSAEEKIS--EKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLP-- 1749
Cdd:TIGR00857  274 RLALIEGLkdGIIDIIATDHAPHTLEEKTKefAAAPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPdk 353

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 688603052  1750 -----AQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYID 1802
Cdd:TIGR00857  354 gtleeGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 8-142 3.92e-76

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: 248.39  E-value: 3.92e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052     8 LVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDEdgefglskwFESSQIHA 87
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPED---------FESDKIHV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 688603052    88 AALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKL 142
Cdd:pfam00988   72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 6-142 1.84e-72

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: 238.04  E-value: 1.84e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052      6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESSQI 85
Cdd:smart01097    3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052     86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKL 142
Cdd:smart01097   74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 802-926 9.64e-58

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: 195.36  E-value: 9.64e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    802 EEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDEsaMPPEIMRKAKQLGFSDKQI 881
Cdd:smart01096    2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDE--LDADLLRKAKRLGFSDRQI 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 688603052    882 AQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTY 926
Cdd:smart01096   80 AKLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
1944-2084 1.64e-54

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 186.86  E-value: 1.64e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1944 HILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQKG 2023
Cdd:pfam02729    1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688603052  2024 ESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGdGVGEHPTQALLDIFTIRE 2084
Cdd:pfam02729   81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1318-1444 1.11e-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: 155.15  E-value: 1.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1318 KNILLSIGSYkNKSELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEEESdcPNKDKQRNImdyLEENHFDL 1397
Cdd:cd01423     1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQ--NDKPSLREL---LAEGKIDL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 688603052 1398 VINLSMRNSGGRRLSsfvtkGYRTRRMAIDFSVPLITDIKCTKLFVQ 1444
Cdd:cd01423    75 VINLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1470-1518 1.62e-05

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: 49.42  E-value: 1.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052  1470 LPGLIDVHVHLR--------EPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIID 1518
Cdd:pfam01979    3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIE 59
PHA03378 PHA03378
EBNA-3B; Provisional
 1819-1975 7.44e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.14  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1819 SATPTATTEVIMDAPKRV---IEAMTPERPRQAAPVDVVRSRAPSPRRSAGDGRFILPPRIHRSSDPGLPPAEEEVSLRA 1895
Cdd:PHA03378  677 SPTGANTMLPIQWAPGTMqppPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARP 756

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1896 PFDA--ELALPAEAYAHPPPLARilsPQAG-----QPQILPHPQTSPLLHPLVGQhiLSVRQFSKEQMSHLFNVAHTLRL 1968
Cdd:PHA03378  757 PAAApgRARPPAAAPGAPTPQPP---PQAPpapqqRPRGAPTPQPPPQAGPTSMQ--LMPRAAPGQQGPTKQILRQLLTG 831


                  ....*..
gi 688603052 1969 MVQKERP 1975
Cdd:PHA03378  832 GVKRGRP 838
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 395-1446 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: 1714.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   395 PRKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGV 474
Cdd:TIGR01369    6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   475 LLTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPV 554
Cdd:TIGR01369   86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   555 LVRSAFALGGLGSGFANNRDEMITLVTQAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGE 632
Cdd:TIGR01369  166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGD 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   633 SIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 712
Cdd:TIGR01369  246 SIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLA 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   713 LGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG 792
Cdd:TIGR01369  326 VGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATG 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   793 FDHTIKP-----ESEEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDEsaMPPEI 867
Cdd:TIGR01369  406 FDLPDREvepdeDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTD--LDPEL 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   868 MRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVF-EQPHVMVIGSG 946
Cdd:TIGR01369  484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKKVLVLGSG 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   947 VYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN 1026
Cdd:TIGR01369  564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1027 NIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVA 1106
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1107 YSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGEVIAIAVSEHVENAGVHSGDATLVTPPQDINQKTMER 1186
Cdd:TIGR01369  724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1187 IKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVG--LMRGNGIV 1264
Cdd:TIGR01369  804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1265 GVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLPTVQTLESLG 1344
Cdd:TIGR01369  884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1345 YNLYASLGTADFYTEHGVKVMAVDWPFEeesdcpnkdKQRNIMDYLEENHFDLVINLSMRNSGgrrlssFVTKGYRTRRM 1424
Cdd:TIGR01369  964 YKLYATEGTAKFLGEAGIKPELVLKVSE---------GRPNILDLIKNGEIELVINTTSKGAG------TATDGYKIRRE 1028

                         1050      1060
                   ....*....|....*....|..
gi 688603052  1425 AIDFSVPLITDIKCTKLFVQAL 1446
Cdd:TIGR01369 1029 ALDYGVPLITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
396-1447 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1451.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  396 RKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVL 475
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  476 LTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVL 555
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  556 VRSAFALGGLGSGFANNRDEMITLVTQAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGES 633
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  634 IVVAPSQTLNDYEYNMLRNTAIKVIRHLGVV-GECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 712
Cdd:PRK05294  248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  713 LGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG 792
Cdd:PRK05294  328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  793 FDHTI-----KPESEEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDesaMPPEI 867
Cdd:PRK05294  408 LDEDLfeeesLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLP---LDAEL 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  868 MRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTY-HGSESDVVfEQPHVMVIGSG 946
Cdd:PRK05294  485 LREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYeEECESNPS-DRKKVLVLGSG 563

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  947 VYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN 1026
Cdd:PRK05294  564 PNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPL 643

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1027 NIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVA 1106
Cdd:PRK05294  644 KLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIV 723

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1107 YSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVaCDGEVIAIA-VSEHVENAGVHSGDATLVTPPQDINQKTME 1185
Cdd:PRK05294  724 YDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIE 802

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1186 RIKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVGLMRGN--GI 1263
Cdd:PRK05294  803 EIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPY 882

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1264 VGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKK-NILLSIgSYKNKSELLPTVQTLES 1342
Cdd:PRK05294  883 VAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLE 961

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1343 LGYNLYASLGTADFYTEHGVKVMAVdwpfeeesdcpNKDKQR--NIMDYLEENHFDLVINlSMRNSGGRRlssfvtKGYR 1420
Cdd:PRK05294  962 LGFKILATSGTAKFLREAGIPVELV-----------NKVHEGrpHIVDLIKNGEIDLVIN-TPTGRQAIR------DGFS 1023

                        1050      1060
                  ....*....|....*....|....*..
gi 688603052 1421 TRRMAIDFSVPLITDIKCTKLFVQALK 1447
Cdd:PRK05294 1024 IRRAALEYKVPYITTLAGARAAVKAIE 1050
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 396-1449 0e+00

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 1109.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  396 RKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVL 475
Cdd:PRK12815    8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  476 LTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVL 555
Cdd:PRK12815   88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  556 VRSAFALGGLGSGFANNRDEMITLVTQAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGES 633
Cdd:PRK12815  168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  634 IVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSL 713
Cdd:PRK12815  248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  714 GIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVGF 793
Cdd:PRK12815  328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  794 DHTIK--PESEEEL----QTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIadhKKLLETYKQDESAMPPEI 867
Cdd:PRK12815  408 SLPIElsGKSDEELlqdlRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHI---VALEKKLAEDGLDLSADL 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  868 MRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHG-SESDVVFEQPHVMVIGSG 946
Cdd:PRK12815  485 LRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGeSEAEPSSEKKKVLILGSG 564

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  947 VYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN 1026
Cdd:PRK12815  565 PIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAI 644

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1027 NIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVA 1106
Cdd:PRK12815  645 NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVV 724

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1107 YSDTDMEKFLssAVAVSKEHPVVISKFIqEAKEIDVDAVaCDGEVIAIA-VSEHVENAGVHSGDATLVTPPQDINQKTME 1185
Cdd:PRK12815  725 YDEPALEAYL--AENASQLYPILIDQFI-DGKEYEVDAI-SDGEDVTIPgIIEHIEQAGVHSGDSIAVLPPQSLSEEQQE 800

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1186 RIKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILG----EEVEAVGLMRGN 1261
Cdd:PRK12815  801 KIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGkslaELGYPNGLWPGS 880

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1262 GIVGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLPTVQTLE 1341
Cdd:PRK12815  881 PFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFA 960

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1342 SLGYNLYASLGTADFYTEHGVKVMAVDWPFEEesdcpnkdkQRNIMDYLEENHFDLVINLSMRNSGGRrlssfvtKGYRT 1421
Cdd:PRK12815  961 QLGFKLLATEGTANWLAEEGITTGVVEKVQEG---------SPSLLERIKQHRIVLVVNTSLSDSASE-------DAIKI 1024

                        1050      1060
                  ....*....|....*....|....*...
gi 688603052 1422 RRMAIDFSVPLITDIKCTKLFVQALKQI 1449
Cdd:PRK12815 1025 RDEALSTHIPVFTELETAQAFLQVLESL 1052
PLN02735 PLN02735
carbamoyl-phosphate synthase
 396-1453 0e+00

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 891.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  396 RKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVL 475
Cdd:PLN02735   24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  476 LTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLG-YPV 554
Cdd:PLN02735  104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  555 LVRSAFALGGLGSGFANNRDEMITLVTQAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGE 632
Cdd:PLN02735  184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  633 SIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVvgEC---NIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAA 709
Cdd:PLN02735  264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  710 KLSLGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDEN 789
Cdd:PLN02735  342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  790 CVGFDHTIKPESE-------EELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDEsa 862
Cdd:PLN02735  422 FSGWGCAKVKELDwdweqlkYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSE-- 499

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  863 MPPEIMRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVFEQPHVMV 942
Cdd:PLN02735  500 LSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLI 579

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  943 IGSGVYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGG 1022
Cdd:PLN02735  580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1023 QLPNNIAMSLHRQ-------------QCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYP 1089
Cdd:PLN02735  660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1090 CLVRPSYVLSGAAMNVAYSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVA-CDGEVIAIAVSEHVENAGVHSG 1168
Cdd:PLN02735  740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1169 DATLVTPPQDINQKTMERIKMIVHAIGQELQVTGPFNLQL-IAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVI 1247
Cdd:PLN02735  820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVM 899

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1248 LGEEVEAVGLMRGNGI--VGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKK-NILLSI 1324
Cdd:PLN02735  900 SGKSLKDLGFTEEVIPahVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSgTVFISL 979

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1325 GSyKNKSELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEeesdcpnkdKQRNIMDYLEENHfdlvINLSMR 1404
Cdd:PLN02735  980 ND-LTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHE---------GRPHAGDMLANGQ----IQLMVI 1045

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*....
gi 688603052 1405 NSGGRRLSSfvTKGYRTRRMAIDFSVPLITDIKCTKLFVQALKQIGQAP 1453
Cdd:PLN02735 1046 TSSGDALDQ--KDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECP 1092
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 401-945 0e+00

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: 660.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  401 LGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVLLTFGG 480
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  481 QTALNCGVELKKQGVLEKykVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVLVRSAF 560
Cdd:COG0458    81 QTALNLAVELEEAGILEG--VKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  561 ALGGLGSGFANNRDEMITLVTQAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGESIVVAP 638
Cdd:COG0458   159 VLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  639 SQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNpeSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLP 718
Cdd:COG0458   239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  719 VLKNsvtnstTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG--FDHT 796
Cdd:COG0458   317 ELGN------DTGFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  797 IKPESEEE--LQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIadhkkLLETYKQDESAMPPEIMRKAKQL 874
Cdd:COG0458   391 VADDDKEEalLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPI-----IVDEIELEEIILVINTLLGAKSL 465

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688603052  875 GFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVFEQPHVMVIGS 945
Cdd:COG0458   466 GDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1466-1812 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: 578.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1466 KLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASS 1545
Cdd:cd01316     1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1546 DNAALLPSIASSTAGLKMYLNDTYSTLKMDNVSLWMEHFEKWPKHLPIVAHAEKQTVAAILLVAQLYQRPVHICHVAKKE 1625
Cdd:cd01316    81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1626 EILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPvigKDKAQVRPMLGTREDMEALWENLDIIDCFATDHAPHSAEEKISEK 1705
Cdd:cd01316   161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLP---RGQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1706 PPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKV 1785
Cdd:cd01316   238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317

                         330       340
                  ....*....|....*....|....*..
gi 688603052 1786 KGKVMRVVLRGEVAYIDGQVLVPPGYG 1812
Cdd:cd01316   318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 943-1436 7.61e-172

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: 537.54  E-value: 7.61e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  943 IGSGVYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGG 1022
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1023 QLPNNIAMSLHRQQ----CRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVL 1098
Cdd:COG0458    81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1099 SGAAMNVAYSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVaCDGE--VIAIAVSEHVENAGVHSGDATLVTPP 1176
Cdd:COG0458   161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVV-RDGEdnVIIVGIMEHIEPAGVHSGDSICVAPP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1177 QDINQKTMERIKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVG 1256
Cdd:COG0458   240 QTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1257 LmrGNGI------VGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKnILLSIGSYKNK 1330
Cdd:COG0458   320 N--DTGFeptldyVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDK 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1331 SELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEeesdcpnkdKQRNIMDYLEENHFDLVINLSMRNSGGRR 1410
Cdd:COG0458   397 EEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSE---------GRPIIVDEIELEEIILVINTLLGAKSLGD 467

                         490       500
                  ....*....|....*....|....*.
gi 688603052 1411 lssfvtkGYRTRRMAIDFSVPLITDI 1436
Cdd:COG0458   468 -------SDGIIRRALAAKVPYVTTL 486
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
4-359 1.30e-166

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 515.78  E-value: 1.30e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    4 KMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESS 83
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   84 QIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIP-----FDNPD 158
Cdd:PRK12564   74 RPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  159 ARNLVKEVSMKAPKVF---NPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEY 232
Cdd:PRK12564  154 GLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEeilALNPDGVFLSNGPGDPAA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  233 CKETVENIRKVacVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDW 312
Cdd:PRK12564  234 LDYAIEMIREL--LEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANL 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 688603052  313 DVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLD 359
Cdd:PRK12564  312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 4-362 1.19e-164

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: 510.33  E-value: 1.19e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    4 KMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPkDEDgefglskwFESS 83
Cdd:COG0505     3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVN-DED--------FESD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   84 QIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIP-----FDNPD 158
Cdd:COG0505    74 RPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLekaraAPGME 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  159 ARNLVKEVSMKAPKVF--NPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEYC 233
Cdd:COG0505   154 GLDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEeilALNPDGVFLSNGPGDPAAL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  234 KETVENIRKVacVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPK-DW 312
Cdd:COG0505   234 DYAIETIREL--LGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDL 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 688603052  313 DVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTVR 362
Cdd:COG0505   312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 6-363 1.27e-163

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: 507.16  E-value: 1.27e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052     6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESSQI 85
Cdd:TIGR01368    1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADN----IPFD-NPDAR 160
Cdd:TIGR01368   72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekARVSpDITGI 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   161 NLVKEVSMKAPKVFNPEGT--VRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEYCKE 235
Cdd:TIGR01368  152 NLVAEVSTKEPYTWGQRGGkgKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeikKYNPDGIFLSNGPGDPAAVEP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   236 TVENIRKVAcveNPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPK-DWDV 314
Cdd:TIGR01368  232 AIETIRKLL---EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEV 308

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 688603052   315 LFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTVRD 363
Cdd:TIGR01368  309 THVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1938-2243 5.03e-138

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: 432.94  E-value: 5.03e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1938 HPLVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCEST 2017
Cdd:COG0540     1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2018 SSTQKGESLVDSVNTMSCY-ADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2096
Cdd:COG0540    81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2097 VGDLKHGRTVHSLARLLTQYRITLRYVAPKNLsMPAEIidfvASKGIkqEEFNSIEEALPDTDVLYMTRIQKERFS---- 2172
Cdd:COG0540   161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEI----EELGV--EVTTDLDEALPDADVVYMLRIQKERFTdglf 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052 2173 -SEKEYnacFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR 2243
Cdd:COG0540   234 pSYREY---KRSYGLTAERLALAKPDAIVMHPGPrnRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 6-361 9.79e-134

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 423.15  E-value: 9.79e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPkDEDgefglskwFESSQI 85
Cdd:PRK12838    3 AYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGIN-ADD--------YESKQP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVvegTPADNIPFDNPDA----RN 161
Cdd:PRK12838   74 QVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASIT---TTDDAHAFDQIKAlvlpKN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  162 LVKEVSMKAPKVFnPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPL---DSNDFDGLFISNGPGNPEYCKETVE 238
Cdd:PRK12838  151 VVAQVSTKEPYTY-GNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLeeiKNLNPDGIVLSNGPGDPKELQPYLP 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  239 NIRKVAcveNPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETL-PKDWDVLFT 317
Cdd:PRK12838  230 EIKKLI---SSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFF 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 688603052  318 NANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTV 361
Cdd:PRK12838  307 NVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMM 350
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
1939-2243 2.84e-124

