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Conserved domains on  [gi|209862992|ref|NP_001129558|]
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dihydropyrimidinase-related protein 3 isoform 1 [Mus musculus]

Protein Classification

D-hydantoinase family protein (domain architecture ID 10797696)

D-hydantoinase family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
15-469 0e+00

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


:

Pssm-ID: 273937  Cd Length: 454  Bit Score: 760.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 94
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEKGVNSFMVYMAYKDLYQV 174
Cdd:TIGR02033  81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  175 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  255 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 334
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  335 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 413
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862992  414 ALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 469
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
 
Name Accession Description Interval E-value
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
15-469 0e+00

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


Pssm-ID: 273937  Cd Length: 454  Bit Score: 760.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 94
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEKGVNSFMVYMAYKDLYQV 174
Cdd:TIGR02033  81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  175 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  255 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 334
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  335 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 413
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862992  414 ALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 469
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
15-464 0e+00

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: 735.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 94
Cdd:cd01314    1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKeKGVNSFMVYMAYKDLYQV 174
Cdd:cd01314   81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 175 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:cd01314  160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 255 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYINSLLASGDLQLSGSAHCTF 334
Cdd:cd01314  240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 335 STAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDA 414
Cdd:cd01314  318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 209862992 415 LKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAG 464
Cdd:cd01314  398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
PRK08323 PRK08323
phenylhydantoinase; Validated
14-473 0e+00

phenylhydantoinase; Validated


Pssm-ID: 236240  Cd Length: 459  Bit Score: 570.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  14 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlivpGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKA 93
Cdd:PRK08323   2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  94 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEkGVNSFMVYMAYKDLYQ 173
Cdd:PRK08323  78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 174 VSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKV 253
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 254 MSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdpttPDYINSL---LASGDLQLSGSA 330
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD----KEHQDALwrgLQDGDLQVVATD 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 331 HCTFSTAQKA-IGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVI 409
Cdd:PRK08323 313 HCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVI 392
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209862992 410 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFS 473
Cdd:PRK08323 393 WDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism];
15-462 6.54e-106

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 223122 [Multi-domain]  Cd Length: 430  Bit Score: 325.05  E-value: 6.54e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:COG0044    3 LLIKNARVVDPGEDEVADILIKDGKIAAIGKNLEPTSGAEIIDAKGLLVLPGLVDLHVHFREP--GFEHKETFETGSRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEvQSLSKEKGVNSFMVYMAYKdlyqV 174
Cdd:COG0044   81 AAGGVTTVVDMPNTKPPIDTAEALEDKLERAKGKSVVDYAFYGGLTKGNLGKLEL-TERGVEAGFKGFMDDSTGA----L 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 175 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARmleMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:COG0044  156 DDDVLEEALEYAAELGALILVHAEDDDLIAEGVMN---EGLRAPELGLAGRPPIAEASAIARDLELARATGARVHICHIS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 255 SKSAADLISQARKKGNVVFGEPitaslgidgT-HYWSKN----WAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGS 329
Cdd:COG0044  233 TKESVELIRAAKAEGIRVTAEV---------TpHHLLLDeediEDLGTLAKVNPPLR-DEEDREALWEALKDGVIDVIAS 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 330 AHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNLYPrKGRIAVGSDSDLVI 409
Cdd:COG0044  303 DHAPHTLEEKRLP---FEEAPSGIPGLETALPLLLT-LVKKGRLSLERLVELLSTNPARIFGLPP-KGAIEEGADADLVL 377
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 209862992 410 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQG 462
Cdd:COG0044  378 VDPDEEWTIRAEELYSKAKNSPFEGFELKGRVVATILRGKVVYEDGEVIAKPG 430
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
62-451 7.57e-26

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


Pssm-ID: 396526 [Multi-domain]  Cd Length: 335  Bit Score: 108.35  E-value: 7.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   62 MVIPGGIDVHTHFQM-----PYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLT--EAYEKW----REWADGKSC 130
Cdd:pfam01979   1 IVLPGLIDAHVHLEMgllrgIVPPEFAYEALALGITTMLKSGTTTVLDMGATTSTGIEAllEAAEELplglRFLGPGCSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  131 CDYALHVDITHWNDSVKQEVQSLSKEKGVnsFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIiaqEQARM 210
Cdd:pfam01979  81 DGGELEGRKALREKLKAGADFIKGMADGV--VFVGLAPHGAPTFTDDELKAALEEAKKYGLPVAIHALETKG---EVEDA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  211 LEMGITGPEghVLSRPEELEAEAVFRAITVASQTNCPLYVTkvmskSAADLISQARKKGNvvfgepitaslgidgthyws 290
Cdd:pfam01979 156 IAAFGGGIE--HGTHLEVAESLGLLDVIKLILAHGVHLSPT-----EANLLAEHLKGAGV-------------------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  291 knwakaaAFVTSPPLSPDPTTPDyINSLLASGDLQLSGSAHCtfstaqkaIGKDNFTAIPEGTNGVEERMSViwdkAVAT 370
Cdd:pfam01979 209 -------AHCPFSNSKLRSGRIA-LRKALEDGVKVGLGTDGA--------ASGNSLNMLEELRLALKLQRLL----YDEE 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  371 GKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDALkivsaknhqsvaeyNIFEGMELRGAPLVVICQGKI 450
Cdd:pfam01979 269 GGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIVKGKI 334

                  .
gi 209862992  451 M 451
Cdd:pfam01979 335 V 335
 
Name Accession Description Interval E-value
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
15-469 0e+00

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


Pssm-ID: 273937  Cd Length: 454  Bit Score: 760.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 94
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEKGVNSFMVYMAYKDLYQV 174
Cdd:TIGR02033  81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  175 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  255 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 334
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  335 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 413
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862992  414 ALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 469
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
15-464 0e+00

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: 735.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 94
Cdd:cd01314    1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKeKGVNSFMVYMAYKDLYQV 174
Cdd:cd01314   81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 175 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:cd01314  160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 255 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYINSLLASGDLQLSGSAHCTF 334
Cdd:cd01314  240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 335 STAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDA 414
Cdd:cd01314  318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 209862992 415 LKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAG 464
Cdd:cd01314  398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
PRK08323 PRK08323
phenylhydantoinase; Validated
14-473 0e+00

phenylhydantoinase; Validated


Pssm-ID: 236240  Cd Length: 459  Bit Score: 570.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  14 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlivpGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKA 93
Cdd:PRK08323   2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  94 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEkGVNSFMVYMAYKDLYQ 173
Cdd:PRK08323  78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 174 VSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKV 253
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 254 MSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdpttPDYINSL---LASGDLQLSGSA 330
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD----KEHQDALwrgLQDGDLQVVATD 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 331 HCTFSTAQKA-IGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVI 409
Cdd:PRK08323 313 HCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVI 392
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209862992 410 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFS 473
Cdd:PRK08323 393 WDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
PLN02942 PLN02942
dihydropyrimidinase
12-483 0e+00

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 547.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  12 SDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGT 91
Cdd:PLN02942   4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  92 KAALAGGTTMIIDHVVPePESSLTEAYEKWREWADgKSCCDYALHVDITHWNDSVKQEVQSLSKEKGVNSFMVYMAYKDL 171
Cdd:PLN02942  84 AAALAGGTTMHIDFVIP-VNGNLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 172 YQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVT 251
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 252 KVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYINSLLASGDLQLSGSAH 331
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 332 CTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWD 411
Cdd:PLN02942 321 CPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209862992 412 PDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSdYVYKRIKAR 483
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKA 471
PRK13404 PRK13404
dihydropyrimidinase; Provisional
15-471 6.01e-116

