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Conserved domains on  [gi|19113967|ref|NP_593055|]
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bifunctional carbamoyl-phosphate synthase/aspartate carbamoyltransferase Ura1 [Schizosaccharomyces pombe]

Protein Classification

trifunctional carbamoyl-phosphate synthase/dihydroorotase/aspartate carbamoyltransferase( domain architecture ID 12782739)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSaseII_lrg super family cl36884
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 473-1517 0e+00

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


The actual alignment was detected with superfamily member TIGR01369:

Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1590.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    473 DAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDS 552
Cdd:TIGR01369    5 DIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    553 IYVTFGGQTALNVGIELKDE--FEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFP 630
Cdd:TIGR01369   85 ILPTFGGQTALNLAVELEESgvLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYP 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    631 VIVRAAYALGGLGSGFADNEAELIDLCTLAFATSP--QVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTG 708
Cdd:TIGR01369  165 VIVRPAFTLGGTGGGIAYNREELKEIAERALSASPinQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTG 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    709 DSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKL 788
Cdd:TIGR01369  245 DSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKL 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    789 GLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSNT 868
Cdd:TIGR01369  325 AVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGAT 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    869 GFNVKD----ALMSIDTELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDISSLPISLL 944
Cdd:TIGR01369  405 GFDLPDrevePDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELL 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    945 KTAKQLGFADVQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDIHFNDK-GVMVLGSGV 1023
Cdd:TIGR01369  485 RRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKkKVLVLGSGP 564

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1024 YRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLETVLDIYEQESSSGIIIAMGGQTANN 1103
Cdd:TIGR01369  565 NRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLN 644

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1104 IALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVY 1183
Cdd:TIGR01369  645 LAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVY 724

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1184 SQSDLHSYLQQAVAINKDHPVVISKYIENAKEIELDAVAREGKMVMHVISEHVENAGVHSGDATLVLPPQDLAPTTIERI 1263
Cdd:TIGR01369  725 NEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRI 804

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1264 VDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPIQPY-PDVDLPRDYVA 1342
Cdd:TIGR01369  805 KDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELgVGKEKEPKYVA 884

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1343 VKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAYLKAMISTGFRLPKKNILISIGSYKEKAELLPYVKKLYENNY 1422
Cdd:TIGR01369  885 VKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKGY 964

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1423 NIFATAGTSDYFMESGVPCKyLADLPAEEANNEYSLsahLANNMIDMYINLPSNNryrrpANYISSGYKSRRLAIDYSVP 1502
Cdd:TIGR01369  965 KLYATEGTAKFLGEAGIKPE-LVLKVSEGRPNILDL---IKNGEIELVINTTSKG-----AGTATDGYKIRREALDYGVP 1035

                         1050
                   ....*....|....*
gi 19113967   1503 LVTNVKCAKLMIEAI 1517
Cdd:TIGR01369 1036 LITTLNTAEAFAEAL 1050
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 61-445 9.93e-162

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: 502.16  E-value: 9.93e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967     61 LELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDrrildeisglpKYFESNQI 140
Cdd:TIGR01368    3 LVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVND-----------EDAESKGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    141 HVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRLLIQKDESPInpssitglGKDWST 220
Cdd:TIGR01368   72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEE--------LVEKAR 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    221 AFEDIpwknpNTENLTSQVSIKEPKLYephpttaiKKADGKIIRILVIDVGMKYNQIRCFLNRGVELLVVPWDYDFT--K 298
Cdd:TIGR01368  144 VSPDI-----TGINLVAEVSTKEPYTW--------GQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeiK 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    299 ETY-DGLFISNGPGDPSLMDLVVDRVKRVLEskTVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYIT 377
Cdd:TIGR01368  211 KYNpDGIFLSNGPGDPAAVEPAIETIRKLLE--KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEIT 288

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113967    378 SQNHGYAVD-ASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFIDVVKR 445
Cdd:TIGR01368  289 SQNHGYAVDpDSLPAGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1535-1862 2.39e-156

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: 486.57  E-value: 2.39e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1535 QTANLPGLINISAFLPEF---TSEAVSDYTKECIASGFTMARFLPFSTSSTLaDKDSLSAVKKLALDHAHCDYNFSVIAS 1611
Cdd:cd01316    1 RTIRLPGLIDVHVHLREPgatHKEDFASGTKAALAGGFTMVRAMPNTNPSIV-DVASLKLVQSLAQAKARCDYAFSIGAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1612 STNEVTISELTSE-SGCLFFHFEKDDSGI-DHVTAVASHFNVWPDTQTVMTDAKSTTLASLLLLASLHNRRIHITNVSSK 1689
Cdd:cd01316   80 STNAATVGELASEaVGLKFYLNETFSTLIlDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1690 DDLNLIVLAKQRSLPVTFDVSVYSLFLNQND-----YPGATFLPTADDQVEIWNKLSYIDCFSIGSIPSRLAKFVGN-TA 1763
Cdd:cd01316  160 EEINLIRLAKARGLKVTCEVSPHHLFLSQDDlprgqYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNkPP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1764 FTGFGVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRLHDQDDSgvQLEVDRSVSW--------SSKDWTPFNGKKL 1835
Cdd:cd01316  240 PGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDT--YVEVDLDEEWtipknplqSKKGWTPFEGKKV 317

                        330       340
                 ....*....|....*....|....*..
gi 19113967 1836 YGSIQSVQFDGHDVFFDGELNFEHTYG 1862
Cdd:cd01316  318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1933-2241 8.19e-133

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: 418.30  E-value: 8.19e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1933 PFYRKHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASAS 2012
Cdd:COG0540    2 SFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 2013 SVNKGESLADTIRTLGCYG-DAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTITFI 2091
Cdd:COG0540   82 SVSKGESLADTIRTLEAYGaDAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAIV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 2092 GDLKYGRTVHSLARLLAFWHVELHLVSPEQLaLPDDVKDdirangLNFIEHRELtKEVVAQSDVLYCTRVQKERFAS--V 2169
Cdd:COG0540  162 GDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEE------LGVEVTTDL-DEALPDADVVYMLRIQKERFTDglF 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113967 2170 DEYEKLKDSFIVDNSVLASAKSHCIVMHPLPRNR--EISEEVDfDQRRAAYFRQMRYGLYIRMALLACVMGATE 2241
Cdd:COG0540  234 PSYREYKRSYGLTAERLALAKPDAIVMHPGPRNRgvEIDSDVD-DTPRSVIFEQVTNGVAVRMALLYLLLGGEE 306
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 473-1517 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: 1590.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    473 DAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDS 552
Cdd:TIGR01369    5 DIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    553 IYVTFGGQTALNVGIELKDE--FEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFP 630
Cdd:TIGR01369   85 ILPTFGGQTALNLAVELEESgvLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYP 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    631 VIVRAAYALGGLGSGFADNEAELIDLCTLAFATSP--QVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTG 708
Cdd:TIGR01369  165 VIVRPAFTLGGTGGGIAYNREELKEIAERALSASPinQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTG 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    709 DSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKL 788
Cdd:TIGR01369  245 DSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKL 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    789 GLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSNT 868
Cdd:TIGR01369  325 AVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGAT 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    869 GFNVKD----ALMSIDTELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDISSLPISLL 944
Cdd:TIGR01369  405 GFDLPDrevePDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELL 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    945 KTAKQLGFADVQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDIHFNDK-GVMVLGSGV 1023
Cdd:TIGR01369  485 RRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKkKVLVLGSGP 564

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1024 YRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLETVLDIYEQESSSGIIIAMGGQTANN 1103
Cdd:TIGR01369  565 NRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLN 644

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1104 IALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVY 1183
Cdd:TIGR01369  645 LAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVY 724

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1184 SQSDLHSYLQQAVAINKDHPVVISKYIENAKEIELDAVAREGKMVMHVISEHVENAGVHSGDATLVLPPQDLAPTTIERI 1263
Cdd:TIGR01369  725 NEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRI 804

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1264 VDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPIQPY-PDVDLPRDYVA 1342
Cdd:TIGR01369  805 KDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELgVGKEKEPKYVA 884

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1343 VKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAYLKAMISTGFRLPKKNILISIGSYKEKAELLPYVKKLYENNY 1422
Cdd:TIGR01369  885 VKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKGY 964

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1423 NIFATAGTSDYFMESGVPCKyLADLPAEEANNEYSLsahLANNMIDMYINLPSNNryrrpANYISSGYKSRRLAIDYSVP 1502
Cdd:TIGR01369  965 KLYATEGTAKFLGEAGIKPE-LVLKVSEGRPNILDL---IKNGEIELVINTTSKG-----AGTATDGYKIRREALDYGVP 1035

                         1050
                   ....*....|....*
gi 19113967   1503 LVTNVKCAKLMIEAI 1517
Cdd:TIGR01369 1036 LITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
473-1528 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1441.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   473 DAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDS 552
Cdd:PRK05294    6 DIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   553 IYVTFGGQTALNVGIELKDE--FEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFP 630
Cdd:PRK05294   86 ILPTMGGQTALNLAVELAESgvLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   631 VIVRAAYALGGLGSGFADNEAELIDLCTLAFATSP--QVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTG 708
Cdd:PRK05294  166 VIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPvtEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   709 DSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVV-GECNIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAK 787
Cdd:PRK05294  246 DSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAK 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   788 LGLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSN 867
Cdd:PRK05294  326 LAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGV 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   868 TGFN-VKDALMSIDT---ELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDISsLPISL 943
Cdd:PRK05294  406 TGLDeDLFEEESLEElreELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLP-LDAEL 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   944 LKTAKQLGFADVQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDIHFNDKGVMVLGSGV 1023
Cdd:PRK05294  485 LREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGP 564

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1024 YRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLETVLDIYEQESSSGIIIAMGGQTANN 1103
Cdd:PRK05294  565 NRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLK 644

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1104 IALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVY 1183
Cdd:PRK05294  645 LAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVY 724

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1184 SQSDLHSYLQQAVAINKDHPVVISKYIENAKEIELDAVArEGKMVM-HVISEHVENAGVHSGDATLVLPPQDLAPTTIER 1262
Cdd:PRK05294  725 DEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIC-DGEDVLiGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEE 803

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1263 IVDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPI--QPYPDVDLPrDY 1340
Cdd:PRK05294  804 IREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLaeLGYTKGLIP-PY 882

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1341 VAVKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAYLKAMISTGFRLPKK-NILISIgSYKEKAELLPYVKKLYE 1419
Cdd:PRK05294  883 VAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLE 961

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1420 NNYNIFATAGTSDYFMESGVPCKYLADLpAEEANNEYSLsahLANNMIDMYINLPSNNRYRRpanyisSGYKSRRLAIDY 1499
Cdd:PRK05294  962 LGFKILATSGTAKFLREAGIPVELVNKV-HEGRPHIVDL---IKNGEIDLVINTPTGRQAIR------DGFSIRRAALEY 1031

                        1050      1060
                  ....*....|....*....|....*....
gi 19113967  1500 SVPLVTNVKCAKLMIEAIcRNLDFSLSTV 1528
Cdd:PRK05294 1032 KVPYITTLAGARAAVKAI-EALKFGELEV 1059
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 480-1021 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: 648.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  480 LGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDSIYVTFGG 559
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  560 QTALNVGIELKDEFEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFPVIVRAAYAL 639
Cdd:COG0458   81 QTALNLAVELEEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  640 GGLGSGFADNEAELIDLCTLAFATSP--QVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTGDSIVVAPSQ 717
Cdd:COG0458  161 GGRGMGIVYNEEELEEYLERALKVSPdhPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  718 TLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNpfTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKLGLNIPLNEV 797
Cdd:COG0458  241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDEL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  798 KNSvTKvtcacFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSNTGFNVKDALM 877
Cdd:COG0458  319 GND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLSLVA 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  878 SIDTELQ---TPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHdisSLPISLLKTAKQLGFAD 954
Cdd:COG0458  393 DDDKEEAlllARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEI---ILVINTLLGAKSLGDSD 469

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113967  955 VQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDIHFNDKGVMVLGS 1021
Cdd:COG0458  470 GIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 61-445 9.93e-162

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: 502.16  E-value: 9.93e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967     61 LELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDrrildeisglpKYFESNQI 140
Cdd:TIGR01368    3 LVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVND-----------EDAESKGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    141 HVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRLLIQKDESPInpssitglGKDWST 220
Cdd:TIGR01368   72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEE--------LVEKAR 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    221 AFEDIpwknpNTENLTSQVSIKEPKLYephpttaiKKADGKIIRILVIDVGMKYNQIRCFLNRGVELLVVPWDYDFT--K 298
Cdd:TIGR01368  144 VSPDI-----TGINLVAEVSTKEPYTW--------GQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeiK 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    299 ETY-DGLFISNGPGDPSLMDLVVDRVKRVLEskTVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYIT 377
Cdd:TIGR01368  211 KYNpDGIFLSNGPGDPAAVEPAIETIRKLLE--KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEIT 288

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113967    378 SQNHGYAVD-ASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFIDVVKR 445
Cdd:TIGR01368  289 SQNHGYAVDpDSLPAGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1535-1862 2.39e-156

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: 486.57  E-value: 2.39e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1535 QTANLPGLINISAFLPEF---TSEAVSDYTKECIASGFTMARFLPFSTSSTLaDKDSLSAVKKLALDHAHCDYNFSVIAS 1611
Cdd:cd01316    1 RTIRLPGLIDVHVHLREPgatHKEDFASGTKAALAGGFTMVRAMPNTNPSIV-DVASLKLVQSLAQAKARCDYAFSIGAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1612 STNEVTISELTSE-SGCLFFHFEKDDSGI-DHVTAVASHFNVWPDTQTVMTDAKSTTLASLLLLASLHNRRIHITNVSSK 1689
Cdd:cd01316   80 STNAATVGELASEaVGLKFYLNETFSTLIlDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1690 DDLNLIVLAKQRSLPVTFDVSVYSLFLNQND-----YPGATFLPTADDQVEIWNKLSYIDCFSIGSIPSRLAKFVGN-TA 1763
Cdd:cd01316  160 EEINLIRLAKARGLKVTCEVSPHHLFLSQDDlprgqYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNkPP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1764 FTGFGVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRLHDQDDSgvQLEVDRSVSW--------SSKDWTPFNGKKL 1835
Cdd:cd01316  240 PGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDT--YVEVDLDEEWtipknplqSKKGWTPFEGKKV 317

                        330       340
                 ....*....|....*....|....*..
gi 19113967 1836 YGSIQSVQFDGHDVFFDGELNFEHTYG 1862
Cdd:cd01316  318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
63-441 3.37e-156

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 486.50  E-value: 3.37e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    63 LEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDRRildeisglpkyFESNQIHV 142
Cdd:PRK12564    9 LEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRED-----------FESDRPHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   143 AAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGrlliqkdespinpsSITGLGKDWSTAF 222
Cdd:PRK12564   78 KGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKG--------------VIATEDFDAEELL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   223 EDIP-WKNPNTENLTSQVSIKEPKLYEPHPTTAIKkadgkiiRILVIDVGMKYNQIRCFLNRGVELLVVPWDYDF---TK 298
Cdd:PRK12564  144 EKARaFPGLLGLDLVKEVSTKEPYPWPGPGGELKY-------KVVAIDFGVKRNILRELAERGCRVTVVPATTTAeeiLA 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   299 ETYDGLFISNGPGDPSLMDLVVDRVKRVLESKtVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYITS 378
Cdd:PRK12564  217 LNPDGVFLSNGPGDPAALDYAIEMIRELLEKK-IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITS 295

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113967   379 QNHGYAVDASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFID 441
Cdd:PRK12564  296 QNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 63-444 2.40e-147

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: 461.80  E-value: 2.40e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   63 LEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDrrildeisglpKYFESNQIHV 142
Cdd:COG0505    9 LEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVND-----------EDFESDRPWV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  143 AAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRLLiqkdESPINPSSItglgKDWSTAF 222
Cdd:COG0505   78 AGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVIS----TGDLDIEEL----LEKARAA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  223 EDIpwknpNTENLTSQVSIKEPKLYEPHPttaikkadGKIIRILVIDVGMKYNQIRCFLNRGVELLVVPwdYDFTKET-- 300
Cdd:COG0505  150 PGM-----EGLDLVKEVSTKEPYEWTEAP--------GAGFHVVALDFGVKRNILRELAERGCRVTVVP--ATTSAEEil 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  301 ---YDGLFISNGPGDPSLMDLVVDRVKRVLESKtVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYIT 377
Cdd:COG0505  215 alnPDGVFLSNGPGDPAALDYAIETIRELLGKG-IPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEIT 293

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113967  378 SQNHGYAVDASSL-SNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFIDVVK 444
Cdd:COG0505  294 SQNHGFAVDEDSLpATDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1933-2241 8.19e-133

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: 418.30  E-value: 8.19e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1933 PFYRKHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASAS 2012
Cdd:COG0540    2 SFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 2013 SVNKGESLADTIRTLGCYG-DAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTITFI 2091
Cdd:COG0540   82 SVSKGESLADTIRTLEAYGaDAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAIV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 2092 GDLKYGRTVHSLARLLAFWHVELHLVSPEQLaLPDDVKDdirangLNFIEHRELtKEVVAQSDVLYCTRVQKERFAS--V 2169
Cdd:COG0540  162 GDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEE------LGVEVTTDL-DEALPDADVVYMLRIQKERFTDglF 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113967 2170 DEYEKLKDSFIVDNSVLASAKSHCIVMHPLPRNR--EISEEVDfDQRRAAYFRQMRYGLYIRMALLACVMGATE 2241
Cdd:COG0540  234 PSYREYKRSYGLTAERLALAKPDAIVMHPGPRNRgvEIDSDVD-DTPRSVIFEQVTNGVAVRMALLYLLLGGEE 306
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
1932-2238 3.79e-119

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 379.03  E-value: 3.79e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1932 SPFYRKHIISVHQVTRSDLHVLFAIAHQMR-IIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTAS 2010
Cdd:PRK00856    1 NPLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2011 ASSVNKGESLADTIRTLGCYG-DAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTIT 2089
Cdd:PRK00856   81 TSSVSKGETLADTIRTLSAMGaDAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2090 FIGDLKYGRTVHSLARLLAFWHVELHLVSPEQLaLPDDVKDdiranglnFIEHRELtKEVVAQSDVLYCTRVQKERF--A 2167
Cdd:PRK00856  161 IVGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPE--------YGVHTDL-DEVIEDADVVMMLRVQKERMdgG 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113967  2168 SVDEYEKLKDSFIVDNSVLASAKSHCIVMHPLPRNR--EISEEVDfDQRRAAYFRQMRYGLYIRMALLACVMG 2238
Cdd:PRK00856  231 LLPSYEEYKRSYGLTAERLALAKPDAIVMHPGPVNRgvEIASDVA-DGPQSVIFEQVTNGVAVRMAVLELLLG 302
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1937-2238 4.17e-112