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 394.05  E-value: 2.84e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1939 PLVGQHILSVRQFSKEQMSHLFNVAHTLR-LMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCEST 2017
Cdd:PRK00856    2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2018 SSTQKGESLVDSVNTMSCY-ADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2096
Cdd:PRK00856   82 SSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2097 VGDLKHGRTVHSLARLLTQYRITLRYVAPKNLsMPAEIIDFvaskgikqEEFNSIEEALPDTDVLYMTRIQKERF----- 2171
Cdd:PRK00856  162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMdggll 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052 2172 SSEKEYnacFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR 2243
Cdd:PRK00856  233 PSYEEY---KRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
PLN02527 PLN02527
aspartate carbamoyltransferase
 1943-2242 6.59e-124

aspartate carbamoyltransferase


Pssm-ID: 178142 [Multi-domain]  Cd Length: 306  Bit Score: 392.96  E-value: 6.59e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1943 QHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHfCES---TSS 2019
Cdd:PLN02527    1 SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLT-TENageFSS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2020 TQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGD 2099
Cdd:PLN02527   80 AAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2100 LKHGRTVHSLARLLTQYR-ITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFS-SEKEY 2177
Cdd:PLN02527  160 LANGRTVRSLAYLLAKYEdVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDLMEVASKCDVLYQTRIQRERFGeRIDLY 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688603052 2178 NACFGQFILTPHIMTGAKRKMVVMHPLPRVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2242
Cdd:PLN02527  240 EAARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLG 304
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1944-2242 3.73e-110

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: 353.20  E-value: 3.73e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1944 HILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCES-TSSTQK 2022
Cdd:TIGR00670    2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVAK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  2023 GESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2102
Cdd:TIGR00670   82 GETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  2103 GRTVHSLARLLTQYRITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFSSEKEYNACFG 2182
Cdd:TIGR00670  162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  2183 QFILTPHIMTGAKRKMVVMHPLPRVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2242
Cdd:TIGR00670  242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 1467-1792 2.60e-104

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: 338.21  E-value: 2.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1467 LIRLPGLIDVHVHLREPGAT-HKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASS 1545
Cdd:cd01302     1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1546 -DNAALLP-SIASSTAGLKMYLNDTYSTLKMDNVSLWMEHFEKWP-KHLPIVAHAEKqtvaaILLVAQLYQRPVHICHVA 1622
Cdd:cd01302    81 gDVTDELKkLFDAGINSLKVFMNYYFGELFDVDDGTLMRTFLEIAsRGGPVMVHAER-----AAQLAEEAGANVHIAHVS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1623 KKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKdKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEE 1700
Cdd:cd01302   156 SGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGA-WGKVNPPLRSKEDREALWEGVknGKIDTIASDHAPHSKEE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1701 KIS----EKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQED---------TYVEVDLEQEWIIP 1767
Cdd:cd01302   235 KESgkdiWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKGTiavgydadlVIVDPKKEWKVTAE 314

                         330       340
                  ....*....|....*....|....*
gi 688603052 1768 KHMqfTKSKWTPFEGMKVKGKVMRV 1792
Cdd:cd01302   315 EIE--SKADWTPFEGMEVTGKPVST 337
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 182-358 6.31e-103

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: 327.15  E-value: 6.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  182 ITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEYCKETVENIRKVAcvENPKPIFGICLG 258
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLL--GKKIPIFGICLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  259 HQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHKPLFSVQ 338
Cdd:cd01744    79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                         170       180
                  ....*....|....*....|
gi 688603052  339 FHPEHMAGPTDLVGLFDVFL 358
Cdd:cd01744   159 FHPEASPGPHDTEYLFDEFL 178
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 516-718 2.33e-100

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: 321.18  E-value: 2.33e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   516 DRKIFVEKMEEINEHVAPSEAAM--SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAFAHT------ 587
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   588 SQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLgiHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGEC 667
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 688603052   668 NIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLP 718
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1470-1816 2.42e-100

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: 330.90  E-value: 2.42e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSD--- 1546
Cdd:COG0044    49 LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGlge 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1547 NAALLPSIASSTA-GLKMYLndTYSTLK-MDNVSLWMEHFEKWPKH-LPIVAHAEKQT---------------------- 1601
Cdd:COG0044   129 NLAELGALAEAGAvAFKVFM--GSDDGNpVLDDGLLRRALEYAAEFgALVAVHAEDPDlirggvmnegktsprlglkgrp 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1602 -------VAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPviGKD-KAQVRPMLGTR 1673
Cdd:COG0044   207 aeaeeeaVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLE--RYGtNFKVNPPLRTE 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1674 EDMEALWENL--DIIDCFATDHAPHSAEEKisEKP----PPGYPGLETMLPLLFT-AVSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:COG0044   285 EDREALWEGLadGTIDVIATDHAPHTLEEK--ELPfaeaPNGIPGLETALPLLLTeLVHKGRLSLERLVELLSTNPARIF 362

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052 1747 SLPA----QEDTY---VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPgYGQDVK 1816
Cdd:COG0044   363 GLPRkgriAVGADadlVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP-RGRFLR 438
PRK08192 PRK08192
aspartate carbamoyltransferase; Provisional
 1942-2242 2.32e-93

aspartate carbamoyltransferase; Provisional


Pssm-ID: 169269 [Multi-domain]  Cd Length: 338  Bit Score: 306.65  E-value: 2.32e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1942 GQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSV---VHFceSTS 2018
Cdd:PRK08192    5 GSHILSVNQLDRDAIQRIFNVADRMEPYALREKRTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVretTGM--ASS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2019 STQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREEL----GTVNGMTI 2094
Cdd:PRK08192   83 SLSKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGIDGMHI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2095 TMVGDLKHGRTVHSLARLLTQY-RITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFSS 2173
Cdd:PRK08192  163 AMVGDLKFGRTVHSLSRLLCMYkNVSFTLVSPKELAMPDYVISDIENAGHKITITDQLEGNLDKADILYLTRIQEERFPS 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688603052 2174 EKEYNACFGQFILTPHIMTG-AKRKMVVMHPLPR-----VNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2242
Cdd:PRK08192  243 QEEANKYRGKFRLNQSIYTQhCKSNTVIMHPLPRdsraqANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLG 317
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 380-784 3.62e-91

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: 322.33  E-value: 3.62e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   380 HLTFPGSPDPNAFVRPRKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITP 459
Cdd:TIGR01369  539 YSTYEGERDDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTF 618

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   460 EYVTQVIKNERPDGVLLTFGGQTALNCGVELKKQGvlekykVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMS 539
Cdd:TIGR01369  619 EDVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATS 692

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   540 VEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAFAHTSQ--VLVDKSLKGWKEIEYEVVrdAYDNCVTV 617
Cdd:TIGR01369  693 VEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAV--SDGEEVLI 770

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   618 CN-MENIDPLGIHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALnpESEQYYIIEVNARLSRSSALA 696
Cdd:TIGR01369  771 PGiMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEVNPRASRTVPFV 848

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   697 SKATGYPLAYVAAKLSLG---IPLPVLKnsvtnsttanfEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGR 773
Cdd:TIGR01369  849 SKATGVPLAKLAVRVMLGkklEELGVGK-----------EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGR 917

                          410
                   ....*....|.
gi 688603052   774 SFEEAFQKALR 784
Cdd:TIGR01369  918 DLAEAFLKAQL 928
pyrC PRK09357
dihydroorotase; Validated
 1467-1802 4.15e-89

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 297.88  E-value: 4.15e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1467 LIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDY----ALFVG 1542
Cdd:PRK09357   49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVlpvgAITKG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1543 ASSDNAALLPSIASstAGLKMYLNDTystLKMDNVSLWMEHFEKWPKH-LPIVAHAE-----------KQTVAAIL---- 1606
Cdd:PRK09357  129 LAGEELTEFGALKE--AGVVAFSDDG---IPVQDARLMRRALEYAKALdLLIAQHCEdpslteggvmnEGEVSARLglpg 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1607 --------------LVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPviGKD-KAQVRPMLG 1671
Cdd:PRK09357  204 ipavaeevmiardvLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLL--TYDpNYKVNPPLR 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1672 TREDMEALWENL--DIIDCFATDHAPHSAEEKISE--KPPPGYPGLETMLPLLFTA-VSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:PRK09357  282 TEEDREALIEGLkdGTIDAIATDHAPHAREEKECEfeAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTINPARIL 361

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688603052 1747 SLPA------QEDTYVEVDLEQEWII-PKHMqFTKSKWTPFEGMKVKGKVMRVVLRGEVAYID 1802
Cdd:PRK09357  362 GLPAgplaegEPADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
PRK11891 PRK11891
aspartate carbamoyltransferase; Provisional
 1943-2242 4.58e-89

aspartate carbamoyltransferase; Provisional


Pssm-ID: 183362 [Multi-domain]  Cd Length: 429  Bit Score: 297.93  E-value: 4.58e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1943 QHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVvhfCEST----S 2018
Cdd:PRK11891   88 PQLLSVDQFSRDSVEALFRVADVMQPIARRQKISRVLEGAVLGNLFFEASTRTRVSFGAAFCRLGGSV---CDTTgftfS 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2019 STQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREE---LG-TVNGMTI 2094
Cdd:PRK11891  165 SMAKGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVINGGDGPGEHPSQALLDLYTIQREfsrLGkIVDGAHI 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2095 TMVGDLKHGRTVHSLARLLTQYR-ITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFSS 2173
Cdd:PRK11891  245 ALVGDLKYGRTVHSLVKLLALYRgLKFTLVSPPTLEMPAYIVEQISRNGHVIEQTDDLAAGLRGADVVYATRIQKERFAD 324

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688603052 2174 EkEYNACFGQFILTPHIMTGA-KRKMVVMHPLPR-----VNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2242
Cdd:PRK11891  325 E-SFEGYTPDFQINQALVDAVcKPDTLIMHPLPRdsrpgANDLSTDLNRDPRLAIFRQTDNGIPVRMAIFAVLLG 398
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 1470-1796 9.54e-89

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: 294.24  E-value: 9.54e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGAS-SDNA 1548
Cdd:cd01318     5 LPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTgSEDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1549 ALLPsiASSTAGLKMYLNDtySTlkmDNVSLWMEHFEKWPKH--LPIVAHAEKQT------------------------- 1601
Cdd:cd01318    85 EELD--KAPPAGYKIFMGD--ST---GDLLDDEETLERIFAEgsVLVTFHAEDEDrlrenrkelkgesahprirdaeaaa 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1602 --VAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKgiqVTCEVAPHHLFLCEDNVPVIGKdKAQVRPMLGTREDMEAL 1679
Cdd:cd01318   158 vaTARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLGT-LGKVNPPLRSREDRKAL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1680 WENL--DIIDCFATDHAPHSAEEKIS--EKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLP---AQE 1752
Cdd:cd01318   234 LQALadGRIDVIASDHAPHTLEEKRKgyPAAPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIKnkgRIA 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 688603052 1753 DTY----VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRG 1796
Cdd:cd01318   314 EGYdadlTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 1467-1802 2.76e-88

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: 294.74  E-value: 2.76e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1467 LIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSD 1546
Cdd:TIGR00857   35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1547 N--AALLPSIASSTAGL--KMYLNDTYSTLKMDNVSLWME-----------HFE---------------KWPKHLPIVA- 1595
Cdd:TIGR00857  115 NqgKELTEAYELKEAGAvgRMFTDDGSEVQDILSMRRALEyaaiagvpialHAEdpdliyggvmhegpsAAQLGLPARPp 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1596 HAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKDkAQVRPMLGTRED 1675
Cdd:TIGR00857  195 EAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLDGN-GKVNPPLREKED 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1676 MEALWENL--DIIDCFATDHAPHSAEEKIS--EKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLP-- 1749
Cdd:TIGR00857  274 RLALIEGLkdGIIDIIATDHAPHTLEEKTKefAAAPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPdk 353

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 688603052  1750 -----AQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYID 1802
Cdd:TIGR00857  354 gtleeGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 1-368 2.08e-87

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 291.32  E-value: 2.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    1 MSLKMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDEdgefglskwF 80
Cdd:CHL00197    2 KKMIPAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLED---------I 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   81 ESSQIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLG-------------------- 140
Cdd:CHL00197   73 ESVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGcisnqnlnlsylrakikesp 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  141 -----KLVVEGTPADNIPFDNPDARNLVKEVSMKAPKVFNpegtVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPL-D 214
Cdd:CHL00197  153 hmpssDLIPRVTTSSYYEWDEKSHPSFYLADNKRPHSSYQ----LKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYqD 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  215 SNDF--DGLFISNGPGNPE---YCKETVENIRKVACvenpkPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPC-IHKg 288
Cdd:CHL00197  229 ILSYqpDGILLSNGPGDPSaihYGIKTVKKLLKYNI-----PIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSgLNQ- 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  289 tsRCYITSQNHGFAVDPETLPKD-WDVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTVRDVKEN 367
Cdd:CHL00197  303 --QVEITSQNHGFAVNLESLAKNkFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSS 380


                  .
gi 688603052  368 K 368
Cdd:CHL00197  381 K 381
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 8-142 3.92e-76

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: 248.39  E-value: 3.92e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052     8 LVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDEdgefglskwFESSQIHA 87
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPED---------FESDKIHV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 688603052    88 AALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKL 142
Cdd:pfam00988   72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 6-349 1.94e-74

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 255.29  E-value: 1.94e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDEDgefglskwfESSQI 85
Cdd:PLN02771   57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDE---------ESRQC 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIPFD-----NPDAR 160
Cdd:PLN02771  128 FLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKmsrswDIVGI 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  161 NLVKEVSMKAPKV----------FNPEG----TVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQP----LDSNDfDGLF 222
Cdd:PLN02771  208 DLISGVSCKSPYEwvdktnpewdFNTNSrdgeSYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPaseaLKMKP-DGVL 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  223 ISNGPGNPE---YCKETV-ENIRKVacvenpkPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQN 298
Cdd:PLN02771  287 FSNGPGDPSavpYAVETVkELLGKV-------PVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQN 359

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 688603052  299 HGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTD 349
Cdd:PLN02771  360 HNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHD 410
PRK04250 PRK04250
dihydroorotase; Provisional
 1464-1809 2.57e-73

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 251.23  E-value: 2.57e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1464 SQKLIrLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYAL-FVG 1542
Cdd:PRK04250   41 KGGII-LPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALnFLI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1543 ASsdNAALLPSI---------ASSTAGLkmYLND---TYSTLkMDNVSLWMEHFE---KWPKHLPIvahAEKQTVAAILL 1607
Cdd:PRK04250  120 AG--NCEKAEEIkadfykifmGASTGGI--FSENfevDYACA-PGIVSVHAEDPElirEFPERPPE---AEVVAIERALE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1608 VAQLYQRPVHICHVAKKEEILIIraaKQKGIQ-VTCEVAPHHLFLCEDNVPVIGKDKaqVRPMLGTREDMEALWENLDII 1686
Cdd:PRK04250  192 AGKKLKKPLHICHISTKDGLKLI---LKSNLPwVSFEVTPHHLFLTRKDYERNPLLK--VYPPLRSEEDRKALWENFSKI 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1687 DCFATDHAPHSAEEKisEKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLP------AQEDTYVEVDL 1760
Cdd:PRK04250  267 PIIASDHAPHTLEDK--EAGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKnygieeGNYANFAVFDM 344

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 688603052 1761 EQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPP 1809
Cdd:PRK04250  345 KKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 6-142 1.84e-72

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: 238.04  E-value: 1.84e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052      6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESSQI 85
Cdd:smart01097    3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052     86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKL 142
Cdd:smart01097   74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
PRK07575 PRK07575
dihydroorotase; Provisional
 1448-1805 2.17e-71

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 246.90  E-value: 2.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1448 QIGQAPRVKTHVDSMTSQKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNsfTMAQK 1527
Cdd:PRK07575   33 AIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQA--ALDDK 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1528 LAKAGCRC--DYALFVGASSDNAALLPSiASSTAGLKMYLNDTYSTLKMDNVSLWMEHFEKwpKHLPIVAHAEKQT---- 1601
Cdd:PRK07575  111 LARAAEKCvvNYGFFIGATPDNLPELLT-ANPTCGIKIFMGSSHGPLLVDEEAALERIFAE--GTRLIAVHAEDQArira 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1602 ----------VA---------AILLVAQL-------YQRPVHICHVAKKEEILIIRAAKqkGIQVTCEVAPHHLFLCEDN 1655
Cdd:PRK07575  188 rraefagisdPAdhsqiqdeeAALLATRLalklskkYQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTDA 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1656 VPVIGKdKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISEKP--PPGYPGLETMLPLLFTAVSEGRLTV 1731
Cdd:PRK07575  266 YERIGT-LAQMNPPLRSPEDNEALWQALrdGVIDFIATDHAPHTLEEKAQPYPnsPSGMPGVETSLPLMLTAAMRGKCTV 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1732 DDIIKRLYENPRKIFSLPAQ---EDTY----VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQ 1804
Cdd:PRK07575  345 AQVVRWMSTAVARAYGIPNKgriAPGYdadlVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQ 424


                  .
gi 688603052 1805 V 1805
Cdd:PRK07575  425 V 425
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 1465-1792 5.73e-69

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: 237.91  E-value: 5.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1465 QKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPN---------------------SFT 1523
Cdd:cd01317     8 EGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAvvellknrakdvgivrvlpigALT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1524 MAQK---------LAKAGCrcdyalfVGASSD-----NAALLPSIASSTAGLKMYL---------------NDTYSTLKM 1574
Cdd:cd01317    88 KGLKgeelteigeLLEAGA-------VGFSDDgkpiqDAELLRRALEYAAMLDLPIivhpedpslagggvmNEGKVASRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1575 DnvslwmehfekwpkhLP-IVAHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCE 1653
Cdd:cd01317   161 G---------------LPgIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1654 DNVPviGKD-KAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKisEKP----PPGYPGLETMLPLLFT-AVS 1725
Cdd:cd01317   226 EALE--SYDtNAKVNPPLRSEEDREALIEALkdGTIDAIASDHAPHTDEEK--DLPfaeaPPGIIGLETALPLLWTlLVK 301