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 352.46  E-value: 6.01e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVIPGGIDVHTHFQMPY-KGMTTVDDFFQGTKA 93
Cdd:PRK13404   6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  94 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSV-KQEVQSLSKEkGVNSFMVYMAYKDLy 172
Cdd:PRK13404  84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 173 QVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTK 252
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 253 VMSKSAADLISQARKKGNVVFGEP------ITAS-LGIDGTHywsknwakAAAFVTSPPLSpDPTTPDYINSLLASGDLQ 325
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 326 LSGSAHCTF---STAQKAIGKDN--FTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 400
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209862992 401 VGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSP 471
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism];
15-462 6.54e-106

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 223122 [Multi-domain]  Cd Length: 430  Bit Score: 325.05  E-value: 6.54e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:COG0044    3 LLIKNARVVDPGEDEVADILIKDGKIAAIGKNLEPTSGAEIIDAKGLLVLPGLVDLHVHFREP--GFEHKETFETGSRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEvQSLSKEKGVNSFMVYMAYKdlyqV 174
Cdd:COG0044   81 AAGGVTTVVDMPNTKPPIDTAEALEDKLERAKGKSVVDYAFYGGLTKGNLGKLEL-TERGVEAGFKGFMDDSTGA----L 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 175 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARmleMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:COG0044  156 DDDVLEEALEYAAELGALILVHAEDDDLIAEGVMN---EGLRAPELGLAGRPPIAEASAIARDLELARATGARVHICHIS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 255 SKSAADLISQARKKGNVVFGEPitaslgidgT-HYWSKN----WAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGS 329
Cdd:COG0044  233 TKESVELIRAAKAEGIRVTAEV---------TpHHLLLDeediEDLGTLAKVNPPLR-DEEDREALWEALKDGVIDVIAS 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 330 AHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNLYPrKGRIAVGSDSDLVI 409
Cdd:COG0044  303 DHAPHTLEEKRLP---FEEAPSGIPGLETALPLLLT-LVKKGRLSLERLVELLSTNPARIFGLPP-KGAIEEGADADLVL 377
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 209862992 410 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQG 462
Cdd:COG0044  378 VDPDEEWTIRAEELYSKAKNSPFEGFELKGRVVATILRGKVVYEDGEVIAKPG 430
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
15-467 1.57e-68

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: 228.33  E-value: 1.57e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:cd01315    2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  95 LAGGTTMIIDhvVP---EPESSLTEAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQSLSK--EKGV---NSFMVYM 166
Cdd:cd01315   80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKLHVDVGF------WGGLVPGNLDQLRPldEAGVvgfKCFLCPS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 167 AYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNC 246
Cdd:cd01315  152 GVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGC 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 247 PLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI------DGthywsknwakAAAFVTSPPLSpDPTTPDYINSLLA 320
Cdd:cd01315  232 RLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFtaedvpDG----------GTEFKCAPPIR-DAANQEQLWEALE 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 321 SGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 400
Cdd:cd01315  301 NGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIA 380
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209862992 401 VGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNlHVTQGAGRFI 467
Cdd:cd01315  381 VGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
61-441 6.46e-62

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: 207.24  E-value: 6.46e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  61 KMVIPGGIDVHTHFQMPYKGmTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDIt 140
Cdd:cd01302    1 LLVLPGFIDIHVHLRDPGGT-TYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 141 hWNDSVKQEVQSLSkEKGVNSFMVYMAYK--DLYQVSNTELYEIFTCLGELGAIAQVHAEngdiiaqeqarmlemgitgp 218
Cdd:cd01302   79 -GPGDVTDELKKLF-DAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 219 eghvlsrpeeleaeavfRAITVASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDgTHYWSKNWAKaaa 298
Cdd:cd01302  137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW--- 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 299 FVTSPPLSPdPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDnFTAIPEGTNGVEERMSVIWdKAVATGKMDENQF 378
Cdd:cd01302  196 GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETL 272
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862992 379 VAVTSTNAAKIFNLYPrKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAP 441
Cdd:cd01302  273 VEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
PRK06189 PRK06189
allantoinase; Provisional
15-458 4.60e-54

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 189.91  E-value: 4.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:PRK06189   5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  95 LAGGTTMIIDHVVPEPESSLT-EAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQSLSK--EKGVNSFMVYMAYK-- 169
Cdd:PRK06189  82 AAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNSgt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 170 DLYQVSNTE-LYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPL 248
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 249 YVTKVMSKSAADLISQARKKG-NV---------VFGEPITASLGIdgthywsknWAKAAafvtsPPLSPDPTTPDYINSL 318
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGvDVsvetcphylLFTEEDFERIGA---------VAKCA-----PPLRSRSQKEELWRGL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 319 LAsGDLQLSGSAH--CTFSTAQKaigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRK 396
Cdd:PRK06189 302 LA-GEIDMISSDHspCPPELKEG----DDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQK 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209862992 397 GRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 458
Cdd:PRK06189 376 GRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
PRK02382 PRK02382
dihydroorotase; Provisional
15-468 5.77e-54

dihydroorotase; Provisional


Pssm-ID: 179417  Cd Length: 443  Bit Score: 189.09  E-value: 5.77e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:PRK02382   4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALhvdithwNDSVKQEVQSLSK--EKGVNSF-MVYMA--YK 169
Cdd:PRK02382  82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGI-------NGGVTGNWDPLESlwERGVFALgEIFMAdsTG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 170 DLyQVSNTELYEIFTCLGELGAIAQVHAENGDIIAqEQARMLEmGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLY 249
Cdd:PRK02382 155 GM-GIDEELFEEALAEAARLGVLATVHAEDEDLFD-ELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 250 VTKVMSKSAADLISqarkkgnvvfGEPITAslgiDGT-HYW---SKNWAKAAAFV-TSPPLSPDPTTPDYINSLlASGDL 324
Cdd:PRK02382 232 IAHISTPEGVDAAR----------REGITC----EVTpHHLflsRRDWERLGTFGkMNPPLRSEKRREALWERL-NDGTI 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 325 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSD 404
Cdd:PRK02382 297 DVVASDHAPHTREEKD---ADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYD 371
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209862992 405 SDLVIWDPDALKIVSAKNHQSVAEYNIFEGMElrGA-PLVVICQGKIMLEDGNLHVTQGAGRFIP 468
Cdd:PRK02382 372 ADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
60-448 4.34e-38

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  Cd Length: 361  Bit Score: 143.63  E-value: 4.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  60 GKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIID--HVVPEPESSltEAYEKWREWADGKSCCDYALHV 137
Cdd:cd01318    1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDmpNTKPPTTTA--EALYEKLRLAAAKSVVDYGLYF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 138 DIThwndsvKQEVQSLSKEKGVNSFMVYMA--YKDLYQVSNTeLYEIFtclGELGAIAQVHAENGDIIAQEQARMLEMGI 215
Cdd:cd01318   77 GVT------GSEDLEELDKAPPAGYKIFMGdsTGDLLDDEET-LERIF---AEGSVLVTFHAEDEDRLRENRKELKGESA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 216 tgpegHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGNV-------VFGEPITASLGidgthy 288
Cdd:cd01318  147 -----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLG------ 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 289 wskNWAKaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAV 368
Cdd:cd01318  216 ---TLGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLT-LV 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 369 ATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQG 448
Cdd:cd01318  283 NKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
PRK08044 PRK08044
allantoinase AllB;
15-422 4.49e-36

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 139.99  E-value: 4.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:PRK08044   5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  95 LAGGTTMIIDHVVPE-PESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQslskEKGVNSFMVYMAY----- 168
Cdd:PRK08044  81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELD----EVGVVGFKCFVATcgdrg 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 169 --KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNC 246
Cdd:PRK08044 157 idNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 247 PLYVTKVMSKSAADLISQARKKGNVVFGEPItaslgidgTHYWSKNWAKAAAFVT----SPPLSPDPTTPDYINSLLaSG 322
Cdd:PRK08044 237 RLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEKLF-NG 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 323 DLQLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVG 402
Cdd:PRK08044 308 EIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPG 383
                        410       420
                 ....*....|....*....|
gi 209862992 403 SDSDLVIWDPDALKIVSAKN 422
Cdd:PRK08044 384 KDADFVFIQPNSSYVLKNED 403
pyrC PRK09357
dihydroorotase; Validated
14-454 3.42e-35