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: 358.98  E-value: 4.17e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1937 KHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVT-ASASSVN 2015
Cdd:TIGR00670    1 RHLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSdSETSSVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   2016 KGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTITFIGDLK 2095
Cdd:TIGR00670   81 KGETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   2096 YGRTVHSLARLLAFWHVELHLVSPEQLALPDDVKDDIRANGLNFIEHRELtKEVVAQSDVLYCTRVQKERFASVDEYEKL 2175
Cdd:TIGR00670  161 YGRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESL-EEVIDEADVLYVTRIQKERFPDPEEYEKV 239

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113967   2176 KDSFIVDNSVLASAKSHCIVMHPLPRNREISEEVDfDQRRAAYFRQMRYGLYIRMALLACVMG 2238
Cdd:TIGR00670  240 KGSYGITLERLEAAKKGVIIMHPLPRVDEIDPSVD-DTPHAKYFKQAFNGVPVRMALLALLLG 301
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 593-795 1.90e-104

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: 332.73  E-value: 1.90e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    593 DRELFARAMDEINEKCAKSASA--SSIEEAIKVSKDISFPVIVRAAYALGGLGSGFADNEAELIDLCTLAFATS------ 664
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    665 PQVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLgiHTGDSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGEC 744
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 19113967    745 NIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKLGLNIPLN 795
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 265-440 6.83e-102

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: 324.06  E-value: 6.83e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  265 ILVIDVGMKYNQIRCFLNRGVELLVVPWDYDF---TKETYDGLFISNGPGDPSLMDLVVDRVKRVLESKtVPVFGICFGH 341
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAeeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK-IPIFGICLGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  342 QIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYITSQNHGYAVDASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQF 421
Cdd:cd01744   80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                        170
                 ....*....|....*....
gi 19113967  422 HPESTPGPRDTEFLFDVFI 440
Cdd:cd01744  160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 61-197 1.42e-72

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: 237.99  E-value: 1.42e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967     61 LELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDRRildeisglpkyFESNQI 140
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPED-----------FESDKI 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 19113967    141 HVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRL 197
Cdd:pfam00988   70 HVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 53-197 8.27e-68

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: 224.56  E-value: 8.27e-68
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967      53 MKDYklmaLELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDrrildeisglp 132
Cdd:smart01097    1 MKAY----LVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVND----------- 65

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113967     133 KYFESNQIHVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRL 197
Cdd:smart01097   66 EDFESDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
1938-2078 1.99e-55

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 189.56  E-value: 1.99e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1938 HIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASASSVNKG 2017
Cdd:pfam02729    1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113967   2018 ESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGnGSKEHPTQAFLDLYTIRE 2078
Cdd:pfam02729   81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 879-1002 1.20e-54

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: 186.50  E-value: 1.20e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967     879 IDTELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDISSLPISLLKTAKQLGFADVQIA 958
Cdd:smart01096    1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 19113967     959 AFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTY 1002
Cdd:smart01096   81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1395-1515 8.25e-48

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: 166.71  E-value: 8.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1395 KNILISIGSYkEKAELLPYVKKLYENNYNIFATAGTSDYFMESGVPCKYLADLPAEEANNEYSLSAHLANNMIDMYINLP 1474
Cdd:cd01423    1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDKPSLRELLAEGKIDLVINLP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19113967 1475 SNNRYRRPANYissgYKSRRLAIDYSVPLVTNVKCAKLMIE 1515
Cdd:cd01423   80 SNRGKRVLDND----YVMRRAADDFAVPLITNPKCAKLFIE 116
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1539-1863 2.33e-16

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: 83.99  E-value: 2.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1539 LPGLINISAFL--PEFTSeavsdytKECIAS--------GFT----MARflpfsTSSTLADKDSLSAVKKLALDHAHCDY 1604
Cdd:COG0044   49 LPGLIDLHVHLrePGLEH-------KEDIETgtraaaagGVTtvvdMPN-----TNPVTDTPEALEFKLARAEEKALVDV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1605 NFSVIASSTNEVTISEL--TSESGCL-FFHFEKDDSG-----------------------IDH---------------VT 1643
Cdd:COG0044  117 GPHGALTKGLGENLAELgaLAEAGAVaFKVFMGSDDGnpvlddgllrraleyaaefgalvAVHaedpdlirggvmnegKT 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1644 AVASHFNVWPD---TQTVMTD---AKSttlasllllaslHNRRIHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLN 1717
Cdd:COG0044  197 SPRLGLKGRPAeaeEEAVARDialAEE------------TGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLT 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1718 QNDYP--GATF-----LPTADDQVEIWNKLS--YIDCfsIGS--IPSRLA-KFVG-NTAFTGF-GVREAIPLLLT-AVNE 1782
Cdd:COG0044  265 DEDLEryGTNFkvnppLRTEEDREALWEGLAdgTIDV--IATdhAPHTLEeKELPfAEAPNGIpGLETALPLLLTeLVHK 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1783 GRLTLKDVVDRFYSNPKAIFRLHDQ---------D----DSGVQLEVDRSVSWSSKDWTPFNGKKLYGSIQSVQFDGHDV 1849
Cdd:COG0044  343 GRLSLERLVELLSTNPARIFGLPRKgriavgadaDlvlfDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVV 422

                        410
                 ....*....|....
gi 19113967 1850 FFDGELNfEHTYGR 1863
Cdd:COG0044  423 YEDGEVV-GEPRGR 435
PRK04250 PRK04250
dihydroorotase; Provisional
 1677-1855 2.33e-13

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 74.42  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1677 HNRRIHITNVSSKDDLNLIvlaKQRSLP-VTFDVSVYSLFLNQNDYPGATF------LPTADDQVEIWNKLSYIDCFSIG 1749
Cdd:PRK04250  196 LKKPLHICHISTKDGLKLI---LKSNLPwVSFEVTPHHLFLTRKDYERNPLlkvyppLRSEEDRKALWENFSKIPIIASD 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1750 SIPSRLA-KFVGNTAFTGfgVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRL--------HDQDDSGVQLEVDRSV 1820
Cdd:PRK04250  273 HAPHTLEdKEAGAAGIPG--LETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIknygieegNYANFAVFDMKKEWTI 350

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 19113967  1821 S----WSSKDWTPFNGKKLYGSIQSVQFDGHDVFFDGEL 1855
Cdd:PRK04250  351 KaeelYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI 389
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 473-1517 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: 1590.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    473 DAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDS 552
Cdd:TIGR01369    5 DIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    553 IYVTFGGQTALNVGIELKDE--FEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFP 630
Cdd:TIGR01369   85 ILPTFGGQTALNLAVELEESgvLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYP 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    631 VIVRAAYALGGLGSGFADNEAELIDLCTLAFATSP--QVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTG 708
Cdd:TIGR01369  165 VIVRPAFTLGGTGGGIAYNREELKEIAERALSASPinQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTG 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    709 DSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKL 788
Cdd:TIGR01369  245 DSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKL 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    789 GLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSNT 868
Cdd:TIGR01369  325 AVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGAT 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    869 GFNVKD----ALMSIDTELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDISSLPISLL 944
Cdd:TIGR01369  405 GFDLPDrevePDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELL 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    945 KTAKQLGFADVQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDIHFNDK-GVMVLGSGV 1023
Cdd:TIGR01369  485 RRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKkKVLVLGSGP 564

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1024 YRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLETVLDIYEQESSSGIIIAMGGQTANN 1103
Cdd:TIGR01369  565 NRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLN 644

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1104 IALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVY 1183
Cdd:TIGR01369  645 LAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVY 724

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1184 SQSDLHSYLQQAVAINKDHPVVISKYIENAKEIELDAVAREGKMVMHVISEHVENAGVHSGDATLVLPPQDLAPTTIERI 1263
Cdd:TIGR01369  725 NEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRI 804

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1264 VDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPIQPY-PDVDLPRDYVA 1342
Cdd:TIGR01369  805 KDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELgVGKEKEPKYVA 884

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1343 VKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAYLKAMISTGFRLPKKNILISIGSYKEKAELLPYVKKLYENNY 1422
Cdd:TIGR01369  885 VKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKGY 964

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1423 NIFATAGTSDYFMESGVPCKyLADLPAEEANNEYSLsahLANNMIDMYINLPSNNryrrpANYISSGYKSRRLAIDYSVP 1502
Cdd:TIGR01369  965 KLYATEGTAKFLGEAGIKPE-LVLKVSEGRPNILDL---IKNGEIELVINTTSKG-----AGTATDGYKIRREALDYGVP 1035

                         1050
                   ....*....|....*
gi 19113967   1503 LVTNVKCAKLMIEAI 1517
Cdd:TIGR01369 1036 LITTLNTAEAFAEAL 1050
carB PRK05294
carbamoyl-phosphate synthase large subunit;
473-1528 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1441.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   473 DAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDS 552
Cdd:PRK05294    6 DIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   553 IYVTFGGQTALNVGIELKDE--FEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFP 630
Cdd:PRK05294   86 ILPTMGGQTALNLAVELAESgvLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   631 VIVRAAYALGGLGSGFADNEAELIDLCTLAFATSP--QVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTG 708
Cdd:PRK05294  166 VIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPvtEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   709 DSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVV-GECNIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAK 787
Cdd:PRK05294  246 DSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAK 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   788 LGLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSN 867
Cdd:PRK05294  326 LAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGV 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   868 TGFN-VKDALMSIDT---ELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDISsLPISL 943
Cdd:PRK05294  406 TGLDeDLFEEESLEElreELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLP-LDAEL 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   944 LKTAKQLGFADVQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDIHFNDKGVMVLGSGV 1023
Cdd:PRK05294  485 LREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGP 564

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1024 YRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLETVLDIYEQESSSGIIIAMGGQTANN 1103
Cdd:PRK05294  565 NRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLK 644

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1104 IALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVY 1183
Cdd:PRK05294  645 LAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVY 724

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1184 SQSDLHSYLQQAVAINKDHPVVISKYIENAKEIELDAVArEGKMVM-HVISEHVENAGVHSGDATLVLPPQDLAPTTIER 1262
Cdd:PRK05294  725 DEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAIC-DGEDVLiGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEE 803

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1263 IVDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPI--QPYPDVDLPrDY 1340
Cdd:PRK05294  804 IREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLaeLGYTKGLIP-PY 882

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1341 VAVKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAYLKAMISTGFRLPKK-NILISIgSYKEKAELLPYVKKLYE 1419
Cdd:PRK05294  883 VAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLE 961

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1420 NNYNIFATAGTSDYFMESGVPCKYLADLpAEEANNEYSLsahLANNMIDMYINLPSNNRYRRpanyisSGYKSRRLAIDY 1499
Cdd:PRK05294  962 LGFKILATSGTAKFLREAGIPVELVNKV-HEGRPHIVDL---IKNGEIDLVINTPTGRQAIR------DGFSIRRAALEY 1031

                        1050      1060
                  ....*....|....*....|....*....
gi 19113967  1500 SVPLVTNVKCAKLMIEAIcRNLDFSLSTV 1528
Cdd:PRK05294 1032 KVPYITTLAGARAAVKAI-EALKFGELEV 1059
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 473-1517 0e+00

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 1078.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   473 DAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDS 552
Cdd:PRK12815    6 DIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   553 IYVTFGGQTALNVGIELKDE--FEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFP 630
Cdd:PRK12815   86 LLATLGGQTALNLAVKLHEDgiLEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   631 VIVRAAYALGGLGSGFADNEAELIDLCTLAFATSP--QVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTG 708
Cdd:PRK12815  166 IIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPihQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   709 DSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKL 788
Cdd:PRK12815  246 DSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   789 GLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSNT 868
Cdd:PRK12815  326 AVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRN 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   869 GFNVKDALMSIDTE-----LQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLIsKHDISSLPISL 943
Cdd:PRK12815  406 GLSLPIELSGKSDEellqdLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKL-AEDGLDLSADL 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   944 LKTAKQLGFADVQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNaVEHDIHF--NDKGVMVLGS 1021
Cdd:PRK12815  485 LRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYF-GESEAEPssEKKKVLILGS 563

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1022 GVYRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLETVLDIYEQESSSGIIIAMGGQTA 1101
Cdd:PRK12815  564 GPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTA 643

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1102 NNIALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNT 1181
Cdd:PRK12815  644 INLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAV 723

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1182 VYSQSDLHSYLQQAVAINkdHPVVISKYIEnAKEIELDAVAREGKMVMHVISEHVENAGVHSGDATLVLPPQDLAPTTIE 1261
Cdd:PRK12815  724 VYDEPALEAYLAENASQL--YPILIDQFID-GKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSEEQQE 800

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1262 RIVDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPIQ--PYPDVDLPR- 1338
Cdd:PRK12815  801 KIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAelGYPNGLWPGs 880

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1339 DYVAVKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAYLKAMISTGFRLPKKN-ILISiGSYKEKAELLPYVKKL 1417
Cdd:PRK12815  881 PFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGtIFIS-VRDEDKPEVTKLARRF 959

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1418 YENNYNIFATAGTSDYFMESGVPCKYLADLpAEEANNEYSLSAHlANNMIDMYINLpsnnryrrPANYISSGYKSRRLAI 1497
Cdd:PRK12815  960 AQLGFKLLATEGTANWLAEEGITTGVVEKV-QEGSPSLLERIKQ-HRIVLVVNTSL--------SDSASEDAIKIRDEAL 1029

                        1050      1060
                  ....*....|....*....|
gi 19113967  1498 DYSVPLVTNVKCAKLMIEAI 1517
Cdd:PRK12815 1030 STHIPVFTELETAQAFLQVL 1049
PLN02735 PLN02735
carbamoyl-phosphate synthase
 453-1517 0e+00

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 931.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   453 QPFKLPGGTIEENRSRhplvDAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVY 532
Cdd:PLN02735    6 TVTRAWSAATKAGKRT----DLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   533 FLPVNADFVRKVIKQERPDSIYVTFGGQTALNVGIELKDE--FEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAK 610
Cdd:PLN02735   82 IAPMTPELVEQVIAKERPDALLPTMGGQTALNLAVALAESgiLEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   611 SASASSIEEAIKVSKDI-SFPVIVRAAYALGGLGSGFADNEAELIDLCT--LAFATSPQVLIERSMKGWKEIEYEVVRDA 687
Cdd:PLN02735  162 SGIATTLDECFEIAEDIgEFPLIIRPAFTLGGTGGGIAYNKEEFETICKagLAASITSQVLVEKSLLGWKEYELEVMRDL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   688 FDNCITVCNMENFDPLGIHTGDSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVvgEC---NIQYALNPFTKEYCIIEVNA 764
Cdd:PLN02735  242 ADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNP 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   765 RLSRSSALASKATGYPLAFTAAKLGLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGE 844
Cdd:PLN02735  320 RVSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   845 VMSIGRTFEEAIQKAIRAIDYSNTGF-NVKDALMSIDTE-----LQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFL 918
Cdd:PLN02735  400 AMALGRTFQESFQKALRSLETGFSGWgCAKVKELDWDWEqlkykLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   919 EKLMGLIRTSQLISKHDISSLPISLLKTAKQLGFADVQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYL 998
Cdd:PLN02735  480 TQLKELVDVEQFLKSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYM 559

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   999 YTTYNAVEHDIHFNDKGVMVLGSGVYRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLE 1078
Cdd:PLN02735  560 YSSYDGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVE 639

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1079 TVLDIYEQESSSGIIIAMGGQTANNIALPLHRE-------------NVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPK 1145
Cdd:PLN02735  640 DVLNVIDLERPDGIIVQFGGQTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPK 719

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1146 WKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQAVAINKDHPVVISKYIENAKEIELDAVA-RE 1224
Cdd:PLN02735  720 GGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSE 799

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1225 GKMVMHVISEHVENAGVHSGDATLVLPPQDLAPTTIERIVDAAAKIGEALNITGPYNIQF-IAKDNEIKVIECNVRASRS 1303
Cdd:PLN02735  800 GNVVIGGIMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRT 879

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1304 FPFVSKVIGVDMISMATDVIMGNPIQP--YPDVDLPRdYVAVKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAY 1381
Cdd:PLN02735  880 VPFVSKAIGHPLAKYASLVMSGKSLKDlgFTEEVIPA-HVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAF 958

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1382 LKAMISTGFRLPKK-NILISIGSyKEKAELLPYVKKLYENNYNIFATAGTSDYFMESGVPCKYLADLPAEEANneysLSA 1460
Cdd:PLN02735  959 AKAQIAAGQRLPLSgTVFISLND-LTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPH----AGD 1033

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 19113967  1461 HLANNMIDMYINLPSNNryrrpANYISSGYKSRRLAIDYSVPLVTNVKCAKLMIEAI 1517
Cdd:PLN02735 1034 MLANGQIQLMVITSSGD-----ALDQKDGRQLRRMALAYKVPIITTVAGALATAQAV 1085
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 480-1021 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: 648.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  480 LGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQERPDSIYVTFGG 559
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  560 QTALNVGIELKDEFEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFPVIVRAAYAL 639
Cdd:COG0458   81 QTALNLAVELEEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  640 GGLGSGFADNEAELIDLCTLAFATSP--QVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLGIHTGDSIVVAPSQ 717
Cdd:COG0458  161 GGRGMGIVYNEEELEEYLERALKVSPdhPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  718 TLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNpfTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKLGLNIPLNEV 797
Cdd:COG0458  241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDEL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  798 KNSvTKvtcacFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSNTGFNVKDALM 877
Cdd:COG0458  319 GND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLSLVA 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  878 SIDTELQ---TPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHdisSLPISLLKTAKQLGFAD 954
Cdd:COG0458  393 DDDKEEAlllARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEI---ILVINTLLGAKSLGDSD 469

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113967  955 VQIAAFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTYNAVEHDIHFNDKGVMVLGS 1021
Cdd:COG0458  470 GIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 1019-1537 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: 569.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1019 LGSGVYRIGSSVEFDWCAVRAVRTLRDRGVKTIMVNYNPETVSTDYDEADRLYFENIGLETVLDIYEQESSSGIIIAMGG 1098
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1099 QTANNIALPLHR----ENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVL 1174
Cdd:COG0458   81 QTALNLAVELEEagilEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1175 SGAAMNTVYSQSDLHSYLQQAVAINKDHPVVISKYIENAKEIELDAVA-REGKMVMHVISEHVENAGVHSGDATLVLPPQ 1253
Cdd:COG0458  161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1254 DLAPTTIERIVDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPI--QPY 1331
Cdd:COG0458  241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLdeLGN 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1332 PDVDLPR-DYVAVKVPQFSFSRLSGADPVLGVEMASTGEVACFGHNKFEAYLKAMISTGFRLPKKnILISIGSYKEKAEL 1410
Cdd:COG0458  321 DTGFEPTlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDKEEA 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1411 LPYVKKLYENNYNIFATAGTSDYFMESGVPCKYLADLPAEEANNEyslsAHLANNMIDMYINLPSNNRYRRpanyisSGY 1490
Cdd:COG0458  400 LLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIV----DEIELEEIILVINTLLGAKSLG------DSD 469