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052 1726 EGRLTVDDIIKRLYENPRKIFSLPAQEDTYVE------VDLEQEWII-PKHMQfTKSKWTPFEGMKVKGKVMRV 1792
Cdd:cd01317   302 GGLLTLPDLIRALSTNPAKILGLPPGRLEVGApadlvlFDPDAEWIVdEETFR-SKSKNTPFDGQKLKGRVLAT 374
PRK09060 PRK09060
dihydroorotase; Validated
 1470-1822 2.57e-64

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 226.73  E-value: 2.57e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNsfTMAQKLAKAGCR--CDYALFVGASSDN 1547
Cdd:PRK09060   55 LPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNPLTTTAE--ALADKLARARHRmhCDFAFYVGGTRDN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1548 AALLPSI--ASSTAGLKMYL-NDTYSTLKMDNVSLwmE------------HFEKWP-----KHLPIVAHAEKQTV----- 1602
Cdd:PRK09060  133 ADELAELerLPGCAGIKVFMgSSTGDLLVEDDEGL--RrilrngrrraafHSEDEYrlrerKGLRVEGDPSSHPVwrdee 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1603 AAIL----LV--AQLYQRPVHICHVAKKEEILIIRAAKQKgiqVTCEVAPHHLFL-CEDNVPVIGKdKAQVRPMLGTRED 1675
Cdd:PRK09060  211 AALLatrrLVrlARETGRRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLaAPECYERLGT-LAQMNPPIRDARH 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1676 MEALWENLD--IIDCFATDHAPHSAEEKisEKP----PPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLP 1749
Cdd:PRK09060  287 RDGLWRGVRqgVVDVLGSDHAPHTLEEK--AKPypasPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIA 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1750 AQ--------EDTYVeVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPGyGQDVKSWSAT 1821
Cdd:PRK09060  365 GKgriavgydADFTI-VDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELVGPPT-GEPVRFLETL 442


                  .
gi 688603052 1822 P 1822
Cdd:PRK09060  443 P 443
GATase pfam00117
Glutamine amidotransferase class-I;
185-359 5.95e-64

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 215.95  E-value: 5.95e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   185 IDCG--IKYNQIRCLCQRGARVTVVPWDQP---LDSNDFDGLFISNGPGNPEYCKETVENIRKVacVENPKPIFGICLGH 259
Cdd:pfam00117    3 IDNGdsFTYNLARALRELGVEVTVVPNDTPaeeILEENPDGIILSGGPGSPGAAGGAIEAIREA--RELKIPILGICLGH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   260 QLLSLVIGAKTYKMK-YGNRGHNQPCIH------KGTSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHK 332
Cdd:pfam00117   81 QLLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160

                          170       180
                   ....*....|....*....|....*..
gi 688603052   333 PLFSVQFHPEHMAGPTDLVGLFDVFLD 359
Cdd:pfam00117  161 PIFGVQFHPESILTPHGPEILFNFFIK 187
PRK02382 PRK02382
dihydroorotase; Provisional
 1470-1816 1.54e-63

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 224.53  E-value: 1.54e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALfVGASSDNAA 1549
Cdd:PRK02382   53 LPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGI-NGGVTGNWD 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1550 LLPSI-------------ASSTAGLKM--------------------------YLNDTYSTLKMDNVSlwmehFEKWPKH 1590
Cdd:PRK02382  132 PLESLwergvfalgeifmADSTGGMGIdeelfeealaeaarlgvlatvhaedeDLFDELAKLLKGDAD-----ADAWSAY 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1591 LPivAHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKqkgiqVTCEVAPHHLFLCEDNVPVIGKdKAQVRPML 1670
Cdd:PRK02382  207 RP--AAAEAAAVERALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGT-FGKMNPPL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1671 GTREDMEALWENLD--IIDCFATDHAPHSAEEK---ISEKPPpGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKI 1745
Cdd:PRK02382  279 RSEKRREALWERLNdgTIDVVASDHAPHTREEKdadIWDAPS-GVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARI 357

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688603052 1746 FSLPAQ---EDTY----VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMrVVLRGEVAYIDGQVLVPPGYGQDVK 1816
Cdd:PRK02382  358 FGLDGKgriAEGYdadlVLVDPDAAREIRGDDLHSKAGWTPFEGMEGVFPEL-TMVRGTVVWDGDDINAKRGRGEFLR 434
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 1443-1809 1.56e-62

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: 221.78  E-value: 1.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1443 VQALKQIGQAPRVKTHVDSmtSQKLIrLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNS 1521
Cdd:cd01315    27 IAAIGPDIANTEAEEVIDA--GGLVV-MPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVEN 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1522 FTMAQKLAKAGCRCDYALFVGASSDNA-ALLPSIASSTAGLKMYLNDTySTLKMDNVSLW--MEHFEKWPKH-LPIVAHA 1597
Cdd:cd01315   104 LEAKLEAAQGKLHVDVGFWGGLVPGNLdQLRPLDEAGVVGFKCFLCPS-GVDEFPAVDDEqlEEAMKELAKTgSVLAVHA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1598 E----------------KQTVAA----------------ILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVA 1645
Cdd:cd01315   183 EnpeitealqeqakakgKRDYRDylasrpvfteveaiqrILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETC 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1646 PHHLFLCEDNVPVIGKdKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISEKPP-----PGYPGLETMLP 1718
Cdd:cd01315   263 PHYLTFTAEDVPDGGT-EFKCAPPIRDAANQEQLWEALenGDIDMVVSDHSPCTPELKLLGKGDffkawGGISGLQLGLP 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1719 LLFT-AVSEGRLTVDDIIKRLYENPRKIFSLPAQEDT--------YVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKV 1789
Cdd:cd01315   342 VMLTeAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRiavgydadFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRV 421

                         410       420
                  ....*....|....*....|
gi 688603052 1790 MRVVLRGEVAYIDGQVLVPP 1809
Cdd:cd01315   422 HATILRGTVVYQDGEVVGEP 441
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 802-926 9.64e-58

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: 195.36  E-value: 9.64e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052    802 EEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDEsaMPPEIMRKAKQLGFSDKQI 881
Cdd:smart01096    2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDE--LDADLLRKAKRLGFSDRQI 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 688603052    882 AQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTY 926
Cdd:smart01096   80 AKLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
ArgF COG0078
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ...
 1940-2243 1.52e-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: 1.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1940 LVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFceSTSS 2019
Cdd:COG0078     3 LKGRHFLSLLDLTPEELRALLDLAAELKAKRKAGIPHRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYL--DPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2020 TQ--KGESLVDSVNTMSCYADVIVLR---HPIpgaVESAARHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMT 2093
Cdd:COG0078    81 SQlgRGESIKDTARVLSRYVDGIMIRtfgHET---LEELAKYAGVPVINGlTD--LFHPCQALADLLTIREHFGKLKGLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2094 ITMVGDlkhGRTV-HSLARLLTQYRITLRYVAPKNLSMPAEIID----FVASKGIKQEEFNSIEEALPDTDVLY------ 2162
Cdd:COG0078   156 VAYVGD---GNNVaNSLLLAAAKLGMDVRIATPEGYEPDPEIVAkakeIAAESGGSITITHDPAEAVKGADVVYtdvwvs 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2163 MTriQKErfsSEKEYNACFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATV 2240
Cdd:COG0078   233 MG--QEE---EAEERIKAFKPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEVIDGPQSVVFDEAENRLHAQKALLAWL 307


                  ...
gi 688603052 2241 LGR 2243
Cdd:COG0078   308 LGG 310
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
1944-2084 1.64e-54

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 186.86  E-value: 1.64e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1944 HILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQKG 2023
Cdd:pfam02729    1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688603052  2024 ESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGdGVGEHPTQALLDIFTIRE 2084
Cdd:pfam02729   81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
PRK09236 PRK09236
dihydroorotase; Reviewed
 1454-1805 1.61e-50

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 186.61  E-value: 1.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1454 RVKTHVDSMTSQKLIR------LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNsfTMAQK 1527
Cdd:PRK09236   31 KIASSISAKSADTVIDaagrylLPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLE--ALEAK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1528 LAKAGCRC--DYALFVGASSDNAALLPSI-ASSTAGLKMYLNDtySTLKM--DNVSLWMEHFEKWPkhLPIVAHAEKQTV 1602
Cdd:PRK09236  109 YQIAAQRSlaNYSFYFGATNDNLDEIKRLdPKRVCGVKVFMGA--STGNMlvDNPETLERIFRDAP--TLIATHCEDTPT 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1603 A-----------------------------------AILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPH 1647
Cdd:PRK09236  185 IkanlakykekygddipaemhplirsaeacykssslAVSL-AKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVH 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1648 HLFLCEDNVPVIGkdkAQVR--PMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKisEKP----PPGYPGLETMLPL 1719
Cdd:PRK09236  264 HLWFDDSDYARLG---NLIKcnPAIKTASDREALRQALadDRIDVIATDHAPHTWEEK--QGPyfqaPSGLPLVQHALPA 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1720 LFTAVSEGRLTVDDIIKRLYENPRKIFSLpaQEDTY---------VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVM 1790
Cdd:PRK09236  339 LLELVHEGKLSLEKVVEKTSHAPAILFDI--KERGFiregywadlVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVA 416

                         410
                  ....*....|....*
gi 688603052 1791 RVVLRGEVAYIDGQV 1805
Cdd:PRK09236  417 TTFVNGQLVYHNGQL 431
allantoinase TIGR03178
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ...
 1467-1809 1.41e-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: 180.66  E-value: 1.41e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1467 LIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASS 1545
Cdd:TIGR03178   47 LVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVP 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1546 DNAALLPSIASSTA-GLKMYLN----DTYSTLKMDNVSLWMEHFEKwpKHLPIVAHAEK--------------------- 1599
Cdd:TIGR03178  127 YNLDDLRELDEAGVvGFKAFLSpsgdDEFPHVDDWQLYKGMRELAR--LGQLLLVHAENpaitsalgeeappqggvgada 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1600 -----------QTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKdKAQVRP 1668
Cdd:TIGR03178  205 ylasrpvfaevEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGT-LAKCAP 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1669 MLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISE---KPPPGYPGLETMLPLLFTAVSEGR-LTVDDIIKRLYENP 1742
Cdd:TIGR03178  284 PIRDLANQEGLWEALlnGLIDCVVSDHSPCTPDLKRAGdffKAWGGIAGLQSTLDVMFDEAVQKRgLPLEDIARLMATNP 363

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052  1743 RKIFSL-------PAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPP 1809
Cdd:TIGR03178  364 AKRFGLaqkgriaPGKDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP 437
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 1447-1812 7.35e-46

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: 172.79  E-value: 7.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1447 KQIGQ----APRVKThVDSmtSQKLIrLPGLIDVHVHLREP--GATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPN 1520
Cdd:cd01314    27 VAIGPnleaPGGVEV-IDA--TGKYV-LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1521 SFTMAQKLAKAGCRCDYALFVGASSDNAAL---LPSIA----SStagLKMYLndTYSTLKMDNVSLWMEHFEKwPKHLPI 1593
Cdd:cd01314   103 AVEKWRGKADGKSVIDYGFHMIITDWTDSVieeLPELVkkgiSS---FKVFM--AYKGLLMVDDEELLDVLKR-AKELGA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1594 VA--HAEKQTVA---------------------------------AILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGI 1638
Cdd:cd01314   177 LVmvHAENGDVIaelqkkllaqgktgpeyhalsrppeveaeatarAIRL-AELAGAPLYIVHVSSKEAADEIARARKKGL 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1639 QVTCEVAPHHLFLCEDNVPVIGKD--KAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISEKP-----PPG 1709
Cdd:cd01314   256 PVYGETCPQYLLLDDSDYWKDWFEgaKYVCSPPLRPKEDQEALWDGLssGTLQTVGSDHCPFNFAQKARGKDdftkiPNG 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1710 YPGLETMLPLLFTA-VSEGRLTVDDIIKRLYENPRKIFSLPAQEDTYVE--------VDLEQEWIIPKHMQFTKSKWTPF 1780
Cdd:cd01314   336 VPGVETRMPLLWSEgVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVgsdadlviWDPNAEKTISADTHHHNVDYNIF 415

                         410       420       430
                  ....*....|....*....|....*....|..
gi 688603052 1781 EGMKVKGKVMRVVLRGEVAYIDGQVLVPPGYG 1812
Cdd:cd01314   416 EGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
 1470-1816 9.28e-46

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: 172.96  E-value: 9.28e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1470 LPGLIDVHVHLREP--GATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSDN 1547
Cdd:TIGR02033   50 LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWN 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1548 AALLPS-----IASSTAGLKMYLndTYSTLKMDNVSLWMEHFEKWPKHLPIV-AHAEK---------------------- 1599
Cdd:TIGR02033  130 DSVLEEhipevKEEGINSFKVFM--AYKNLLMVDDEELFEILKRLKELGALLqVHAENgdiiaelqarmlaqgitgpeyh 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1600 ----------QTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKD--KAQVR 1667
Cdd:TIGR02033  208 alsrppeleaEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKPGFEgaKYVCS 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1668 PMLGTREDMEALWE--NLDIIDCFATDHAPHSAEEKIS------EKPPPGYPGLETMLPLLFTA-VSEGRLTVDDIIKRL 1738
Cdd:TIGR02033  288 PPLREPEDQDALWSalSSGALQTVGSDHCTFNFAQKKAigkddfTKIPNGGPGVEERMSLLFDEgVAKGRITLEKFVEVT 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1739 YENPRKIFSLPAQEDTYVE--------VDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPG 1810
Cdd:TIGR02033  368 STNPAKIFNLYPRKGTIAVgsdadiviWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAG 447


                   ....*.
gi 688603052  1811 YGQDVK 1816
Cdd:TIGR02033  448 AGRFVK 453
PRK06189 PRK06189
allantoinase; Provisional
 1470-1816 3.33e-45

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 171.04  E-value: 3.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSDNA 1548
Cdd:PRK06189   53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1549 ALLPSIASSTA-GLKMYLND--TYSTLKMDNVSLWmEHFEKWPKHLPIVA-HAEK-------QTVAA------------- 1604
Cdd:PRK06189  133 EHLRELAEAGViGFKAFMSNsgTDEFRSSDDLTLY-EGMKEIAALGKILAlHAESdaltrhlTTQARqqgktdvrdyles 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1605 ------------ILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKdKAQVRPMLGT 1672
Cdd:PRK06189  212 rpvvaeleavqrALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGA-VAKCAPPLRS 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1673 REDMEALWENL--DIIDCFATDHAPHSAEEKISE---KPPPGYPGLETMLPLLFT-AVSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:PRK06189  291 RSQKEELWRGLlaGEIDMISSDHSPCPPELKEGDdffLVWGGISGGQSTLLVMLTeGYIERGIPLETIARLLATNPAKRF 370

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052 1747 SLP-------AQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVlVPPGYGQDVK 1816
Cdd:PRK06189  371 GLPqkgrlevGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV-FPPPRGQLLR 446
PRK00779 PRK00779
ornithine carbamoyltransferase; Provisional
 1939-2241 1.07e-44

ornithine carbamoyltransferase; Provisional


Pssm-ID: 234835 [Multi-domain]  Cd Length: 304  Bit Score: 164.88  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1939 PLVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFceSTS 2018
Cdd:PRK00779    1 MLMGRHFLSLDDLSPEELEELLDLAAELKKKRKAGEPHPPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIFL--SPR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2019 STQ--KGESLVDSVNTMSCYADVIVLR---HPIpgaVESAARHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGM 2092
Cdd:PRK00779   79 DTQlgRGEPIEDTARVLSRYVDAIMIRtfeHET---LEELAEYSTVPVINGlTD--LSHPCQILADLLTIYEHRGSLKGL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2093 TITMVGDlkhGRTV-HSLARLLTQYRITLRYVAPKNLSMPAEIIDFVA-SKGIKQEEFNSIEEALPDTDVLY------MT 2164
Cdd:PRK00779  154 KVAWVGD---GNNVaNSLLLAAALLGFDLRVATPKGYEPDPEIVEKIAkETGASIEVTHDPKEAVKGADVVYtdvwvsMG 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688603052 2165 RiQKERfssEKEYNAcFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVL 2241
Cdd:PRK00779  231 Q-EAEA---EERLKA-FAPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEVIDGPQSVVWDEAENRLHAQKALLAWLL 304
pyrC PRK00369
dihydroorotase; Provisional
 1470-1810 3.61e-44