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 137.25  E-value: 3.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  14 RLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTK 92
Cdd:PRK09357   2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  93 AALAGGTTMiidhVV------PEPESSLTEAYEKWRewADGKSCCDyaLHV--DIThwndsVKQEVQSLS-----KEKGV 159
Cdd:PRK09357  79 AAAAGGFTT----VVampntkPVIDTPEVVEYVLDR--AKEAGLVD--VLPvgAIT-----KGLAGEELTefgalKEAGV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 160 NSFMvymayKDLYQVSNTEL-YEIFTCLGELG-AIAQvHAE----NGDIIAQEQARMLEMGITGpeghvlsRPEELEAEA 233
Cdd:PRK09357 146 VAFS-----DDGIPVQDARLmRRALEYAKALDlLIAQ-HCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVM 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 234 VFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGnvvfgEPITA------------SLGIDGTHYwsknwaKAAafvt 301
Cdd:PRK09357 213 IARDVLLAEATGARVHICHVSTAGSVELIRWAKALG-----IKVTAevtphhllltdeDLLTYDPNY------KVN---- 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 302 sPPLSpdptTPDYINSL---LASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQF 378
Cdd:PRK09357 278 -PPLR----TEEDREALiegLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQL 349
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209862992 379 VAVTSTNAAKIFNLYPrkGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLED 454
Cdd:PRK09357 350 LEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
52-442 6.81e-31

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: 123.89  E-value: 6.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  52 GVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMII--DHVVPEPESSLTEAYEKWREWADGKS 129
Cdd:cd01317    1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVVcmPNTNPVIDNPAVVELLKNRAKDVGIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 130 CCDY--ALhvdithwndSVKQEVQSLS-----KEKGVNSFMvymayKDLYQVSNTELyeIFTCLgELGAIAQ----VHAE 198
Cdd:cd01317   79 RVLPigAL---------TKGLKGEELTeigelLEAGAVGFS-----DDGKPIQDAEL--LRRAL-EYAAMLDlpiiVHPE 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 199 NGDIIAQeqARMLEMGITGPEGhVLSRPEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGnvvfgEPIT 278
Cdd:cd01317  142 DPSLAGG--GVMNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LPVT 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 279 ASLGIdgtHYWS------KNWAkaAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEG 352
Cdd:cd01317  214 AEVTP---HHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPG 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 353 TNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPrkGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIF 432
Cdd:cd01317  285 IIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPF 362
                        410
                 ....*....|
gi 209862992 433 EGMELRGAPL 442
Cdd:cd01317  363 DGQKLKGRVL 372
PRK07575 PRK07575
dihydroorotase; Provisional
12-457 8.56e-31

dihydroorotase; Provisional


Pssm-ID: 236055  Cd Length: 438  Bit Score: 124.79  E-value: 8.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  12 SDRLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQG 90
Cdd:PRK07575   2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  91 TKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSkekGVNSFMVYMaYKD 170
Cdd:PRK07575  80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTANPTC---GIKIFMGSS-HGP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 171 LYQVSNTELYEIFTCLGELgaIAqVHAENGDIIAQEQARMleMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYV 250
Cdd:PRK07575 156 LLVDEEAALERIFAEGTRL--IA-VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHI 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 251 TKVMSKSAADLISQArkKGNVVFGEPITASLGIDGTHYwsknwAKAAAFV-TSPPLSpDPTTPDYINSLLASGDLQLSGS 329
Cdd:PRK07575 231 LHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAY-----ERIGTLAqMNPPLR-SPEDNEALWQALRDGVIDFIAT 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 330 AHCTFSTAQKAIGKDNftaIPEGTNGVEERMSVIWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVI 409
Cdd:PRK07575 303 DHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADLVL 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 209862992 410 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNL 457
Cdd:PRK07575 378 VDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
PRK09060 PRK09060
dihydroorotase; Validated
15-465 2.89e-30

dihydroorotase; Validated


Pssm-ID: 181632  Cd Length: 444  Bit Score: 123.49  E-value: 2.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:PRK09060   7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNdsvKQEVQSLSKEKGVNSFMVYM--AYKDLY 172
Cdd:PRK09060  84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDN---ADELAELERLPGCAGIKVFMgsSTGDLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 173 QVSNTELYEIftclgeLGAI---AQVHAEngdiiaqEQARMLEMGITGPEGHVLSRPEELEAEAVFRA----ITVASQTN 245
Cdd:PRK09060 161 VEDDEGLRRI------LRNGrrrAAFHSE-------DEYRLRERKGLRVEGDPSSHPVWRDEEAALLAtrrlVRLARETG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 246 CPLYVTKVMSKSAADLISQARkkgNVVFGEPITASLGIDGTHYWSKNWAKAaafVTSPPLSpDPTTPDYINSLLASGDLQ 325
Cdd:PRK09060 228 RRIHVLHVSTAEEIDFLADHK---DVATVEVTPHHLTLAAPECYERLGTLA---QMNPPIR-DARHRDGLWRGVRQGVVD 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 326 LSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDS 405
Cdd:PRK09060 301 VLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDA 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 406 DLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGR 465
Cdd:PRK09060 376 DFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
PRK04250 PRK04250
dihydroorotase; Provisional
20-455 1.38e-28

dihydroorotase; Provisional


Pssm-ID: 235265  Cd Length: 398  Bit Score: 117.56  E-value: 1.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  20 GRIVNDDQSFYADIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVIPGGIDVHTH---FQMPYKgmTTVDdffQGTKAALA 96
Cdd:PRK04250   4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHlrdFEESYK--ETIE---SGTKAALH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  97 GGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEkgvnsFMVyMAYKDLYQVSN 176
Cdd:PRK04250  77 GGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKI-----FMG-ASTGGIFSENF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 177 TELYEiftclgELGAIAQVHAENGDIIAQEqarmlemgitgPEghvlsRPEELEAEAVFRAITVASQTNCPLYVTKVMSK 256
Cdd:PRK04250 151 EVDYA------CAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 257 SAADLISQARKkgnvvfgEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSpdpTTPDYINSLLASGDLQLSGSAHCTFST 336
Cdd:PRK04250 209 DGLKLILKSNL-------PWVSFEVTPHHLFLTRKDYERNPLLKVYPPLR---SEEDRKALWENFSKIPIIASDHAPHTL 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 337 AQKAIGKdnfTAIPegtnGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNlYPRKGrIAVGSDSDLVIWDPDALK 416
Cdd:PRK04250 279 EDKEAGA---AGIP----GLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEW 348
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 209862992 417 IVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDG 455
Cdd:PRK04250 349 TIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
PLN02795 PLN02795
allantoinase
20-467 1.30e-27

allantoinase


Pssm-ID: 178392  Cd Length: 505  Bit Score: 116.41  E-value: 1.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  20 GRIVNDDQSFYADIYMEDGLIKQIGDNLIVPG---GVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALA 96
Cdd:PLN02795  51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAAA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  97 GGTTMIIDhvVP---EPESSLTEAYEKWREWADGKsccdyaLHVDITHWNDSVKQEVQSLSKEK--------GVNSFMVY 165
Cdd:PLN02795 129 GGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPENAHNASVLEelldagalGLKSFMCP 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 166 MAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQarMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTN 245
Cdd:PLN02795 201 SGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDTR 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 246 -------CPLYVTKVM-SKSAADLISQARKKGNVVFGEPITASLGI------DGthywsknwakAAAFVTSPPLSpDPTT 311
Cdd:PLN02795 279 pggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFsaeeipDG----------DTRYKCAPPIR-DAAN 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 312 PDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFN 391
Cdd:PLN02795 348 RELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAG 426
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 392 LyPRKGRIAVGSDSDLVIWDPDALKIVSAK-----NHQSVAEYnifEGMELRGAPLVVICQGKIMLEDGNlHVTQGAGRF 466
Cdd:PLN02795 427 L-DSKGAIAPGKDADIVVWDPEAEFVLDESypiyhKHKSLSPY---LGTKLSGKVIATFVRGNLVFLEGK-HAKQACGSP 501

