|
Name |
Accession |
Description |
Interval |
E-value |
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
17-471 |
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 [Multi-domain] Cd Length: 454 Bit Score: 756.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 96
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQV 176
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 257 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 337 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPD 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947725 416 AVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
17-466 |
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: 740.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 96
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKdKGVNSFMVYMAYKDLYQV 176
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 257 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYINSLLASGDLQLSGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 337 STAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDA 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622947725 417 VKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAG 466
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
16-475 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 572.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 16 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlivpGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKA 95
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 96 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIkDKGVNSFMVYMAYKDLYQ 175
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 176 VSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 256 MSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdpttPDYINSL---LASGDLQLSGSA 332
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD----KEHQDALwrgLQDGDLQVVATD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 333 HCTFSTAQKA-IGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVI 411
Cdd:PRK08323 313 HCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947725 412 WDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFS 475
Cdd:PRK08323 393 WDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-485 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 550.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 12 ITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQ 91
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 92 GTKAALAGGTTMIIDHVVPePESSLTEAYEKWREWADgKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYK 171
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIP-VNGNLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 172 DLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 252 VTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYINSLLASGDLQLSGS 331
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 332 AHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVI 411
Cdd:PLN02942 319 DHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIII 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947725 412 WDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSdYVYKRIKAR 485
Cdd:PLN02942 399 LNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKA 471
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-470 |
1.38e-127 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 380.98 E-value: 1.38e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 18 LIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAAL 97
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 98 AGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLiKDKGVNSFMVYMAYKDLYQVS 177
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGAL-AEAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 178 NTE-LYEIFTCLGELGAIAQVHAENGDIIAQeqtRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVM 256
Cdd:COG0044 158 DDGlLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 257 SKSAADLISQARKKGNVVFGE--P----ITAS-LGIDGTHYwsknwakaaafVTSPPLSpdptTPDYINSL---LASGDL 326
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPLR----TEEDREALwegLADGTI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 327 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSD 406
Cdd:COG0044 300 DVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGAD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947725 407 SDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGRFIP 470
Cdd:COG0044 376 ADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLR 438
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
17-473 |
5.85e-117 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 355.16 E-value: 5.85e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVIPGGIDVHTHFQMPY-KGMTTVDDFFQGTKA 95
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 96 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSV-KQEVQNLIKDkGVNSFMVYMAYKDLy 174
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 175 QVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTK 254
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 255 VMSKSAADLISQARKKGNVVFGEP------ITAS-LGIDGTHywsknwakAAAFVTSPPLSpDPTTPDYINSLLASGDLQ 327
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 328 LSGSAHCTF---STAQKAIGKDN--FTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIS 402
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947725 403 VGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSP 473
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
17-469 |
6.74e-67 |
|
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: 224.09 E-value: 6.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 97 LAGGTTMIIDhvVP---EPESSLTEAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQNLIK--DKGV---NSFMVYM 168
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKLHVDVGF------WGGLVPGNLDQLRPldEAGVvgfKCFLCPS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 169 AYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNC 248
Cdd:cd01315 152 GVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 249 PLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI------DGthywsknwakAAAFVTSPPLSpDPTTPDYINSLLA 322
Cdd:cd01315 232 RLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFtaedvpDG----------GTEFKCAPPIR-DAANQEQLWEALE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 323 SGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIS 402
Cdd:cd01315 301 NGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIA 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947725 403 VGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNlHVTQGAGRFI 469
Cdd:cd01315 381 VGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
63-443 |