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 19113967 1491 KSRRLAIDYSVPLVTNVKCAKLMIEAICRNLDFSLSTVDFQSSFQTA 1537
Cdd:COG0458  470 GIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYST 516
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 61-445 9.93e-162

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: 502.16  E-value: 9.93e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967     61 LELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDrrildeisglpKYFESNQI 140
Cdd:TIGR01368    3 LVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVND-----------EDAESKGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    141 HVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRLLIQKDESPInpssitglGKDWST 220
Cdd:TIGR01368   72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEE--------LVEKAR 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    221 AFEDIpwknpNTENLTSQVSIKEPKLYephpttaiKKADGKIIRILVIDVGMKYNQIRCFLNRGVELLVVPWDYDFT--K 298
Cdd:TIGR01368  144 VSPDI-----TGINLVAEVSTKEPYTW--------GQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeiK 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    299 ETY-DGLFISNGPGDPSLMDLVVDRVKRVLEskTVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYIT 377
Cdd:TIGR01368  211 KYNpDGIFLSNGPGDPAAVEPAIETIRKLLE--KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEIT 288

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113967    378 SQNHGYAVD-ASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFIDVVKR 445
Cdd:TIGR01368  289 SQNHGYAVDpDSLPAGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
 1535-1862 2.39e-156

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: 486.57  E-value: 2.39e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1535 QTANLPGLINISAFLPEF---TSEAVSDYTKECIASGFTMARFLPFSTSSTLaDKDSLSAVKKLALDHAHCDYNFSVIAS 1611
Cdd:cd01316    1 RTIRLPGLIDVHVHLREPgatHKEDFASGTKAALAGGFTMVRAMPNTNPSIV-DVASLKLVQSLAQAKARCDYAFSIGAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1612 STNEVTISELTSE-SGCLFFHFEKDDSGI-DHVTAVASHFNVWPDTQTVMTDAKSTTLASLLLLASLHNRRIHITNVSSK 1689
Cdd:cd01316   80 STNAATVGELASEaVGLKFYLNETFSTLIlDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1690 DDLNLIVLAKQRSLPVTFDVSVYSLFLNQND-----YPGATFLPTADDQVEIWNKLSYIDCFSIGSIPSRLAKFVGN-TA 1763
Cdd:cd01316  160 EEINLIRLAKARGLKVTCEVSPHHLFLSQDDlprgqYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNkPP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1764 FTGFGVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRLHDQDDSgvQLEVDRSVSW--------SSKDWTPFNGKKL 1835
Cdd:cd01316  240 PGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDT--YVEVDLDEEWtipknplqSKKGWTPFEGKKV 317

                        330       340
                 ....*....|....*....|....*..
gi 19113967 1836 YGSIQSVQFDGHDVFFDGELNFEHTYG 1862
Cdd:cd01316  318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
63-441 3.37e-156

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 486.50  E-value: 3.37e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    63 LEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDRRildeisglpkyFESNQIHV 142
Cdd:PRK12564    9 LEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRED-----------FESDRPHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   143 AAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGrlliqkdespinpsSITGLGKDWSTAF 222
Cdd:PRK12564   78 KGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKG--------------VIATEDFDAEELL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   223 EDIP-WKNPNTENLTSQVSIKEPKLYEPHPTTAIKkadgkiiRILVIDVGMKYNQIRCFLNRGVELLVVPWDYDF---TK 298
Cdd:PRK12564  144 EKARaFPGLLGLDLVKEVSTKEPYPWPGPGGELKY-------KVVAIDFGVKRNILRELAERGCRVTVVPATTTAeeiLA 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   299 ETYDGLFISNGPGDPSLMDLVVDRVKRVLESKtVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYITS 378
Cdd:PRK12564  217 LNPDGVFLSNGPGDPAALDYAIEMIRELLEKK-IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITS 295

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113967   379 QNHGYAVDASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFID 441
Cdd:PRK12564  296 QNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 63-444 2.40e-147

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: 461.80  E-value: 2.40e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   63 LEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDrrildeisglpKYFESNQIHV 142
Cdd:COG0505    9 LEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVND-----------EDFESDRPWV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  143 AAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRLLiqkdESPINPSSItglgKDWSTAF 222
Cdd:COG0505   78 AGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVIS----TGDLDIEEL----LEKARAA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  223 EDIpwknpNTENLTSQVSIKEPKLYEPHPttaikkadGKIIRILVIDVGMKYNQIRCFLNRGVELLVVPwdYDFTKET-- 300
Cdd:COG0505  150 PGM-----EGLDLVKEVSTKEPYEWTEAP--------GAGFHVVALDFGVKRNILRELAERGCRVTVVP--ATTSAEEil 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  301 ---YDGLFISNGPGDPSLMDLVVDRVKRVLESKtVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYIT 377
Cdd:COG0505  215 alnPDGVFLSNGPGDPAALDYAIETIRELLGKG-IPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEIT 293

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113967  378 SQNHGYAVDASSL-SNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFIDVVK 444
Cdd:COG0505  294 SQNHGFAVDEDSLpATDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 1933-2241 8.19e-133

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: 418.30  E-value: 8.19e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1933 PFYRKHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASAS 2012
Cdd:COG0540    2 SFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 2013 SVNKGESLADTIRTLGCYG-DAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTITFI 2091
Cdd:COG0540   82 SVSKGESLADTIRTLEAYGaDAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAIV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 2092 GDLKYGRTVHSLARLLAFWHVELHLVSPEQLaLPDDVKDdirangLNFIEHRELtKEVVAQSDVLYCTRVQKERFAS--V 2169
Cdd:COG0540  162 GDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEE------LGVEVTTDL-DEALPDADVVYMLRIQKERFTDglF 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113967 2170 DEYEKLKDSFIVDNSVLASAKSHCIVMHPLPRNR--EISEEVDfDQRRAAYFRQMRYGLYIRMALLACVMGATE 2241
Cdd:COG0540  234 PSYREYKRSYGLTAERLALAKPDAIVMHPGPRNRgvEIDSDVD-DTPRSVIFEQVTNGVAVRMALLYLLLGGEE 306
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
1932-2238 3.79e-119

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 379.03  E-value: 3.79e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1932 SPFYRKHIISVHQVTRSDLHVLFAIAHQMR-IIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTAS 2010
Cdd:PRK00856    1 NPLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2011 ASSVNKGESLADTIRTLGCYG-DAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTIT 2089
Cdd:PRK00856   81 TSSVSKGETLADTIRTLSAMGaDAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2090 FIGDLKYGRTVHSLARLLAFWHVELHLVSPEQLaLPDDVKDdiranglnFIEHRELtKEVVAQSDVLYCTRVQKERF--A 2167
Cdd:PRK00856  161 IVGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPE--------YGVHTDL-DEVIEDADVVMMLRVQKERMdgG 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113967  2168 SVDEYEKLKDSFIVDNSVLASAKSHCIVMHPLPRNR--EISEEVDfDQRRAAYFRQMRYGLYIRMALLACVMG 2238
Cdd:PRK00856  231 LLPSYEEYKRSYGLTAERLALAKPDAIVMHPGPVNRgvEIASDVA-DGPQSVIFEQVTNGVAVRMAVLELLLG 302
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 53-444 7.05e-118

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 377.69  E-value: 7.05e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    53 MKDYklmaLELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPdrrildeisglP 132
Cdd:PRK12838    1 MKAY----LILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGIN-----------A 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   133 KYFESNQIHVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRLLIQKDEspinpssit 212
Cdd:PRK12838   66 DDYESKQPQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDA--------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   213 glgkdwsTAFEDIPwKNPNTENLTSQVSIKEPKLYephPTTaikkadGKiiRILVIDVGMKYNQIRCFLNRGVELLVVPw 292
Cdd:PRK12838  137 -------HAFDQIK-ALVLPKNVVAQVSTKEPYTY---GNG------GK--HVALIDFGYKKSILRSLSKRGCKVTVLP- 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   293 dYDFTKETY-----DGLFISNGPGDPSLMDLVVDRVKRVLESktVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCT 367
Cdd:PRK12838  197 -YDTSLEEIknlnpDGIVLSNGPGDPKELQPYLPEIKKLISS--YPILGICLGHQLIALALGADTEKLPFGHRGANHPVI 273

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113967   368 CMISGRCYITSQNHGYAVDASSLS-NGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFIDVVK 444
Cdd:PRK12838  274 DLTTGRVWMTSQNHGYVVDEDSLDgTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMME 351
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 1937-2238 4.17e-112

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: 358.98  E-value: 4.17e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1937 KHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVT-ASASSVN 2015
Cdd:TIGR00670    1 RHLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSdSETSSVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   2016 KGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTITFIGDLK 2095
Cdd:TIGR00670   81 KGETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   2096 YGRTVHSLARLLAFWHVELHLVSPEQLALPDDVKDDIRANGLNFIEHRELtKEVVAQSDVLYCTRVQKERFASVDEYEKL 2175
Cdd:TIGR00670  161 YGRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESL-EEVIDEADVLYVTRIQKERFPDPEEYEKV 239

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113967   2176 KDSFIVDNSVLASAKSHCIVMHPLPRNREISEEVDfDQRRAAYFRQMRYGLYIRMALLACVMG 2238
Cdd:TIGR00670  240 KGSYGITLERLEAAKKGVIIMHPLPRVDEIDPSVD-DTPHAKYFKQAFNGVPVRMALLALLLG 301
PLN02527 PLN02527
aspartate carbamoyltransferase
 1937-2240 1.88e-108

aspartate carbamoyltransferase


Pssm-ID: 178142 [Multi-domain]  Cd Length: 306  Bit Score: 348.66  E-value: 1.88e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1937 KHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAvTASA---SS 2013
Cdd:PLN02527    1 SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLT-TENAgefSS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2014 VNKGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTITFIGD 2093
Cdd:PLN02527   80 AAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2094 LKYGRTVHSLARLLAFWH-VELHLVSPEQLALPDDVKDDIRANGLNFIEHRELtKEVVAQSDVLYCTRVQKERFA-SVDE 2171
Cdd:PLN02527  160 LANGRTVRSLAYLLAKYEdVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDL-MEVASKCDVLYQTRIQRERFGeRIDL 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113967  2172 YEKLKDSFIVDNSVLASAKSHCIVMHPLPRNREISEEVDFDQrRAAYFRQMRYGLYIRMALLACVMGAT 2240
Cdd:PLN02527  239 YEAARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDP-RAAYFRQAKNGLFIRMALLKLLLGGW 306
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 593-795 1.90e-104

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: 332.73  E-value: 1.90e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    593 DRELFARAMDEINEKCAKSASA--SSIEEAIKVSKDISFPVIVRAAYALGGLGSGFADNEAELIDLCTLAFATS------ 664
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    665 PQVLIERSMKGWKEIEYEVVRDAFDNCITVCNMENFDPLgiHTGDSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGEC 744
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 19113967    745 NIQYALNPFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKLGLNIPLN 795
Cdd:pfam02786  159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 265-440 6.83e-102

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: 324.06  E-value: 6.83e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  265 ILVIDVGMKYNQIRCFLNRGVELLVVPWDYDF---TKETYDGLFISNGPGDPSLMDLVVDRVKRVLESKtVPVFGICFGH 341
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAeeiLKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK-IPIFGICLGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  342 QIMARAAGASTTKMKFGNRGHNIPCTCMISGRCYITSQNHGYAVDASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQF 421
Cdd:cd01744   80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                        170
                 ....*....|....*....
gi 19113967  422 HPESTPGPRDTEFLFDVFI 440
Cdd:cd01744  160 HPEASPGPHDTEYLFDEFL 178
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 53-451 1.05e-89

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 297.86  E-value: 1.05e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    53 MKDYKLMALELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPdrriLDEIsglp 132
Cdd:CHL00197    1 MKKMIPAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGIN----LEDI---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   133 kyfESNQIHVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLG---------RLLIQK-D 202
Cdd:CHL00197   73 ---ESVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGcisnqnlnlSYLRAKiK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   203 ESPINPSSitGLGKDWSTAfEDIPWKNPNTENLTSQVSIKEPKLYEphpttaikkadgkiIRILVIDVGMKYNQIRCFLN 282
Cdd:CHL00197  150 ESPHMPSS--DLIPRVTTS-SYYEWDEKSHPSFYLADNKRPHSSYQ--------------LKIIVIDFGVKYNILRRLKS 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   283 RGVELLVVPWDYDF-TKETY--DGLFISNGPGDPSLMDLVVDRVKRVLEsKTVPVFGICFGHQIMARAAGASTTKMKFGN 359
Cdd:CHL00197  213 FGCSITVVPATSPYqDILSYqpDGILLSNGPGDPSAIHYGIKTVKKLLK-YNIPIFGICMGHQILSLALEAKTFKLKFGH 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   360 RGHNIPCTcmISGRCYITSQNHGYAVDASSL-SNGWKELFVNANDGSNEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDV 438
Cdd:CHL00197  292 RGLNHPSG--LNQQVEITSQNHGFAVNLESLaKNKFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEY 369

                         410
                  ....*....|...
gi 19113967   439 FIDVVKRSADAKS 451
Cdd:CHL00197  370 FIEIIKHSKSSKN 382
PRK08192 PRK08192
aspartate carbamoyltransferase; Provisional
 1934-2238 8.19e-87

aspartate carbamoyltransferase; Provisional


Pssm-ID: 169269 [Multi-domain]  Cd Length: 338  Bit Score: 287.78  E-value: 8.19e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1934 FYRKHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTA-SAS 2012
Cdd:PRK08192    3 FQGSHILSVNQLDRDAIQRIFNVADRMEPYALREKRTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVRETTGmASS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2013 SVNKGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREEL----GSVNGLTI 2088
Cdd:PRK08192   83 SLSKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGIDGMHI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2089 TFIGDLKYGRTVHSLARLLA-FWHVELHLVSPEQLALPDDVKDDIRANGlnfieHR-ELTKEV---VAQSDVLYCTRVQK 2163
Cdd:PRK08192  163 AMVGDLKFGRTVHSLSRLLCmYKNVSFTLVSPKELAMPDYVISDIENAG-----HKiTITDQLegnLDKADILYLTRIQE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2164 ERFASVDEYEKLKDSFIVDNSVLAS-AKSHCIVMHPLPRN-REISEEVDFD---QRRAAYFRQMRYGLYIRMALLACVMG 2238
Cdd:PRK08192  238 ERFPSQEEANKYRGKFRLNQSIYTQhCKSNTVIMHPLPRDsRAQANELDNDlnsHPNLAIFRQADNGLLIRMALFALTLG 317
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 461-862 8.39e-84

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: 299.99  E-value: 8.39e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    461 TIEENRSRHPLVDAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADF 540
Cdd:TIGR01369  541 TYEGERDDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFED 620

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    541 VRKVIKQERPDSIYVTFGGQTALNvgieLKDEFEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEA 620
Cdd:TIGR01369  621 VMNIIELEKPEGVIVQFGGQTPLN----LAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEA 696

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    621 IKVSKDISFPVIVRAAYALGGLGSGFADNEAELIDLCTLAFATSPQ--VLIERSMKGWKEIEYEVVRDafDNCITVCN-M 697
Cdd:TIGR01369  697 VEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAVSD--GEEVLIPGiM 774

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    698 ENFDPLGIHTGDSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNpfTKEYCIIEVNARLSRSSALASKAT 777
Cdd:TIGR01369  775 EHIEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK--DGEVYVIEVNPRASRTVPFVSKAT 852

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    778 GYPLAFTAAKLGLNIPLNEVknSVTKvtcacfEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQ 857
Cdd:TIGR01369  853 GVPLAKLAVRVMLGKKLEEL--GVGK------EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFL 924


                   ....*
gi 19113967    858 KAIRA 862
Cdd:TIGR01369  925 KAQLS 929
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 470-875 5.62e-81

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 291.87  E-value: 5.62e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   470 PLVDAKRVLILGSGGLSIGQAGEFDYSGSQAIKALREEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKQER 549
Cdd:PRK12815  551 PSSEKKKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAEN 630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   550 PDSIYVTFGGQTALNVGIELkdefEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISF 629
Cdd:PRK12815  631 IKGVIVQFGGQTAINLAKGL----EEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGY 706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   630 PVIVRAAYALGGLGSGFADNEAELIDLCTLAFATSPQVLIERSMKGwKEIEYEVVRDAFDncITVCN-MENFDPLGIHTG 708
Cdd:PRK12815  707 PVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDG-KEYEVDAISDGED--VTIPGiIEHIEQAGVHSG 783

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   709 DSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALnpFTKEYCIIEVNARLSRSSALASKATGYPLAFTAAKL 788
Cdd:PRK12815  784 DSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL--ANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKV 861

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   789 GLNIPLNEVKNSVTkvtcacFEPSLDYVVVKIPRWDLKKFTRVSTQLSSAMKSVGEVMSIGRTFEEAIQKAIRAIDYSNT 868
Cdd:PRK12815  862 LLGKSLAELGYPNG------LWPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIP 935

                         410
                  ....*....|..
gi 19113967   869 G-----FNVKDA 875
Cdd:PRK12815  936 SygtifISVRDE 947
PRK11891 PRK11891
aspartate carbamoyltransferase; Provisional
 1936-2240 4.48e-77

aspartate carbamoyltransferase; Provisional


Pssm-ID: 183362 [Multi-domain]  Cd Length: 429  Bit Score: 263.26  E-value: 4.48e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1936 RKHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTA-SASSV 2014
Cdd:PRK11891   87 KPQLLSVDQFSRDSVEALFRVADVMQPIARRQKISRVLEGAVLGNLFFEASTRTRVSFGAAFCRLGGSVCDTTGfTFSSM 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2015 NKGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREE---LGS-VNGLTITF 2090
Cdd:PRK11891  167 AKGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVINGGDGPGEHPSQALLDLYTIQREfsrLGKiVDGAHIAL 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2091 IGDLKYGRTVHSLARLLAFWH-VELHLVSPEQLALPDDVKDDIRANGlNFIEHRELTKEVVAQSDVLYCTRVQKERFASv 2169
Cdd:PRK11891  247 VGDLKYGRTVHSLVKLLALYRgLKFTLVSPPTLEMPAYIVEQISRNG-HVIEQTDDLAAGLRGADVVYATRIQKERFAD- 324