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 166.48  E-value: 3.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNsfTMAQKLA--KAGCRCDYALFVGASSD- 1546
Cdd:PRK00369   46 LPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPE--AITEKLAelEYYSRVDYFVYSGVTKDp 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1547 -NAALLPsiassTAGLKMYLND--TYSTLKMDNVS--LWMEHFE-----KWPKHLPIVAHAEkqtVAAILLVaQLYQRpV 1616
Cdd:PRK00369  124 eKVDKLP-----IAGYKIFPEDleREETFRVLLKSrkLKILHPEvplalKSNRKLRRNCWYE---IAALYYV-KDYQN-V 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1617 HICHVAKKEeilIIRAAKQKGIqvTCEVAPHHLFL-----CEDNV-PVIgKDKAQVRPMLgtredmEALWEnldiIDCFA 1690
Cdd:PRK00369  194 HITHASNPR---TVRLAKELGF--TVDITPHHLLVngekdCLTKVnPPI-RDINERLWLL------QALSE----VDAIA 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1691 TDHAPHSAEEKISEKP--PPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQE------DTYVEVDLEq 1762
Cdd:PRK00369  258 SDHAPHSSFEKLQPYEvcPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIPYGEikegyrANFTVIQFE- 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 688603052 1763 EWiiPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPG 1810
Cdd:PRK00369  337 DW--RYSTKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKG 382
PRK01211 PRK01211
dihydroorotase; Provisional
 1470-1798 4.78e-44

dihydroorotase; Provisional


Pssm-ID: 179247 [Multi-domain]  Cd Length: 409  Bit Score: 166.57  E-value: 4.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSDNAA 1549
Cdd:PRK01211   45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1550 LLPSIassTAGLKMYLNDTYSTLKMDNVSLWMEHFEKwpKHLPIVAHAEKQ------------------------TVAAI 1605
Cdd:PRK01211  125 ILDER---SIGLKVYMGGTTNTNGTDIEGGEIKKINE--ANIPVFFHAELSeclrkhqfesknlrdhdlarpiecEIKAV 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1606 LLVAQLYQRPVHICHVAKKEEILiiraakqkgiQVTCEVAPHHLFLcEDNVPV--IGKdkaqVRPMLGTREDMEALWENL 1683
Cdd:PRK01211  200 KYVKNLDLKTKIIAHVSSIDVIG----------RFLREVTPHHLLL-NDDMPLgsYGK----VNPPLRDRWTQERLLEEY 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1684 --DIIDCFATDHAPHSAEEKIS-EKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQ--EDTY--- 1755
Cdd:PRK01211  265 isGRFDILSSDHAPHTEEDKQEfEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKGkiEEGYdad 344

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 688603052 1756 -VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKvMRVVLRGEV 1798
Cdd:PRK01211  345 fMAFDFTNIKKINDKRLHSKCPVSPFNGFDAIFP-SHVIMRGEV 387
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1318-1444 1.11e-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: 155.15  E-value: 1.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1318 KNILLSIGSYkNKSELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEEESdcPNKDKQRNImdyLEENHFDL 1397
Cdd:cd01423     1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQ--NDKPSLREL---LAEGKIDL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 688603052 1398 VINLSMRNSGGRRLSsfvtkGYRTRRMAIDFSVPLITDIKCTKLFVQ 1444
Cdd:cd01423    75 VINLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
pyrB PRK13814
aspartate carbamoyltransferase;
1944-2243 3.77e-43

aspartate carbamoyltransferase;


Pssm-ID: 139876 [Multi-domain]  Cd Length: 310  Bit Score: 161.04  E-value: 3.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1944 HILSVRQFSKEQMSHLFNVA-HTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQK 2022
Cdd:PRK13814    7 HLLNMRSLTRDHIEKLIQRAnYFLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2023 GESLVDSVNTMSCYA-DVIVLRHPIPGAVESAARHCRRPV-INAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2100
Cdd:PRK13814   87 GETLFDTIKTLEAMGvYFFIVRHSENETPEQIAKQLSSGVvINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2101 KHGRTVHSLAR-LLTQYRITLRYVAPKNLsMPaeiiDFVASKGIKQeeFNSIEEALPDTDVLYMTRIQKERFSSEKEYNA 2179
Cdd:PRK13814  167 RHSRVANSLMDgLVTMGVPEIRLVGPSSL-LP----DKVGNDSIKK--FTELKPSLLNSDVIVTLRLQKERHDNSVDIDA 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688603052 2180 CFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR 2243
Cdd:PRK13814  240 FRGSFRLTPEKLYSAKPDAIVMHPGPvnREVEINSDVADNQQSVILQQVRNGVAMRMAVLELFLLR 305
PRK08323 PRK08323
phenylhydantoinase; Validated
 1470-1816 4.89e-40

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 156.10  E-value: 4.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREP--GATHKEDFSSGTAAALAGGITMVC--AMPNTNPAIIDpnSFTMAQKLAKAGCRCDYAlFVGASS 1545
Cdd:PRK08323   48 MPGGIDPHTHMEMPfgGTVSSDDFETGTRAAACGGTTTIIdfALQPKGQSLRE--ALEAWHGKAAGKAVIDYG-FHMIIT 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1546 D-NAALLPSIAS-STAG---LKMYLndTY-STLKMDNVSLwMEHFEKWPKH--LPIVaHAE---------KQTVA----- 1603
Cdd:PRK08323  125 DwNEVVLDEMPElVEEGitsFKLFM--AYkGALMLDDDEL-LRALQRAAELgaLPMV-HAEngdaiaylqAKLLAegktg 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1604 -------------------AILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKDKA 1664
Cdd:PRK08323  201 peyhalsrppevegeatnrAIML-AELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEG 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1665 QVR---PMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISE------KPPPGYPGLETMLPLLFTA-VSEGRLTVD 1732
Cdd:PRK08323  280 AKYvmsPPLRDKEHQDALWRGLqdGDLQVVATDHCPFCFEQKKQLgrgdftKIPNGTPGVEDRMPLLFSEgVMTGRITLN 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1733 DIIKRLYENPRKIFSLPAQEDTyVEV---------DLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDG 1803
Cdd:PRK08323  360 RFVELTSTNPAKIFGLYPRKGT-IAVgadadiviwDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDG 438

                         410
                  ....*....|...
gi 688603052 1804 QVLVPPGYGQDVK 1816
Cdd:PRK08323  439 EFRGKAGHGRFLK 451
OTCace pfam00185
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
2093-2240 1.22e-39

Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;


Pssm-ID: 425511 [Multi-domain]  Cd Length: 154  Bit Score: 145.06  E-value: 1.22e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  2093 TITMVGDlKHGRTVHSLARLLTQYRITLRYVAPKNLSMPAEIID----FVASKGIKQEEFNSIEEALPDTDVLYMTRIQK 2168
Cdd:pfam00185    1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVLDkakkIAEKSGGSIEITDDPAEAVKGADVVYTDVWQS 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688603052  2169 ERFSSEKE--YNAcFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATV 2240
Cdd:pfam00185   80 MGQEKEREerLKA-FKPYQVNEELMKLAKKDAIFMHCLPahRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLALL 154
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 1470-1813 2.70e-39

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 154.47  E-value: 2.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREP---GATHKEDFSSGTAAALAGGITMVC--AMPNTNPAIidPNSFTMAQKLAKAGCRCDYAL-FVGA 1543
Cdd:PRK13404   53 LPGGVDSHCHIDQPsgdGIMMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSL--REAVEDYHRRAAGKAVIDYAFhLIVA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1544 SSDNAAL---LPS-IASSTAGLKMYLndTYSTLKMDNV-------------SLWMEHFE-----KW------------PK 1589
Cdd:PRK13404  131 DPTEEVLteeLPAlIAQGYTSFKVFM--TYDDLKLDDRqildvlavarrhgAMVMVHAEnhdmiAWltkrllaagltaPK 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1590 H----LPIVAHAEKqTVAAILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKDKAQ 1665
Cdd:PRK13404  209 YhaisRPMLAEREA-THRAIAL-AELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDRPGMEGAK 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1666 --VRPMLGTREDMEALWENLD--IIDCFATDHAPHSAEEKISEKP----------PPGYPGLETMLPLLFTA-VSEGRLT 1730
Cdd:PRK13404  287 yiCSPPPRDKANQEAIWNGLAdgTFEVFSSDHAPFRFDDTDGKLAaganpsfkaiANGIPGIETRLPLLFSEgVVKGRIS 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1731 VDDIIKRLYENPRKIFSLPAQEDTYV---EVDL-----EQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYID 1802
Cdd:PRK13404  367 LNRFVALTSTNPAKLYGLYPRKGAIAigaDADIaiwdpDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVED 446

                         410
                  ....*....|.
gi 688603052 1803 GQVLVPPGYGQ 1813
Cdd:PRK13404  447 GELVAERGSGQ 457
pyrB PRK13376
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ...
 1942-2242 2.76e-37

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


Pssm-ID: 237369 [Multi-domain]  Cd Length: 525  Bit Score: 149.53  E-value: 2.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1942 GQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLD---ILKGKV-MASMFYEVSTRTSSSF--AAAMHRlGGSVVHFCE 2015
Cdd:PRK13376    7 GRTLAVIEDLSVEEQLFLYEKTRELKQRWYEGEDVSefrIKKRDVgIYIVFVEPSTRTKESFinAAKFHK-NVKVNIFDS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2016 STSSTQKGESLVDSVNTMSCYAD--VIVLRHPIPG--------AVESAARH-CRRPV-INAGDGVGEHPTQALLDIFTIR 2083
Cdd:PRK13376   86 EHSSFNKQESYTDTFNMLTGYSDysIFIVRTRLEGvcrlleekVSEFASRNgIEVPAfINAGDGKHEHPTQELLDEFTFL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2084 EELGTVNG-MTITMVGDLKHGRTVHSLARLLTQYR-ITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVL 2161
Cdd:PRK13376  166 EQNNFDNSfIHIALVGDLLHGRTVHSKVNGLKIFKnVKVDLIAPEELAMPEHYVEKMKKNGFEVRIFSSIEEYLSQKDVA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2162 ---YMTRIQKERFSS---EKEY----NACFGQFILtPHIMTGAKrkmvVMHPLPRVN---EISVEVDTDPRAAYFRQAEN 2228
Cdd:PRK13376  246 kiwYFTRLQLERMGEdilEKEHilrkAVTFRKEFL-DKLPEGVK----FYHPLPRHKvypTIPTFLDTLPLNGWETQAIN 320

                         330
                  ....*....|....
gi 688603052 2229 GMYIRMALLATVLG 2242
Cdd:PRK13376  321 GYWVRIVLLSMLGG 334
PLN02342 PLN02342
ornithine carbamoyltransferase
 1911-2242 3.60e-37

ornithine carbamoyltransferase


Pssm-ID: 177976 [Multi-domain]  Cd Length: 348  Bit Score: 144.55  E-value: 3.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1911 PPPLARILSPQAGQP-QILPHPQTSPLLHPLVG----QHILSVRQFSKEQMSHLFNVAHTLRLMVQK-ERPLDILKGKVM 1984
Cdd:PLN02342    9 RSPSAVSSSSRARRGlVVCAASSSAAAPSPIKGkskpKHFLHIDDFDKEEILGLLDRAKEVKALLKSgDRSFQPFKGKSM 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1985 ASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINA 2064
Cdd:PLN02342   89 AMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQLGKREETRDIARVLSRYNDIIMARVFAHQDVLDLAEYSSVPVING 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2065 GDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkHGRTVHSLARLLTQYRITLRYVAPKNLSMPAEIIDFVASKGI- 2143
Cdd:PLN02342  169 LTDY-NHPCQIMADALTIIEHIGRLEGTKVVYVGD--GNNIVHSWLLLAAVLPFHFVCACPKGYEPDAKTVEKARAAGIs 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2144 KQEEFNSIEEALPDTDVLY------MTriQKERFSSEKEynaCFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVD 2215
Cdd:PLN02342  246 KIEITNDPAEAVKGADVVYtdvwasMG--QKEEAEKRKK---AFQGFQVNEALMKLAGPQAYFMHCLPaeRGVEVTDGVM 320

                         330       340
                  ....*....|....*....|....*..
gi 688603052 2216 TDPRAAYFRQAENGMYIRMALLATVLG 2242
Cdd:PLN02342  321 EAPNSIVFPQAENRMHAQNAIMLHQLG 347
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 803-883 2.79e-36

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: 132.50  E-value: 2.79e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   803 EELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKqdeSAMPPEIMRKAKQLGFSDKQIA 882
Cdd:pfam02787    1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAG---LDLDAELLREAKRLGFSDRQIA 77


                   .
gi 688603052   883 Q 883
Cdd:pfam02787   78 K 78
PRK07369 PRK07369
dihydroorotase; Provisional
 1465-1792 4.90e-33

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 134.34  E-value: 4.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1465 QKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGC--RCDY--ALF 1540
Cdd:PRK07369   51 SGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPLDNPATLARLQQQAQQIPpvQLHFwgALT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1541 VGASSDNAALLPSIASSTA-G------------LKMYLndTYSTLKMDNVSLWMEHFE----------KWPKHL---PIV 1594
Cdd:PRK07369  131 LGGQGKQLTELAELAAAGVvGftdgqplenlalLRRLL--EYLKPLGKPVALWPCDRSlagngvmregLLALRLglpGDP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1595 AHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLcedNVPVIGKDKAQVR--PMLGT 1672
Cdd:PRK07369  209 ASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLL---DTEALASYDPNLRldPPLGN 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1673 REDMEALWENLD--IIDCFATDHAPHSAEEKI---SEKpPPGYPGLETMLPLLF-TAVSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:PRK07369  286 PSDRQALIEGVRtgVIDAIAIDHAPYTYEEKTvafAEA-PPGAIGLELALPLLWqNLVETGELSALQLWQALSTNPARCL 364

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 688603052 1747 SL------PAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRV 1792
Cdd:PRK07369  365 GQeppslaPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRVLQT 416
PRK07627 PRK07627
dihydroorotase; Provisional
 1441-1800 3.07e-32

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 132.11  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1441 LFVQALK--QIGQAP---RVKTHVDSmtsQKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPA 1515
Cdd:PRK07627   23 LYVAAGKiaAIGQAPagfNADKTIDA---SGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1516 IIDPNSFTM----AQK--------------------------LAKAGCrcdyalfVGASS------DNAALLPSIA-SST 1558
Cdd:PRK07627  100 LDEPGLVEMlkfrARNlnqahvyplgaltvglkgevltemveLTEAGC-------VGFSQanvpvvDTQVLLRALQyAST 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1559 AGLKMYLNDTYSTLKMDNVSlwmeHFEKWPKHL---PIVAHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQ 1635
Cdd:PRK07627  173 FGFTVWLRPLDAFLGRGGVA----ASGAVASRLglsGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1636 KGIQVTCEVAPHHLFLCEDNvpvIGKDKAQVR--PMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKI---SEKpPP 1708
Cdd:PRK07627  249 EGLPVTCDVGVNHVHLIDVD---IGYFDSQFRldPPLRSQRDREAIRAALadGTIDAICSDHTPVDDDEKLlpfAEA-TP 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1709 GYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQE-------DTYVeVDLEQEWIIPKHMQFTKSKWTPFE 1781
Cdd:PRK07627  325 GATGLELLLPLTLKWADEAKVPLARALARITSAPARVLGLPAGRlaegapaDLCV-FDPDAHWRVEPRALKSQGKNTPFL 403

                         410
                  ....*....|....*....
gi 688603052 1782 GMKVKGKVMRVVLRGEVAY 1800
Cdd:PRK07627  404 GYELPGRVRATLVAGQVAF 422
PLN02795 PLN02795
allantoinase
 1470-1803 3.31e-32

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 133.75  E-value: 3.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSDNA 1548
Cdd:PLN02795   98 MPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPENA 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1549 A---LLPSIASSTA-GLKMYL-----NDTYSTLKmdnvslwmEHFEKWPKHL-----PIVAHAEKQTVAAI--------- 1605
Cdd:PLN02795  178 HnasVLEELLDAGAlGLKSFMcpsgiNDFPMTTA--------THIKAALPVLakygrPLLVHAEVVSPVESdsrldadpr 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1606 LLVAQLYQRP----------------------------VHICHVAKKEEIL-IIRAAKQKGIQVTCEVAPHHL-FLCEDn 1655
Cdd:PLN02795  250 SYSTYLKSRPpsweqeairqllevakdtrpggvaegahVHIVHLSDAESSLeLIKEAKAKGDSVTVETCPHYLaFSAEE- 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1656 VPViGKDKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISE-----KPPPGYPGLETMLPLLFTAVSEGR 1728
Cdd:PLN02795  329 IPD-GDTRYKCAPPIRDAANRELLWKALldGDIDMLSSDHSPSPPDLKLLEegnflRAWGGISSLQFVLPATWTAGRAYG 407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1729 LTVDDIIKRLYENPRKIFSLPA--------QEDTYV-----EVDLEQEWIIpkhmQFTKSKWTPFEGMKVKGKVMRVVLR 1795
Cdd:PLN02795  408 LTLEQLARWWSERPAKLAGLDSkgaiapgkDADIVVwdpeaEFVLDESYPI----YHKHKSLSPYLGTKLSGKVIATFVR 483


                  ....*...
gi 688603052 1796 GEVAYIDG 1803
Cdd:PLN02795  484 GNLVFLEG 491
PRK08044 PRK08044
allantoinase AllB;
1462-1800 1.04e-30