3.45e-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: 208.01 E-value: 3.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 63 KMVIPGGIDVHTHFQMPYKGmTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDIt 142
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGT-TYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 143 hWNDSVKQEVQNLIkDKGVNSFMVYMAYK--DLYQVSNTELYEIFTCLGELGAIAQVHAEngdiiaqeqtrmlemgitgp 220
Cdd:cd01302 79 -GPGDVTDELKKLF-DAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 221 eghvlsrpeeleaeavfRAITIASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDgTHYWSKNWAKaaa 300
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW--- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 301 FVTSPPLSPdPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDnFTAIPEGTNGVEERMSVIWdKAVATGKMDENQF 380
Cdd:cd01302 196 GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETL 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947725 381 VAVTSTNAAKIFNLYPrKGRISVGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAP 443
Cdd:cd01302 273 VEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
17-470 |
5.97e-54 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 189.52 E-value: 5.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 97 LAGGTTMIIDHVVPEPESSLT-EAYEKWREWADGKsccdyaLHVDITHWNDSVKQEVQNL--IKDKGVNSFMVYMAY--- 170
Cdd:TIGR03178 79 AAGGITTYIDMPLNSIPATTTrASLEAKFEAAKGK------LAVDVGFWGGLVPYNLDDLreLDEAGVVGFKAFLSPsgd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 171 KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPL 250
Cdd:TIGR03178 153 DEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 251 YVTKVMSKSAADLISQARKKGNVVFGEPItaslgidgTHYWSKNWAK----AAAFVTSPPLSPDPTTPDYINSLLAsGDL 326
Cdd:TIGR03178 233 HVVHLSSAEAVELITEAKQEGLDVTVETC--------PHYLTLTAEEvpdgGTLAKCAPPIRDLANQEGLWEALLN-GLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 327 QLSGSAHCTFSTAQKAigKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSD 406
Cdd:TIGR03178 304 DCVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKD 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947725 407 SDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGRFIP 470
Cdd:TIGR03178 381 ADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
17-460 |
2.78e-53 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 187.60 E-value: 2.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 97 LAGGTTMIIDHVVPEPESSLT-EAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQNLIK--DKGVNSFMVYMAYK-- 171
Cdd:PRK06189 82 AAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 172 DLYQVSNTE-LYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPL 250
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 251 YVTKVMSKSAADLISQARKKG-NV---------VFGEPITASLGIdgthywsknWAKAAafvtsPPLSPDPTTPDYINSL 320
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGvDVsvetcphylLFTEEDFERIGA---------VAKCA-----PPLRSRSQKEELWRGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 321 LAsGDLQLSGSAH--CTFSTAQKaigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRK 398
Cdd:PRK06189 302 LA-GEIDMISSDHspCPPELKEG----DDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQK 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622947725 399 GRISVGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 460
Cdd:PRK06189 376 GRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
17-470 |
7.46e-53 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 186.40 E-value: 7.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALhvdithwNDSVKQEVQNL--IKDKGVNSF-MVYMA--YK 171
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGI-------NGGVTGNWDPLesLWERGVFALgEIFMAdsTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 172 DLyQVSNTELYEIFTCLGELGAIAQVHAENGDIIAqEQTRMLEmGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLY 251
Cdd:PRK02382 155 GM-GIDEELFEEALAEAARLGVLATVHAEDEDLFD-ELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 252 VTKVMSKSAADLISqarkkgnvvfGEPITAslgiDGT-HYW---SKNWAKAAAFV-TSPPLSPDPTTPDYINSLlASGDL 326
Cdd:PRK02382 232 IAHISTPEGVDAAR----------REGITC----EVTpHHLflsRRDWERLGTFGkMNPPLRSEKRREALWERL-NDGTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 327 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSD 406
Cdd:PRK02382 297 DVVASDHAPHTREEKD---ADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYD 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947725 407 SDLVIWDPDAVKIISAKNHQSAAEYNIFEGMElrGA-PLVVICQGKIMLEDGNLHVTQGAGRFIP 470
Cdd:PRK02382 372 ADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
33-456 |
1.27e-47 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 171.47 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 33 ADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIIDHVVPEP 112
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMPNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 113 ESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQVSNteLYEIFTCLGELG 192
Cdd:TIGR00857 83 PIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGRMFTDDGSEVQDILS--MRRALEYAAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 193 AIAQVHAENGDIIAQEQTRMLEMgitGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKGN 272
Cdd:TIGR00857 161 VPIALHAEDPDLIYGGVMHEGPS---AAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 273 VVFGEPITASLGIDGTHYW-SKNWAKaaafvTSPPLSPdPTTPDYINSLLASGDLQLSGSAHCTFSTAQKaigKDNFTAI 351
Cdd:TIGR00857 238 KITAEVTPHHLLLSEEDVArLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHTLEEK---TKEFAAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 352 PEGTNGVEERMSVIWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSDSDLVIWDPDAVKIISAKNHQSAAEY 431
Cdd:TIGR00857 309 PPGIPGLETALPLLLQLLVK-GLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKN 386
|
410 420
....*....|....*....|....*
gi 1622947725 432 NIFEGMELRGAPLVVICQGKIMLED 456
Cdd:TIGR00857 387 TPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
62-450 |
1.09e-36 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 140.16 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 62 GKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIID--HVVPEPESSltEAYEKWREWADGKSCCDYALHV 139
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDmpNTKPPTTTA--EALYEKLRLAAAKSVVDYGLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 140 DIThwndsvKQEVQNLIKDKGVNSFMVYMA--YKDLYQVSNTeLYEIFtclGELGAIAQVHAENGDIIAQEQTRMLEMGI 217
Cdd:cd01318 77 GVT------GSEDLEELDKAPPAGYKIFMGdsTGDLLDDEET-LERIF---AEGSVLVTFHAEDEDRLRENRKELKGESA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 218 tgpegHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKGNV-------VFGEPITASLGidgthy 290
Cdd:cd01318 147 -----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLG------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 291 wskNWAKaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAV 370