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113967  2170 DEYEKLKDSFIVDNSVL-ASAKSHCIVMHPLPRN-----REISEEVDFDQrRAAYFRQMRYGLYIRMALLACVMGAT 2240
Cdd:PRK11891  325 ESFEGYTPDFQINQALVdAVCKPDTLIMHPLPRDsrpgaNDLSTDLNRDP-RLAIFRQTDNGIPVRMAIFAVLLGVE 400
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 40-436 7.74e-76

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 259.14  E-value: 7.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    40 CSPSPAFYSVNG------EMKDYKLMaleLEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPT 113
Cdd:PLN02771   35 CSSSPLTSDGAGvverpwKTSDARLV---LEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPH 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   114 VGNYGV-PDrrilDEisglpkyfESNQIHVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGS 192
Cdd:PLN02771  112 IGNTGVnFD----DE--------ESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   193 MLGrlLIQKDESPINpSSITGLGKDWSTAFEDipwknpntenLTSQVSIKEPklYE------PHPTTAIKKADGKIIRIL 266
Cdd:PLN02771  180 LIG--VLSTEDSKTD-EELLKMSRSWDIVGID----------LISGVSCKSP--YEwvdktnPEWDFNTNSRDGESYHVI 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   267 VIDVGMKYNQIRCFLNRGVELLVVPWDY---DFTKETYDGLFISNGPGDPSLMDLVVDRVKRVLesKTVPVFGICFGHQI 343
Cdd:PLN02771  245 AYDFGIKHNILRRLASYGCKITVVPSTWpasEALKMKPDGVLFSNGPGDPSAVPYAVETVKELL--GKVPVFGICMGHQL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   344 MARAAGASTTKMKFGNRGHNIPCTCMISGRCYITSQNHGYAVDASSLSNGWKELFVNANDGSNEGIYNTEYPFFSVQFHP 423
Cdd:PLN02771  323 LGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHP 402

                         410
                  ....*....|...
gi 19113967   424 ESTPGPRDTEFLF 436
Cdd:PLN02771  403 EASPGPHDSDNAF 415
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 61-197 1.42e-72

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: 237.99  E-value: 1.42e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967     61 LELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDRRildeisglpkyFESNQI 140
Cdd:pfam00988    1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPED-----------FESDKI 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 19113967    141 HVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRL 197
Cdd:pfam00988   70 HVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 53-197 8.27e-68

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: 224.56  E-value: 8.27e-68
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967      53 MKDYklmaLELEDKSVLQGYSFGADHSVSGELVFQTGMVGYPESLTDPSYRGQILVFTFPTVGNYGVPDrrildeisglp 132
Cdd:smart01097    1 MKAY----LVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVND----------- 65

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113967     133 KYFESNQIHVAAIIISSYSQNYSHFLAHSSLGEWLKEQGIPGIFGIDTRALTKKIRDQGSMLGRL 197
Cdd:smart01097   66 EDFESDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
GATase pfam00117
Glutamine amidotransferase class-I;
266-442 6.95e-60

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 204.39  E-value: 6.95e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    266 LVIDVGM--KYNQIRCFLNRGVELLVVPWDYDFT---KETYDGLFISNGPGDPSLMDLVVDRVKRVLESKtVPVFGICFG 340
Cdd:pfam00117    1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIREARELK-IPILGICLG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    341 HQIMARAAGASTTKMK-FGNRGHNIPC----TCMISG--RCYITSQNHGYAVDASSLSNGWKELFVNANDGSNEGIYNTE 413
Cdd:pfam00117   80 HQLLALAFGGKVVKAKkFGHHGKNSPVgddgCGLFYGlpNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKK 159

                          170       180
                   ....*....|....*....|....*....
gi 19113967    414 YPFFSVQFHPESTPGPRDTEFLFDVFIDV 442
Cdd:pfam00117  160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
1938-2078 1.99e-55

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 189.56  E-value: 1.99e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1938 HIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASASSVNKG 2017
Cdd:pfam02729    1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113967   2018 ESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGnGSKEHPTQAFLDLYTIRE 2078
Cdd:pfam02729   81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 879-1002 1.20e-54

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: 186.50  E-value: 1.20e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967     879 IDTELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDISSLPISLLKTAKQLGFADVQIA 958
Cdd:smart01096    1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 19113967     959 AFMNSTELAVRRIRTEAGIRPFVKQIDTVAAEFPAFTNYLYTTY 1002
Cdd:smart01096   81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
ArgF COG0078
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ...
 1932-2239 1.20e-53

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: 191.03  E-value: 1.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1932 SPFYRKHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASA 2011
Cdd:COG0078    1 TNLKGRHFLSLLDLTPEELRALLDLAAELKAKRKAGIPHRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYLDPGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 2012 SSVNKGESLADTIRTLGCYGDAIVLR---HPSIEsaRIAANfSPVPIING-GNgsKEHPTQAFLDLYTIREELGSVNGLT 2087
Cdd:COG0078   81 SQLGRGESIKDTARVLSRYVDGIMIRtfgHETLE--ELAKY-AGVPVINGlTD--LFHPCQALADLLTIREHFGKLKGLK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 2088 ITFIGDlkyGRTV-HSLARLLAFWHVELHLVSPEQLALPDDVKDDIRANGLNFIEHRELT---KEVVAQSDVLYcTRV-- 2161
Cdd:COG0078  156 VAYVGD---GNNVaNSLLLAAAKLGMDVRIATPEGYEPDPEIVAKAKEIAAESGGSITIThdpAEAVKGADVVY-TDVwv 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 2162 -------QKERfasvdeYEKLKDsFIVDNSVLASAKSHCIVMHPLP--RNREISEEVdFDQRRAAYFRQMRYGLYIRMAL 2232
Cdd:COG0078  232 smgqeeeAEER------IKAFKP-YQVNEELMALAKPDAIFMHCLPahRGEEVTDEV-IDGPQSVVFDEAENRLHAQKAL 303


                 ....*..
gi 19113967 2233 LACVMGA 2239
Cdd:COG0078  304 LAWLLGG 310
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
 1395-1515 8.25e-48

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: 166.71  E-value: 8.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1395 KNILISIGSYkEKAELLPYVKKLYENNYNIFATAGTSDYFMESGVPCKYLADLPAEEANNEYSLSAHLANNMIDMYINLP 1474
Cdd:cd01423    1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDKPSLRELLAEGKIDLVINLP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19113967 1475 SNNRYRRPANYissgYKSRRLAIDYSVPLVTNVKCAKLMIE 1515
Cdd:cd01423   80 SNRGKRVLDND----YVMRRAADDFAVPLITNPKCAKLFIE 116
pyrB PRK13814
aspartate carbamoyltransferase;
1938-2233 5.64e-45

aspartate carbamoyltransferase;


Pssm-ID: 139876 [Multi-domain]  Cd Length: 310  Bit Score: 166.05  E-value: 5.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1938 HIISVHQVTRSDLHVLFAIAHQ-MRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASASSVNK 2016
Cdd:PRK13814    7 HLLNMRSLTRDHIEKLIQRANYfLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2017 GESLADTIRTLGCYGDA-IVLRHPSIESA-RIAANFSPVPIINGGNGSKEHPTQAFLDLYTIREELGSVNGLTITFIGDL 2094
Cdd:PRK13814   87 GETLFDTIKTLEAMGVYfFIVRHSENETPeQIAKQLSSGVVINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2095 KYGRTVHSLARLLAFWHV-ELHLVSPEQLaLPDDVKDDiranglNFIEHRELtKEVVAQSDVLYCTRVQKERFASVDEYE 2173
Cdd:PRK13814  167 RHSRVANSLMDGLVTMGVpEIRLVGPSSL-LPDKVGND------SIKKFTEL-KPSLLNSDVIVTLRLQKERHDNSVDID 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113967  2174 KLKDSFIVDNSVLASAKSHCIVMHPLPRNREISEEVDF-DQRRAAYFRQMRYGLYIRMALL 2233
Cdd:PRK13814  239 AFRGSFRLTPEKLYSAKPDAIVMHPGPVNREVEINSDVaDNQQSVILQQVRNGVAMRMAVL 299
PRK00779 PRK00779
ornithine carbamoyltransferase; Provisional
 1937-2237 5.65e-44

ornithine carbamoyltransferase; Provisional


Pssm-ID: 234835 [Multi-domain]  Cd Length: 304  Bit Score: 162.95  E-value: 5.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1937 KHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLcTMFFE-PSTRTSSSFDAAMQRLGGKVVAVTASASSVN 2015
Cdd:PRK00779    5 RHFLSLDDLSPEELEELLDLAAELKKKRKAGEPHPPLKGKTL-AMIFEkPSTRTRVSFEVGMAQLGGHAIFLSPRDTQLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2016 KGESLADTIRTLGCYGDAIVLR---HPSIEsaRIAANfSPVPIING-GNgsKEHPTQAFLDLYTIREELGSVNGLTITFI 2091
Cdd:PRK00779   84 RGEPIEDTARVLSRYVDAIMIRtfeHETLE--ELAEY-STVPVINGlTD--LSHPCQILADLLTIYEHRGSLKGLKVAWV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2092 GDlkyGRTV-HSL---ARLLAFwhvELHLVSPEQLA-LPDDVKDDIRANGlnfiEHRELT---KEVVAQSDVLYcTRVqk 2163
Cdd:PRK00779  159 GD---GNNVaNSLllaAALLGF---DLRVATPKGYEpDPEIVEKIAKETG----ASIEVThdpKEAVKGADVVY-TDV-- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2164 erFASV---DEYE-KLKD--SFIVDNSVLASAKSHCIVMHPLPRNR--EISEEVdFDQRRAAYFRQMRYGLYIRMALLAC 2235
Cdd:PRK00779  226 --WVSMgqeAEAEeRLKAfaPYQVNEELMALAKPDAIFMHCLPAHRgeEVTDEV-IDGPQSVVWDEAENRLHAQKALLAW 302


                  ..
gi 19113967  2236 VM 2237
Cdd:PRK00779  303 LL 304
OTCace pfam00185
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
2087-2234 9.10e-33

Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;


Pssm-ID: 425511 [Multi-domain]  Cd Length: 154  Bit Score: 125.41  E-value: 9.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   2087 TITFIGDlKYGRTVHSLARLLAFWHVELHLVSPEQLALPDDVKDDIRANGLN---FIEHRELTKEVVAQSDVLYCTRVQ- 2162
Cdd:pfam00185    1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVLDKAKKIAEKsggSIEITDDPAEAVKGADVVYTDVWQs 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113967   2163 ----KERFasvDEYEKLKDsFIVDNSVLASAKSHCIVMHPLPRNR--EISEEVdFDQRRAAYFRQMRYGLYIRMALLA 2234
Cdd:pfam00185   80 mgqeKERE---ERLKAFKP-YQVNEELMKLAKKDAIFMHCLPAHRgeEVTDDV-FDGPRSVVFDQAENRLHAQKALLA 152
PLN02342 PLN02342
ornithine carbamoyltransferase
 1937-2239 8.70e-31

ornithine carbamoyltransferase


Pssm-ID: 177976 [Multi-domain]  Cd Length: 348  Bit Score: 126.06  E-value: 8.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1937 KHIISVHQVTRSDLHVLFAIAHQMRIIVERQgviDLCY----GKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASAS 2012
Cdd:PLN02342   46 KHFLHIDDFDKEEILGLLDRAKEVKALLKSG---DRSFqpfkGKSMAMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2013 SVNKGESLADTIRTLGCYGDAIVLR---HPSIESariAANFSPVPIINGGNgSKEHPTQAFLDLYTIREELGSVNGLTIT 2089
Cdd:PLN02342  123 QLGKREETRDIARVLSRYNDIIMARvfaHQDVLD---LAEYSSVPVINGLT-DYNHPCQIMADALTIIEHIGRLEGTKVV 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2090 FIGDlkyGRT-VHSLARLLAFWHVELHLVSPEQLAlPD-DVKDDIRANGLNFIEHRELTKEVVAQSDVLYcTRV-----Q 2162
Cdd:PLN02342  199 YVGD---GNNiVHSWLLLAAVLPFHFVCACPKGYE-PDaKTVEKARAAGISKIEITNDPAEAVKGADVVY-TDVwasmgQ 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2163 KErfasvdEYEKLK---DSFIVDNSVLASAKSHCIVMHPLPRNR--EISEEVdFDQRRAAYFRQMRYGLYIRMALLACVM 2237
Cdd:PLN02342  274 KE------EAEKRKkafQGFQVNEALMKLAGPQAYFMHCLPAERgvEVTDGV-MEAPNSIVFPQAENRMHAQNAIMLHQL 346


                  ..
gi 19113967  2238 GA 2239
Cdd:PLN02342  347 GK 348
pyrB PRK13376
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ...
 1981-2241 1.12e-30

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


Pssm-ID: 237369 [Multi-domain]  Cd Length: 525  Bit Score: 129.49  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1981 MFFEPSTRTSSSF-DAAMQRLGGKVVAVTASASSVNKGESLADTIRTLGCYGD-AIVLRHPSIESA-----RIAANFS-- 2051
Cdd:PRK13376   56 VFVEPSTRTKESFiNAAKFHKNVKVNIFDSEHSSFNKQESYTDTFNMLTGYSDySIFIVRTRLEGVcrlleEKVSEFAsr 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2052 ---PVP-IINGGNGSKEHPTQAFLDLYTIREELGSVNG-LTITFIGDLKYGRTVHSLAR-LLAFWHVELHLVSPEQLALP 2125
Cdd:PRK13376  136 ngiEVPaFINAGDGKHEHPTQELLDEFTFLEQNNFDNSfIHIALVGDLLHGRTVHSKVNgLKIFKNVKVDLIAPEELAMP 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2126 DDVKDDIRANGLNFIEHRELtKEVVAQSDVL---YCTRVQKERFASvDEYEK---LKDSFIVDNSVLASAKSHCIVMHPL 2199
Cdd:PRK13376  216 EHYVEKMKKNGFEVRIFSSI-EEYLSQKDVAkiwYFTRLQLERMGE-DILEKehiLRKAVTFRKEFLDKLPEGVKFYHPL 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 19113967  2200 PRNREISEEVDF--DQRRAAYFRQMRYGLYIRMALLACVMGATE 2241
Cdd:PRK13376  294 PRHKVYPTIPTFldTLPLNGWETQAINGYWVRIVLLSMLGGALE 337
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 882-959 3.32e-30

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: 115.17  E-value: 3.32e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113967    882 ELQTPSDQRLFAIANAMASGYSVDRIWELTRIDKWFLEKLMGLIRTSQLISKHDiSSLPISLLKTAKQLGFADVQIAA 959
Cdd:pfam02787    2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAG-LDLDAELLREAKRLGFSDRQIAK 78
PRK02102 PRK02102
ornithine carbamoyltransferase; Validated
 1975-2200 1.38e-26

ornithine carbamoyltransferase; Validated


Pssm-ID: 179366 [Multi-domain]  Cd Length: 331  Bit Score: 113.06  E-value: 1.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1975 GKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASASSVNKGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVP 2054
Cdd:PRK02102   46 GKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLGPNDSQLGKKESIEDTARVLGRMYDGIEYRGFKQEIVEELAKYSGVP 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2055 IINGGNgSKEHPTQAFLDLYTIREELGSVNGLTITFIGDlkyGR--TVHSLARLLAFWHVELHLVSPEQLALPDDVKDDI 2132
Cdd:PRK02102  126 VWNGLT-DEWHPTQMLADFMTMKEHFGPLKGLKLAYVGD---GRnnMANSLMVGGAKLGMDVRICAPKELWPEEELVALA 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113967  2133 RA----NGlNFIEHRELTKEVVAQSDVLYcTRV------QKERfasvDEYEKLKDSFIVDNSVL-ASAKSHCIVMHPLP 2200
Cdd:PRK02102  202 REiakeTG-AKITITEDPEEAVKGADVIY-TDVwvsmgeEDEW----EERIKLLKPYQVNMDLMkATGNPDVIFMHCLP 274
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 1117-1332 8.33e-25

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: 106.11  E-value: 8.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1117 GTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYvlSGAAMNT--VYSQSDLHSYLQQ 1194
Cdd:COG0439   43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPAD--GAGSRGVrvVRDEEELEAALAE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1195 AVAINK----DHPVVISKYIENaKEIELDAVAREGKMVMHVISEHvENAGVHSGDATLVLPPqDLAPTTIERIVDAAAKI 1270
Cdd:COG0439  121 ARAEAKagspNGEVLVEEFLEG-REYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGELVARA 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113967 1271 GEALNI-TGPYNIQFI-AKDNEIKVIECNVRAS--RSFPFVSKVIGVDMISMATDVIMGNPIQPYP 1332
Cdd:COG0439  198 LRALGYrRGAFHTEFLlTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPRILDP 263
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1151-1328 3.04e-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: 3.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1151 SFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQAVAINK----DHPVVISKYIENAKEIELDAVAREGK 1226
Cdd:pfam02786   26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPaafgNPQVLVEKSLKGPKHIEYQVLRDAHG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1227 MVMHVISehVENA-GVHSGDATLVLPPQDLAPTTIERIVDAAAKIGEALNITGPYNIQFI--AKDNEIKVIECNVRASRS 1303
Cdd:pfam02786  106 NCITVCN--RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQVE 183

                          170       180
                   ....*....|....*....|....*
gi 19113967   1304 FPFVSKVIGVDMISMATDVIMGNPI 1328
Cdd:pfam02786  184 HALAEKATGYDLAKEAAKIALGYPL 208
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 1409-1505 1.31e-21

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: 91.01  E-value: 1.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1409 ELLPYVKKLYENNYNIFATAGTSDYFMESGVPCKYLADLPAEEANN-EYSLSAHLANNMIDMYINLPSNNRYRRPanyis 1487
Cdd:pfam02142    1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGRPGgRVQIGDLIKNGEIDLVINTLYPFKATVH----- 75

                           90
                   ....*....|....*...
gi 19113967   1488 SGYKSRRLAIDYSVPLVT 1505
Cdd:pfam02142   76 DGYAIRRAAENIDIPGPT 93
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 1539-1842 2.68e-21