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 128.05  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1462 MTSQKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNSFTMAQKLAKAGCRCDYALF 1540
Cdd:PRK08044   44 MDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1541 VGASSDNAALLPSIAS-STAGLKMYLN--------------DTYSTLK---------------MDNVSLWMEHFEKWPKH 1590
Cdd:PRK08044  124 GGLVSYNLDRLHELDEvGVVGFKCFVAtcgdrgidndfrdvNDWQFYKgaqklgelgqpvlvhCENALICDELGEEAKRE 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1591 LPIVAHA---------EKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGK 1661
Cdd:PRK08044  204 GRVTAHDyvasrpvftEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGT 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1662 dKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISE--KPPPGYPGLETMLPLLF-TAVSEGRLTVDDIIK 1736
Cdd:PRK08044  284 -LAKCSPPIRDLENQKGMWEKLfnGEIDCLVSDHSPCPPEMKAGNimEAWGGIAGLQNCMDVMFdEAVQKRGMSLPMFGK 362

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688603052 1737 RLYENPRKIFSL-------PAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAY 1800
Cdd:PRK08044  363 LMATNAADIFGLqqkgriaPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
PRK09059 PRK09059
dihydroorotase; Validated
 1465-1800 1.69e-27

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 118.21  E-value: 1.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1465 QKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKagcrcDYAL----- 1539
Cdd:PRK09059   54 AGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDVALVEFVKRTAR-----DTAIvnihp 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1540 -------FVGASSDNAALLpsiasSTAGLKMYLNDTYS---TLKMDNVSLWMEHFEkwpkhLPIVAHAEKQTVAA----- 1604
Cdd:PRK09059  129 aaaitkgLAGEEMTEFGLL-----RAAGAVAFTDGRRSvanTQVMRRALTYARDFD-----AVIVHETRDPDLGGngvmn 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1605 -------------------ILL-----VAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNvpvIG 1660
Cdd:PRK09059  199 eglfaswlglsgipreaevIPLerdlrLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNEND---IG 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1661 KDKAQVR--PMLGTREDMEALWENLD--IIDCFATDHAPHSAEEK---ISEKPPpGYPGLETMLPLLFTAVSEGRLTVDD 1733
Cdd:PRK09059  276 EYRTFFKlsPPLRTEDDRVAMVEAVAsgTIDIIVSSHDPQDVDTKrlpFSEAAA-GAIGLETLLAAALRLYHNGEVPLLR 354

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052 1734 IIKRLYENPRKIFSLP-------AQEDTYVeVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAY 1800
Cdd:PRK09059  355 LIEALSTRPAEIFGLPagtlkpgAPADIIV-IDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVY 427
PRK14805 PRK14805
ornithine carbamoyltransferase; Provisional
 1943-2242 2.45e-27

ornithine carbamoyltransferase; Provisional


Pssm-ID: 237819 [Multi-domain]  Cd Length: 302  Bit Score: 114.40  E-value: 2.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1943 QHILSVRQFSKEQMSHLFNVAHTLrlmvqKERPLD---ILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSS 2019
Cdd:PRK14805    2 KHLLSIKELTQQQLLDLLALAKTI-----KANPAEyrqALAGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2020 TQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGD 2099
Cdd:PRK14805   77 LGKRESVADFAANLSCWADAIVARVFSHSTIEQLAEHGSVPVINALCDL-YHPCQALADFLTLAEQFGDVSKVKLAYVGD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2100 lkhGRTV-HSLARLLTQYRITLRYVAPKNLSMPAEII----DFVASKGIKQEEFNSIeEALPDTDVLYM-TRIQKERFSS 2173
Cdd:PRK14805  156 ---GNNVtHSLMYGAAILGATMTVICPPGHFPDGQIVaeaqELAAKSGGKLVLTSDI-EAIEGHDAIYTdTWISMGDDTP 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688603052 2174 EKEYNACFGQFILTPHIM--TGAKRkmvVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2242
Cdd:PRK14805  232 LAEIKAKFAPYQVNKALMekAGATF---VMHCQPahRGVEITSEVMDGEGSLILQQAENRMHAQNAVLVTLLS 301
PRK02102 PRK02102
ornithine carbamoyltransferase; Validated
 1940-2242 1.24e-25

ornithine carbamoyltransferase; Validated


Pssm-ID: 179366 [Multi-domain]  Cd Length: 331  Bit Score: 110.36  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1940 LVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSS 2019
Cdd:PRK02102    5 LKGRSFLKLLDFTPEEIEYLIDLSIELKAAKKAGIEHQYLEGKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLGPNDSQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2020 TQKGESLVDSVNTMSCYADVIVLR---HPIpgaVESAARHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITM 2096
Cdd:PRK02102   85 LGKKESIEDTARVLGRMYDGIEYRgfkQEI---VEELAKYSGVPVWNGLTDE-WHPTQMLADFMTMKEHFGPLKGLKLAY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2097 VGDlkhGR--TVHSL----ARLLTQYRItlryVAPKNLSMPAEIIDfvASKGIKQEEFNSI------EEALPDTDVLYmT 2164
Cdd:PRK02102  161 VGD---GRnnMANSLmvggAKLGMDVRI----CAPKELWPEEELVA--LAREIAKETGAKItitedpEEAVKGADVIY-T 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2165 RI---------QKERFSSEKEYNacfgqfILTPHIMTGAKRKMVVMHPLP-----------------RVNEISV--EVDT 2216
Cdd:PRK02102  231 DVwvsmgeedeWEERIKLLKPYQ------VNMDLMKATGNPDVIFMHCLPafhdtetkvgkeiaekyGLKGLEVtdEVFE 304

                         330       340
                  ....*....|....*....|....*.
gi 688603052 2217 DPRAAYFRQAENGMYIRMALLATVLG 2242
Cdd:PRK02102  305 SKYSIVFDEAENRMHTIKAVMVATLG 330
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 191-342 1.82e-24

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: 102.61  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  191 YNQIRCLCQRGARVTVVPWDQPLDSN----DFDGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLVI 266
Cdd:cd01743    12 YNLVQYLRELGAEVVVVRNDEITLEElellNPDAIVISPGPGHPEDAGISLEIIRALA---GKVPILGVCLGHQAIAEAF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  267 GAKTYKMKYGNRG------HNQPCIHKGTSR-----CYitsqnHGFAVDPETLPKDWDVLftnanDQTSEGIV----HNH 331
Cdd:cd01743    89 GGKVVRAPEPMHGktseihHDGSGLFKGLPQpftvgRY-----HSLVVDPDPLPDLLEVT-----ASTEDGVImalrHRD 158

                         170
                  ....*....|.
gi 688603052  332 KPLFSVQFHPE 342
Cdd:cd01743   159 LPIYGVQFHPE 169
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1074-1250 3.21e-22

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: 96.99  E-value: 3.21e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1074 SDTESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDTDMEKFLSSAVAVSKE----HPVVISKFIQEAKEIDVDAVAcDG 1149
Cdd:pfam02786   25 ETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnPQVLVEKSLKGPKHIEYQVLR-DA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1150 EVIAIAVSEhVENA-GVHSGDATLVTPPQDINQKTMERIKMIVHAIGQELQVTGPFNLQLI--AKDDQLKVIECNVRVSR 1226
Cdd:pfam02786  104 HGNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQV 182

                          170       180
                   ....*....|....*....|....
gi 688603052  1227 SFPYVSKTLGVDLVALATRVILGE 1250
Cdd:pfam02786  183 EHALAEKATGYDLAKEAAKIALGY 206
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1332-1434 4.91e-22

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: 92.17  E-value: 4.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1332 ELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEEesDCPNKDKQrnIMDYLEENHFDLVINLSMRNSGGRRl 1411
Cdd:pfam02142    1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGE--GRPGGRVQ--IGDLIKNGEIDLVINTLYPFKATVH- 75

                           90       100
                   ....*....|....*....|...
gi 688603052  1412 ssfvtKGYRTRRMAIDFSVPLIT 1434
Cdd:pfam02142   76 -----DGYAIRRAAENIDIPGPT 93
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 1034-1252 4.51e-21

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: 95.32  E-value: 4.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1034 RQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDTDME 1113
Cdd:COG0439    36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1114 KFLSSAVA----VSKEHPVVISKFIqEAKEIDVDAVACDGEVIAIAVSEHvENAGVHSGDATLVTPPqDINQKTMERIKM 1189
Cdd:COG0439   116 AALAEARAeakaGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGE 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052 1190 IVHAIGQELQV-TGPFNLQ-LIAKDDQLKVIECNVRVS--RSFPYVSKTLGVDLVALATRVILGEEV 1252
Cdd:COG0439   193 LVARALRALGYrRGAFHTEfLLTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 191-342 1.42e-19

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: 88.56  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  191 YNQIRCLCQRGARVTVVPWDQP----LDSNDFDGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLVI 266
Cdd:COG0512    12 YNLVQYLGELGAEVVVVRNDEItleeIEALAPDGIVLSPGPGTPEEAGISLEVIRAFA---GKIPILGVCLGHQAIGEAF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  267 GAKTYKMKygnrghnQPcIHKGTSRCYITSQN--------------HGFAVDPETLPkdwDVLFTNAndQTSEGIV---- 328
Cdd:COG0512    89 GGKVVRAP-------EP-MHGKTSPITHDGSGlfaglpnpftatryHSLVVDRETLP---DELEVTA--WTEDGEImgir 155

                         170
                  ....*....|....
gi 688603052  329 HNHKPLFSVQFHPE 342
Cdd:COG0512   156 HRELPIEGVQFHPE 169
PRK04284 PRK04284
ornithine carbamoyltransferase; Provisional
 1940-2243 5.55e-19

ornithine carbamoyltransferase; Provisional


Pssm-ID: 235269 [Multi-domain]  Cd Length: 332  Bit Score: 90.57  E-value: 5.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1940 LVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSS 2019
Cdd:PRK04284    4 LRNRSFLTLLDFTPKEIEYLLDLSEDLKRAKYAGIEVQKLKGKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGPTGSQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2020 TQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINaGDGVGEHPTQALLDIFTIREEL-GTVNGMTITMVG 2098
Cdd:PRK04284   84 MGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSGVPVWN-GLTDEDHPTQVLADFLTAKEHLkKPYKDIKFTYVG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2099 DlkhGR--TVHSLARLLTQYRITLRYVAPKNLSMPAEIID----FVASKGIKQEEFNSIEEALPDTDVLYM--------- 2163
Cdd:PRK04284  163 D---GRnnVANALMQGAAIMGMDFHLVCPKELNPDDELLNkckeIAAETGGKITITDDIDEGVKGSDVIYTdvwvsmgep 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2164 TRIQKERFSSEKEYNacfgqfiLTPHIMTGAKRKMVV-MHPLPRVN-------------------EISVEVDTDPRAAYF 2223
Cdd:PRK04284  240 DEVWEERIKLLKPYQ-------VNKEMMKKTGNPNAIfEHCLPSFHdldtkvgkeifekyglkemEVTDEVFESKASVVF 312

                         330       340
                  ....*....|....*....|
gi 688603052 2224 RQAENGMYIRMALLATVLGR 2243
Cdd:PRK04284  313 DEAENRMHTIKAVMVATLGE 332
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 191-342 9.59e-19

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: 86.38  E-value: 9.59e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   191 YNQIRCLCQRGARVtVVPWDQPLDSNDFDGLF-----ISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLV 265
Cdd:TIGR00566   13 YNLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTPNEAGISLEAIRHFA---GKLPILGVCLGHQAMGQA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   266 IGAKT---YKMKYG---NRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHKPLFSVQF 339
Cdd:TIGR00566   89 FGGDVvraNTVMHGktsEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQF 168


                   ...
gi 688603052   340 HPE 342
Cdd:TIGR00566  169 HPE 171
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 191-342 1.04e-17

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 83.26  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  191 YN---QIRCLcqrGARVTVVPWDQP----LDSNDFDGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLS 263
Cdd:PRK05670   13 YNlvqYLGEL---GAEVVVYRNDEItleeIEALNPDAIVLSPGPGTPAEAGISLELIREFA---GKVPILGVCLGHQAIG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  264 LVIGA-----------KTYKMKygnrgHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTnANDQTSEGIVHNHK 332
Cdd:PRK05670   87 EAFGGkvvrakeimhgKTSPIE-----HDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAW-TDDGEIMGVRHKEL 160

                         170
                  ....*....|
gi 688603052  333 PLFSVQFHPE 342
Cdd:PRK05670  161 PIYGVQFHPE 170
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
191-342 4.37e-17

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 82.40  E-value: 4.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  191 YNQIRCLCQRGARVTVVPWDQP------LDSNDFDGLFISNGPGNPEYCKETVENIRkvACVENPKPIFGICLGHQLLSL 264
Cdd:PRK07765   14 FNLVQYLGQLGVEAEVWRNDDPrladeaAVAAQFDGVLLSPGPGTPERAGASIDMVR--ACAAAGTPLLGVCLGHQAIGV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  265 VIGA-----------KTYKMKYGNRGhnqpcIHKGTSRCYITSQNHGFAVDPETLPKDWDVLftnanDQTSEGIV----H 329
Cdd:PRK07765   92 AFGAtvdrapellhgKTSSVHHTGVG-----VLAGLPDPFTATRYHSLTILPETLPAELEVT-----ARTDSGVImavrH 161

                         170
                  ....*....|...
gi 688603052  330 NHKPLFSVQFHPE 342
Cdd:PRK07765  162 RELPIHGVQFHPE 174
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 181-342 6.50e-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: 81.92  E-value: 6.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  181 RITAIDCGI---KYNQI--RCLCQRGARVTVV--------PWDQPLDsnDFDGLFISNGPGNP----EYCKETVENIRKV 243
Cdd:COG0518     1 KILILDHDPfggQYPGLiaRRLREAGIELDVLrvyageilPYDPDLE--DPDGLILSGGPMSVydedPWLEDEPALIREA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  244 acVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRG------HNQPCIHKGTSRCYITSQNHGFAVDpeTLPKDWDVLFT 317
Cdd:COG0518    79 --FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelTEADPLFAGLPDEFTVWMSHGDTVT--ELPEGAEVLAS 154

                         170       180
                  ....*....|....*....|....*
gi 688603052  318 NANDQTsEGIVHNhKPLFSVQFHPE 342
Cdd:COG0518   155 SDNCPN-QAFRYG-RRVYGVQFHPE 177
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1332-1434 5.12e-16

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: 75.20  E-value: 5.12e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   1332 ELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMA--VDWPFEEesdcpnkdkQRNIMDYLEENHFDLVINLSMRNSggr 1409
Cdd:smart00851    1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVVKtlHPKVHGG---------IPQILDLIKNGEIDLVINTLYPFE--- 68

                            90       100
                    ....*....|....*....|....*
gi 688603052   1410 rlSSFVTKGYRTRRMAIDFSVPLIT 1434
Cdd:smart00851   69 --AQAHEDGYSIRRAAENIDIPGPT 91
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 1473-1745 5.69e-16

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: 80.46  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1473 LIDVHVHLREPGATH------------------KEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCR 1534
Cdd:cd01292     1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1535 CDYALFVGASSDNA------------ALLPSIASSTAGLKMYLNDTYSTLKMDNVslwMEHFEKWPKH-LPIVAHAEKQT 1601
Cdd:cd01292    81 IRVVLGLGIPGVPAavdedaeallleLLRRGLELGAVGLKLAGPYTATGLSDESL---RRVLEEARKLgLPVVIHAGELP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1602 VA--AILLVAQLYQRP--VHICHVA---KKEEILIIRAakqkgiQVTCEVAPHHLFLcednvpvigkdkaqvrpMLGTRE 1674
Cdd:cd01292   158 DPtrALEDLVALLRLGgrVVIGHVShldPELLELLKEA------GVSLEVCPLSNYL-----------------LGRDGE 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688603052 1675 DMEALWENLD--IIDCFATDHAPHsaeekisekpppgypGLETMLPLLFTAVSE---GRLTVDDIIKRLYENPRKI 1745
Cdd:cd01292   215 GAEALRRLLElgIRVTLGTDGPPH---------------PLGTDLLALLRLLLKvlrLGLSLEEALRLATINPARA 275
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 194-344 1.13e-15

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: 77.29  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  194 IRCLCQRGARVTVVPW---DQPLDSNDFDGLFISNGPGNPEYC-----KETVENIRKvaCVENPKPIFGICLGHQLLSLV 265
Cdd:cd01741    20 LREAGAETIEIDVVDVyagELLPDLDDYDGLVILGGPMSVDEDdypwlKKLKELIRQ--ALAAGKPVLGICLGHQLLARA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  266 IGAKTYKMKYGnrghnqPCIhkGTSRCYITSQNH---GFAVDPET-------------LPKDWDVLFTNANDqtsegivH 329
Cdd:cd01741    98 LGGKVGRNPKG------WEI--GWFPVTLTEAGKadpLFAGLPDEfpvfhwhgdtvveLPPGAVLLASSEAC-------P 162