Cdd:cd01318 216 ---TLGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLT-LV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 371 ATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQG 450
Cdd:cd01318 283 NKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
17-424 |
4.48e-35 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 137.29 E-value: 4.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 97 LAGGTTMIIDHVVPE-PESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEvqnlIKDKGVNSFMVYMAY----- 170
Cdd:PRK08044 81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHE----LDEVGVVGFKCFVATcgdrg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 171 --KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNC 248
Cdd:PRK08044 157 idNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 249 PLYVTKVMSKSAADLISQARKKGNVVFGEPITaslgidgtHYWSKNWAKAAAFVT----SPPLSPDPTTPDYINSLLaSG 324
Cdd:PRK08044 237 RLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEKLF-NG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 325 DLQLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVG 404
Cdd:PRK08044 308 EIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPG 383
|
410 420
....*....|....*....|
gi 1622947725 405 SDSDLVIWDPDAVKIISAKN 424
Cdd:PRK08044 384 KDADFVFIQPNSSYVLKNED 403
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
16-456 |
6.19e-35 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 136.48 E-value: 6.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 16 RLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTK 94
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 95 AALAGGTTMiidhVV------PEPESSLTEAYEKWRewADGKSCCDyaLHV--DIThwndsVKQEVQNL-----IKDKGV 161
Cdd:PRK09357 79 AAAAGGFTT----VVampntkPVIDTPEVVEYVLDR--AKEAGLVD--VLPvgAIT-----KGLAGEELtefgaLKEAGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 162 NSFMvymayKDLYQVSNTEL-YEIFTCLGELG-AIAQvHAE----NGDIIAQEQTRMLEMGITGpeghvlsRPEELEAEA 235
Cdd:PRK09357 146 VAFS-----DDGIPVQDARLmRRALEYAKALDlLIAQ-HCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 236 VFRAITIASQTNCPLYVTKVMSKSAADLISQARKKGnvvfgEPITA------------SLGIDGTHYwsknwaKAAafvt 303
Cdd:PRK09357 213 IARDVLLAEATGARVHICHVSTAGSVELIRWAKALG-----IKVTAevtphhllltdeDLLTYDPNY------KVN---- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 304 sPPLSpdptTPDYINSL---LASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQF 380
Cdd:PRK09357 278 -PPLR----TEEDREALiegLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQL 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947725 381 VAVTSTNAAKIFNLYPrkGRISVGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLED 456
Cdd:PRK09357 350 LEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
54-444 |
1.36e-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: 125.81 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 54 GVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTmiidHVVPEPESslteayekwREWADgkscc 133
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVID----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 134 dyalhvdithwNDSVKQEVQNLIKDKGVNSFMVYMAY-KDLYQVSNTELYEiftcLGELGAIA----------------- 195
Cdd:cd01317 61 -----------NPAVVELLKNRAKDVGIVRVLPIGALtKGLKGEELTEIGE----LLEAGAVGfsddgkpiqdaellrra 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 196 -----------QVHAENGDIIAQEQtrMLEMGITGPEGhVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLI 264
Cdd:cd01317 126 leyaamldlpiIVHPEDPSLAGGGV--MNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 265 SQARKKGnvvfgEPITASLGIdgtHYWS------KNWAkaAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFST 338
Cdd:cd01317 203 RKAKAKG-----LPVTAEVTP---HHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 339 AQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPrkGRISVGSDSDLVIWDPDAVK 418
Cdd:cd01317 272 EEKDLP---FAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEW 346
|
410 420
....*....|....*....|....*.
gi 1622947725 419 IISAKNHQSAAEYNIFEGMELRGAPL 444
Cdd:cd01317 347 IVDEETFRSKSKNTPFDGQKLKGRVL 372
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
14-459 |
3.77e-30 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 122.86 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 14 SDRLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQG 92
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 93 TKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIkdkGVNSFMVYMaYKD 172
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTANPTC---GIKIFMGSS-HGP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 173 LYQVSNTELYEIFTCLGELgaIAqVHAENgdiiaqeQTRMLE-----MGITGPEGHVLSRPEELEAEAVFRAITIASQTN 247
Cdd:PRK07575 156 LLVDEEAALERIFAEGTRL--IA-VHAED-------QARIRArraefAGISDPADHSQIQDEEAALLATRLALKLSKKYQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 248 CPLYVTKVMSKSAADLISQArkKGNVVFGEPITASLGIDGTHYwsknwAKAAAFV-TSPPLSpDPTTPDYINSLLASGDL 326
Cdd:PRK07575 226 RRLHILHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAY-----ERIGTLAqMNPPLR-SPEDNEALWQALRDGVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 327 QLSGSAHCTFSTAQKAIGKDNftaIPEGTNGVEERMSVIWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSD 406
Cdd:PRK07575 298 DFIATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYD 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1622947725 407 SDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNL 459
Cdd:PRK07575 373 ADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
22-457 |
4.66e-29 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 119.10 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 22 GRIVNDDQSFYADIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVIPGGIDVHTH---FQMPYKgmTTVDdffQGTKAALA 98
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHlrdFEESYK--ETIE---SGTKAALH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 99 GGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVdITHWNDSVKQEVQNLIKDKgvnsFMVyMAYKDLYQVSN 178
Cdd:PRK04250 77 GGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNF-LIAGNCEKAEEIKADFYKI----FMG-ASTGGIFSENF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 179 TELYEiftclgELGAIAQVHAENGDIIAQEqtrmlemgitgPEghvlsRPEELEAEAVFRAITIASQTNCPLYVTKVMSK 258
Cdd:PRK04250 151 EVDYA------CAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 259 SAADLISQARKkgnvvfgEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSpdpTTPDYINSLLASGDLQLSGSAHCTFST 338
Cdd:PRK04250 209 DGLKLILKSNL-------PWVSFEVTPHHLFLTRKDYERNPLLKVYPPLR---SEEDRKALWENFSKIPIIASDHAPHTL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 339 AQKAIGKdnfTAIPegtnGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNlYPRKGrISVGSDSDLVIWDPDAVK 418
Cdd:PRK04250 279 EDKEAGA---AGIP----GLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEW 348
|
410 420 430
....*....|....*....|....*....|....*....