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: 97.46  E-value: 2.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1539 LPGLINISAFLPEFTSEAVS-DYTKECIAS---GFTMARFLPFsTSSTLADKDSLSAVKKLALDHAHCDYNFSVIASS-- 1612
Cdd:cd01302    4 LPGFIDIHVHLRDPGGTTYKeDFESGSRAAaagGVTTVIDMPN-TGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGPgd 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1613 -TNEVTISELTSESGCLFFHFEKDDSGIDH-VTAVASHFNVWPDTQT-VMTDAKSTTLASLLLlaslhNRRIHITNVSSK 1689
Cdd:cd01302   83 vTDELKKLFDAGINSLKVFMNYYFGELFDVdDGTLMRTFLEIASRGGpVMVHAERAAQLAEEA-----GANVHIAHVSSG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1690 DDLNLIVLAKQRSLPVTFDVSVYSLFLNQNDYP--GATF-----LPTADDQVEIWNKLS--YIDCFSIGSIPSRLA-KFV 1759
Cdd:cd01302  158 EALELIKFAKNKGVKVTCEVCPHHLFLDESMLRlnGAWGkvnppLRSKEDREALWEGVKngKIDTIASDHAPHSKEeKES 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1760 GN---TAFTGF-GVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRL---------HDQDDSGVQLEVDRSVS----W 1822
Cdd:cd01302  238 GKdiwKAPPGFpGLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLypkgtiavgYDADLVIVDPKKEWKVTaeeiE 317

                        330       340
                 ....*....|....*....|
gi 19113967 1823 SSKDWTPFNGKKLYGSIQSV 1842
Cdd:cd01302  318 SKADWTPFEGMEVTGKPVST 337
PRK14805 PRK14805
ornithine carbamoyltransferase; Provisional
 1937-2239 1.34e-20

ornithine carbamoyltransferase; Provisional


Pssm-ID: 237819 [Multi-domain]  Cd Length: 302  Bit Score: 94.75  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1937 KHIISVHQVTRSDLHVLFAIAHQMRIIVE--RQGVIdlcyGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASASSV 2014
Cdd:PRK14805    2 KHLLSIKELTQQQLLDLLALAKTIKANPAeyRQALA----GKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2015 NKGESLADTIRTLGCYGDAIVLR---HPSIESariAANFSPVPIINGGNgSKEHPTQAFLDLYTIREELGSVNGLTITFI 2091
Cdd:PRK14805   78 GKRESVADFAANLSCWADAIVARvfsHSTIEQ---LAEHGSVPVINALC-DLYHPCQALADFLTLAEQFGDVSKVKLAYV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2092 GDlkyGRTV-HSLARLLAFWHVELHLVSPEQlALPD-----DVKDDIRANGLNFIEHRELtkEVVAQSDVLYC-TRVQKE 2164
Cdd:PRK14805  154 GD---GNNVtHSLMYGAAILGATMTVICPPG-HFPDgqivaEAQELAAKSGGKLVLTSDI--EAIEGHDAIYTdTWISMG 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2165 RFASVDEyekLKDSFI---VDNSVLASAKSHcIVMHPLPRNR--EISEEVdFDQRRAAYFRQMRYGLYIRMALLACVMGA 2239
Cdd:PRK14805  228 DDTPLAE---IKAKFApyqVNKALMEKAGAT-FVMHCQPAHRgvEITSEV-MDGEGSLILQQAENRMHAQNAVLVTLLSQ 302
PRK04284 PRK04284
ornithine carbamoyltransferase; Provisional
 1975-2240 7.07e-20

ornithine carbamoyltransferase; Provisional


Pssm-ID: 235269 [Multi-domain]  Cd Length: 332  Bit Score: 93.27  E-value: 7.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1975 GKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASASSVNKGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVP 2054
Cdd:PRK04284   45 GKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGPTGSQMGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSGVP 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2055 IINGGNgSKEHPTQAFLDLYTIREEL-GSVNGLTITFIGDlkyGR--TVHSLARLLAFWHVELHLVSPEQLALPDDVKDD 2131
Cdd:PRK04284  125 VWNGLT-DEDHPTQVLADFLTAKEHLkKPYKDIKFTYVGD---GRnnVANALMQGAAIMGMDFHLVCPKELNPDDELLNK 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2132 IRA----NGLNfIEHRELTKEVVAQSDVLYcTRVQKERFASVDEYE---KLKDSFIVDNSVLASAKS-HCIVMHPLP--- 2200
Cdd:PRK04284  201 CKEiaaeTGGK-ITITDDIDEGVKGSDVIY-TDVWVSMGEPDEVWEeriKLLKPYQVNKEMMKKTGNpNAIFEHCLPsfh 278

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113967  2201 ----------------RNREISEEVdFDQRRAAYFRQMRYglyiRMALLACVMGAT 2240
Cdd:PRK04284  279 dldtkvgkeifekyglKEMEVTDEV-FESKASVVFDEAEN----RMHTIKAVMVAT 329
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 265-425 1.46e-18

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: 85.66  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  265 ILVID-----VGMKYNQIRcflNRGVELLVVPWD----YDFTKETYDGLFISNGPGDPSLMDLVVDRVKRVleSKTVPVF 335
Cdd:cd01743    1 ILLIDnydsfTYNLVQYLR---ELGAEVVVVRNDeitlEELELLNPDAIVISPGPGHPEDAGISLEIIRAL--AGKVPIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  336 GICFGHQIMARAAGAS-----------TTKMKFGNRG--HNIPcTCMISGRcYitsqnHGYAVDASSLSngwKELFVNAN 402
Cdd:cd01743   76 GVCLGHQAIAEAFGGKvvrapepmhgkTSEIHHDGSGlfKGLP-QPFTVGR-Y-----HSLVVDPDPLP---DLLEVTAS 145

                        170       180
                 ....*....|....*....|....*
gi 19113967  403 DGSNE--GIYNTEYPFFSVQFHPES 425
Cdd:cd01743  146 TEDGVimALRHRDLPIYGVQFHPES 170
PRK12562 PRK12562
ornithine carbamoyltransferase subunit F; Provisional
 1932-2120 1.91e-17

ornithine carbamoyltransferase subunit F; Provisional


Pssm-ID: 105755  Cd Length: 334  Bit Score: 86.27  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1932 SPFYRKHIISVHQVTRSDLHVLFAIAHQMRIIVERQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASA 2011
Cdd:PRK12562    2 SGFYKKHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2012 SSVNKGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNgSKEHPTQAFLDLYTIREEL--GSVNGLTIT 2089
Cdd:PRK12562   82 SQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWNGLT-NEFHPTQLLADLLTMQEHLpgKAFNEMTLV 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 19113967  2090 FIGDLKyGRTVHSLARLLAFWHVELHLVSPE 2120
Cdd:PRK12562  161 YAGDAR-NNMGNSMLEAAALTGLDLRLVAPQ 190
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 574-781 6.90e-17

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 83.00  E-value: 6.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  574 EQLGVKvlGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKDISFPVIVRAAYALGGLGSGFADNEAEL 653
Cdd:COG0439   37 EELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  654 IDLCTLAFA------TSPQVLIERSMKGwKEIEYEVVrdAFDNCITVCNM---ENFDPLGIHTGDsivVAPSQtLTDEDY 724
Cdd:COG0439  115 EAALAEARAeakagsPNGEVLVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELR 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  725 NMLRTTAVNVIRHLGVV-GECNIQYALNPfTKEYCIIEVNARLS--RSSALASKATGYPL 781
Cdd:COG0439  188 AEIGELVARALRALGYRrGAFHTEFLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDL 246
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 1539-1863 2.33e-16

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: 83.99  E-value: 2.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1539 LPGLINISAFL--PEFTSeavsdytKECIAS--------GFT----MARflpfsTSSTLADKDSLSAVKKLALDHAHCDY 1604
Cdd:COG0044   49 LPGLIDLHVHLrePGLEH-------KEDIETgtraaaagGVTtvvdMPN-----TNPVTDTPEALEFKLARAEEKALVDV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1605 NFSVIASSTNEVTISEL--TSESGCL-FFHFEKDDSG-----------------------IDH---------------VT 1643
Cdd:COG0044  117 GPHGALTKGLGENLAELgaLAEAGAVaFKVFMGSDDGnpvlddgllrraleyaaefgalvAVHaedpdlirggvmnegKT 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1644 AVASHFNVWPD---TQTVMTD---AKSttlasllllaslHNRRIHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLN 1717
Cdd:COG0044  197 SPRLGLKGRPAeaeEEAVARDialAEE------------TGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLT 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1718 QNDYP--GATF-----LPTADDQVEIWNKLS--YIDCfsIGS--IPSRLA-KFVG-NTAFTGF-GVREAIPLLLT-AVNE 1782
Cdd:COG0044  265 DEDLEryGTNFkvnppLRTEEDREALWEGLAdgTIDV--IATdhAPHTLEeKELPfAEAPNGIpGLETALPLLLTeLVHK 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1783 GRLTLKDVVDRFYSNPKAIFRLHDQ---------D----DSGVQLEVDRSVSWSSKDWTPFNGKKLYGSIQSVQFDGHDV 1849
Cdd:COG0044  343 GRLSLERLVELLSTNPARIFGLPRKgriavgadaDlvlfDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVV 422

                        410
                 ....*....|....
gi 19113967 1850 FFDGELNfEHTYGR 1863
Cdd:COG0044  423 YEDGEVV-GEPRGR 435
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 265-425 1.95e-15

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


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 76.62  E-value: 1.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  265 ILVID-----VgmkYN---QIRCFlnrGVELLVVPWD----YDFTKETYDGLFISNGPGDPS---LMDLVVDRVKRvles 329
Cdd:COG0512    1 ILLIDnydsfT---YNlvqYLGEL---GAEVVVVRNDeitlEEIEALAPDGIVLSPGPGTPEeagISLEVIRAFAG---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  330 kTVPVFGICFGHQIMARAAGAS-----------TTKMKFGNRG--HNIPcTCMISGRcYitsqnHGYAVDASSLSngwKE 396
Cdd:COG0512   71 -KIPILGVCLGHQAIGEAFGGKvvrapepmhgkTSPITHDGSGlfAGLP-NPFTATR-Y-----HSLVVDRETLP---DE 139

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19113967  397 LFVNANDGSNE--GIYNTEYPFFSVQFHPES 425
Cdd:COG0512  140 LEVTAWTEDGEimGIRHRELPIEGVQFHPES 170
PRK04523 PRK04523
N-acetylornithine carbamoyltransferase; Reviewed
 1937-2238 2.56e-15

N-acetylornithine carbamoyltransferase; Reviewed


Pssm-ID: 235304 [Multi-domain]  Cd Length: 335  Bit Score: 79.79  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1937 KHIISVHQVTRSDLHVLFAIAHQMRiiveRQGVIDLCYGKLLCTMFFEPSTRTSSSFDAAMQRLGGK-VVAVTASAS--- 2012
Cdd:PRK04523    4 KHFLNTQDWSRAELDALLTQAAAFK----RNKLGSALKGKSIALVFFNPSLRTRTSFELGAFQLGGHaVVLQPGKDAwpi 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2013 -----SVNKG---ESLADTIRTLGCYGDAIVLR-------------HPSIESariAANFSPVPIINggNGSKEHPTQAFL 2071
Cdd:PRK04523   80 efelgAVMDGeteEHIREVARVLSRYVDLIGVRafpkfvdwskdrqDQVLNS---FAKYSTVPVIN--METITHPCQELA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2072 DLYTIREELGsvngltiTFIGDLKYGRT------------VHSLARLLAFWHVELHLVSP-EQLALPDDVKD----DIRA 2134
Cdd:PRK04523  155 HALALQEHFG-------TTLRGKKYVLTwtyhpkplntavANSALLIATRLGMDVTLLCPtPDYILDERYMDwaeqNAAE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2135 NGLNF-IEHREltKEVVAQSDVLYCTRVQKERFASVDEYEK-LKDS---FIVDNSVLASAK----SHCIvmhPLPRNREI 2205
Cdd:PRK04523  228 SGGSLtVSHDI--DSAYAGADVVYAKSWGALPFFGNWEPEKpIRDQyqhFIVDERKMALTNngvfSHCL---PLRRNVKV 302

                         330       340       350
                  ....*....|....*....|....*....|...
gi 19113967  2206 SEEVdFDQRRAAYFRQMRYGLYIRMALLACVMG 2238
Cdd:PRK04523  303 TDAV-MDSPNCIAIDEAENRLHVQKAIMAALAS 334
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
476-823 7.75e-15

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 78.82  E-value: 7.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  476 RVLILGS--GGLSIgqagefdysgsqaIKALREEGIYTILINPN-IATIQTSKGLADKVYFLPVNAD------FVRKVIK 546
Cdd:COG3919    7 RVVVLGGdiNALAV-------------ARSLGEAGVRVIVVDRDpLGPAARSRYVDEVVVVPDPGDDpeafvdALLELAE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  547 QERPDSIYVTfgGQTALNVGIELKDEFEQlGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVSKD 626
Cdd:COG3919   74 RHGPDVLIPT--GDEYVELLSRHRDELEE-HYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAED 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  627 ISFPVIVRAAYALGGLGSGF--------ADNEAELIDLCTLAFATSPQVLIErsmkgwkeieyEVVrDAFDNCITVCNM- 697
Cdd:COG3919  151 LGFPVVVKPADSVGYDELSFpgkkkvfyVDDREELLALLRRIAAAGYELIVQ-----------EYI-PGDDGEMRGLTAy 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  698 --ENFDPLGIHTGDSIVVAPSQ--------TLTDEDynmLRTTAVNVIRHLGVVGECNIQYALNPFTKEYCIIEVNARLS 767
Cdd:COG3919  219 vdRDGEVVATFTGRKLRHYPPAggnsaareSVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFW 295

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113967  768 RSSALASKAtGYPLAFTAAKLGLNIPLNEVKNSVTKVTCACFEPSLDYVVVKIPRW 823
Cdd:COG3919  296 RSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGVLWRVLPGDLLLRYLRDGEL 350
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 265-426 9.47e-15

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: 74.49  E-value: 9.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  265 ILVIDVGMKYNQI--RCFLNRGVELLVVPWDYDF---TKETYDGLFISNGPgdPSLMDLVVDRV-KRVLESKtVPVFGIC 338
Cdd:cd01742    1 ILILDFGSQYTHLiaRRVRELGVYSEILPNTTPLeeiKLKNPKGIILSGGP--SSVYEEDAPRVdPEIFELG-VPVLGIC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  339 FGHQIMARAAGASTTKmkfGNRGHNIPCTCMISGRCYI------TSQ---NHGYAVDAssLSNGWKELFVNANDGsNEGI 409
Cdd:cd01742   78 YGMQLIAKALGGKVER---GDKREYGKAEIEIDDSSPLfeglpdEQTvwmSHGDEVVK--LPEGFKVIASSDNCP-VAAI 151

                        170
                 ....*....|....*..
gi 19113967  410 YNTEYPFFSVQFHPEST 426
Cdd:cd01742  152 ANEEKKIYGVQFHPEVT 168
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 476-793 1.13e-14

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 77.62  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   476 RVLILGSGGlsigqagefdysGSQAIKALREE-GIYTIL---INPNIATIQtskgLADKVYFLP-VNA----DFVRKVIK 546
Cdd:PRK12767    3 NILVTSAGR------------RVQLVKALKKSlLKGRVIgadISELAPALY----FADKFYVVPkVTDpnyiDRLLDICK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   547 QERPDSIYVTFggQTALNVGIELKDEFEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKCAKSASASSIEEAIKVS-- 624
Cdd:PRK12767   67 KEKIDLLIPLI--DPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALak 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   625 KDISFPVIVRAAYALGGLGSGFADNEAELidlcTLAFATSPQVLIERSMKGwKEIEYEVVRDAFDNCITVCNMENFDPLG 704
Cdd:PRK12767  145 GELQFPLFVKPRDGSASIGVFKVNDKEEL----EFLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIEVRA 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   705 ihtGDSivvapSQTLTDEDYNmLRTTAVNVIRHLGVVGECNIQYALNPftKEYCIIEVNARLSrssalaskaTGYPLAFT 784
Cdd:PRK12767  220 ---GET-----SKGVTVKDPE-LFKLAERLAEALGARGPLNIQCFVTD--GEPYLFEINPRFG---------GGYPLSYM 279


                  ....*....
gi 19113967   785 AaklGLNIP 793
Cdd:PRK12767  280 A---GANEP 285
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 264-427 1.57e-14

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: 74.98  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  264 RILVIDVGM---KYNQI--RCFLNRGVELLVV------PWDYDFTKETYDGLFISNGP-----GDPSLMDLVvDRVKRVL 327
Cdd:COG0518    1 KILILDHDPfggQYPGLiaRRLREAGIELDVLrvyageILPYDPDLEDPDGLILSGGPmsvydEDPWLEDEP-ALIREAF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  328 ESKtVPVFGICFGHQIMARAAGASTTKmkfgNRGHNIpctcmisGR--CYITSQN---------------HGYAVDAssL 390
Cdd:COG0518   80 ELG-KPVLGICYGAQLLAHALGGKVEP----GPGREI-------GWapVELTEADplfaglpdeftvwmsHGDTVTE--L 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19113967  391 SNGWKELFVNANDgSNEGIYNTEyPFFSVQFHPESTP 427
Cdd:COG0518  146 PEGAEVLASSDNC-PNQAFRYGR-RVYGVQFHPEVTH 180
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 1680-1839 8.28e-14

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: 75.74  E-value: 8.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1680 RIHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLNQND---Y-PGATFLP---TADDQVEIWNKLS--YIDCFSIGS 1750
Cdd:cd01317  187 RVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEAlesYdTNAKVNPplrSEEDREALIEALKdgTIDAIASDH 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1751 IP-SRLAKFVG--NTAFTGFGVREAIPLLLT-AVNEGRLTLKDVVDRFYSNPKAIFRL--------HDQD----DSGVQL 1814
Cdd:cd01317  267 APhTDEEKDLPfaEAPPGIIGLETALPLLWTlLVKGGLLTLPDLIRALSTNPAKILGLppgrlevgAPADlvlfDPDAEW 346

                        170       180
                 ....*....|....*....|....*
gi 19113967 1815 EVDRSVSWSSKDWTPFNGKKLYGSI 1839
Cdd:cd01317  347 IVDEETFRSKSKNTPFDGQKLKGRV 371
PRK04250 PRK04250
dihydroorotase; Provisional
 1677-1855 2.33e-13

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 74.42  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1677 HNRRIHITNVSSKDDLNLIvlaKQRSLP-VTFDVSVYSLFLNQNDYPGATF------LPTADDQVEIWNKLSYIDCFSIG 1749
Cdd:PRK04250  196 LKKPLHICHISTKDGLKLI---LKSNLPwVSFEVTPHHLFLTRKDYERNPLlkvyppLRSEEDRKALWENFSKIPIIASD 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1750 SIPSRLA-KFVGNTAFTGfgVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRL--------HDQDDSGVQLEVDRSV 1820
Cdd:PRK04250  273 HAPHTLEdKEAGAAGIPG--LETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIknygieegNYANFAVFDMKKEWTI 350