                         170       180
                  ....*....|....*....|
gi 688603052  330 NH-----KPLFSVQFHPEHM 344
Cdd:cd01741   163 NQafrygDRALGLQFHPEER 182
PRK03515 PRK03515
ornithine carbamoyltransferase subunit I; Provisional
 1937-2241 1.62e-15

ornithine carbamoyltransferase subunit I; Provisional


Pssm-ID: 179587 [Multi-domain]  Cd Length: 336  Bit Score: 80.14  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1937 LHPLVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVhfCES 2016
Cdd:PRK03515    1 MNQFYQRHFLRLLDFTPAELNSLLQLAAKLKADKKNGKEEQKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVT--YLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2017 TSSTQKG--ESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINagdGVGE--HPTQALLDIFTIREEL--GTVN 2090
Cdd:PRK03515   79 PSGSQIGhkESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYAGVPVWN---GLTNefHPTQLLADLLTMQEHLpgKAFN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2091 GMTITMVGDLKH--GRTVHSLARLLTqyrITLRYVAPK----NLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYM- 2163
Cdd:PRK03515  156 EMTLAYAGDARNnmGNSLLEAAALTG---LDLRLVAPKacwpEAALVTECRALAQKNGGNITLTEDIAEGVKGADFIYTd 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2164 --------TRIQKERFSSEKEYNACFGQFILT--PHI------------MTGAKRKMVVMHPLPRVNEISVEVDTDPRAA 2221
Cdd:PRK03515  233 vwvsmgepKEVWAERIALLRPYQVNSKMMQLTgnPQVkflhclpafhddQTTLGKKMAEEYGLHGGMEVTDEVFESAHSI 312

                         330       340
                  ....*....|....*....|.
gi 688603052 2222 YFRQAENGMY-IRMALLATVL 2241
Cdd:PRK03515  313 VFDQAENRLHtIKAVMVATLS 333
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 182-342 1.86e-15

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: 76.58  E-value: 1.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   182 ITAIDCGIKYNQI--RCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPgNPEYCKETVENIRKVacVENPKPIFGIC 256
Cdd:TIGR00888    1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTTPLEeirEKNPKGIILSGGP-SSVYAENAPRADEKI--FELGVPVLGIC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   257 LGHQLLSLVIGAKTYKMKYGNRGH------NQPCIHKGTSRCYITSQNHGFAVdpETLPKDWDVLFTNANDQTsEGIVHN 330
Cdd:TIGR00888   78 YGMQLMAKQLGGEVGRAEKREYGKaeleilDEDDLFRGLPDESTVWMSHGDKV--KELPEGFKVLATSDNCPV-AAMAHE 154

                          170
                   ....*....|..
gi 688603052   331 HKPLFSVQFHPE 342
Cdd:TIGR00888  155 EKPIYGVQFHPE 166
MGS_CPS_II cd01424
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ...
 1319-1436 2.17e-15

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: 74.05  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1319 NILLSIgSYKNKSELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVdwpfeeesdcpNKDKQR--NIMDYLEENHFD 1396
Cdd:cd01424     2 TVFISV-ADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVV-----------NKVSEGrpNIVDLIKNGEIQ 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 688603052 1397 LVINLSmrnSGGRrlssFVTKGYRTRRMAIDFSVPLITDI 1436
Cdd:cd01424    70 LVINTP---SGKR----AIRDGFSIRRAALEYKVPYFTTL 102
PLN02942 PLN02942
dihydropyrimidinase
 1470-1816 3.19e-15

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 81.04  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVHLREP--GATHKEDFSSGTAAALAGGITMVC--AMPnTNPAIIDpnSFTMAQKLAKAGCrCDYALFVGAS- 1544
Cdd:PLN02942   56 MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTMHIdfVIP-VNGNLLA--GYEAYEKKAEKSC-MDYGFHMAITk 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1545 -SDNAALLPSIASSTAGL---KMYLndTYSTLKMDNVSLWMEHFEKWPK--HLPIVaHAE-------------------- 1598
Cdd:PLN02942  132 wDDTVSRDMETLVKEKGInsfKFFM--AYKGSLMVTDELLLEGFKRCKSlgALAMV-HAEngdavfegqkrmielgitgp 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1599 -------------KQTVAAILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLceDNVPVIGKD--- 1662
Cdd:PLN02942  209 eghalsrppllegEATARAIRL-AKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVL--DDSKLWDPDfti 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1663 --KAQVRPMLGTREDMEALWENLD--IIDCFATDHAPHSAEEKIS-----EKPPPGYPGLETMLPLLF-TAVSEGRLTVD 1732
Cdd:PLN02942  286 asKYVMSPPIRPAGHGKALQAALSsgILQLVGTDHCPFNSTQKAFgkddfRKIPNGVNGIEERMHLVWdTMVESGQISPT 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1733 DIIKRLYENPRKIFS--------LPAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQ 1804
Cdd:PLN02942  366 DYVRVTSTECAKIFNiyprkgaiLAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGE 445

                         410
                  ....*....|..
gi 688603052 1805 VLVPPGYGQDVK 1816
Cdd:PLN02942  446 LKVVRGSGRYIE 457
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 505-716 7.21e-15

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: 76.83  E-value: 7.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  505 GTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAF 584
Cdd:COG0439    43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  585 AHT------SQVLVDKSLKGwKEIEYEVVrdAYDNCVTVCNM---ENIDPLGIHTGEsivVAPSQtLNDYEYNMLRNTAI 655
Cdd:COG0439   123 AEAkagspnGEVLVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVA 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052  656 KVIRHLGVV-GECNIQYALNPESEqYYIIEVNARLS--RSSALASKATGYPLAYVAAKLSLGIP 716
Cdd:COG0439   196 RALRALGYRrGAFHTEFLLTPDGE-PYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
PRK12562 PRK12562
ornithine carbamoyltransferase subunit F; Provisional
 1943-2243 9.48e-15

ornithine carbamoyltransferase subunit F; Provisional


Pssm-ID: 105755  Cd Length: 334  Bit Score: 77.79  E-value: 9.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1943 QHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQK 2022
Cdd:PRK12562    7 KHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2023 GESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINaGDGVGEHPTQALLDIFTIREEL--GTVNGMTITMVGDL 2100
Cdd:PRK12562   87 KESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWN-GLTNEFHPTQLLADLLTMQEHLpgKAFNEMTLVYAGDA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2101 KH--GRTVHSLARLLTqyrITLRYVAPK----NLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLY------MTRIQK 2168
Cdd:PRK12562  166 RNnmGNSMLEAAALTG---LDLRLVAPQacwpEASLVAECSALAQKHGGKITLTEDIAAGVKGADFIYtdvwvsMGEPKE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2169 ---ERFSSEKEYNACFGQFILT--PHI------------MTGAKRKMVVMHPLPRVNEISVEVDTDPRAAYFRQAENGMY 2231
Cdd:PRK12562  243 kwaERIALLRGYQVNSKMMALTgnPQVkflhclpafhddQTTLGKKMAKEFGLHGGMEVTDEVFESPASIVFDQAENRMH 322

                         330
                  ....*....|..
gi 688603052 2232 IRMALLATVLGR 2243
Cdd:PRK12562  323 TIKAVMVATLAK 334
PRK08417 PRK08417
metal-dependent hydrolase;
1470-1800 9.50e-15

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 78.59  E-value: 9.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1470 LPGLIDVHVhlrepgATHKEDFSSGT-----AAALAGGITMVCAMPNTNPAIIDPNSFTMAQ------------------ 1526
Cdd:PRK08417   29 LPALVDLNV------SLKNDSLSSKNlksleNECLKGGVGSIVLYPDSTPAIDNEIALELINsaqrelpmqifpsirald 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1527 ---KLA------KAGCRCDYAlfvgASSDNAALLPSIA------SSTAGLKMYLNDTYSTLKMDNVSLWMEhfekwpKHL 1591
Cdd:PRK08417  103 edgKLSniatllKKGAKALEL----SSDLDANLLKVIAqyakmlDVPIFCRCEDSSFDDSGVMNDGELSFE------LGL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1592 P-IVAHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFL----CED-NVpvigkdKAQ 1665
Cdd:PRK08417  173 PgIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILddsaCENfNT------AAK 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1666 VRPMLGTREDMEALWENLD--IIDCFATDHAPHSAEEK--ISEKPPPGYPGLETMLPLLFT-AVSEGRLTVDDIIKRLYE 1740
Cdd:PRK08417  247 LNPPLRSKEDRLALLEALKegKIDFLTSLHSAKSNSKKdlAFDEAAFGIDSICEYFSLCYTyLVKEGIITWSELSRFTSY 326

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688603052 1741 NPRKIFSLPAQEDT------YVEVDLEQEWIIPKhmqftksKWTPFEGMKVKGKVMRVVLRGEVAY 1800
Cdd:PRK08417  327 NPAQFLGLNSGEIEvgkeadLVLFDPNESTIIDD-------NFSLYSGDELYGKIEAVIIKGKLYL 385
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 1032-1254 1.99e-14

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 76.85  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1032 LHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTES--AVNFCETVGYPCLVRPSYVLSGAAMNVAYSD 1109
Cdd:PRK12767   91 FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDfkAALAKGELQFPLFVKPRDGSASIGVFKVNDK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1110 TDMEKFLSSAVavskehPVVISKFIQEaKEIDVDA-VACDGEVIAIAVSEHVEnagVHSGDA-TLVTPPQDINQKTMERI 1187
Cdd:PRK12767  171 EELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETsKGVTVKDPELFKLAERL 240

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052 1188 kmivhaiGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPyVSKTLGVDLVALATRVILGEEVEA 1254
Cdd:PRK12767  241 -------AEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYP-LSYMAGANEPDWIIRNLLGGENEP 299
PRK14804 PRK14804
ornithine carbamoyltransferase; Provisional
 1943-2241 1.42e-13

ornithine carbamoyltransferase; Provisional


Pssm-ID: 173265 [Multi-domain]  Cd Length: 311  Bit Score: 73.91  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1943 QHILSVRQFSKEQMSHLFNVAhtlrLMVQKERP--LDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSST 2020
Cdd:PRK14804    7 KHLISWEDWSDSEILDLLDFA----VHVKKNRVnyAGHMSGRSLAMLFQKTSTRTRVSFEVAMTEMGGHGIYLDWMASNF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2021 Q------KGESLVDSVNTMSC----YADVIVLRHpipGAvesaarhcRRPVINAGDGVGeHPTQALLDIFTIREELGTV- 2089
Cdd:PRK14804   83 QlsdidlEARYLSRNVSVIMArlkkHEDLLVMKN---GS--------QVPVINGCDNMF-HPCQSLADIMTIALDSPEIp 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2090 -NGMTITMVGdlKHGRTVHSLARLLTQYRITLRYVAP--KNLSMPAEIIDFVASKGIKQEEFNsIEEALPDTDVLYMTRI 2166
Cdd:PRK14804  151 lNQKQLTYIG--VHNNVVNSLIGITAALGIHLTLVTPiaAKENIHAQTVERAKKKGTLSWEMN-LHKAVSHADYVYTDTW 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2167 QKERFSSEKEYNACFGQFI--LTPHIMTGA---KRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLAT 2239
Cdd:PRK14804  228 LDMEFFNDPSYADKKKQRMelMMPYQINSSlmeKTNAKVMHDMPihAGYEITREVVLSDRSIIFQQAENRLDAQKAVILK 307


                  ..
gi 688603052 2240 VL 2241
Cdd:PRK14804  308 LL 309
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
191-342 2.25e-13

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 70.66  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  191 YNQIRCLCQRGARVTVVPWDQpLDSNDFDGL-----FISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLV 265
Cdd:PRK06774   13 YNLYQYFCELGTEVMVKRNDE-LQLTDIEQLapshlVISPGPCTPNEAGISLAVIRHFA---DKLPILGVCLGHQALGQA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  266 IGAKTYKMKYGNRG------HNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVL-FTNANDQTSE--GIVHNHKPLFS 336
Cdd:PRK06774   89 FGARVVRARQVMHGktsaicHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTaWSERGGEMDEimGIRHRTLPLEG 168


                  ....*.
gi 688603052  337 VQFHPE 342
Cdd:PRK06774  169 VQFHPE 174
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 206-342 2.58e-13

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: 70.26  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  206 VVPWDQPLDS---NDFDGLFISNGP------GNPEYCKETVENIrkvacvenpKPIFGICLGHQLLSLVIGAKTYKMKYG 276
Cdd:cd01742    27 ILPNTTPLEEiklKNPKGIILSGGPssvyeeDAPRVDPEIFELG---------VPVLGICYGMQLIAKALGGKVERGDKR 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688603052  277 NRGH------NQPCIHKGTSRcyiTSQ---NHGFAVdpETLPKDWDVLFTNANDQTsEGIVHNHKPLFSVQFHPE 342
Cdd:cd01742    98 EYGKaeieidDSSPLFEGLPD---EQTvwmSHGDEV--VKLPEGFKVIASSDNCPV-AAIANEEKKIYGVQFHPE 166
PRK01713 PRK01713
ornithine carbamoyltransferase; Provisional
 1940-2241 2.61e-13

ornithine carbamoyltransferase; Provisional


Pssm-ID: 167263 [Multi-domain]  Cd Length: 334  Bit Score: 73.48  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1940 LVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSS 2019
Cdd:PRK01713    5 LKNRHLLSLVNHTEREIKYLLDLSRDLKRAKYAGTEQQRLKGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYIDPNSSQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2020 TQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINagdGVGE--HPTQALLDIFTIREELGT-VNGMTITM 2096
Cdd:PRK01713   85 IGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFN---GLTDefHPTQMLADVLTMIENCDKpLSEISYVY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2097 VGDLKHGRTvHSLARLLTQYRITLRYVAPKNLSMPAEIID----FVASKGIKQEEFNSIEEALPDTDVlymtrIQKERFS 2172
Cdd:PRK01713  162 IGDARNNMG-NSLLLIGAKLGMDVRICAPKALLPEASLVEmcekFAKESGARITVTDDIDKAVKGVDF-----VHTDVWV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2173 SEKEYNACFGQFI-------LTPHIM--TGaKRKMVVMHPLPRVN---------------------EISVEVDTDPRAAY 2222
Cdd:PRK01713  236 SMGEPLETWGERIkllmpyqVTPELMkrTG-NPKVKFMHCLPAFHnsetkvgrqiaekypelangiEVTEDVFESPMNIA 314

                         330
                  ....*....|....*....
gi 688603052 2223 FRQAENGMYIRMALLATVL 2241
Cdd:PRK01713  315 FEQAENRMHTIKAVMVASL 333
PRK13566 PRK13566
anthranilate synthase component I;
199-342 3.20e-13

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 75.34  E-value: 3.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  199 QRGARVTVVPWDQP---LDSNDFDGLFISNGPGNPE--YCKETVEnirkvACVENPKPIFGICLGHQLLSLVIGAKTYKM 273
Cdd:PRK13566  548 QTGAEVTTVRYGFAeemLDRVNPDLVVLSPGPGRPSdfDCKATID-----AALARNLPIFGVCLGLQAIVEAFGGELGQL 622

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  274 KYGNRG------HNQPC-IHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTnandqTSEGIV----HNHKPLFSVQFHPE 342
Cdd:PRK13566  623 AYPMHGkpsrirVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDELLVTAE-----TEDGVImaieHKTLPVAAVQFHPE 697
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
221-383 7.45e-13

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 73.60  E-value: 7.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  221 LFISNGPGNPEYCKETVENIRKVACVenpKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGT------SRCYI 294
Cdd:PRK14607   48 IVISPGPGRPEEAGISVEVIRHFSGK---VPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKglfrgiPNPTV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  295 TSQNHGFAVDPETLPKDWDVLfTNANDQTSEGIVHNHKPLFSVQFHPEHMaGPTDLVGLFDVFLDTVRdvkENKAGKSVK 374
Cdd:PRK14607  125 ATRYHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPESI-LTEEGKRILKNFLNYQR---EEIDIKSYL 199

                         170
                  ....*....|.
gi 688603052  375 QRLM--EHLTF 383
Cdd:PRK14607  200 KKLVegEDLSF 210
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 397-708 1.13e-12

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 71.45  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  397 KVLVLGSGGlsigqagefdysGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLP-IT-PEYVTQVI---KNERP 471
Cdd:PRK12767    3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkVTdPNYIDRLLdicKKEKI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  472 DGVLLTFGGQTALNCG--VELKKQGVLekykvrVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAA--A 547
Cdd:PRK12767   71 DLLIPLIDPELPLLAQnrDRFEEIGVK------VLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAAlaK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  548 ERLGYPVLVRSAFALGGLGSGFANNRDEmitlVTQAFAHTSQVLVDKSLKGwKEIEYEVVRDAYDNCVTVCNMENIDPLG 627
Cdd:PRK12767  145 GELQFPLFVKPRDGSASIGVFKVNDKEE----LEFLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIEVRA 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  628 ihtGESI--VVAPSQTLNDYeynmlrntAIKVIRHLGVVGECNIQYALNPEseQYYIIEVNARLSrssalaskaTGYPLA 705
Cdd:PRK12767  220 ---GETSkgVTVKDPELFKL--------AERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFG---------GGYPLS 277


                  ...
gi 688603052  706 YVA 708
Cdd:PRK12767  278 YMA 280
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
191-342 1.55e-12

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 68.40  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  191 YNQIRCLCQRGARVtVVPWDQPLDSNDFDGL-----FISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLV 265
Cdd:PRK08007   13 WNLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTPDEAGISLDVIRHYA---GRLPILGVCLGHQAMAQA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  266 IGAKTYKMKYGNRGHNQPCIHKGT------SRCYITSQNHGFAVDPETLPKDWDVlftNANDQTSE--GIVHNHKPLFSV 337
Cdd:PRK08007   89 FGGKVVRAAKVMHGKTSPITHNGEgvfrglANPLTVTRYHSLVVEPDSLPACFEV---TAWSETREimGIRHRQWDLEGV 165