gi 1622947725 419 IISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDG 457
Cdd:PRK04250 349 TIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
17-467 |
5.36e-29 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 119.64 E-value: 5.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMvYMAYKDLYQV 176
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELERLPGCAGIKVFM-GSSTGDLLVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 177 SNTELYEIftclgeLGAI---AQVHAEngdiiaqEQTRMLEMGITGPEGHVLSRPEELEAEAVFRA----ITIASQTNCP 249
Cdd:PRK09060 163 DDEGLRRI------LRNGrrrAAFHSE-------DEYRLRERKGLRVEGDPSSHPVWRDEEAALLAtrrlVRLARETGRR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 250 LYVTKVMSKSAADLISQARkkgNVVFGEPITASLGIDGTHYWSKNWAKAaafVTSPPLSpDPTTPDYINSLLASGDLQLS 329
Cdd:PRK09060 230 IHVLHVSTAEEIDFLADHK---DVATVEVTPHHLTLAAPECYERLGTLA---QMNPPIR-DARHRDGLWRGVRQGVVDVL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 330 GSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSDSDL 409
Cdd:PRK09060 303 GSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDADF 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947725 410 VIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGR 467
Cdd:PRK09060 378 TIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-469 |
1.14e-27 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 116.80 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 12 ITSDRLLIKGGRIVNDdqsfyadIYMEDGLIKQIGDNLIVPG---GVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDD 88
Cdd:PLN02795 48 LYSKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 89 FFQGTKAALAGGTTMIIDhvVP---EPESSLTEAYEKWREWADGKsccdyaLHVDITHWNDSVKQEVQNLIKDK------ 159
Cdd:PLN02795 119 FPTGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPENAHNASVLEelldag 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 160 --GVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQtrMLEMGITGPEGHVLSRPEELEAEAVF 237
Cdd:PLN02795 191 alGLKSFMCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 238 RAITIASQTN-------CPLYVTKVM-SKSAADLISQARKKGNVVFGEPITASLGI------DGthywsknwakAAAFVT 303
Cdd:PLN02795 269 QLLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFsaeeipDG----------DTRYKC 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 304 SPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGkMDENQFVAV 383
Cdd:PLN02795 339 APPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 384 TSTNAAKIFNLyPRKGRISVGSDSDLVIWDPDAVKIISA------KNHQSAAeyniFEGMELRGAPLVVICQGKIMLEDG 457
Cdd:PLN02795 417 WSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAEFVLDEsypiyhKHKSLSP----YLGTKLSGKVIATFVRGNLVFLEG 491
|
490
....*....|..
gi 1622947725 458 NlHVTQGAGRFI 469
Cdd:PLN02795 492 K-HAKQACGSPI 502
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
32-470 |
1.52e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 106.10 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 32 YADIYMEDGLIKQIGDNLivpGGVKTIEANGkMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIIDHVVPE 111
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 112 PESSLTEAYEKWREWADGKSCCDYALHVDITHWNdsvkqevqNLIKDKGVNSFMVYMAYKDLYQVSNTELYEIfTCLGEL 191
Cdd:PRK01211 89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNN--------ALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 192 GAIAQVHAENGDIIAQEQTRMLEMgitgpEGHVLSRPEELEAEAVFRAITIASQtncplyvTKVMS-KSAADLISQarkk 270
Cdd:PRK01211 160 NIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIAhVSSIDVIGR---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 271 gnvvFGEPITASlgidgtHYWSKNWAKAAAF-VTSPPLSPDPTTPDYINSLLaSGDLQLSGSAHCTFSTAQKAigkdNFT 349
Cdd:PRK01211 224 ----FLREVTPH------HLLLNDDMPLGSYgKVNPPLRDRWTQERLLEEYI-SGRFDILSSDHAPHTEEDKQ----EFE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 350 AIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRISVGSDSDLVIWDPDAVKIISAKNHQSAA 429
Cdd:PRK01211 289 YAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKC 365
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1622947725 430 EYNIFEGMELRgAPLVVICQGKIMLEDGNLhVTQGAGRFIP 470
Cdd:PRK01211 366 PVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVP 404
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-453 |
3.25e-22 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 97.96 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 64 MVIPGGIDVHTHFQM------PYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLT--EAYEKWRE--WADGKSCC 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgiPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEAllEAAEELPLglRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 134 ---DYALHVDITHWNDSVKQEvqNLIKDKGVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIiaqEQT 210
Cdd:pfam01979 81 ldtDGELEGRKALREKLKAGA--EFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKG---EVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 211 RMLEMGITGPEghVLSRPEELEAEAVFRAITIASQTNCPLYVTkvmskSAADLISQARKKGNVvfgepitasLGIDGTHY 290
Cdd:pfam01979 156 DAIAAFGGGIE--HGTHLEVAESGGLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 291 WSKNWAKAAAfvtspplspdpttpdyinsLLASGDLQLSGSAHCtfstaqkaIGKDNFTAIPEGTNGVEERmsviwdkAV 370
Cdd:pfam01979 220 LRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ-------FD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 371 ATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDavkiisaknhqsaaEYNIFEGMELRGAPLVVICQG 450
Cdd:pfam01979 266 PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKG 331
|
...