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 19113967  1821 S----WSSKDWTPFNGKKLYGSIQSVQFDGHDVFFDGEL 1855
Cdd:PRK04250  351 KaeelYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI 389
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1036-1328 6.34e-13

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 73.86  E-value: 6.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1036 AVRAVRTLRDRGVKTIMVnynpetvstdYDEADR--LY------------------FENIglETVLDIYEQESSSGIIIA 1095
Cdd:PRK08654   14 AIRVMRACRELGIKTVAV----------YSEADKnaLFvkyadeaypigpappsksYLNI--ERIIDVAKKAGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1096 MGGQTAN-NIALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKE--LTSFDEADKFCDTVGYPVLVRPSY 1172
Cdd:PRK08654   82 YGFLAENpEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEegIEDIEEAKEIAEEIGYPVIIKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1173 VLSGAAMNTVYSQSDLHSYLQ--QAVAIN--KDHPVVISKYIENAKEIELDAVAREGKMVMHV------IS-EH---VEN 1238
Cdd:PRK08654  162 GGGGIGMRVVYSEEELEDAIEstQSIAQSafGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLgdrecsIQrRHqklIEE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1239 AgvhsgdatlvlPPQDLAPTTIERIVDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSFPFVSKVIGVDMISM 1318
Cdd:PRK08654  242 A-----------PSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKE 310

                         330
                  ....*....|
gi 19113967  1319 ATDVIMGNPI 1328
Cdd:PRK08654  311 QIKIAAGEEL 320
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 1077-1306 7.35e-13

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 72.22  E-value: 7.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1077 LETVLDIYEQESSSGIIiamggqTANNIALPL---HRE-----NVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKE 1148
Cdd:PRK12767   58 IDRLLDICKKEKIDLLI------PLIDPELPLlaqNRDrfeeiGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1149 LTSFDEADKFCDT--VGYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQAVAInkdhpvVISKYIEnAKEIELDA-VAREG 1225
Cdd:PRK12767  132 PESLEDFKAALAKgeLQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPNL------IIQEFIE-GQEYTVDVlCDLNG 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1226 KMVMHVISEHVEnagVHSGDAtlvlppqDLAPTTI-ERIVDAAAKIGEALNITGPYNIQFIAKDNEIKVIECNVRASRSF 1304
Cdd:PRK12767  205 EVISIVPRKRIE---VRAGET-------SKGVTVKdPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGY 274


                  ..
gi 19113967  1305 PF 1306
Cdd:PRK12767  275 PL 276
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 265-425 8.10e-13

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 69.00  E-value: 8.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   265 ILVID-----VgmkYN---QIRCFlnrGVELLVVPWD----YDFTKETYDGLFISNGPGDPSLMDLVVDRVKRVleSKTV 332
Cdd:PRK05670    2 ILLIDnydsfT---YNlvqYLGEL---GAEVVVYRNDeitlEEIEALNPDAIVLSPGPGTPAEAGISLELIREF--AGKV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   333 PVFGICFGHQIMARAAGAS-----------TTKMKFGNRG--HNIPcTCMISGRcYitsqnHGYAVDASSLSngwKELFV 399
Cdd:PRK05670   74 PILGVCLGHQAIGEAFGGKvvrakeimhgkTSPIEHDGSGifAGLP-NPFTVTR-Y-----HSLVVDRESLP---DCLEV 143

                         170       180
                  ....*....|....*....|....*...
gi 19113967   400 NA--NDGSNEGIYNTEYPFFSVQFHPES 425
Cdd:PRK05670  144 TAwtDDGEIMGVRHKELPIYGVQFHPES 171
MGS_CPS_II cd01424
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ...
 1396-1515 1.46e-12

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: 65.96  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1396 NILISIgSYKEKAELLPYVKKLYENNYNIFATAGTSDYFMESGVPCKYLADLpAEEANNeysLSAHLANNMIDMYINLPS 1475
Cdd:cd01424    2 TVFISV-ADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKV-SEGRPN---IVDLIKNGEIQLVINTPS 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19113967 1476 NNRYRRPanyissGYKSRRLAIDYSVPLVTNVKCAKLMIE 1515
Cdd:cd01424   77 GKRAIRD------GFSIRRAALEYKVPYFTTLDTARAAVE 110
PRK01713 PRK01713
ornithine carbamoyltransferase; Provisional
 1915-2127 1.61e-12

ornithine carbamoyltransferase; Provisional


Pssm-ID: 167263 [Multi-domain]  Cd Length: 334  Bit Score: 71.17  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1915 MTPNFKPSHeLVQLINSSPFYRKHIISVhqvTRSDLHVLFAIAHQMRIiverqgvidlcYGKLLCTMFFEPSTRTSSSFD 1994
Cdd:PRK01713    1 MAFNLKNRH-LLSLVNHTEREIKYLLDL---SRDLKRAKYAGTEQQRL-----------KGKNIALIFEKTSTRTRCAFE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1995 AAMQRLGGKVVAVTASASSVNKGESLADTIRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNgSKEHPTQAFLDLY 2074
Cdd:PRK01713   66 VAAYDQGAQVTYIDPNSSQIGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFNGLT-DEFHPTQMLADVL 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19113967  2075 TIREELGS-VNGLTITFIGDLKyGRTVHSLARLLAFWHVELHLVSPEQLaLPDD 2127
Cdd:PRK01713  145 TMIENCDKpLSEISYVYIGDAR-NNMGNSLLLIGAKLGMDVRICAPKAL-LPEA 196
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 1677-1839 7.57e-11

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: 66.20  E-value: 7.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1677 HNRRIHITNVSSKDDLNLIVLAKQRslpVTFDVSVYSLFLNQNDY-PGATF------LPTADDQVEIWNKLSYIDCFSIG 1749
Cdd:cd01318  170 HGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYdRLGTLgkvnppLRSREDRKALLQALADGRIDVIA 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1750 S-----IPSRLAKFVGNTAfTGF-GVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRL---------HDQDDSGVQL 1814
Cdd:cd01318  247 SdhaphTLEEKRKGYPAAP-SGIpGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIknkgriaegYDADLTVVDL 325

                        170       180
                 ....*....|....*....|....*....
gi 19113967 1815 EVDRSVSWS---SKD-WTPFNGKKLYGSI 1839
Cdd:cd01318  326 KEERTIRAEefhSKAgWTPFEGFEVTGFP 354
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 574-864 2.46e-10

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 65.43  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   574 EQLGVKVLGTPIDTIITTEDRELFARAMDEINEKC--AKSASASSIEEAIKVSKDISFPVIVRAAYALGGLGSGFADNEA 651
Cdd:PRK06111   96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpGITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQ 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   652 ELIDlctlAFATS----------PQVLIERSMKGWKEIEYEVVRDAFDNCitvcnmenfdplgIHTGD---SI------V 712
Cdd:PRK06111  176 ELTK----AFESNkkraanffgnGEMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkV 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   713 V--APSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPfTKEYCIIEVNARLSRSSALASKATGY----------- 779
Cdd:PRK06111  239 IeeAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDE-QKNFYFLEMNTRLQVEHPVTEEITGIdlveqqlriaa 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   780 --PLAFTAAKLGLNIPLNEVK-NSVTKVTcacFEPSLDyvvvKIPRWDLKK--FTRVSTQLSSAMK-------SVGEVMS 847
Cdd:PRK06111  318 geKLSFTQDDIKRSGHAIEVRiYAEDPKT---FFPSPG----KITDLTLPGgeGVRHDHAVENGVTvtpfydpMIAKLIA 390

                         330
                  ....*....|....*..
gi 19113967   848 IGRTFEEAIQKAIRAID 864
Cdd:PRK06111  391 HGETREEAISRLHDALE 407
PRK14804 PRK14804
ornithine carbamoyltransferase; Provisional
 1937-2214 1.17e-09

ornithine carbamoyltransferase; Provisional


Pssm-ID: 173265 [Multi-domain]  Cd Length: 311  Bit Score: 61.97  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1937 KHIISVHQVTRSDLHVL--FAIaHQMRIIVERQGVIDlcyGKLLCTMFFEPSTRTSSSFDAAMQRLGGKVVAVTASASSV 2014
Cdd:PRK14804    7 KHLISWEDWSDSEILDLldFAV-HVKKNRVNYAGHMS---GRSLAMLFQKTSTRTRVSFEVAMTEMGGHGIYLDWMASNF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2015 nkgeSLADT---IRTLGCYGDAIVLRHPSIESARIAANFSPVPIINGGNgSKEHPTQAFLDLYTIREELGSV--NGLTIT 2089
Cdd:PRK14804   83 ----QLSDIdleARYLSRNVSVIMARLKKHEDLLVMKNGSQVPVINGCD-NMFHPCQSLADIMTIALDSPEIplNQKQLT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  2090 FIGdlKYGRTVHSLARLLAFWHVELHLVSPeqLALPDDVKDDI--RANGLNFIEHRELTKEVVAQSDVLYCTRVQKERFA 2167
Cdd:PRK14804  158 YIG--VHNNVVNSLIGITAALGIHLTLVTP--IAAKENIHAQTveRAKKKGTLSWEMNLHKAVSHADYVYTDTWLDMEFF 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113967  2168 SVDEYEKLKDSFI-------VDNSVLasAKSHCIVMHPLP--RNREISEEVDFDQR 2214
Cdd:PRK14804  234 NDPSYADKKKQRMelmmpyqINSSLM--EKTNAKVMHDMPihAGYEITREVVLSDR 287
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 299-424 1.71e-09

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: 59.57  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  299 ETYDGLFISNGP------GDPSLMDLVvDRVKRVLESKtVPVFGICFGHQIMARAAGASTTKMKFG-----------NRG 361
Cdd:cd01741   45 DDYDGLVILGGPmsvdedDYPWLKKLK-ELIRQALAAG-KPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtltEAG 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113967  362 HNIPCTCMISGRcyITS-QNHGYAVDAssLSNGWKELFvnANDGSNEGIYNTEYPFFSVQFHPE 424
Cdd:cd01741  123 KADPLFAGLPDE--FPVfHWHGDTVVE--LPPGAVLLA--SSEACPNQAFRYGDRALGLQFHPE 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 265-426 2.80e-09

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: 58.87  E-value: 2.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    265 ILVIDVGMKYNQI--RCFLNRGVELLVVPWDY---DFTKETYDGLFISNGPGdpSLMDLVVDRV-KRVLESKtVPVFGIC 338
Cdd:TIGR00888    1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTTpleEIREKNPKGIILSGGPS--SVYAENAPRAdEKIFELG-VPVLGIC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    339 FGHQIMARAAG---ASTTKMKFGN------------RGHNIPCTCMISgrcyitsqnHGYAVDAssLSNGWKELFVNANd 403
Cdd:TIGR00888   78 YGMQLMAKQLGgevGRAEKREYGKaeleildeddlfRGLPDESTVWMS---------HGDKVKE--LPEGFKVLATSDN- 145

                          170       180
                   ....*....|....*....|...
gi 19113967    404 GSNEGIYNTEYPFFSVQFHPEST 426
Cdd:TIGR00888  146 CPVAAMAHEEKPIYGVQFHPEVT 168
PRK13566 PRK13566
anthranilate synthase component I;
248-425 3.92e-09

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 61.86  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   248 EPHPTTAIKKAD-GKIIRILVID-----VGMKYNQIRCflnRGVELLVVPWDYD---FTKETYDGLFISNGPGDPSlmDL 318
Cdd:PRK13566  511 KNLSAEEPDAAAvGEGKRVLLVDhedsfVHTLANYFRQ---TGAEVTTVRYGFAeemLDRVNPDLVVLSPGPGRPS--DF 585

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   319 VVDRVKRVLESKTVPVFGICFGHQIMARAAG---------ASTTKMKFGNRG-----HNIPcTCMISGRcYitsqnHGYA 384
Cdd:PRK13566  586 DCKATIDAALARNLPIFGVCLGLQAIVEAFGgelgqlaypMHGKPSRIRVRGpgrlfSGLP-EEFTVGR-Y-----HSLF 658

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 19113967   385 VDASSLSngwKELFVNA--NDGSNEGIYNTEYPFFSVQFHPES 425
Cdd:PRK13566  659 ADPETLP---DELLVTAetEDGVIMAIEHKTLPVAAVQFHPES 698
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1036-1316 3.97e-09

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 61.27  E-value: 3.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1036 AVRAVRTLRDRGVKTIMVnynpetvstdYDEADR-----------------------LYFENIGLETVLdiyeqESSSGI 1092
Cdd:PRK05586   14 AVRIIRACREMGIETVAV----------YSEADKdalhvqladeavcigpasskdsyLNIQNIISATVL-----TGAQAI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1093 IIAMGGQTANNIALPLHRE-NVKILGTSPEMIDGAENRFKFSRMLDDIGVD-QPKWK-ELTSFDEADKFCDTVGYPVLVR 1169
Cdd:PRK05586   79 HPGFGFLSENSKFAKMCKEcNIVFIGPDSETIELMGNKSNAREIMIKAGVPvVPGSEgEIENEEEALEIAKEIGYPVMVK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1170 PSYVLSGAAMNTVYSQSDLHSYLQQAVAINK----DHPVVISKYIENAKEIELDAVAREGKMVMHVISEhvenagvhsgD 1245
Cdd:PRK05586  159 ASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaafgDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGER----------D 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1246 ATLVLPPQDL---APTTI------ERIVDAAAKIGEALNITGPYNIQFIA-KDNEIKVIECNVRASRSFPFVSKVIGVDM 1315
Cdd:PRK05586  229 CSLQRRNQKVleeAPSPVmteelrKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDL 308


                  .
gi 19113967  1316 I 1316
Cdd:PRK05586  309 V 309
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
304-509 4.23e-09

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 61.66  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   304 LFISNGPGDPSLMDLVVDRVKRVleSKTVPVFGICFGHQIMARAAGASTTKMKFGNRGHnipcTCMIS----------GR 373
Cdd:PRK14607   48 IVISPGPGRPEEAGISVEVIRHF--SGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGK----TSPIDhngkglfrgiPN 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   374 CYITSQNHGYAVDASSLSNGWkELFVNANDGSNEGIYNTEYPFFSVQFHPESTpGPRDTEFLFDVFIDVVKRSADAKSLq 453
Cdd:PRK14607  122 PTVATRYHSLVVEEASLPECL-EVTAKSDDGEIMGIRHKEHPIFGVQFHPESI-LTEEGKRILKNFLNYQREEIDIKSY- 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113967   454 pfkLPGGTIEENRSRHPLVDAKRVLIlgSGGLSIGQAGEFdysgsqaIKALREEGI 509
Cdd:PRK14607  199 ---LKKLVEGEDLSFEEAEDVMEDIT--DGNATDAQIAGF-------LTALRMKGE 242
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 1137-1295 5.31e-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: 57.65  E-value: 5.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1137 DDIGVDQPKWKELTSFDEADKFCDTVGYPVLV---RPSYvlSGAAMNTVYSQSDLhsylQQAVAINKDHPVVISKYIENA 1213
Cdd:pfam02222    1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADL----PQAWEELGDGPVIVEEFVPFD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1214 KEIELDAV-AREGKMVMHVISEHVEnagvHSGDATLVLPPQDLAPTTIERIVDAAAKIGEALNITGPYNIQ-FIAKDNEI 1291
Cdd:pfam02222   75 RELSVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVTEDGDL 150


                   ....
gi 19113967   1292 KVIE 1295
Cdd:pfam02222  151 LINE 154
pyrC PRK09357
dihydroorotase; Validated
 1680-1852 5.73e-09

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 60.59  E-value: 5.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1680 RIHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLNQNDYPG--ATF-----LPTADDQVEIWNKLS--YIDCFSIGS 1750
Cdd:PRK09357  226 RVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTydPNYkvnppLRTEEDREALIEGLKdgTIDAIATDH 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1751 IP-SRLAKFVG--NTAFTGFGVREAIPLLLTA-VNEGRLTLKDVVDRFYSNPKAIFRLHDqddsgVQLEV---------- 1816
Cdd:PRK09357  306 APhAREEKECEfeAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTINPARILGLPA-----GPLAEgepadlvifd 380

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 19113967  1817 -DRSVSWSSKDW------TPFNGKKLYGSIQSVQFDGHDVFFD 1852
Cdd:PRK09357  381 pEAEWTVDGEDFaskgknTPFIGMKLKGKVVYTIVDGKIVYQD 423
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 302-440 7.50e-09

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: 57.59  E-value: 7.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  302 DGLFISNGPG-DPSL-----------MDLVVDR-----VKRVLESKtVPVFGICFGHQIMARAAGasttkmkfGNRGHNI 364
Cdd:cd01745   55 DGLLLTGGGDvDPPLygeephpelgpIDPERDAfelalLRAALERG-KPILGICRGMQLLNVALG--------GTLYQDI 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113967  365 pctcmisgrcYITSqNHGYAVDAssLSNGWKELFVnANDGSNEGIYNTEYPF-FSVQFHPESTPgPRDTEF--LFDVFI 440
Cdd:cd01745  126 ----------RVNS-LHHQAIKR--LADGLRVEAR-APDGVIEAIESPDRPFvLGVQWHPEWLA-DTDPDSlkLFEAFV 189
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 265-364 7.59e-09

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: 55.68  E-value: 7.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  265 ILVIDVGMKYNQ-----IRCFLNRGVELLVVPWD-----YDFTKETYDGLFISNGPGDPSLMDL---VVDRVKRVLESKt 331
Cdd:cd01653    1 VAVLLFPGFEELelaspLDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPDDLARdeaLLALLREAAAAG- 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 19113967  332 VPVFGICFGHQIMARAAGASTTKMKFGNRGHNI 364
Cdd:cd01653   80 KPILGICLGAQLLVLGVQFHPEAIDGAEAGARL 112
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
264-425 1.36e-08

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 57.37  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   264 RILVID-----VgmkYNQIRCFLNRGVELLVV------PWDYDFTKETYDGLFISNGPGDPSLMDLVVDRVkRVLESKTV 332
Cdd:PRK07765    2 RILVVDnydsfV---FNLVQYLGQLGVEAEVWrnddprLADEAAVAAQFDGVLLSPGPGTPERAGASIDMV-RACAAAGT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   333 PVFGICFGHQIMARAAGAS-----------TTKMKFGNRGhnipctcMISG--RCYITSQNHGYAVDASSLSNgwkELFV 399
Cdd:PRK07765   78 PLLGVCLGHQAIGVAFGATvdrapellhgkTSSVHHTGVG-------VLAGlpDPFTATRYHSLTILPETLPA---ELEV 147