                  ....*
gi 688603052  338 QFHPE 342
Cdd:PRK08007  166 QFHPE 170
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
219-342 2.22e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 67.91  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  219 DGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLVIGAKTYKM------KYGNRGHNQPCIHKGTSRC 292
Cdd:PRK07649   45 DFLMISPGPCSPNEAGISMEVIRYFA---GKIPIFGVCLGHQSIAQVFGGEVVRAerlmhgKTSLMHHDGKTIFSDIPNP 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 688603052  293 YITSQNHGFAVDPETLPKDWDVlftnaNDQTSEG----IVHNHKPLFSVQFHPE 342
Cdd:PRK07649  122 FTATRYHSLIVKKETLPDCLEV-----TSWTEEGeimaIRHKTLPIEGVQFHPE 170
PRK00758 PRK00758
GMP synthase subunit A; Validated
 181-342 2.91e-12

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 67.18  E-value: 2.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  181 RITAIDCGIKYNQI--RCLCQRGARVTVVPWDQPLDSND--FDGLFISNGP-----GNpeyCKETVENIrKVacvenpkP 251
Cdd:PRK00758    1 KIVVVDNGGQYNHLihRTLRYLGVDAKIIPNTTPVEEIKafEDGLILSGGPdieraGN---CPEYLKEL-DV-------P 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  252 IFGICLGHQLLSLVIGAKTYKMKYGNRG--------HNQpcIHKGTSRCYITSQNHGFAVdpETLPKDWDVLFTNANDQT 323
Cdd:PRK00758   70 ILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDD--ILKGLPPEIRVWASHADEV--KELPDGFEILARSDICEV 145

                         170
                  ....*....|....*....
gi 688603052  324 sEGIVHNHKPLFSVQFHPE 342
Cdd:PRK00758  146 -EAMKHKEKPIYGVQFHPE 163
PRK04523 PRK04523
N-acetylornithine carbamoyltransferase; Reviewed
 1943-2243 3.29e-12

N-acetylornithine carbamoyltransferase; Reviewed


Pssm-ID: 235304 [Multi-domain]  Cd Length: 335  Bit Score: 70.16  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1943 QHILSVRQFSKEQMSHLFNVAHTLRlmvqKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVV----------- 2011
Cdd:PRK04523    4 KHFLNTQDWSRAELDALLTQAAAFK----RNKLGSALKGKSIALVFFNPSLRTRTSFELGAFQLGGHAVvlqpgkdawpi 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2012 HFCESTSSTQ-KGESLVDSVNTMSCYADVIVLRHPIPGA----------VESAARHCRRPVINAGDGVgeHPTQALLDIF 2080
Cdd:PRK04523   80 EFELGAVMDGeTEEHIREVARVLSRYVDLIGVRAFPKFVdwskdrqdqvLNSFAKYSTVPVINMETIT--HPCQELAHAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2081 TIREELG-TVNGMTI------------TMVGD------LKHGRTVhSLARLLTQYRITLRYVApknlsmPAEiiDFVASK 2141
Cdd:PRK04523  158 ALQEHFGtTLRGKKYvltwtyhpkplnTAVANsalliaTRLGMDV-TLLCPTPDYILDERYMD------WAE--QNAAES 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2142 GIKQEEFNSIEEALPDTDVLYM----TRIQKERFSSEKEYNACFGQFILTPHIMtGAKRKMVVMHPLP-RVN-EISVEVD 2215
Cdd:PRK04523  229 GGSLTVSHDIDSAYAGADVVYAkswgALPFFGNWEPEKPIRDQYQHFIVDERKM-ALTNNGVFSHCLPlRRNvKVTDAVM 307

                         330       340
                  ....*....|....*....|....*...
gi 688603052 2216 TDPRAAYFRQAENGMYIRMALLATVLGR 2243
Cdd:PRK04523  308 DSPNCIAIDEAENRLHVQKAIMAALASQ 335
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
191-342 1.27e-11

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 65.67  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  191 YNQIRCLCQRGARVTVVPWDQPldsnDFDG--------LFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLL 262
Cdd:PRK08857   13 YNLYQYFCELGAQVKVVRNDEI----DIDGiealnpthLVISPGPCTPNEAGISLQAIEHFA---GKLPILGVCLGHQAI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  263 SLVIGAKTYKMKYGNRGHNQPCIH------KGTSRCYITSQNHGFAVDPETLPKDWDVL-FTNANDQTSE---GIVHNHK 332
Cdd:PRK08857   86 AQVFGGQVVRARQVMHGKTSPIRHtgrsvfKGLNNPLTVTRYHSLVVKNDTLPECFELTaWTELEDGSMDeimGFQHKTL 165

                         170
                  ....*....|
gi 688603052  333 PLFSVQFHPE 342
Cdd:PRK08857  166 PIEAVQFHPE 175
trpG CHL00101
anthranilate synthase component 2
 191-344 1.29e-11

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 65.52  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  191 YNQIRCLCQRGARVTVVPWDQ----PLDSNDFDGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLVI 266
Cdd:CHL00101   13 YNLVQSLGELNSDVLVCRNDEidlsKIKNLNIRHIIISPGPGHPRDSGISLDVISSYA---PYIPILGVCLGHQSIGYLF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  267 GAKTYKMKYGNRG------HNQPCIHKGTSRCYITSQNHGFAVDPETLPKDwdvLFTNAndQTSEGIV----HNH-KPLF 335
Cdd:CHL00101   90 GGKIIKAPKPMHGktskiyHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSP---LEITA--WTEDGLImacrHKKyKMLR 164


                  ....*....
gi 688603052  336 SVQFHPEHM 344
Cdd:CHL00101  165 GIQFHPESL 173
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
394-718 1.33e-11

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 68.80  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  394 RPRKVLVLGS--GGLSIgqagefdysgsqaIKAMKEENIQTILINPN-IATVQTSKGLADKVYFLPITP------EYVTQ 464
Cdd:COG3919     4 MRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVVDRDpLGPAARSRYVDEVVVVPDPGDdpeafvDALLE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  465 VIKNERPDgVLLTFGgqtalNCGVEL--KKQGVLEKYkVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQ 542
Cdd:COG3919    71 LAERHGPD-VLIPTG-----DEYVELlsRHRDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  543 AVAAAERLGYPVLV--------RSAFALGGLGSGFANNRDEMITLVTQAFAHTSQVLVDkslkgwkeiEYEVVRDAYDNC 614
Cdd:COG3919   144 LDALAEDLGFPVVVkpadsvgyDELSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQ---------EYIPGDDGEMRG 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  615 VTVCNMENIDPLGIHTGESIVVAPSQ----TLNDYEYNM-LRNTAIKVIRHLGVVGECNIQYALNPESEQYYIIEVNARL 689
Cdd:COG3919   215 LTAYVDRDGEVVATFTGRKLRHYPPAggnsAARESVDDPeLEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRF 294

                         330       340
                  ....*....|....*....|....*....
gi 688603052  690 SRSSALASKAtGYPLAYVAAKLSLGIPLP 718
Cdd:COG3919   295 WRSLYLATAA-GVNFPYLLYDDAVGRPLE 322
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 194-268 2.54e-11

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: 62.62  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  194 IRCLCQRGARVTVVPWDQP-----LDSNDFDGLFISNGPGNPEYCKETVENIRKV-ACVENPKPIFGICLGHQLlsLVIG 267
Cdd:cd01653    18 LDALREAGAEVDVVSPDGGpvesdVDLDDYDGLILPGGPGTPDDLARDEALLALLrEAAAAGKPILGICLGAQL--LVLG 95


                  .
gi 688603052  268 A 268
Cdd:cd01653    96 V 96
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 524-788 6.26e-11

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 66.98  E-value: 6.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  524 MEEINEHVAP--SEAAMSVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMitlvTQAFAHTSQ----------VL 591
Cdd:PRK06111  123 MQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL----TKAFESNKKraanffgngeMY 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  592 VDKSLKGWKEIEYEVVRDAYDNCVtvcnmenidplgiHTGE---SI------VV--APSQTLNDYEYNMLRNTAIKVIRH 660
Cdd:PRK06111  199 IEKYIEDPRHIEIQLLADTHGNTV-------------YLWErecSVqrrhqkVIeeAPSPFLDEETRKAMGERAVQAAKA 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  661 LGVVGECNIQYaLNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLPVLKNSVTNSTTA---------- 730
Cdd:PRK06111  266 IGYTNAGTIEF-LVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIKRSGHAievriyaedp 344

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688603052  731 -NFEPSLDycvvKVPRWDLSK--FLRVSTKIGSSMK-------SVGEVMAIGRSFEEAFQKALRMVDE 788
Cdd:PRK06111  345 kTFFPSPG----KITDLTLPGgeGVRHDHAVENGVTvtpfydpMIAKLIAHGETREEAISRLHDALEE 408
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 194-262 8.73e-11

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: 60.29  E-value: 8.73e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688603052  194 IRCLCQRGARVTVVPWDQP-----LDSNDFDGLFISNGPGNPEYCKETVENIRKV-ACVENPKPIFGICLGHQLL 262
Cdd:cd03128    18 LDALREAGAEVDVVSPDGGpvesdVDLDDYDGLILPGGPGTPDDLAWDEALLALLrEAAAAGKPVLGICLGAQLL 92
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 1064-1224 2.97e-09

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: 58.42  E-value: 2.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1064 GISQPRWKELSDTESAVNFCETVGYPCLV---RPSYvlSGAAMNVAYSDTDMEKFLSSAvavsKEHPVVISKFIQEAKEI 1140
Cdd:pfam02222    4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEEL----GDGPVIVEEFVPFDREL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1141 DVDAV-ACDGEVIAIAVSEHVEnagvHSGDATLVTPPQDINQKTMERIKMIVHAIGQELQVTGPFNLQL-IAKDDQLKVI 1218
Cdd:pfam02222   78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELfVTEDGDLLIN 153


                   ....*.
gi 688603052  1219 ECNVRV 1224
Cdd:pfam02222  154 ELAPRP 159
PRK07200 PRK07200
aspartate/ornithine carbamoyltransferase family protein; Validated
 1952-2162 3.83e-09

aspartate/ornithine carbamoyltransferase family protein; Validated


Pssm-ID: 235961 [Multi-domain]  Cd Length: 395  Bit Score: 61.29  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1952 SKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQKGESLVDSVN 2031
Cdd:PRK07200   30 TPDELKAVLDVADALRALREENISTKVFNSGLGISVFRDNSTRTRFSYASACNLLGLEVQDLDEGKSQIAHGETVRETAN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2032 TMSCYADVIVLR------------HPIPGAVESAARHC---RRP-VINAGDGVgEHPTQALLDIFTIREELGTVN---GM 2092
Cdd:PRK07200  110 MISFMADVIGIRddmyigkgnaymREVGAAVDDGYKQGvlpQRPtLVNLQCDI-DHPTQSMADLLHLIEHFGGLEnlkGK 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 2093 TITMVGDL--KHGRTV---HSLARLLTQYRITLRYVAPKNLSMPAEIIDfVASK-----GIKQEEFNSIEEALPDTDVLY 2162
Cdd:PRK07200  189 KIAMTWAYspSYGKPLsvpQGIIGLMTRFGMDVTLAHPEGYDLMPEVVE-VAKKnakasGGSFRQVNSMEEAFKDADIVY 267
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
539-724 7.05e-09

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 60.89  E-value: 7.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  539 SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEM-------ITLVTQAFAhTSQVLVDKSLKGWKEIEYEVVRDAY 611
Cdd:PRK07178  139 DLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELeqnfprvISEATKAFG-SAEVFLEKCIVNPKHIEVQILADSH 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  612 DNCVTV----CNMENidplgiHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNPESEqYYIIEVNA 687
Cdd:PRK07178  218 GNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGE-VYFMEMNT 290

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 688603052  688 RLSRSSALASKATGYPLAYVAAKLSLGIPLPVLKNSV 724
Cdd:PRK07178  291 RVQVEHTITEEITGIDIVREQIRIASGLPLSYKQEDI 327
PRK06895 PRK06895
anthranilate synthase component II;
207-342 1.04e-08

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 57.05  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  207 VPWD----QPLDSND---FDGLFISNGPGNPEYCKETVENIRKVacvENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRG 279
Cdd:PRK06895   26 VPMQvvnvEDLDLDEvenFSHILISPGPDVPRAYPQLFAMLERY---HQHKSILGVCLGHQTLCEFFGGELYNLNNVRHG 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052  280 HNQPCIHKGTSRCYitsQN----------HGFAVDPETLPKDwdvlfTNANDQTSEGIV----HNHKPLFSVQFHPE 342
Cdd:PRK06895  103 QQRPLKVRSNSPLF---DGlpeefniglyHSWAVSEENFPTP-----LEITAVCDENVVmamqHKTLPIYGVQFHPE 171
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 244-357 2.01e-08

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: 56.43  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  244 ACVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQpcihkgtsrcyitsqnhgfAVDpeTLPKDWDVLFTnANDQT 323
Cdd:cd01745    95 AALERGKPILGICRGMQLLNVALGGTLYQDIRVNSLHHQ-------------------AIK--RLADGLRVEAR-APDGV 152

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 688603052  324 SEGIVH-NHKPLFSVQFHPEHMA-GPTDLVGLFDVF 357
Cdd:cd01745   153 IEAIESpDRPFVLGVQWHPEWLAdTDPDSLKLFEAF 188
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
497-689 4.50e-08

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 58.07  E-value: 4.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  497 EKYKVRVLGTPVASIEMTEDrKIFVEK-MEEINEHVAP--SEAAMSVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNR 573
Cdd:PRK08654   96 EKAGIVFIGPSSDVIEAMGS-KINAKKlMKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSE 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  574 DEMITLV--TQAFAHT----SQVLVDKSLKGWKEIEYEVVRDAYDNCvtvcnmenidplgIHTGES-----------IVV 636
Cdd:PRK08654  175 EELEDAIesTQSIAQSafgdSTVFIEKYLEKPRHIEIQILADKHGNV-------------IHLGDRecsiqrrhqklIEE 241

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 688603052  637 APSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALnpESEQYYIIEVNARL 689
Cdd:PRK08654  242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY--SNGNFYFLEMNTRL 292
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 244-342 1.21e-07

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: 54.57  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   244 ACVENPKPIFGICLGHQLLSLVIGAKTY---KMKYGNRGHNQPC------------IHKGT--SRCYITSQ---N--HGF 301
Cdd:pfam07722  100 AALARGKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshavnVEPGSllASLLGSEEfrvNslHHQ 179

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 688603052   302 AVDpeTLPKDWDVLFTnANDQTSEGIVH--NHKPLFSVQFHPE 342
Cdd:pfam07722  180 AID--RLAPGLRVEAV-APDGTIEAIESpnAKGFALGVQWHPE 219
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
495-718 1.35e-07

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 56.68  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  495 VLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAP-SEAAM-SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANN 572
Cdd:PRK08462   96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGALkSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  573 RDEMITLVT-------QAFAHTSqVLVDKSLKGWKEIEYEVVRDAYDNCVTV----CNMENidplgiHTGESIVVAPSQT 641
Cdd:PRK08462  176 ESDLENLYLaaesealSAFGDGT-MYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVV 248

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052  642 LNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLP 718
Cdd:PRK08462  249 LDEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP 324
PLN02335 PLN02335
anthranilate synthase
 220-342 3.26e-07

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 53.26  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  220 GLFISNGPGNPEYCKETVENIRKVAcvenPK-PIFGICLGHQLLSLVIGAKTYKMKYG-NRGHNQPCIH---------KG 288
Cdd:PLN02335   65 GVLISPGPGTPQDSGISLQTVLELG----PLvPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYdekgeeglfSG 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 688603052  289 TSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHN-HKPLFSVQFHPE 342
Cdd:PLN02335  141 LPNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRkYKHIQGVQFHPE 195
PRK06849 PRK06849
hypothetical protein; Provisional
 1037-1224 5.13e-07

hypothetical protein; Provisional


Pssm-ID: 235876 [Multi-domain]  Cd Length: 389  Bit Score: 54.28  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1037 CRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNF-CETVGYPCLVRPSYVLSGAAMNVaysdTDMEKF 1115
Cdd:PRK06849  101 CEVLHFDFELLLLLHNKWEFAEQARSLGLSVPKTYLITDPEAIRNFmFKTPHTPYVLKPIYSRFVRRVDL----LPKEAA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1116 LSSaVAVSKEHPVVISKFIQeAKEIDVDAVACDGEVIAIA--VSEHVENAGVHSGDATLVTPpqdinqktmeRIKMIVHA 1193
Cdd:PRK06849  177 LKE-LPISKDNPWVMQEFIQ-GKEYCSYSIVRSGELRAHScyKPEYCAGSGAQIAFQPINHP----------RIEEFVTH 244

                         170       180       190
                  ....*....|....*....|....*....|..
gi 688603052 1194 IGQELQVTGPFNLQLI-AKDDQLKVIECNVRV 1224
Cdd:PRK06849  245 FVKELNYTGQISFDFIeTENGDAYPIECNPRT 276
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 504-686 4.02e-06