gi 1622947725 451 KIM 453
Cdd:pfam01979 332 KIV 334
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
15-460 |
1.69e-20 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 94.17 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 15 DRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTK 94
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 95 AALAGGTTMIID--HVVPepeSSLT-EAYEKWREWADGKSCCDYALHVDIThwNDSVkQEVQNLIKDK--GVNSFM---- 165
Cdd:PRK09236 80 AAVAGGITSFMEmpNTNP---PTTTlEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRLDPKRvcGVKVFMgast 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 166 ----VymaykDLYQVsnteLYEIFTCLGELgaIAqVHAENGDIIAQEQTRMLEM---GITgPEGHVLSRpeelEAEAVFR 238
Cdd:PRK09236 154 gnmlV-----DNPET----LERIFRDAPTL--IA-THCEDTPTIKANLAKYKEKygdDIP-AEMHPLIR----SAEACYK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 239 ----AITIASQTNCPLYVTKVMSKSAADLISQ---ARKKgnvvfgepITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDP 311
Cdd:PRK09236 217 ssslAVSLAKKHGTRLHVLHISTAKELSLFENgplAEKR--------ITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 312 TTPDYINSLLASGDLQLSGSAHCTFSTAQKaigKDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKI 391
Cdd:PRK09236 289 SDREALRQALADDRIDVIATDHAPHTWEEK---QGPYFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAIL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947725 392 FNLyPRKGRISVGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 460
Cdd:PRK09236 365 FDI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
13-428 |
2.02e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 71.92 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 13 TSDRLLIKGGRIVNDDQSFY---ADIYMEDGLIKQIGDN--LIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMT--- 84
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVefe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 85 -------TVDDFFQGTK---AALAGGTTMIIDH------VVPEPESSLTEAYEKWREWADGKS-CCDYALHvdiTHWNDS 147
Cdd:COG1228 86 agggitpTVDLVNPADKrlrRALAAGVTTVRDLpggplgLRDAIIAGESKLLPGPRVLAAGPAlSLTGGAH---ARGPEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 148 VKQEVQNLIKDkGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAqeqtRMLEMGITGPEgHVLSR 227
Cdd:COG1228 163 ARAALRELLAE-GADYIKVFAEGGA-PDFSLEELRAILEAAHALGLPVAAHAHQADDIR----LAVEAGVDSIE-HGTYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 228 PEEleaeavfraitiasqtncplyvtkvmsksAADLIsqaRKKGNVVfgepitaslgidgthywsknwakaaafvtsppL 307
Cdd:COG1228 236 DDE-----------------------------VADLL---AEAGTVV--------------------------------L 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 308 SPDPTTPDYINSLLASGDLQLSGSAHC-TFSTAQK--------AIGKDNFTAIPEGTNGVEErmsvIWdKAVATGkMDEN 378
Cdd:COG1228 252 VPTLSLFLALLEGAAAPVAAKARKVREaALANARRlhdagvpvALGTDAGVGVPPGRSLHRE----LA-LAVEAG-LTPE 325
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1622947725 379 Q-FVAVTStNAAKIFNLYPRKGRISVGSDSDLVIWDPDAVKIISAKNHQSA 428
Cdd:COG1228 326 EaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAYLEDVRA 375
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
17-122 |
4.96e-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: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPG--GVKTIEANGKMVIPGGIDVHTHFQM------------- 78
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947725 79 --------PYKGMTTVDDFFQGTKAALA----GGTTMIIDHVVPEPEsSLTEAYEK 122
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPD-AVAEAAEE 135
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
34-468 |
2.36e-12 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 68.63 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 34 DIYMEDGlIKQIGDNLIVpgGVKTIEANGK---------MVIPGGIDVHTHF---QMPYKgmttvDDFFQGTKAALAGGT 101
Cdd:PRK00369 8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHLrglKLSYK-----EDVASGTSEAAYGGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 102 TMIIDHVVPEPESSLTEAY-EKWREWADGkSCCDYALHVDIThwnDSVKqEVQNLikdkGVNSFMVYMayKDLyqvsntE 180