                 .
gi 209862992 467 I 467
Cdd:PLN02795 502 I 502
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
62-451 7.57e-26

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


Pssm-ID: 396526 [Multi-domain]  Cd Length: 335  Bit Score: 108.35  E-value: 7.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   62 MVIPGGIDVHTHFQM-----PYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLT--EAYEKW----REWADGKSC 130
Cdd:pfam01979   1 IVLPGLIDAHVHLEMgllrgIVPPEFAYEALALGITTMLKSGTTTVLDMGATTSTGIEAllEAAEELplglRFLGPGCSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  131 CDYALHVDITHWNDSVKQEVQSLSKEKGVnsFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIiaqEQARM 210
Cdd:pfam01979  81 DGGELEGRKALREKLKAGADFIKGMADGV--VFVGLAPHGAPTFTDDELKAALEEAKKYGLPVAIHALETKG---EVEDA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  211 LEMGITGPEghVLSRPEELEAEAVFRAITVASQTNCPLYVTkvmskSAADLISQARKKGNvvfgepitaslgidgthyws 290
Cdd:pfam01979 156 IAAFGGGIE--HGTHLEVAESLGLLDVIKLILAHGVHLSPT-----EANLLAEHLKGAGV-------------------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  291 knwakaaAFVTSPPLSPDPTTPDyINSLLASGDLQLSGSAHCtfstaqkaIGKDNFTAIPEGTNGVEERMSViwdkAVAT 370
Cdd:pfam01979 209 -------AHCPFSNSKLRSGRIA-LRKALEDGVKVGLGTDGA--------ASGNSLNMLEELRLALKLQRLL----YDEE 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  371 GKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDALkivsaknhqsvaeyNIFEGMELRGAPLVVICQGKI 450
Cdd:pfam01979 269 GGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIVKGKI 334

                  .
gi 209862992  451 M 451
Cdd:pfam01979 335 V 335
PRK01211 PRK01211
dihydroorotase; Provisional
30-468 3.91e-23

dihydroorotase; Provisional


Pssm-ID: 179247  Cd Length: 409  Bit Score: 101.86  E-value: 3.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  30 YADIYMEDGLIKQIGDNLivpGGVKTIEANGkMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIIDHVVPE 109
Cdd:PRK01211  15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 110 PESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSlskekgvnSFMVYMAYKDLYQVSNTELYEIfTCLGEL 189
Cdd:PRK01211  89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERSI--------GLKVYMGGTTNTNGTDIEGGEI-KKINEA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 190 GAIAQVHAENGDIIAQEQARMLEMgitgpEGHVLSRPEELEAEAVFRAITVASQtncplyvTKVMS-KSAADLISQarkk 268
Cdd:PRK01211 160 NIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIAhVSSIDVIGR---- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 269 gnvvFGEPITASlgidgtHYWSKNWAKAAAF-VTSPPLSPDPTTPDYINSLLaSGDLQLSGSAHCTFSTAQKAigkdNFT 347
Cdd:PRK01211 224 ----FLREVTPH------HLLLNDDMPLGSYgKVNPPLRDRWTQERLLEEYI-SGRFDILSSDHAPHTEEDKQ----EFE 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 348 AIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVA 427
Cdd:PRK01211 289 YAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKC 365
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 209862992 428 EYNIFEGMELRgAPLVVICQGKIMLEDGNLhVTQGAGRFIP 468
Cdd:PRK01211 366 PVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVP 404
PRK09236 PRK09236
dihydroorotase; Reviewed
13-458 3.67e-22

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 99.17  E-value: 3.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  13 DRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTK 92
Cdd:PRK09236   2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  93 AALAGGTTMIID--HVVPepeSSLT-EAYEKWREWADGKSCCDYALHVDIThwNDSVkQEVQSLSKEK--GVNSFM---- 163
Cdd:PRK09236  80 AAVAGGITSFMEmpNTNP---PTTTlEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRLDPKRvcGVKVFMgast 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 164 ----VymaykDLYQVsnteLYEIFTCLGELgaIAqVHAENGDIIAQEQARMLEM---GITgPEGHVLSRpeelEAEAVFR 236
Cdd:PRK09236 154 gnmlV-----DNPET----LERIFRDAPTL--IA-THCEDTPTIKANLAKYKEKygdDIP-AEMHPLIR----SAEACYK 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 237 ----AITVASQTNCPLYVTKVMSKSAADLISQ---ARKKgnvvfgepITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDP 309
Cdd:PRK09236 217 ssslAVSLAKKHGTRLHVLHISTAKELSLFENgplAEKR--------ITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTA 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 310 TTPDYINSLLASGDLQLSGSAHCTFSTAQKaigKDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKI 389
Cdd:PRK09236 289 SDREALRQALADDRIDVIATDHAPHTWEEK---QGPYFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAIL 364
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209862992 390 FNLyPRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 458
Cdd:PRK09236 365 FDI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
15-120 4.67e-13

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 71.08  E-value: 4.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPG--GVKTIEANGKMVIPGGIDVHTHFQM------------- 76
Cdd:cd01298    1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862992  77 --------PYKGMTTVDDFFQGTKAALA----GGTTMIIDHVVPEPEsSLTEAYEK 120
Cdd:cd01298   81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPD-AVAEAAEE 135
pyrC PRK00369
dihydroorotase; Provisional
32-466 6.91e-12

dihydroorotase; Provisional


Pssm-ID: 234738  Cd Length: 392  Bit Score: 67.48  E-value: 6.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  32 DIYMEDGlIKQIGDNLIVpgGVKTIEANGK---------MVIPGGIDVHTHF---QMPYKgmttvDDFFQGTKAALAGGT 99
Cdd:PRK00369   8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHLrglKLSYK-----EDVASGTSEAAYGGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 100 TMIIDHVVPEPESSLTEAY-EKWREWADGkSCCDYALHVDIThwnDSVKqEVQSLskekGVNSFMVYMayKDLyqvsntE 178
Cdd:PRK00369  80 TLVADMPNTIPPLNTPEAItEKLAELEYY-SRVDYFVYSGVT---KDPE-KVDKL----PIAGYKIFP--EDL------E 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 179 LYEIFTCLGELGAIAQVHAEngdiiaqeqarmLEMGITGPEGhvLSRPEELEAEAVFRAITVASqtncpLYVTKVmskSA 258
Cdd:PRK00369 143 REETFRVLLKSRKLKILHPE------------VPLALKSNRK--LRRNCWYEIAALYYVKDYQN-----VHITHA---SN 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 259 ADLISQARKKGnvvFGEPITAS-LGIDG-THYWSKnwakaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGsaHCTFST 336
Cdd:PRK00369 201 PRTVRLAKELG---FTVDITPHhLLVNGeKDCLTK---------VNPPIR-DINERLWLLQALSEVDAIASD--HAPHSS 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 337 AQKaigKDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIwdpdaLK 416
Cdd:PRK00369 266 FEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTV-----IQ 334
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 209862992 417 IVSAKNHQ--SVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRF 466
Cdd:PRK00369 335 FEDWRYSTkySKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPF 386
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
15-465 1.37e-11