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: 50.01  E-value: 4.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   504 LGTPVASIEMTEdRKIFVEKMEEINEHVApseaamsveqavaaaERLGYPVLVRSAfalgGLGSGF----ANNRDEMITL 579
Cdd:pfam07478    5 AGLPVVPFVTFT-RADWKLNPKEWCAQVE---------------EALGYPVFVKPA----RLGSSVgvskVESREELQAA 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052   580 VTQAFAHTSQVLVDKSLKGwKEIEYEVvrdaydncvtvcnMENIDPlgiHTGESIVVAPSQTLNDYE------------- 646
Cdd:pfam07478   65 IEEAFQYDEKVLVEEGIEG-REIECAV-------------LGNEDP---EVSPVGEIVPSGGFYDYEakyiddsaqivvp 127

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 688603052   647 -------YNMLRNTAIKVIRHLGVVGECNIQYALnPESEQYYIIEVN 686
Cdd:pfam07478  128 adleeeqEEQIQELALKAYKALGCRGLARVDFFL-TEDGEIVLNEVN 173
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 201-342 5.67e-06

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: 50.40  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  201 GARVtvVPWDQPLDSNDFDGLFIS-NG---PG-----NPEYCKETVENIRKVACVENPK----PIFGICLGHQLLSLVIG 267
Cdd:cd01747    33 GARV--VPIWINESEEYYDKLFKSiNGilfPGgavdiDTSGYARTAKIIYNLALERNDAgdyfPVWGTCLGFELLTYLTS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  268 ----------AKTYKMKYGNRGHNQPC----------IHKGTSRCyITSQNHGFAVDPETLPKD------WDVLFTNAND 321
Cdd:cd01747   111 getllleateATNSALPLNFTEDALQSrlfkrfppdlLKSLATEP-LTMNNHRYGISPENFTENgllsdfFNVLTTNDDW 189

                         170       180
                  ....*....|....*....|....
gi 688603052  322 QTSEGIV---HNHKPLFSVQFHPE 342
Cdd:cd01747   190 NGVEFIStveAYKYPIYGVQWHPE 213
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 964-1248 6.50e-06

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: 50.32  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  964 IMELRKMGYKTIMVNYnpetvstdydmcDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN-NIAMSLHRQQCRILGt 1042
Cdd:COG0189    20 IEAAQRRGHEVEVIDP------------DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPPFYGlALLRQLEAAGVPVVN- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1043 SPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYvlSGAAMNVAYSDTDMEkfLSSAVAV 1122
Cdd:COG0189    87 DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLD--GSGGRGVFLVEDEDA--LESILEA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1123 SKEH---PVVISKFIQEAKEIDVDAVACDGEVIA----IAVSEHVENAGVHSGDATLVTPPQDInqktMERIKMIVHAIG 1195
Cdd:COG0189   163 LTELgsePVLVQEFIPEEDGRDIRVLVVGGEPVAairrIPAEGEFRTNLARGGRAEPVELTDEE----RELALRAAPALG 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 688603052 1196 qeLQVTGpfnLQLIAKDDQLKVIECNVRVsrSFPYVSKTLGVDLVALATRVIL 1248
Cdd:COG0189   239 --LDFAG---VDLIEDDDGPLVLEVNVTP--GFRGLERATGVDIAEAIADYLE 284
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
522-717 7.32e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 50.87  E-value: 7.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  522 EKMEEINEHVAP-SEAAM-SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAFAHTS------QVLVD 593
Cdd:PRK05586  121 EIMIKAGVPVVPgSEGEIeNEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaafgddSMYIE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  594 KSLKGWKEIEYEVVRDAYDNCVTV----CNMENidplgiHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNI 669
Cdd:PRK05586  201 KFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTI 274

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 688603052  670 QYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPL 717
Cdd:PRK05586  275 EFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
ATPgrasp_Ter pfam15632
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ...
 1139-1256 1.02e-05

ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434824 [Multi-domain]  Cd Length: 131  Bit Score: 47.22  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1139 EIDVDAVACDGEVIAIavsehVENAGVHSGDATLVTPPQDINqktmerikmIVHAIGQELQVTGPFNLQLIAKDDQLKVI 1218
Cdd:pfam15632   15 EYSVDCLAGHGELIAA-----VPRRKGDGGIQTLEDDPELIE---------AARRLAEAFGLDGLFNVQFRYDGDGPKLL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 688603052  1219 ECNVRVSRSFPYVSKTlGVDLVALATRVILGEEVEAVG 1256
Cdd:pfam15632   81 EINPRMSGGIGYSCLA-GVNLPYLALKLLLGLETPDPV 117
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 539-689 1.57e-05

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 49.80  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  539 SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLV--TQAFAHTS----QVLVDKSLKGWKEIEYEVVRDAYD 612
Cdd:PRK08591  140 DEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFsmARAEAKAAfgnpGVYMEKYLENPRHIEIQVLADGHG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  613 NcvtvcnmenidplGIHTGE---SI------VV--APSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYaLNPESEQYY 681
Cdd:PRK08591  220 N-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNGEFY 285


                  ....*...
gi 688603052  682 IIEVNARL 689
Cdd:PRK08591  286 FIEMNTRI 293
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1470-1518 1.62e-05

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: 49.42  E-value: 1.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052  1470 LPGLIDVHVHLR--------EPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIID 1518
Cdd:pfam01979    3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIE 59
DHOase cd01294
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ...
 1468-1784 1.87e-05

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: 49.20  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1468 IRLPGLIDVHVHLREpGATHKedFSSGTAAAlAGGITMVcaMPNTNPAIIDpNSFTMAQK--LAKA--GCRCDY--ALFV 1541
Cdd:cd01294     1 LTIPRPDDMHLHLRD-GAMLK--LVLPYTAR-GFSRAIV--MPNLKPPVTT-TADALAYRerILAAdpGPNFTPlmTLYL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1542 GASSDNAALLPSIASST-AGLKMYLND--TYSTLKMDNVSLWMEHFEKWPKH-LPIVAHAEKQTVAAILL---------V 1608
Cdd:cd01294    74 TENTTPEELREAKKKGGiRGVKLYPAGatTNSQGGVTDLEKIYPVLEAMQKLgMPLLVHGEVPDFKIDVLdreakfipvL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1609 AQLYQR-P---VHICHVAKKEEILIIRAAKQKgiqVTCEVAPHHLFLCEDNVpVIGKDKAQV--RPMLGTREDMEALwen 1682
Cdd:cd01294   154 EPLAQRfPklkIVLEHITTADAVEYVKSCNEN---VAATITPHHLLLTRDDL-LGGGLNPHLycKPVAKRPEDREAL--- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1683 LDIIDC------FATDHAPHSAEEKISEKPPPGYPGLETMLPLLFTAVSE-GRLtvDDIIKRLYENPRKIFSLPAQEDTY 1755
Cdd:cd01294   227 RKAATSghpkffLGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEhNAL--DKLEAFASDNGPNFYGLPPNKKTI 304

                         330       340
                  ....*....|....*....|....*....
gi 688603052 1756 VEVdlEQEWIIPKHMQFTKSKWTPFEGMK 1784
Cdd:cd01294   305 TLV--KEPWKVPEKIPFGNNGVVPFRAGE 331
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1035-1253 5.21e-05

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 48.17  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1035 QQCRI--LGTSPEFIDNAENRFKFSRMLDTIGIS-QPRWK-ELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDT 1110
Cdd:PRK05586   96 KECNIvfIGPDSETIELMGNKSNAREIMIKAGVPvVPGSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1111 DMEKFLSSAVAVSK----EHPVVISKFIQEAKEIDVDAVAcdgeviaiavsehvENAG--VHSG--DATLvtppQDINQK 1182
Cdd:PRK05586  176 ELIKAFNTAKSEAKaafgDDSMYIEKFIENPKHIEFQILG--------------DNYGnvVHLGerDCSL----QRRNQK 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1183 TME-----------RIKMIVHAIGQELQV------TGPFnlqLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATR 1245
Cdd:PRK05586  238 VLEeapspvmteelRKKMGEIAVKAAKAVnyknagTIEF---LLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIK 314


                  ....*...
gi 688603052 1246 VILGEEVE 1253
Cdd:PRK05586  315 IAYGEKLS 322
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 214-404 5.81e-05

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 48.31  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  214 DSNDFDGLFISNGPGNPE------YCKETVENIRKVacvenpkPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHK 287
Cdd:PLN02889  128 EEKAFDNIVISPGPGSPTcpadigICLRLLLECRDI-------PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHN 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  288 GtSRCY--ITS-QNHGFAV--------DPETLPKD-----W--------------------------------DVLFTNA 319
Cdd:PLN02889  201 G-CRLFddIPSgRNSGFKVvryhslviDAESLPKElvpiaWtsssdtlsflesqksglvpdayesqigqsgssDPFSSKL 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  320 NDQTS---------------EGIVHNHKPLFSVQFHPEHMAgPTDLVGLFDVFLDTVRDVKENKAGKSVKQRLMEHLTFP 384
Cdd:PLN02889  280 KNGTSwpsshsermqngkilMGIMHSTRPHYGLQFHPESIA-TCYGRQIFKNFREITQDYWLRLRSTSLRRRNSNLTANM 358

                         250       260
                  ....*....|....*....|
gi 688603052  385 GSPDPNAFVRPRKVLVLGSG 404
Cdd:PLN02889  359 QVPDASQLFKVPRRGQLGNG 378
PHA03378 PHA03378
EBNA-3B; Provisional
 1819-1975 7.44e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.14  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1819 SATPTATTEVIMDAPKRV---IEAMTPERPRQAAPVDVVRSRAPSPRRSAGDGRFILPPRIHRSSDPGLPPAEEEVSLRA 1895
Cdd:PHA03378  677 SPTGANTMLPIQWAPGTMqppPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARP 756

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052 1896 PFDA--ELALPAEAYAHPPPLARilsPQAG-----QPQILPHPQTSPLLHPLVGQhiLSVRQFSKEQMSHLFNVAHTLRL 1968
Cdd:PHA03378  757 PAAApgRARPPAAAPGAPTPQPP---PQAPpapqqRPRGAPTPQPPPQAGPTSMQ--LMPRAAPGQQGPTKQILRQLLTG 831


                  ....*..
gi 688603052 1969 MVQKERP 1975
Cdd:PHA03378  832 GVKRGRP 838
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 1043-1247 7.88e-05

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 46.96  E-value: 7.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1043 SPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSyVLSGAAMNVAYSDTDMEKFLSSAVAV 1122
Cdd:TIGR00768   79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPV-FGSWGRGVSLARDRQAAESLLEHFEQ 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1123 SKEHPVV--ISKFIQEAKEIDVDAVACDGEVIA----IAVSEHVENagVHSGDATL---VTPPQ-DINQKTMERIKMIVH 1192
Cdd:TIGR00768  158 LNGPQNLflVQEYIKKPGGRDIRVFVVGDEVVAaiyrITSGHWRSN--LARGGKAEpcsLTEEIeELAIKAAKALGLDVA 235

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 688603052  1193 AIgqelqvtgpfnlQLIAKDDQLKVIECNVRVsrSFPYVSKTLGVDLVALATRVI 1247
Cdd:TIGR00768  236 GV------------DLLESEDGLLVNEVNANP--EFKNSVKTTGVNIAGKLLDYI 276
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
 1081-1141 8.36e-05

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 47.13  E-value: 8.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688603052 1081 NFCETVGYPCLVRPSYVLSGAAMNVAYSDTDMEKFLSSAVAVskEHPVVISKFIqEAKEID 1141
Cdd:PRK14570  165 DIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFI-EAREIE 222
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 522-704 9.52e-05

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 47.50  E-value: 9.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  522 EKMEEINEHvapseaamsveqavaaAERLGYPVLVRSAFALGGLGSGFANNRDEMI------TLVTQAFAHTSQVLVDKS 595
Cdd:PRK08463  139 ESMEEIKIF----------------ARKIGYPVILKASGGGGGRGIRVVHKEEDLEnafescKREALAYFNNDEVFMEKY 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  596 LKGWKEIEYEVVRDAYDNCVTVCnmENIDPLGIHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNp 675
Cdd:PRK08463  203 VVNPRHIEFQILGDNYGNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD- 279

                         170       180
                  ....*....|....*....|....*....
gi 688603052  676 ESEQYYIIEVNARLSRSSALASKATGYPL 704
Cdd:PRK08463  280 DYNRFYFMEMNTRIQVEHGVTEEITGIDL 308
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 212-269 1.26e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 45.73  E-value: 1.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052  212 PLDSNDFDGLFISNGPGNP----EYC-----KETVENIRKvaCVENPKPIFGICLGHQLLSLVIGAK 269
Cdd:PRK08250   40 PENADGFDLLIVMGGPQSPrttrEECpyfdsKAEQRLINQ--AIKAGKAVIGVCLGAQLIGEALGAK 104
guaA PRK00074
GMP synthase; Reviewed
 251-342 2.40e-04

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 46.19  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  251 PIFGICLGHQLLSLVIGAK---TYKMKYGN---RGHNQPCIHKGTSRCYITSQNHGFAVdpETLPKDWDVLFTNANDQTS 324
Cdd:PRK00074   77 PVLGICYGMQLMAHQLGGKverAGKREYGRaelEVDNDSPLFKGLPEEQDVWMSHGDKV--TELPEGFKVIASTENCPIA 154

                          90
                  ....*....|....*...
gi 688603052  325 eGIVHNHKPLFSVQFHPE 342
Cdd:PRK00074  155 -AIANEERKFYGVQFHPE 171
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 200-262 1.94e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 41.48  E-value: 1.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052  200 RGARVTV-VPWDQpLDSNDFDGLFISNGPGnPEYC---KETVENIRKVAcvENPKPIFGICLGHQLL 262
Cdd:cd03169    59 PGHRFAVtADFDE-VDPDDYDALVIPGGRA-PEYLrldEKVLAIVRHFA--EANKPVAAICHGPQIL 121
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 1063-1158 2.48e-03

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 41.53  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  1063 IGISQPRWKELSDtESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDTDMEKFLssAVAVSKEHPVVISKFIqEAKEIDV 1142
Cdd:pfam07478   13 VTFTRADWKLNPK-EWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAI--EEAFQYDEKVLVEEGI-EGREIEC 88

                           90
                   ....*....|....*.
gi 688603052  1143 dAVACDGEVIAIAVSE 1158
Cdd:pfam07478   89 -AVLGNEDPEVSPVGE 103
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 539-688 3.60e-03

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 42.76  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  539 SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAF--AHTS----QVLVDKSLKGWKEIEYEVVRDAYD 612
Cdd:COG1038   143 DLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARreAKAAfgddEVFLEKYIERPKHIEVQILGDKHG 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  613 NCVtvcnmenidplgiHTGE---SI------VV--APSQTLNDYEYNMLRNTAIKVIRHLGVVGecniqyA-----LNPE 676
Cdd:COG1038   223 NIV-------------HLFErdcSVqrrhqkVVeiAPAPNLDEELREAICEAAVKLAKAVGYVN------AgtvefLVDD 283

                         170
                  ....*....|..
gi 688603052  677 SEQYYIIEVNAR 688
Cdd:COG1038   284 DGNFYFIEVNPR 295
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1073-1146 4.68e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 41.89  E-value: 4.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688603052 1073 LSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDTDMEKFLSSA--VAVS--KEHPVVISKFIQEAKEIDVDAVA 1146
Cdd:PRK08654  138 IEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTqsIAQSafGDSTVFIEKYLEKPRHIEIQILA 215
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 187-262 6.01e-03

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 39.71  E-value: 6.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688603052   187 CGIKYNqirCLCQRGARVTVVPWDQPLDSNDFDGLFISNGPGnPEYCKETVENIRKV-ACVENPKPIFGICLGHQLL 262
Cdd:TIGR01382   33 SKEAGT---TVGKHGYSVTVDATIDEVNPEEYDALVIPGGRA-PEYLRLNNKAVRLVrEFVEKGKPVAAICHGPQLL 105
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 397-603 6.60e-03

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: 40.86  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  397 KVLVLgSGGLSigqaGEFD---YSGSQAIKAMKEENIQTILInpniatvqtskgladkvyflPITPEYVTQVIKNERPDG 473
Cdd:COG1181     2 RVAVL-FGGRS----AEREvslKSGRAVAAALDKAGYDVVPI--------------------GIDVEDLPAALKELKPDV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  474 VLL----TFGGQTALncgvelkkQGVLEKYKVRVLGTPVASIEMTED----RKIFveKMEEINehVAPSEAAMSVEQAVA 545
Cdd:COG1181    57 VFPalhgRGGEDGTI--------QGLLELLGIPYTGSGVLASALAMDkaltKRVL--AAAGLP--TPPYVVLRRGELADL 124

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688603052  546 AA--ERLGYPVLVRSAFAlgglGSGF----ANNRDEMITLVTQAFAHTSQVLVDKSLKGwKEIE 603
Cdd:COG1181   125 EAieEELGLPLFVKPARE----GSSVgvskVKNAEELAAALEEAFKYDDKVLVEEFIDG-REVT 183
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 531-598 8.52e-03

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 40.48  E-value: 8.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688603052  531 VAPSEAAMSVEQAVAAAERLGYPVLVRSafALGG--LGSGFANNRDEMITLVTQAFAHTSQVLVDKSLKG 598
Cdd:PRK01372  113 TPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGssVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKG 180
 
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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