Cdd:PRK00369 80 TLVADMPNTIPPLNTPEAItEKLAELEYY-SRVDYFVYSGVT---KDPE-KVDKL----PIAGYKIFP--EDL------E 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 181 LYEIFTCLGELGAIAQVHAEngdiiaqeqtrmLEMGITGPEGhvLSRPEELEAEAVFRAITIASqtncpLYVTKVmskSA 260
Cdd:PRK00369 143 REETFRVLLKSRKLKILHPE------------VPLALKSNRK--LRRNCWYEIAALYYVKDYQN-----VHITHA---SN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 261 ADLISQARKKGnvvFGEPITAS-LGIDG-THYWSKnwakaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGsaHCTFST 338
Cdd:PRK00369 201 PRTVRLAKELG---FTVDITPHhLLVNGeKDCLTK---------VNPPIR-DINERLWLLQALSEVDAIASD--HAPHSS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 339 AQKaigKDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRISVGSDSDLViwdpdavk 418
Cdd:PRK00369 266 FEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFT-------- 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622947725 419 IISAKNHQ-----SAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRF 468
Cdd:PRK00369 332 VIQFEDWRystkySKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
66-466 |
4.97e-12 |
|
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: 67.48 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 66 IPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIidHVVPEPESSL--TEAYEKWREWADGKSCCDYALHVDITH 143
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIvdVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 144 WNDSVKQEVqnliKDKGVNSFMVymaykdlyqvsnteLYEIFTCLgELGAIAQVhaengdiiaqeqTRMLEmgiTGPEgh 223
Cdd:cd01316 81 TNAATVGEL----ASEAVGLKFY--------------LNETFSTL-ILDKITAW------------ASHFN---AWPS-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 224 vlSRPEELEAEAVFRA--ITIASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI---DGTHYWSknwaka 298
Cdd:cd01316 125 --TKPIVTHAKSQTLAavLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLsqdDLPRGQY------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 299 aafvtspPLSPDPTTPDYINSL---LASGDLQLSGSAHCTFstAQKAIGKdnftaIPEGTNGVEERMSVIWdKAVATGKM 375
Cdd:cd01316 197 -------EVRPFLPTREDQEALwenLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 376 DENQFVAVTSTNAAKIFNLYPRkgrisvgSDSDLVIwDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLE 455
Cdd:cd01316 262 TIEDIVDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFI 333
|
410
....*....|.
gi 1622947725 456 DGNLHVTQGAG 466
Cdd:cd01316 334 DGEIVAPPGFG 344
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
17-467 |
2.08e-10 |
|
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: 62.70 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVndDQS----FYADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHfqmpYKGMTTVDDFFqg 92
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 93 TKAALAGGTTMIIDH-------VVPEPESSLTEAYEKWREWADGK-----SCCDYALHVD-----------ITHWNDSVK 149
Cdd:cd01297 73 RPSSRQGVTTVVLGNcgvspapANPDDLARLIMLMEGLVALGEGLpwgwaTFAEYLDALEarppavnvaalVGHAALRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 150 --------------QEVQNLIkDKGVNS----FMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENgdiiaQEQTR 211
Cdd:cd01297 153 vmgldareateeelAKMRELL-REALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRY-----EGDSI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 212 MlemgitgpeghvlsrpeeleaEAVFRAITIASQTNCPLYVT--KVMSKS-------AADLISQARKKGNVVFGE--PIT 280
Cdd:cd01297 227 L---------------------EALDELLRLGRETGRPVHIShlKSAGAPnwgkidrLLALIEAARAEGLQVTADvyPYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 281 ASLGidgthywsknwAKAAAFVTSPPlspdpttpdyinsLLASGDLQLSGSAH----CTFStaqKAIGKdnftaipegtn 356
Cdd:cd01297 286 AGSE-----------DDVRRIMAHPV-------------VMGGSDGGALGKPHprsyGDFT---RVLGH----------- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 357 GVEERMSVIWDKAVAtgKMdenqfvavtSTNAAKIFNLYPRkGRISVGSDSDLVIWDPDAVKI---ISAKNHQSaaeyni 433
Cdd:cd01297 328 YVRERKLLSLEEAVR--KM---------TGLPARVFGLADR-GRIAPGYRADIVVFDPDTLADratFTRPNQPA------ 389
|
490 500 510
....*....|....*....|....*....|....