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 66.55  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVndDQS----FYADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHfqmpYKGMTTVDDFFqg 90
Cdd:cd01297    2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  91 TKAALAGGTTMIIDH-------VVPEPESSLTEAYEKWREWADGK-----SCCDYALHVD------------------IT 140
Cdd:cd01297   73 RPSSRQGVTTVVLGNcgvspapANPDDLARLIMLMEGLVALGEGLpwgwaTFAEYLDALEarppavnvaalvghaalrRA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 141 HWNDSVKQ----EVQSLSK--EKGVNS----FMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAEN-GDIIAQEQAR 209
Cdd:cd01297  153 VMGLDAREateeELAKMREllREALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYeGDSILEALDE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 210 MLEMGitgpeghvlsrpEELEAEAVFRAITVASQTNCPLYvtkvmsKSAADLISQARKKGNVVFGE--PITASLGidgth 287
Cdd:cd01297  233 LLRLG------------RETGRPVHISHLKSAGAPNWGKI------DRLLALIEAARAEGLQVTADvyPYGAGSE----- 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 288 ywsknwAKAAAFVTSPPlspdpttpdyinsLLASGDLQLSGSAH----CTFStaqKAIGKdnftaipegtnGVEERMSVI 363
Cdd:cd01297  290 ------DDVRRIMAHPV-------------VMGGSDGGALGKPHprsyGDFT---RVLGH-----------YVRERKLLS 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 364 WDKAVAtgKMdenqfvavtSTNAAKIFNLYPRkGRIAVGSDSDLVIWDPDALKIVS---AKNHQSvaeynifEGMELrga 440
Cdd:cd01297  337 LEEAVR--KM---------TGLPARVFGLADR-GRIAPGYRADIVVFDPDTLADRAtftRPNQPA-------EGIEA--- 394
                        490       500
                 ....*....|....*....|....*
gi 209862992 441 plvVICQGKIMLEDGnLHVTQGAGR 465
Cdd:cd01297  395 ---VLVNGVPVVRDG-AFTGARPGR 415
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
64-464 1.51e-11

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: 65.93  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  64 IPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIidHVVPEPESSL--TEAYEKWREWADGKSCCDYALHVDITH 141
Cdd:cd01316    5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIvdVASLKLVQSLAQAKARCDYAFSIGATS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 142 WNDSVKQEVQSlskeKGVNSFMVymaykdlyqvsnteLYEIFTCLgELGAIAQVhaengdiiaqeqARMLEmgiTGPEgh 221
Cdd:cd01316   81 TNAATVGELAS----EAVGLKFY--------------LNETFSTL-ILDKITAW------------ASHFN---AWPS-- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 222 vlSRPEELEAEAVFRA--ITVASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI---DGTHYWSknwaka 296
Cdd:cd01316  125 --TKPIVTHAKSQTLAavLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLsqdDLPRGQY------ 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 297 aafvtspPLSPDPTTPDYINSL---LASGDLQLSGSAHCTFstAQKAIGKdnftaIPEGTNGVEERMSVIWdKAVATGKM 373
Cdd:cd01316  197 -------EVRPFLPTREDQEALwenLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRL 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 374 DENQFVAVTSTNAAKIFNLYPRkgriavgSDSDLVIwDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLE 453
Cdd:cd01316  262 TIEDIVDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFI 333
                        410
                 ....*....|.
gi 209862992 454 DGNLHVTQGAG 464
Cdd:cd01316  334 DGEIVAPPGFG 344
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
12-218 6.26e-10

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 223479 [Multi-domain]  Cd Length: 421  Bit Score: 61.31  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  12 SDRLLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHF-QMPYKG------- 80
Cdd:COG0402    1 MTMLLIRGDLLLTNDPEgriEDGDLVIEDGKIVAIGANAEGPPDEEVIDAKGKLVLPGFVNAHTHLdQTLLRGladdlpl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  81 --------------MTTVDDFFQGTKAA----LAGGTTMIIDH--VVPEPESSLTEAYEKWRE-WADGKSCCDYAL--HV 137
Cdd:COG0402   81 lewleryvwprearLLTEEDLYARALLAllemLRNGTTTARTHvdVVAESADAAFEAALEVGLrAVLGPVLQDVAFpdPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 138 DITHWNDSVKQEVQSLSKEKGVNSFMVymAYKDLYQVSNTELYEIFTCLGELGAIAQVH-AENGDiiaqEQARMLEMGIT 216
Cdd:COG0402  161 AETDEELEETEELLREAHGLGRDVVGL--APHFPYTVSPELLESLDELARKYGLPVHIHlAETLD----EVERVLEPYGA 234

                 ..
gi 209862992 217 GP 218
Cdd:COG0402  235 RP 236
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
15-411 2.50e-09

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423  Cd Length: 380  Bit Score: 59.09  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFqmpYKGMTtvDDFFQGTK 92
Cdd:PRK09237   1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHV---YPGST--PYGDEPDE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  93 AALAGGTTMIIDhvvpepesslteayekwrewADGKSCCDYalhvdithwnDSVKQEVQSLSKEKgvnsfmVYmAYKDLY 172
Cdd:PRK09237  76 VGVRSGVTTVVD--------------------AGSAGADNF----------DDFRKLTIEASKTR------VL-AFLNIS 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 173 QV---SNTELYEIFTClgELGAIAQVHAENGDIIAQEQARMlEMGITGPEGhvlSRPEEleaeavfRAITVASQTNCPLY 249
Cdd:PRK09237 119 RIgllAQDELADLEDI--DADAVAEAVKRNPDFIVGIKARM-SSSVVGDNG---IEPLE-------LAKAIAAEANLPLM 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 250 VTKVMSKSAADLISQARKKGNVVfgepitaslgidgTHYWSKnwaKAAAFVTspplsPDPTTPDYINSLLASGdLQLS-- 327
Cdd:PRK09237 186 VHIGNPPPSLEEILELLRPGDIL-------------THCFNG---KPNRILD-----EDGELRPSVLEALERG-VRLDvg 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 328 -GSAHCTFSTAQKAIGKD-NFTAIpeGT--------NGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKG 397
Cdd:PRK09237 244 hGTASFSFKVAEAAIAAGiLPDTI--STdiycrnriNGPVYSLATVMSKFLALG-MPLEEVIAAVTKNAADALRL-PELG 319
                        410
                 ....*....|....
gi 209862992 398 RIAVGSDSDLVIWD 411
Cdd:PRK09237 320 RLQVGSDADLTLFT 333
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
14-218 2.05e-08

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 56.55  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  14 RLLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHF-QMPYKGMTtvDDF-- 87
Cdd:PRK07228   2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQTLFRGIA--DDLel 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  88 ----------FQGTKAA--------------LAGGTTMIIDHV-VPEPESSLTEAYEKWREWADGKSCCDYALHVDIT-- 140
Cdd:PRK07228  80 ldwlkdriwpLEAAHDAesmyysallgigelIESGTTTIVDMEsVHHTDSAFEAAGESGIRAVLGKVMMDYGDDVPEGlq 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 141 -HWNDSVKQEVQSLSKEKGVNSFMVYMAYKDLYQVSNTElyeifTCLGELGAIAQ-------VHA-EN-GDIIAQEQARM 210
Cdd:PRK07228 160 eDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTE-----ELLRGVRDLADeygvrihTHAsENrGEIETVEEETG 234
                        250
                 ....*....|....*
gi 209862992 211 L-------EMGITGP 218
Cdd:PRK07228 235 MrnihyldEVGLTGE 249
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
15-73 2.90e-08

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 56.05  E-value: 2.90e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 73
Cdd:cd00854    1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
PRK09061 PRK09061
D-glutamate deacylase; Validated
5-102 5.10e-08