                         170       180
                  ....*....|....*....|....*...
gi 19113967   400 NA--NDGSNEGIYNTEYPFFSVQFHPES 425
Cdd:PRK07765  148 TArtDSGVIMAVRHRELPIHGVQFHPES 175
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1036-1359 1.60e-08

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 59.66  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1036 AVRAVRTLRDRGVKTIMVnynpetvstdYDEADR--LYFEN------IG----------LETVLDIYEQESSSGIIIAMG 1097
Cdd:PRK06111   14 AVRIIRTCQKLGIRTVAI----------YSEADRdaLHVKMadeaylIGgprvqesylnLEKIIEIAKKTGAEAIHPGYG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1098 GQTAN-NIALPLHRENVKILGTSPEMIdgaenrfkfSRMLDDI---------------GVDQPkwkeLTSFDEADKFCDT 1161
Cdd:PRK06111   84 LLSENaSFAERCKEEGIVFIGPSADII---------AKMGSKIearramqaagvpvvpGITTN----LEDAEEAIAIARQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1162 VGYPVLVRPSYVLSGAAMNTVYSQSDlhsyLQQAVAINK--------DHPVVISKYIENAKEIELdavaregkmvmHVIS 1233
Cdd:PRK06111  151 IGYPVMLKASAGGGGIGMQLVETEQE----LTKAFESNKkraanffgNGEMYIEKYIEDPRHIEI-----------QLLA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1234 EHVENAgVHSGDATLVL-----------PPQDLAPTTIERIVDAAAKIGEALNITGPYNIQFIA-KDNEIKVIECNVRAS 1301
Cdd:PRK06111  216 DTHGNT-VYLWERECSVqrrhqkvieeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVdEQKNFYFLEMNTRLQ 294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19113967  1302 RSFPFVSKVIGVDMISMATDVIMGNPIqPYPDVDLPRDYVAVKVpqfsfsRLSGADPV 1359
Cdd:PRK06111  295 VEHPVTEEITGIDLVEQQLRIAAGEKL-SFTQDDIKRSGHAIEV------RIYAEDPK 345
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 265-344 2.04e-08

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: 53.74  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  265 ILVIDVGMKYNQ-----IRCFLNRGVELLVVPWD-----YDFTKETYDGLFISNGPGDPSLMDL---VVDRVKRVLESKt 331
Cdd:cd03128    1 VAVLLFGGSEELelaspLDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPDDLAWdeaLLALLREAAAAG- 79

                         90
                 ....*....|...
gi 19113967  332 VPVFGICFGHQIM 344
Cdd:cd03128   80 KPVLGICLGAQLL 92
PRK07575 PRK07575
dihydroorotase; Provisional
 1677-1859 2.57e-08

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 58.92  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1677 HNRRIHITNVSSKDDLNLivLAKQRSLPVTFDVSVYSLFLNQNDY----PGATFLP---TADDQVEIWNKL--SYIDCFS 1747
Cdd:PRK07575  224 YQRRLHILHLSTAIEAEL--LRQDKPSWVTAEVTPQHLLLNTDAYerigTLAQMNPplrSPEDNEALWQALrdGVIDFIA 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1748 IGSIPSRL---AKFVGNTAFTGFGVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRL---------HDQDDSGVQLE 1815
Cdd:PRK07575  302 TDHAPHTLeekAQPYPNSPSGMPGVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGIpnkgriapgYDADLVLVDLN 381

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 19113967  1816 VDRSVS----WSSKDWTPFNGKKLYGSIQSVQFDGHDVFFDGELNFEH 1859
Cdd:PRK07575  382 TYRPVRreelLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVNTEV 429
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 1139-1297 2.92e-08

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: 56.17  E-value: 2.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1139 IGVDQPKWKELTSfDEADKFCDTVGYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQavAINKDHPVVISKYIEnAKEIEL 1218
Cdd:pfam07478   13 VTFTRADWKLNPK-EWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEE--AFQYDEKVLVEEGIE-GREIEC 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1219 dAVAREGKMVMHVISEHVENAGV------HSGDATLVLPPQDLAPTTIERIVDAAAKIGEALNITGPYNIQ-FIAKDNEI 1291
Cdd:pfam07478   89 -AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDfFLTEDGEI 167


                   ....*.
gi 19113967   1292 KVIECN 1297
Cdd:pfam07478  168 VLNEVN 173
PRK00758 PRK00758
GMP synthase subunit A; Validated
 264-445 3.60e-08

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 55.63  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   264 RILVIDVGMKYNQI--RCFLNRGVELLVVPWDYDFT--KETYDGLFISNGPgdpslmDLvvDRVKRV---LESKTVPVFG 336
Cdd:PRK00758    1 KIVVVDNGGQYNHLihRTLRYLGVDAKIIPNTTPVEeiKAFEDGLILSGGP------DI--ERAGNCpeyLKELDVPILG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   337 ICFGHQIMARAAGASTTKMKFGNRGhnipctcmiSGRCYITSQN---HGYA----VDAS------SLSNGWKELfvnANd 403
Cdd:PRK00758   73 ICLGHQLIAKAFGGEVGRGEYGEYA---------LVEVEILDEDdilKGLPpeirVWAShadevkELPDGFEIL---AR- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 19113967   404 gSN----EGIYNTEYPFFSVQFHPESTPGPRDTEfLFDVFIDVVKR 445
Cdd:PRK00758  140 -SDicevEAMKHKEKPIYGVQFHPEVAHTEYGEE-IFKNFLEICGK 183
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
1036-1336 4.69e-08

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 57.83  E-value: 4.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1036 AVRAVRTLRDRGVKTIMVnynpetvstdYDEADR--LYFEN------IG----LETVLDI------YEQESSSGIIIAMG 1097
Cdd:PRK08462   16 ALRAIRTIQEMGKEAIAI----------YSTADKdaLYLKYadakicIGgaksSESYLNIpaiisaAEIFEADAIFPGYG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1098 GQTAN-NIALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKE--LTSFDEADKFCDTVGYPVLVRPSYVL 1174
Cdd:PRK08462   86 FLSENqNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDgaLKSYEEAKKIAKEIGYPVILKAAAGG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1175 SGAAMNTVYSQSDL-HSYL---QQAVAINKDHPVVISKYIENAKEIELDAVAREGKMVMHvISEhvENAGVHSGDATLV- 1249
Cdd:PRK08462  166 GGRGMRVVEDESDLeNLYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIH-VGE--RDCSLQRRHQKLIe 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1250 -LPPQDLAPTTIERIVDAAAKIGEALNITGPYNIQFIAKDN-EIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNP 1327
Cdd:PRK08462  243 eSPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNlDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322


                  ....*....
gi 19113967  1328 IQPYPDVDL 1336
Cdd:PRK08462  323 LPSQESIKL 331
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 1040-1344 5.50e-08

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 58.32  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1040 VRTLRDRGVKTIMVNYNPE-----------TVSTDYDEADRLYFENIGLETVLDIYeqeSSSGIIIAMGGQTANNIALPl 1108
Cdd:PRK02186   20 LRKALLRGFTPYFLTANRGkypfldairvvTISADTSDPDRIHRFVSSLDGVAGIM---SSSEYFIEVASEVARRLGLP- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1109 hrenvkilGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVYSQSDL 1188
Cdd:PRK02186   96 --------AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1189 HSYLQQAVAInKDHPVVISKYIENAK-EIELDAVAReGKMVMHVISEHVENAGvHSGDATLVLpPQDLAPTTIERIVDAA 1267
Cdd:PRK02186  168 AAHCAALRRA-GTRAALVQAYVEGDEySVETLTVAR-GHQVLGITRKHLGPPP-HFVEIGHDF-PAPLSAPQRERIVRTV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1268 AKIGEALNIT-GPYNIQFIAKDNEIKVIECNVR-ASRSFP-FVSKVIGVDMISMATDVIMGNPiqpyPDVDL-PRDYVAV 1343
Cdd:PRK02186  244 LRALDAVGYAfGPAHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLGVA----AFADPtAKRYGAI 319


                  .
gi 19113967  1344 K 1344
Cdd:PRK02186  320 R 320
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
568-698 6.57e-08

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 57.69  E-value: 6.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   568 ELKDEFEQLGVKVLGTPIDTIittedrelfaRAM-DEINEKCA-KSA----------SASSIEEAIKVSKDISFPVIVRA 635
Cdd:PRK08654   90 EFAKACEKAGIVFIGPSSDVI----------EAMgSKINAKKLmKKAgvpvlpgteeGIEDIEEAKEIAEEIGYPVIIKA 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113967   636 AYALGGLGSGFADNEAELIDL--CTLAFATS----PQVLIERSMKGWKEIEYEVVRDAFDNCITVCNME 698
Cdd:PRK08654  160 SAGGGGIGMRVVYSEEELEDAieSTQSIAQSafgdSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRE 228
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 1681-1855 1.10e-07

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: 56.84  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1681 IHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLNQNDYP-----GATF-----LPTADDQVEIWNKLSYIDCFSIGS 1750
Cdd:cd01314  233 LYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWkdwfeGAKYvcsppLRPKEDQEALWDGLSSGTLQTVGS 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1751 --IPSRLA-KFVGNTAFT-----GFGVREAIPLLLTA-VNEGRLTLKDVVDRFYSNPKAIFRLHDQ--------DDSGVQ 1813
Cdd:cd01314  313 dhCPFNFAqKARGKDDFTkipngVPGVETRMPLLWSEgVAKGRITLEKFVELTSTNPAKIFGLYPRkgtiavgsDADLVI 392

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 19113967 1814 LEVDRSVSWSSK------DWTPFNGKKLYGSIQSVQFDGHDVFFDGEL 1855
Cdd:cd01314  393 WDPNAEKTISADthhhnvDYNIFEGMKVKGWPVVTISRGKVVVEDGEL 440
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
265-425 1.46e-07

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 53.77  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   265 ILVIDV--GMKYNQIRCFLNRGVELLVVPWDyDFTKETYDGL-----FISNGPGDPSLMDLVVDRVKRVleSKTVPVFGI 337
Cdd:PRK08007    2 ILLIDNydSFTWNLYQYFCELGADVLVKRND-ALTLADIDALkpqkiVISPGPCTPDEAGISLDVIRHY--AGRLPILGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   338 CFGHQIMARAAGASTTKMKFGNRGHNIPCTCMISG------RCYITSQNHGYAVDASSLSNGWKelfVNANDGSNE--GI 409
Cdd:PRK08007   79 CLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGI 155

                         170
                  ....*....|....*.
gi 19113967   410 YNTEYPFFSVQFHPES 425
Cdd:PRK08007  156 RHRQWDLEGVQFHPES 171
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
568-766 3.48e-07

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 55.11  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   568 ELKDEFEQLGVKVLGTPIDTIITTEDRELFARAMDEINEKC--AKSASASSIEEAIKVSKDISFPVIVRAAYALGGLGSG 645
Cdd:PRK07178   89 ELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVtpGSEGNLADLDEALAEAERIGYPVMLKATSGGGGRGIR 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   646 FADNEAEL-------IDLCTLAFAtSPQVLIERSMKGWKEIEYEVVRDAFDNCITV----CNMENfdplgiHTGDSIVVA 714
Cdd:PRK07178  169 RCNSREELeqnfprvISEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIA 241

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19113967   715 PSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFTKEYcIIEVNARL 766
Cdd:PRK07178  242 PSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVY-FMEMNTRV 292
PRK09060 PRK09060
dihydroorotase; Validated
 1539-1860 7.23e-07

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 54.16  E-value: 7.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1539 LPGLINISAFLPEFTSEAVSDY---TKECIASGFTmARF-LPfSTSSTLADKDSLSAVKKLALDHAHCDYNFSVIASSTN 1614
Cdd:PRK09060   55 LPGVIDSQVHFREPGLEHKEDLetgSRAAVLGGVT-AVFeMP-NTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1615 EVTISELTSESGC----LF----------------------------FHFE-----KDDSGIDHVTAVASHfNVWPD--- 1654
Cdd:PRK09060  133 ADELAELERLPGCagikVFmgsstgdllveddeglrrilrngrrraaFHSEdeyrlRERKGLRVEGDPSSH-PVWRDeea 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1655 ----TQTVMTDAKSttlasllllaslHNRRIHITNVSSKDDLNLIVLAKQRslpVTFDVSVYSLFLNQND-YPG-ATF-- 1726
Cdd:PRK09060  212 allaTRRLVRLARE------------TGRRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLAAPEcYERlGTLaq 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1727 ----LPTADDQVEIWNKLS--YIDCfsIGS--IP-SRLAKF-------VGNTaftgfGVREAIPLLLTAVNEGRLTLKDV 1790
Cdd:PRK09060  277 mnppIRDARHRDGLWRGVRqgVVDV--LGSdhAPhTLEEKAkpypaspSGMT-----GVQTLVPIMLDHVNAGRLSLERF 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1791 VDRFYSNPKAIF------RL---HDQDDSGVQLEVDRSV--SW--SSKDWTPFNGKKLYGSIQSVQFDGHDVFFDGELNF 1857
Cdd:PRK09060  350 VDLTSAGPARIFgiagkgRIavgYDADFTIVDLKRRETItnEWiaSRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELVG 429


                  ...
gi 19113967  1858 EHT 1860
Cdd:PRK09060  430 PPT 432
PLN02347 PLN02347
GMP synthetase
 265-448 7.75e-07

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 54.31  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   265 ILVIDVGMKYNQI--RCFLNRGVELLVVPWDYDF---TKETYDGLFISNGP------GDPSLMDLVVDRVkrvlESKTVP 333
Cdd:PLN02347   13 VLILDYGSQYTHLitRRVRELGVYSLLLSGTASLdriASLNPRVVILSGGPhsvhveGAPTVPEGFFDYC----RERGVP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   334 VFGICFGHQIMARAAG---ASTTKMKFGNRGHNIPCTCMI-----SGRCYITSQNHGYavDASSLSNGWKELFVNANdGS 405
Cdd:PLN02347   89 VLGICYGMQLIVQKLGgevKPGEKQEYGRMEIRVVCGSQLfgdlpSGETQTVWMSHGD--EAVKLPEGFEVVAKSVQ-GA 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 19113967   406 NEGIYNTEYPFFSVQFHPESTPGPRDTEFLFDVFIDVVKRSAD 448
Cdd:PLN02347  166 VVAIENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTAD 208
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
265-425 9.69e-07

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 51.40  E-value: 9.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   265 ILVIDV--GMKYNQIRCFLNRGVELLVVPWD----YDFTKETYDGLFISNGPGDPSLMDLVVDRVKRVleSKTVPVFGIC 338
Cdd:PRK06774    2 LLLIDNydSFTYNLYQYFCELGTEVMVKRNDelqlTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHF--ADKLPILGVC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   339 FGHQIMARAAGASTTKMKFGNRGHNIPCTCMISG------RCYITSQNHGYAVDASSLSNGWKELFVNANDGSNE---GI 409
Cdd:PRK06774   80 LGHQALGQAFGARVVRARQVMHGKTSAICHSGQGvfrglnQPLTVTRYHSLVIAADSLPGCFELTAWSERGGEMDeimGI 159

                         170
                  ....*....|....*.
gi 19113967   410 YNTEYPFFSVQFHPES 425
Cdd:PRK06774  160 RHRTLPLEGVQFHPES 175
PRK06849 PRK06849
hypothetical protein; Provisional
 1105-1300 1.03e-06

hypothetical protein; Provisional


Pssm-ID: 235876 [Multi-domain]  Cd Length: 389  Bit Score: 53.51  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1105 ALPLHRENVKILGTSPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKF-CDTVGYPVLVRPSYVLSGAAMNTVY 1183
Cdd:PRK06849   93 AKEELSAYCEVLHFDFELLLLLHNKWEFAEQARSLGLSVPKTYLITDPEAIRNFmFKTPHTPYVLKPIYSRFVRRVDLLP 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1184 SQSDLHSylqqaVAINKDHPVVISKYIEnAKEIELDAVAREGKMVMH--VISEHVENAGVHSgdatlvlppqDLAPTTIE 1261
Cdd:PRK06849  173 KEAALKE-----LPISKDNPWVMQEFIQ-GKEYCSYSIVRSGELRAHscYKPEYCAGSGAQI----------AFQPINHP 236

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 19113967  1262 RIVDAAAKIGEALNITGPYNIQFI-AKDNEIKVIECNVRA 1300
Cdd:PRK06849  237 RIEEFVTHFVKELNYTGQISFDFIeTENGDAYPIECNPRT 276
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 615-766 1.46e-06

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 53.27  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   615 SSIEEAIKVSKDISFPVIVRAAYALGGLGSGFADNEAELIDLCTLAFATS------PQVLIERSMKGWKEIEYEVVRDAF 688
Cdd:PRK08591  139 DDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAkaafgnPGVYMEKYLENPRHIEIQVLADGH 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   689 DNcitvcnmenfdplGIHTGD---SI------VV--APSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPfTKEY 757
Cdd:PRK08591  219 GN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEK-NGEF 284


                  ....*....
gi 19113967   758 CIIEVNARL 766
Cdd:PRK08591  285 YFIEMNTRI 293
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
615-766 2.19e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 52.44  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   615 SSIEEAIKVSKDISFPVIVRAAYALGGLGSGFADNEAELIDLCTLAFATS------PQVLIERSMKGWKEIEYEVVRDAF 688
Cdd:PRK08462  141 KSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEAlsafgdGTMYMEKFINNPRHIEVQILGDKH 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   689 DNCITV----CNMENfdplgiHTGDSIVVAPSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFTKEYcIIEVNA 764
Cdd:PRK08462  221 GNVIHVgerdCSLQR------RHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFY-FMEMNT 293


                  ..
gi 19113967   765 RL 766
Cdd:PRK08462  294 RL 295
guaA PRK00074
GMP synthase; Reviewed
 264-438 3.03e-06

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 52.36  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   264 RILVIDVGMKYNQ-----IRCFlnrGVELLVVPWDY---DFTKETYDGLFISNGP------GDPSLmdlvvdrVKRVLES 329
Cdd:PRK00074    5 KILILDFGSQYTQliarrVREL---GVYSEIVPYDIsaeEIRAFNPKGIILSGGPasvyeeGAPRA-------DPEIFEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   330 KtVPVFGICFGHQIMARAAG---ASTTKMKFGnrghniPCTCMISGRCYI------TSQ---NHGYAVDAssLSNGWKEL 397
Cdd:PRK00074   75 G-VPVLGICYGMQLMAHQLGgkvERAGKREYG------RAELEVDNDSPLfkglpeEQDvwmSHGDKVTE--LPEGFKVI 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 19113967   398 fvnandGSNEG-----IYNTEYPFFSVQFHPESTPGPRDTE----FLFDV 438
Cdd:PRK00074  146 ------ASTENcpiaaIANEERKFYGVQFHPEVTHTPQGKKllenFVFDI 189
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 1677-1855 4.02e-06