gi 1622947725 434 fEGMELrgaplvVICQGKIMLEDGnLHVTQGAGR 467
Cdd:cd01297 390 -EGIEA------VLVNGVPVVRDG-AFTGARPGR 415
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
35-455 |
1.48e-09 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 60.10 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 35 IYMEDGLIKQIGDNLivpGGVKTIEANGKMVIPGGIDVhthfqmpykGMTTVDDFFQGT------KAALAGGttmiIDHV 108
Cdd:PRK08417 1 IRIKDGKITEIGSDL---KGEEILDAKGKTLLPALVDL---------NVSLKNDSLSSKnlksleNECLKGG----VGSI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 109 VPEPESSlteayekwrewadgKSCCD-YALHVDithwndsvkqevQNLIKDKGVNSFMVYMAYKDlyqvsNTELYEIFTc 187
Cdd:PRK08417 65 VLYPDST--------------PAIDNeIALELI------------NSAQRELPMQIFPSIRALDE-----DGKLSNIAT- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 188 LGELGAIAqVHAE---NGDIIAQ--EQTRMLEM-------------------GITGPEGHVLSRPEELEAEAVFRAITIA 243
Cdd:PRK08417 113 LLKKGAKA-LELSsdlDANLLKViaQYAKMLDVpifcrcedssfddsgvmndGELSFELGLPGIPSIAETKEVAKMKELA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 244 SQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHywSKNWAKAAAFvtSPPLSpDPTTPDYINSLLAS 323
Cdd:PRK08417 192 KFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSA--CENFNTAAKL--NPPLR-SKEDRLALLEALKE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 324 GDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRISV 403
Cdd:PRK08417 267 GKIDFLTSLHSAKSNSKKDLA---FDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEV 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622947725 404 GSDSDLVIWDPDAVKIISAKnhqsaaeYNIFEGMELRGAPLVVICQGKIMLE 455
Cdd:PRK08417 342 GKEADLVLFDPNESTIIDDN-------FSLYSGDELYGKIEAVIIKGKLYLE 386
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-122 |
2.82e-09 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 59.45 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 16 RLLIKGGRIV--NDDQSFYAD--IYMEDGLIKQIGDNLIVP---GGVKTIEANGKMVIPGGIDVHTH-FQMPYKGMT--- 84
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLAddl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947725 85 -----------------TVDDFFQGTKAA----LAGGTTMIIDH--VVPEPESSLTEAYEK 122
Cdd:COG0402 81 plldwleeyiwplearlDPEDVYAGALLAlaemLRSGTTTVADFyyVHPESADALAEAAAE 141
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
17-75 |
4.35e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 58.71 E-value: 4.35e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947725 17 LLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
16-467 |
1.97e-08 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 57.01 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 16 RLLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVIPGGIDVHTHFQMP-------YKGMTTV 86
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAHGQSVaayrmqaFDGVTTA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 87 DDFFQGT--------KAALAG-----GTTM------IIDHVVPEPESSLtEAYEKW---REWADGKSccdyalhvdithw 144
Cdd:PRK09061 98 LELEAGVlpvarwyaEQAGEGrplnyGASVgwtparIAVLTGPQAEGTI-ADFGKAlgdPRWQERAA------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 145 NDSVKQEVQNLIK---DKGVNSFMVYMAYkdLYQVSNTELYEIFTCLGELGAIAQVHAEngdiiaqeqtrmlEMGITGPE 221
Cdd:PRK09061 164 TPAELAEILELLEqglDEGALGIGIGAGY--APGTGHKEYLELARLAARAGVPTYTHVR-------------YLSNVDPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 222 GHVlsrpeeleaEAVFRAITIASQTNCPLYVTKVMSKS------AADLISQARKKGNVVFGE--P-ITASLGID------ 286
Cdd:PRK09061 229 SSV---------DAYQELIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVTTEayPyGAGSTVVGaaffdp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 287 ------GTHYWSKNW----------AKAAAFVTSPPLSP---------DPTTPDYINSLLASGDLQLSGSAHCTFSTAQK 341
Cdd:PRK09061 300 gwlermGLGYGSLQWvetgerlltrEELAKLRANDPGGLvlihfldedNPRDRALLDRSVLFPGAAIASDAMPWTWSDGT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 342 AIGKDNFTAIPEG-----TNG---------VEERMSVIWDKAVAtgKMdenqfvavtSTNAAKIFN----LYPRKGRISV 403
Cdd:PRK09061 380 VYEGDAWPLPEDAvshprSAGtfarflreyVRERKALSLLEAIR--KC---------TLMPAQILEdsvpAMRRKGRLQA 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947725 404 GSDSDLVIWDPDavKIISAKNHQSAAEYNifEGMELrgaplvVICQGKIMLEDGNLHVTQGAGR 467
Cdd:PRK09061 449 GADADIVVFDPE--TITDRATFEDPNRPS--EGVRH------VLVNGVPVVSNGELVRDARPGR 502
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
16-220 |
2.19e-08 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 56.55 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 16 RLLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHF-QMPYKGMTtvDDF-- 89
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQTLFRGIA--DDLel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 90 ----------FQGTKAA--------------LAGGTTMIIDHV-VPEPESSLTEAYEKWREWADGKSCCDYALHVDIT-- 142