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 55.47  E-value: 5.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   5 SRNKIRQSDRLLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVIPGGIDVHTHfqmpykGMT 82
Cdd:PRK09061  11 LMPASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH------GQS 82
                         90       100
                 ....*....|....*....|
gi 209862992  83 TVDDFFQgtkaALAGGTTMI 102
Cdd:PRK09061  83 VAAYRMQ----AFDGVTTAL 98
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
32-411 1.35e-07

Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238632 [Multi-domain]  Cd Length: 338  Bit Score: 53.49  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  32 DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFqmpYKGMTTVDDffQGTKAALAGGTTMIIDhvvpepe 111
Cdd:cd01307    1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHV---YQGGTRYGD--RPDMIGVKSGVTTVVD------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 112 sslteayekwrewADGKSCCDYalhvdithwnDSVKQEVQSLSKEKgvnsfmVYmAYKDLY---QVSNTELYEIFTClgE 188
Cdd:cd01307   69 -------------AGSAGADNI----------DGFRYTVIERSATR------VY-AFLNISrvgLVAQDELPDPDNI--D 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 189 LGAIAQVHAENGDIIAQEQARMlEMGITGPEGhvlSRPEELEAEAvfraitvASQTNCPLYvtkVMSKSAADLISQA--- 265
Cdd:cd01307  117 EDAVVAAAREYPDVIVGLKARA-SKSVVGEWG---IKPLELAKKI-------AKEADLPLM---VHIGSPPPILDEVvpl 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 266 RKKGNVVfgepitaslgidgTHYWSknwAKAAAFVTspplsPDPTTPDYINSLLASG---DLQlSGSAHCTFSTAQKAIG 342
Cdd:cd01307  183 LRRGDVL-------------THCFN---GKPNGIVD-----EEGEVLPLVRRARERGvifDVG-HGTASFSFRVARAAIA 240
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209862992 343 KD-NFTAI------PEGTNGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVIWD 411
Cdd:cd01307  241 AGlLPDTIssdihgRNRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFD 314
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
68-274 1.92e-07

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


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 52.72  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  68 IDVHTHFQMP----------------YKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCC 131
Cdd:cd01292    2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 132 DYALHVDITH--------WNDSVKQEVQSLsKEKGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDII 203
Cdd:cd01292   82 RVVLGLGIPGvpaavdedAEALLLELLRRG-LELGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDP 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209862992 204 AQEQARMLEMGITGPE---GHVLSRPEELEAEAVFRAITVASqTNCPLYVTKVMSKSAADLISQARKKGNVVFG 274
Cdd:cd01292  160 TRALEDLVALLRLGGRvviGHVSHLDPELLELLKEAGVSLEV-CPLSNYLLGRDGEGAEALRRLLELGIRVTLG 232
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
6-103 2.29e-07

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 223933 [Multi-domain]  Cd Length: 584  Bit Score: 53.46  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   6 RNKIRQSD-----RLLIKGGRIVN--DDQSFYADIYMEDGLIkqIGDNL-IVPGGVKTIEANGKMVIPGGIDVHTHFQMp 77
Cdd:COG1001   12 RRLVAVARgrakaDLVLKNGRIVDvvTGEIYKGDIAIAGGRI--VGVIGeYRAEATEVIDAAGRYIVPGFIDAHLHIES- 88
                         90       100
                 ....*....|....*....|....*.
gi 209862992  78 ykGMTTVDDFfqgTKAALAGGTTMII 103
Cdd:COG1001   89 --SMLTPSEF---ARAVLPHGTTTVV 109
PRK07627 PRK07627
dihydroorotase; Provisional
14-454 3.72e-07

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 52.76  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  14 RLLIKGGRIVN-----DDQsfyADIYMEDGLIKQIGDnliVPGGV---KTIEANGKMVIPGGIDVHTHFQMP-YKGMTTV 84
Cdd:PRK07627   2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREPgYEYKATL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  85 DDFFQgtkAALAGGTTMII-----DHVVPEPEssLTEAYeKWREWADGKSccdyalHVDithwndSVKQEVQSLSKEKgv 159
Cdd:PRK07627  76 ESEMA---AAVAGGVTSLVcppdtDPVLDEPG--LVEML-KFRARNLNQA------HVY------PLGALTVGLKGEV-- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 160 nsfmvymaykdlyqvsNTELYEiftcLGELGAIAQVHAENGDIIAQEQARMLEMGIT-------------------GPEG 220
Cdd:PRK07627 136 ----------------LTEMVE----LTEAGCVGFSQANVPVVDTQVLLRALQYASTfgftvwlrpldaflgrggvAASG 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 221 HVLSR------PEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGnvvfgEPITASLGIDGTH------- 287
Cdd:PRK07627 196 AVASRlglsgvPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEG-----LPVTCDVGVNHVHlidvdig 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 288 YWSKNwakaaaFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIgkdNFTAIPEGTNGVEERMSVIWDKA 367
Cdd:PRK07627 271 YFDSQ------FRLDPPLR-SQRDREAIRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPLTLKWA 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 368 VATgKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQ 447
Cdd:PRK07627 341 DEA-KVPLARALARITSAPARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVA 417

                 ....*..
gi 209862992 448 GKIMLED 454
Cdd:PRK07627 418 GQVAFER 424
PRK10657 PRK10657
isoaspartyl dipeptidase; Provisional
379-466 5.76e-07

isoaspartyl dipeptidase; Provisional


Pssm-ID: 182623  Cd Length: 388  Bit Score: 51.75  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 379 VAVTSTNAAKIFNLYpRKGRIAVGSDSDLVIWDpDALKIVSaknhqsvaeynifegmelrgaplvVICQGKIMLEDGNLH 458
Cdd:PRK10657 329 LKPLTSNVARFLKLN-GKGEILPGKDADLLVLD-DDLRIEQ------------------------VIAKGKLMVKDGKAL 382

                 ....*...
gi 209862992 459 VTqgaGRF 466
Cdd:PRK10657 383 VK---GTF 387
Amidohydro_3 pfam07969
Amidohydrolase family;
379-434 5.82e-07

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 52.15  E-value: 5.82e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209862992  379 VAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEG 434
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
343-413 8.68e-07

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 224733 [Multi-domain]  Cd Length: 380  Bit Score: 51.11  E-value: 8.68e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209862992 343 KDNFTAIPEGT-NGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 413
Cdd:COG1820  294 ADGARRLEDGTlAGSTLTMDEAVRNLVEWGGISLAEAVRMASLNPAKALGLDDRLGSIKPGKDADLVVLDDD 365
PRK08204 PRK08204
hypothetical protein; Provisional
13-111 8.97e-07

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 51.54  E-value: 8.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  13 DRLLIKGGRIVNDDQSF----YADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVIPGGIDVHTH--------------- 73
Cdd:PRK08204   2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHRHtwqsvlrgigadwtl 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 209862992  74 ---FQMPYKGMTTV---DDFFQGTKA----ALAGGTTMIID--HVVPEPE 111
Cdd:PRK08204  81 qtyFREIHGNLGPMfrpEDVYIANLLgaleALDAGVTTLLDwsHINNSPE 130
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
31-126 1.86e-06

Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 50.32  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  31 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH------FQMP-----------------YKGMTTVDDF 87
Cdd:cd01293   15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHldktftGGRWpnnsggtlleaiiaweeRKLLLTAEDV 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 209862992  88 FQ----GTKAALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 126
Cdd:cd01293   95 KEraerALELAIAHGTTAIRTHVDVDPAAGLKaleallELREEWADLID 143
PRK07369 PRK07369
dihydroorotase; Provisional
31-439 2.03e-06

dihydroorotase; Provisional


Pssm-ID: 236002  Cd Length: 418  Bit Score: 50.37  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  31 ADIYMEDGLIKQIGDNLI-VPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMI------- 102
Cdd:PRK07369  22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVailpdtf 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 103 --IDHvvPEPESSL-----TEAYEKWREWADgksccdyalhvdITHwNDSVKQ--EVQSLSkEKGVNSFMVYMAYKDLYQ 173
Cdd:PRK07369 100 ppLDN--PATLARLqqqaqQIPPVQLHFWGA------------LTL-GGQGKQltELAELA-AAGVVGFTDGQPLENLAL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 174 VSNTELYeiftcLGELGAIAQVHAEN----GDIIAQEQARMLEMGITGpeghvlsRPEELEAEAVFRAITVASQTNCPLY 249
Cdd:PRK07369 164 LRRLLEY-----LKPLGKPVALWPCDrslaGNGVMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGTPVH 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 250 VTKVMSKSAADLISQARKKGnvvfgEPITASlgidgTHYWSKNWAKAAAFVTSPPLSPDPT--TPDYINSLLA---SGDL 324
Cdd:PRK07369 232 LMRISTARSVELIAQAKARG-----LPITAS-----TTWMHLLLDTEALASYDPNLRLDPPlgNPSDRQALIEgvrTGVI 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 325 QLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRkgRIAVGSD 404
Cdd:PRK07369 302 DAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SLAPGQP 376
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 209862992 405 SDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRG 439
Cdd:PRK07369 377 AELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKG 411
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
15-86 2.72e-06

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 224490 [Multi-domain]  Cd Length: 535  Bit Score: 50.03  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRI--VNDDQSFYADIYMEDGLIKQIGD----NLIVPGGVKTIEANGKMVIPGGIDVHTH--------FQMPYKG 80
Cdd:COG1574    7 LILHNGRIytMDEARPTAEAVAIKDGRIVAVGSdaelKALAGPATEVIDLKGKFVLPGFVDAHLHlisgglslLELNLDG 86

                 ....*.
gi 209862992  81 MTTVDD 86
Cdd:COG1574   87 VRSLDD 92
Urease_alpha cd00375
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ...
31-103 3.54e-06

Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.


Pssm-ID: 238221  Cd Length: 567  Bit Score: 49.63  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  31 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 98
Cdd:cd00375   83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151

                 ....*
gi 209862992  99 TTMII 103
Cdd:cd00375  152 ITTMI 156
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
15-126 6.50e-06

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 226179 [Multi-domain]  Cd Length: 579  Bit Score: 48.79  E-value: 6.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVND--DQSFYADIYMEDGLIKQIGDNLIV-PGGVKTIEANGKMVIPGGIDVHTHfqmpYKGMTTVDDFFQgt 91
Cdd:COG3653    8 VVIRDGLIFDGtgNPPFTTDVGIRDGVIAAVAKGALDgTGCPEEVDAAGRIVAPGFIDVHTH----YDAEVLLDPGLR-- 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 209862992  92 KAALAGGTTMII-------------DH---------VVPEPESSLTEAYEKWREWAD 126
Cdd:COG3653   82 PSVRHGVTTVVLgncgistapanseDAddlfsrveaVGREFVFGALRDNQTWSTFAE 138
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
14-413 6.99e-06

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


Pssm-ID: 224149 [Multi-domain]  Cd Length: 406  Bit Score: 48.52  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  14 RLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLI-VPGGVKTIEANGKMVIPGGIDVHTH----------FQM----- 76
Cdd:COG1228   11 MLATLAGRGLPGLGIIEdGAVLIEDGKIVAVGPEEIdIPAGAEVIDAKGKTVTPGLIDAHTHlgfggsrggeFELreaga 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  77 PY------KGMTTVDDffQGTKAALAGGTTMIIDHVVPEPESSLTEAyekwrewADGKSccDYALHVDITHWNDSVKQEV 150
Cdd:COG1228   91 SYteilaaGGGILPLD--RGFTTARDGGLKATALPRLKRAGSAGVTT-------GERKS--GYGLDLETEGGHLRAAAGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 151 QSLSKEKGVNSFMVYMAYKDLYQvSNTELYEIFTCLGELGAIAQVHAENGDIiaqeqarmlemgitGPEGHVLSRPEELE 230
Cdd:COG1228  160 KESRPVAVGSTPLAAHGVPEERK-ATREAYVAGARLLIKIVATGGLASFVDA--------------FCEGGQFSPEEIRA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 231 A--EAVFRAITVASQTNCplyvtkvmsksaADLISQARKKGNVVFGEPITAslgidgthywskNWAKAAAFVTSPPLSPD 308
Cdd:COG1228  225 VlaAALKAGIPVKAHAHG------------ADGIKLAIRLGAKSAEHGTLL------------DHETAALLAEKGAGTPV 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 309 PT-TPDYINSLLASgdlqlsgsahcTFSTAQK--------AIGKDNFTAIPEGTNGVEERMsviwdkAVATGkMDENQ-F 378
Cdd:COG1228  281 PVlLPRTKFELREL-----------DYKPARKlidagvkvAIGTDHNPGTSHGSLALEMAL------AVRLG-MTPEEaL 342
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 209862992 379 VAVTsTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 413
Cdd:COG1228  343 KAAT-INAAKALGLADKVGSLEPGKDADLVVWDGD 376
ureC PRK13308
urease subunit alpha; Reviewed
31-102 8.98e-06

urease subunit alpha; Reviewed


Pssm-ID: 183965  Cd Length: 569  Bit Score: 48.55  E-value: 8.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  31 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 98
Cdd:PRK13308  87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155

                 ....*
gi 209862992  99 -TTMI 102
Cdd:PRK13308 156 iTTML 160
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
15-76 1.16e-05

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 47.87  E-value: 1.16e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209862992  15 LLIKGGRIVNDD--QSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQM 76
Cdd:PRK08393   3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
14-72 1.31e-05

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967  Cd Length: 383  Bit Score: 47.48  E-value: 1.31e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 209862992  14 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvkTIEANGKMVIPGGIDVHT 72
Cdd:PRK15446   3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
15-91 1.55e-05

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 47.57  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVIPGGIDVHTHFQMP-YKGM---TTVDDF 87
Cdd:PRK06380   3 ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTaSKGLfddVDLEEF 80

                 ....
gi 209862992  88 FQGT 91
Cdd:PRK06380  81 LMKT 84
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
17-73 1.92e-05

Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.


Pssm-ID: 238629  Cd Length: 541  Bit Score: 47.41  E-value: 1.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  17 IKGGRIVNDDQSFYA---DIYMEDGlikQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 73
Cdd:cd01304    1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
PRK09356 PRK09356
imidazolonepropionase; Validated
15-74 2.73e-05

imidazolonepropionase; Validated


Pssm-ID: 236478 [Multi-domain]  Cd Length: 406  Bit Score: 46.70  E-value: 2.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIV---NDDQSFY-----ADIYMEDGLIKQIGDNLIVPGGV--KTIEANGKMVIPGGIDVHTHF 74
Cdd:PRK09356   5 LLWTNAQLAtmdGGGMGELgiiedGAIAIEDGKIVWVGPEADLPAAYaaEVIDAGGKLVTPGLIDCHTHL 74
UreC COG0804
Urease alpha subunit [Amino acid transport and metabolism];
15-102 5.05e-05

Urease alpha subunit [Amino acid transport and metabolism];


Pssm-ID: 223875  Cd Length: 568  Bit Score: 46.17  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIG--------DNLIVPGGVKT--IEANGKMVIPGGIDVHTHFQMPykgmttv 84
Cdd:COG0804   69 LVITNALIIDYWGIVKADIGIKDGRIAGIGkagnpdimDGVTIIIGPSTeiIAGEGKIVTAGGIDTHIHFICP------- 141
                         90
                 ....*....|....*....
gi 209862992  85 ddffQGTKAALAGG-TTMI 102
Cdd:COG0804  142 ----QQIEEALASGiTTMI 156
PRK07203 PRK07203
putative aminohydrolase SsnA;
15-74 8.24e-05