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: 51.91  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1677 HNRRIHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLNQNDYP-GATFLPTA------DDQVEIWNKL--SYIDCFS 1747
Cdd:cd01315  229 TGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPdGGTEFKCAppirdaANQEQLWEALenGDIDMVV 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1748 IGSIPSRLA-KFVGNTAFTGF-----GVREAIPLLLT-AVNEGRLTLKDVVDRFYSNPKAIFRLH----------DQDDS 1810
Cdd:cd01315  309 SDHSPCTPElKLLGKGDFFKAwggisGLQLGLPVMLTeAVNKRGLSLEDIARLMCENPAKLFGLShqkgriavgyDADFV 388

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 19113967 1811 GVQLEVDRSVSWSSKDW----TPFNGKKLYGSIQSVQFDGHDVFFDGEL 1855
Cdd:cd01315  389 VWDPEEEFTVDAEDLYYknkiSPYVGRTLKGRVHATILRGTVVYQDGEV 437
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 265-425 5.69e-06

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: 49.02  E-value: 5.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    265 ILVIDV--GMKYNQIRCFLNRGVELLVVPWDYDFTKE----TYDGLFISNGPGDPSLMDLVVDRVKRVleSKTVPVFGIC 338
Cdd:TIGR00566    2 VLMIDNydSFTYNLVQYFCELGAEVVVKRNDSLTLQEiealLPLLIVISPGPCTPNEAGISLEAIRHF--AGKLPILGVC 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    339 FGHQIMARAAGASTTKMKFGNRGHNIPCTCMISGRC------YITSQNHGYAVDASSLSNGWKelfVNANDGSNE---GI 409
Cdd:TIGR00566   80 LGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFP---VTAWEEENIeimAI 156

                          170
                   ....*....|....*.
gi 19113967    410 YNTEYPFFSVQFHPES 425
Cdd:TIGR00566  157 RHRDLPLEGVQFHPES 172
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 289-446 2.53e-05

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


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 48.47  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  289 VVPWDYDFTKETYDGLFIS-NG---PG-----DPSL-MDLVVDRVKRVLESKT----VPVFGICFGHQ-IMARAAGASTT 353
Cdd:cd01747   36 VVPIWINESEEYYDKLFKSiNGilfPGgavdiDTSGyARTAKIIYNLALERNDagdyFPVWGTCLGFElLTYLTSGETLL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  354 KMKFGNRGHNIPCT-------CMISGRCY-----------ITSQNHGYAVDASS------LSNGWKELFVNANDGSNEGI 409
Cdd:cd01747  116 LEATEATNSALPLNftedalqSRLFKRFPpdllkslatepLTMNNHRYGISPENftenglLSDFFNVLTTNDDWNGVEFI 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19113967  410 YNTE---YPFFSVQFHPE----------STPGPRD----TEFLFDVFIDVVKRS 446
Cdd:cd01747  196 STVEaykYPIYGVQWHPEknafewkkssSIPHSEEairlTQYFANFFVNEARKS 249
trpG CHL00101
anthranilate synthase component 2
 265-425 3.33e-05

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 47.03  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   265 ILVIDV--GMKYNQIRCFLNRGVELLVVPWD----YDFTKETYDGLFISNGPGDPSLMDLVVDRVKRVLEskTVPVFGIC 338
Cdd:CHL00101    2 ILIIDNydSFTYNLVQSLGELNSDVLVCRNDeidlSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAP--YIPILGVC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   339 FGHQIMARAAGASTTKMK----------FGNRG---HNIPCTcmisgrcYITSQNHGYAVDASSLSNgwkELFVNA--ND 403
Cdd:CHL00101   80 LGHQSIGYLFGGKIIKAPkpmhgktskiYHNHDdlfQGLPNP-------FTATRYHSLIIDPLNLPS---PLEITAwtED 149

                         170       180
                  ....*....|....*....|...
gi 19113967   404 GSNEGIYNTEYPF-FSVQFHPES 425
Cdd:CHL00101  150 GLIMACRHKKYKMlRGIQFHPES 172
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 614-766 3.93e-05

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 48.98  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   614 ASSIEEAIKVSKDISFPVIVRAayALGGLGSG--FADNEAELIDLCTLA-------FAtSPQVLIERSMKGWKEIEYEVV 684
Cdd:PRK12999  142 IDDIEEALEFAEEIGYPIMLKA--SAGGGGRGmrIVRSEEELEEAFERAkreakaaFG-NDEVYLEKYVENPRHIEVQIL 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   685 RDAFDNCITV----CnmenfdplgihtgdSI------VV--APSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNP 752
Cdd:PRK12999  219 GDKHGNVVHLyerdC--------------SVqrrhqkVVeiAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDA 284

                         170
                  ....*....|....
gi 19113967   753 FTKEYcIIEVNARL 766
Cdd:PRK12999  285 DGNFY-FIEVNPRI 297
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 1681-1884 3.94e-05

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 48.54  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1681 IHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLNQND-----YPGATFL---P--TADDQVEIWNKLS--YIDCFSI 1748
Cdd:PRK13404  237 ILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDldrpgMEGAKYIcspPprDKANQEAIWNGLAdgTFEVFSS 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1749 GSIPSRL----AKFV--GNTAFTGF-----GVREAIPLLLTA-VNEGRLTLKDVVDRFYSNPKAIFRLH----------D 1806
Cdd:PRK13404  317 DHAPFRFddtdGKLAagANPSFKAIangipGIETRLPLLFSEgVVKGRISLNRFVALTSTNPAKLYGLYprkgaiaigaD 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1807 QD----DSGVQLEVDRSVSWSSKDWTPFNGKKLYGSIQSVQFDGHDVFFDGELNFEHTYGRdYSSASLADKSKATRKVSA 1882
Cdd:PRK13404  397 ADiaiwDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQ-FLARSLPDRARPNGRLEP 475


                  ..
gi 19113967  1883 LM 1884
Cdd:PRK13404  476 EL 477
ATPgrasp_Ter pfam15632
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ...
 1203-1346 4.24e-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: 45.30  E-value: 4.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1203 PVVISKYIENAkEIELDAVAREGKMVMHVIsehveNAGVHSGDATLVlppqdlaptTIERIVDAAAKIGEALNITGPYNI 1282
Cdd:pfam15632    4 PLLVMEYLPGP-EYSVDCLAGHGELIAAVP-----RRKGDGGIQTLE---------DDPELIEAARRLAEAFGLDGLFNV 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113967   1283 QFIAKDNEIKVIECNVRASRSFPfVSKVIGVDMISMATDVIMGNPIQPYPDVDLPRDYVAVKVP 1346
Cdd:pfam15632   69 QFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPDPVEPRLGLRVREIEKV 131
PRK02382 PRK02382
dihydroorotase; Provisional
 1680-1834 4.58e-05

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 48.49  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1680 RIHITNVSSKDDLNLIvlakqRSLPVTFDVSVYSLFLNQNDYPG-ATF------LPTADDQVEIWNKLS--YIDCF---- 1746
Cdd:PRK02382  229 RIHIAHISTPEGVDAA-----RREGITCEVTPHHLFLSRRDWERlGTFgkmnppLRSEKRREALWERLNdgTIDVVasdh 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1747 ----------SIGSIPSRLAkfvgntaftgfGVREAIPLLLTAVNEGRLTLKDVVDRFYSNPKAIFRL---------HDQ 1807
Cdd:PRK02382  304 aphtreekdaDIWDAPSGVP-----------GVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLdgkgriaegYDA 372

                         170       180       190
                  ....*....|....*....|....*....|.
gi 19113967  1808 D----DSGVQLEVDRSVSWSSKDWTPFNGKK 1834
Cdd:PRK02382  373 DlvlvDPDAAREIRGDDLHSKAGWTPFEGME 403
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 302-424 5.11e-05

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


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 46.87  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    302 DGLFISNGPG-DPSL-----------MDLVVDR-----VKRVLESKtVPVFGICFGHQIMARAAGAST---TKMKFGNRG 361
Cdd:pfam07722   60 DGLLLTGGPNvDPHFygeepsesggpYDPARDAyelalIRAALARG-KPILGICRGFQLLNVALGGTLyqdIQEQPGFTD 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967    362 HNIPCTCMIS----------GRCY--ITSQN-------HGYAVDAssLSNGWKelfVNA--NDGSNEGIY--NTEYPFFS 418
Cdd:pfam07722  139 HREHCQVAPYapshavnvepGSLLasLLGSEefrvnslHHQAIDR--LAPGLR---VEAvaPDGTIEAIEspNAKGFALG 213


                   ....*.
gi 19113967    419 VQFHPE 424
Cdd:pfam07722  214 VQWHPE 219
PLN02335 PLN02335
anthranilate synthase
 303-425 1.30e-04

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 45.56  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   303 GLFISNGPGDPSLMDLVVDRVKRVleSKTVPVFGICFGHQIMARAAGASTTKMKFG-NRGHNIPCT-------CMISG-- 372
Cdd:PLN02335   65 GVLISPGPGTPQDSGISLQTVLEL--GPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHydekgeeGLFSGlp 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19113967   373 RCYITSQNHGYAVDASSLSNGWKELFVNANDGSNEGIYNTEYPFFS-VQFHPES 425
Cdd:PLN02335  143 NPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPES 196
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1148-1328 1.52e-04

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 46.72  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1148 ELTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQA-----VAINKDHpVVISKYIENAKEIELDAVA 1222
Cdd:PRK08591  137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMAraeakAAFGNPG-VYMEKYLENPRHIEIQVLA 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1223 -REGkmvmhvisehveNAgVHSG--DATL------VL---PPQDLAPTTIERIVDAAAKIGEALNITGPYNIQFI-AKDN 1289
Cdd:PRK08591  216 dGHG------------NA-IHLGerDCSLqrrhqkVLeeaPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLyEKNG 282

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 19113967  1290 EIKVIECNVRASRSFPFVSKVIGVDMISMATDVIMGNPI 1328
Cdd:PRK08591  283 EFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 294-425 1.96e-04

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 46.76  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   294 YDFTKETYDGLFISNGPGDPSLMDLVVDRVKRVLESKTVPVFGICFGHQIMARAAGASTTKMK------------FGNR- 360
Cdd:PLN02889  125 YLYEEKAFDNIVISPGPGSPTCPADIGICLRLLLECRDIPILGVCLGHQALGYVHGARIVHAPepvhgrlseiehNGCRl 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   361 GHNIPC------------------------------TCMISGRCYITSQNHGYAVDA---------------SSLSNG-- 393
Cdd:PLN02889  205 FDDIPSgrnsgfkvvryhslvidaeslpkelvpiawTSSSDTLSFLESQKSGLVPDAyesqigqsgssdpfsSKLKNGts 284

                         170       180       190
                  ....*....|....*....|....*....|....
gi 19113967   394 WKELFVNANDGSN--EGIYNTEYPFFSVQFHPES 425
Cdd:PLN02889  285 WPSSHSERMQNGKilMGIMHSTRPHYGLQFHPES 318
purT PRK09288
formate-dependent phosphoribosylglycinamide formyltransferase;
474-633 3.12e-04

formate-dependent phosphoribosylglycinamide formyltransferase;


Pssm-ID: 236454 [Multi-domain]  Cd Length: 395  Bit Score: 45.51  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   474 AKRVLILGSGGLSigqaGEFdysgsqAIKALREeGIYTILIN--PNIATIQtskgLADKVYFLPV-NADFVRKVIKQERP 550
Cdd:PRK09288   12 ATRVMLLGSGELG----KEV------AIEAQRL-GVEVIAVDryANAPAMQ----VAHRSHVIDMlDGDALRAVIEREKP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   551 DSIyVTfggQT-ALNVgiELKDEFEQLGVKVLGTPIDTIITTeDRELFAR-AMDEINEKCAKSASASSIEEAIKVSKDIS 628
Cdd:PRK09288   77 DYI-VP---EIeAIAT--DALVELEKEGFNVVPTARATRLTM-NREGIRRlAAEELGLPTSPYRFADSLEELRAAVEEIG 149


                  ....*
gi 19113967   629 FPVIV 633
Cdd:PRK09288  150 YPCVV 154
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 1140-1299 3.12e-04

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: 46.23  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1140 GVDQPkwkeLTSFDEADKFCDTVGYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQAV-----AINKDHpVVISKYIENAK 1214
Cdd:COG1038  136 GTEGP----VDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARreakaAFGDDE-VFLEKYIERPK 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1215 EIELDAVAREGKMVMH-------VISEH---VENAgvhsgdatlvlPPQDLAPTTIERIVDAAAKIGEALNITGPYNIQF 1284
Cdd:COG1038  211 HIEVQILGDKHGNIVHlferdcsVQRRHqkvVEIA-----------PAPNLDEELREAICEAAVKLAKAVGYVNAGTVEF 279

                        170
                 ....*....|....*.
gi 19113967 1285 -IAKDNEIKVIECNVR 1299
Cdd:COG1038  280 lVDDDGNFYFIEVNPR 295
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
618-781 3.54e-04

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 45.47  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   618 EEAIKVSKDISFPVIVRAAYALGGLGSGFADNEAELIDlctlAFATSPQ----------VLIERSMKGWKEIEYEVVRDA 687
Cdd:PRK05586  142 EEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIK----AFNTAKSeakaafgddsMYIEKFIENPKHIEFQILGDN 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   688 FDNCITVCNMEnfdpLGIHTGDSIVV--APSQTLTDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPfTKEYCIIEVNAR 765
Cdd:PRK05586  218 YGNVVHLGERD----CSLQRRNQKVLeeAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDK-DGNFYFMEMNTR 292

                         170
                  ....*....|....*.
gi 19113967   766 LSRSSALASKATGYPL 781
Cdd:PRK05586  293 IQVEHPITEMITGVDL 308
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
304-425 4.53e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 43.71  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   304 LFISNGPGDPSLMDLVVDRVKRVleSKTVPVFGICFGHQIMARAAGASTTKMKFGNRGHNIPCTCmiSGRCYITSQN--- 380
Cdd:PRK08857   47 LVISPGPCTPNEAGISLQAIEHF--AGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSVFKGLNnpl 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19113967   381 -----HGYAVDASSLS-----NGWKELfvnaNDGSNE---GIYNTEYPFFSVQFHPES 425
Cdd:PRK08857  123 tvtryHSLVVKNDTLPecfelTAWTEL----EDGSMDeimGFQHKTLPIEAVQFHPES 176
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 299-349 6.98e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 43.41  E-value: 6.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113967   299 ETYDGLFISngpGDPSLmdlVVDR----------VKRVLESKtVPVFGICFGHQIMARAAG 349
Cdd:PRK09065   53 DDFAGVIIT---GSWAM---VTDRldwsertadwLRQAAAAG-MPLLGICYGHQLLAHALG 106
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
 1160-1224 1.49e-03

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 43.28  E-value: 1.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113967  1160 DTVGYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQAVAInkDHPVVISKYIEnAKEIELDAVARE 1224
Cdd:PRK14570  168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFIE-AREIECSVIGNE 229
MGS-like cd00532
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ...
 1397-1507 2.98e-03

MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 238297 [Multi-domain]  Cd Length: 112  Bit Score: 39.42  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967 1397 ILISIgSYKEKAELLPYVKKLYENNYNIFATAGTSDYFMESGVPCKYLADLPaeEANNEYSLSAHLANNMIDMYINLPSN 1476
Cdd:cd00532    2 VFLSV-SDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRH--EDGEPTVDAAIAEKGKFDVVINLRDP 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 19113967 1477 nryRRPANYISSGYKSRRLAIDYSVPLVTNV 1507
Cdd:cd00532   79 ---RRDRCTDEDGTALLRLARLYKIPVTTPN 106
ddl PRK01966
D-alanine--D-alanine ligase;
1134-1297 3.63e-03

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 42.03  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1134 RMLDDIGVDQPKWKELTSFDEADKFCDTV----GYPVLVRPSYVLSGAAMNTVYSQSDLHSYLQQAVAInkDHPVVISKY 1209
Cdd:PRK01966  129 RLLAAAGIPVAPYVVLTRGDWEEASLAEIeaklGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY--DRKVLVEQG 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967  1210 IeNAKEIELdAVArEGKMVMHVISEHVENAGVHS-------GDATLVLPPqDLAPTTIERIVDAAAKIGEALNITGPYNI 1282
Cdd:PRK01966  207 I-KGREIEC-AVL-GNDPKASVPGEIVKPDDFYDyeakyldGSAELIIPA-DLSEELTEKIRELAIKAFKALGCSGLARV 282

                         170
                  ....*....|....*.
gi 19113967  1283 QFI-AKDNEIKVIECN 1297
Cdd:PRK01966  283 DFFlTEDGEIYLNEIN 298
ddl PRK01966
D-alanine--D-alanine ligase;
610-680 5.43e-03

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 41.26  E-value: 5.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113967   610 KSASASSIEEAIKvsKDISFPVIVRAAyalgGLGSGF----ADNEAELIDLCTLAFATSPQVLIERSMKGwKEIE 680
Cdd:PRK01966  146 RGDWEEASLAEIE--AKLGLPVFVKPA----NLGSSVgiskVKNEEELAAALDLAFEYDRKVLVEQGIKG-REIE 213
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 1119-1314 5.99e-03

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: 40.79  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1119 SPEMIDGAENRFKFSRMLDDIGVDQPKWKELTSFDEADKFCDTVGYPVLVRPSYVLSG---AAMNTVYSQSDLHSYLQQA 1195
Cdd:TIGR00768   79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGrgvSLARDRQAAESLLEHFEQL 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113967   1196 VAINKDHpvVISKYIENAKEIELDAVAREGKMV--MHVISEHVENAGVHSGDATlvlppqdlAPTTI-ERIVDAAAKIGE 1272
Cdd:TIGR00768  159 NGPQNLF--LVQEYIKKPGGRDIRVFVVGDEVVaaIYRITSGHWRSNLARGGKA--------EPCSLtEEIEELAIKAAK 228

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 19113967   1273 ALNItGPYNIQFIAKDNEIKVIECNvrASRSFPFVSKVIGVD 1314
Cdd:TIGR00768  229 ALGL-DVAGVDLLESEDGLLVNEVN--ANPEFKNSVKTTGVN 267
PRK07627 PRK07627
dihydroorotase; Provisional
 1680-1720 9.05e-03

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 40.82  E-value: 9.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 19113967  1680 RIHITNVSSKDDLNLIVLAKQRSLPVTFDVSVYSLFLNQND 1720
Cdd:PRK07627  228 RVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVD 268
 
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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