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 45.31  E-value: 8.24e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209862992  15 LLIKGGRIV-NDDQSFY---ADIYMEDGLIKQIGDNlivpGGVKT-------IEANGKMVIPGGIDVHTHF 74
Cdd:PRK07203   2 LLIGNGTAItRDPAKPViedGAIAIEGNVIVEIGTT----DELKAkypdaefIDAKGKLIMPGLINSHNHI 68
ureC PRK13206
urease subunit alpha; Reviewed
31-103 1.02e-04

urease subunit alpha; Reviewed


Pssm-ID: 237304  Cd Length: 573  Bit Score: 45.09  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  31 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 98
Cdd:PRK13206  89 ADVGIRDGRIVAIGkagnpdimdgvhPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICP-----------QIVDEALAAG 157

                 ....*
gi 209862992  99 TTMII 103
Cdd:PRK13206 158 ITTLI 162
ureC PRK13207
urease subunit alpha; Reviewed
31-102 1.42e-04

urease subunit alpha; Reviewed


Pssm-ID: 237305  Cd Length: 568  Bit Score: 44.40  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  31 ADIYMEDGLIKQIG--------DN--LIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG-T 99
Cdd:PRK13207  85 ADIGIKDGRIVAIGkagnpdiqDGvdIIIGPGTEVIAGEGLIVTAGGIDTHIHFICP-----------QQIEEALASGvT 153

                 ...
gi 209862992 100 TMI 102
Cdd:PRK13207 154 TMI 156
ureB PRK13985
urease subunit alpha;
3-99 1.75e-04

urease subunit alpha;


Pssm-ID: 184438  Cd Length: 568  Bit Score: 44.12  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   3 SPSRNKIRqsdrLLIKGGRIVNDDQSFYADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDV 70
Cdd:PRK13985  59 NPSKEELD----LIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLSVGPATEALAGEGLIVTAGGIDT 134
                         90       100
                 ....*....|....*....|....*....
gi 209862992  71 HTHFQMPYKGMTTvddFFQGTKAALAGGT 99
Cdd:PRK13985 135 HIHFISPQQIPTA---FASGVTTMIGGGT 160
PRK10657 PRK10657
isoaspartyl dipeptidase; Provisional
15-74 1.84e-04

isoaspartyl dipeptidase; Provisional


Pssm-ID: 182623  Cd Length: 388  Bit Score: 44.04  E-value: 1.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIvnddqsfYA-------DIYMEDGLIKQIGDNLIVPGG---VKTIEANGKMVIPGGIDVHTHF 74
Cdd:PRK10657   3 TLLKNAHV-------YApedlgkkDILIAGGKIIAIADNINIPDIvpdIEVIDASGKILVPGFIDQHVHI 65
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
33-74 2.08e-04

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 43.79  E-value: 2.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 209862992  33 IYMEDGLIKQIGD----NLIVPGGVKTIEANGKMVIPGGIDVHTHF 74
Cdd:cd01296    1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
37-73 2.49e-04

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 43.45  E-value: 2.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 209862992  37 DGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 73
Cdd:cd01309    1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
16-73 2.81e-04

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 224733 [Multi-domain]  Cd Length: 380  Bit Score: 43.41  E-value: 2.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  16 LIKGGRIVnDDQSFYADIYM--EDGLIKQIGDNLIvPGGVKTIEANGKMVIPGGIDVHTH 73
Cdd:COG1820    3 ALKNGRIF-TGHGVLDGGAVviEDGKIEAVVPAEL-PADAEIIDLKGALLVPGFIDLHIH 60
PRK05985 PRK05985
cytosine deaminase; Provisional
31-126 3.44e-04

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 43.00  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  31 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGM--------TTVDDFFQGTK---------- 92
Cdd:PRK05985  17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDpwypnepgPSLRERIANERrrraasghpa 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 209862992  93 ---------AALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 126
Cdd:PRK05985  97 aeralalarAAAAAGTTAMRSHVDVDPDAGLRhleavlAARETLRGLID 145
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
32-73 3.77e-04

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 224150  Cd Length: 575  Bit Score: 43.24  E-value: 3.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 209862992  32 DIYMEDGlikQIGDNLIVPG-GVKTIEANGKMVIPGGIDVHTH 73
Cdd:COG1229   25 DICVKDG---KIVEESEVSEsKAKVIDASGKLVMPGGVDSHSH 64
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
366-419 3.80e-04

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 42.68  E-value: 3.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 209862992 366 KAVATGKMDENQFVAVTStNAAKIFNLYPRKGRIAVGSDSDLVIWDPDALKIVS 419
Cdd:cd01309  294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTS 346
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
381-460 4.25e-04

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633  Cd Length: 387  Bit Score: 42.76  E-value: 4.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992 381 VTSTNAAKIFNLYPrKGRIAVGSDSDLVIWDPDaLKIVSaknhqsvaeynifegmelrgaplvVICQGKIMLEDGNLHVT 460
Cdd:cd01308  330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD-LDINS------------------------VIAKGQIMVRNGKLLVK 383
PRK09059 PRK09059
dihydroorotase; Validated
15-103 7.56e-04

dihydroorotase; Validated


Pssm-ID: 181631  Cd Length: 429  Bit Score: 41.94  E-value: 7.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  15 LLIKGGRIVNDDQSF--YADIYMEDGLIKQIGD---NLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQ 89
Cdd:PRK09059   5 ILLANARIIDPSRGLdeIGTVLIEDGVIVAAGKgagNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIAS 82
                         90
                 ....*....|....
gi 209862992  90 GTKAALAGGTTMII 103
Cdd:PRK09059  83 ASRAAAAGGVTSII 96
PRK07583 PRK07583
cytosine deaminase;
1-73 9.19e-04

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 41.89  E-value: 9.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992   1 MYSPSRnkIRQSDRLLIKGGRI------------VNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGI 68
Cdd:PRK07583   1 MSSFFS--LPESGRYWLKNARVpaalleggvppgDTLEGLVLVDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFV 78

                 ....*
gi 209862992  69 DVHTH 73
Cdd:PRK07583  79 DMHTH 83
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
14-74 3.47e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 39.84  E-value: 3.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209862992  14 RLLIKGGRIV---NDDQSFYAD--IYMEDGLIKQIGDNLIVPG-GVKTIEANGKMVIPGGIDVHTHF 74
Cdd:PRK08203   2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHF 68
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
32-74 5.17e-03

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for photochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 39.60  E-value: 5.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 209862992  32 DIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVIPGGIDVHTHF 74
Cdd:cd01300    1 AVAVRDGRIVAVGSDaeakALKGPATEVIDLKGKTVLPGFIDSHSHL 47
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
367-411 7.34e-03

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 38.78  E-value: 7.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 209862992 367 AVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWD 411
Cdd:cd01296  304 ACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
15-87 8.10e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 38.96  E-value: 8.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209862992  15 LLIKGGRIVNDDQSFY--ADIYMEDGLIKQIGDNliVPGGVKT-IEANGKMVIPGGIDVHTHFQMP-YKGMTtvDDF 87
Cdd:PRK06038   4 IIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDADTvIDAKGSVVMPGLVNTHTHAAMTlFRGYA--DDL 76
PLN02303 PLN02303
urease
29-102 9.39e-03

urease


Pssm-ID: 215172 [Multi-domain]  Cd Length: 837  Bit Score: 38.96  E-value: 9.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209862992  29 FYADIYMEDGLIKQIG------------DNLIVpgGVKT--IEANGKMVIPGGIDVHTHFQMPYkgmttvddffQGTKAA 94
Cdd:PLN02303 350 YKADIGIKDGLIVGIGkagnpdvmdgvtSNMIV--GVNTevIAGEGMIVTAGGIDCHVHFICPQ----------LATEAI 417

                 ....*...
gi 209862992  95 LAGGTTMI 102
Cdd:PLN02303 418 ASGITTLV 425
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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