Cdd:PRK07228 80 ldwlkdriwpLEAAHDAesmyysallgigelIESGTTTIVDMEsVHHTDSAFEAAGESGIRAVLGKVMMDYGDDVPEGlq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 143 -HWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQVSNTElyeifTCLGELGAIAQ-------VHA-ENGDIIA--QEQTR 211
Cdd:PRK07228 160 eDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTE-----ELLRGVRDLADeygvrihTHAsENRGEIEtvEEETG 234
|
250
....*....|....*
gi 1622947725 212 ML------EMGITGP 220
Cdd:PRK07228 235 MRnihyldEVGLTGE 249
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-75 |
3.36e-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: 55.66 E-value: 3.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947725 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
70-276 |
1.11e-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: 53.49 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 70 IDVHTHFQMP----------------YKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCC 133
Cdd:cd01292 2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 134 DYALHVDITH----WNDSVKQEVQNLIKD---KGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDIIA 206
Cdd:cd01292 82 RVVLGLGIPGvpaaVDEDAEALLLELLRRgleLGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947725 207 QEQTRMLEMGITGPE---GHVLSRPEELEAEAVFRAITIASqTNCPLYVTKVMSKSAADLISQARKKGNVVFG 276
Cdd:cd01292 161 RALEDLVALLRLGGRvviGHVSHLDPELLELLKEAGVSLEV-CPLSNYLLGRDGEGAEALRRLLELGIRVTLG 232
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
17-75 |
1.12e-07 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 54.43 E-value: 1.12e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947725 17 LLIKGGRI------VNDDQsfyADIYMEDGlikQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
18-75 |
1.58e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 53.56 E-value: 1.58e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947725 18 LIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNliVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-106 |
2.21e-07 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 53.57 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVN--DDQSFYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVIPGGIDVHTHFQmpyKGMTTVDDFfqgTK 94
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHIE---SSMVTPAEF---AR 78
|
90
....*....|...
gi 1622947725 95 AALAGGTT-MIID 106
Cdd:COG1001 79 AVLPHGTTtVIAD 91
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-413 |
2.99e-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: 52.72 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 34 DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFqmpYKGMTTVDDffQGTKAALAGGTTMIIDhvvpepe 113
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHV---YQGGTRYGD--RPDMIGVKSGVTTVVD------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 114 sslteayekwrewADGKSCcdyalhvdithwnDSVKQEVQNLIKDKGVNsfmVYmAYKDLY---QVSNTELYEIFTClgE 190
Cdd:cd01307 69 -------------AGSAGA-------------DNIDGFRYTVIERSATR---VY-AFLNISrvgLVAQDELPDPDNI--D 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 191 LGAIAQVHAENGDIIAQEQTRMlEMGITGPEGhvlSRPEELEAEavfraitIASQTNCPLYvtkVMSKSAADLISQA--- 267
Cdd:cd01307 117 EDAVVAAAREYPDVIVGLKARA-SKSVVGEWG---IKPLELAKK-------IAKEADLPLM---VHIGSPPPILDEVvpl 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 268 RKKGNVVfgepitaslgidgTHYWSknwAKAAAFVTspplsPDPTTPDYINSLLASG---DLQlSGSAHCTFSTAQKAIG 344
Cdd:cd01307 183 LRRGDVL-------------THCFN---GKPNGIVD-----EEGEVLPLVRRARERGvifDVG-HGTASFSFRVARAAIA 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947725 345 KD-NFTAI------PEGTNGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKGRISVGSDSDLVIWD 413
Cdd:cd01307 241 AGlLPDTIssdihgRNRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFD 314
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
16-456 |
6.78e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 51.99 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 16 RLLIKGGRIVN-----DDQsfyADIYMEDGLIKQIGDnliVPGGV---KTIEANGKMVIPGGIDVHTHFQMP-YKGMTTV 86
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREPgYEYKATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 87 DDFFQgtkAALAGGTTMII-----DHVVPEPEssLTEAYeKWREWADGKSccdyalHV-DITHWNDSVKQEVQnlikdkg 160
Cdd:PRK07627 76 ESEMA---AAVAGGVTSLVcppdtDPVLDEPG--LVEML-KFRARNLNQA------HVyPLGALTVGLKGEVL------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 161 vnsfmvymaykdlyqvsnTELYEiftcLGELGAIAQVHAENGDIIAQEQTRMLEMGIT-------------------GPE 221
Cdd:PRK07627 137 ------------------TEMVE----LTEAGCVGFSQANVPVVDTQVLLRALQYASTfgftvwlrpldaflgrggvAAS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 222 GHVLSR------PEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKgnvvfGEPITASLGIDGTH------ 289
Cdd:PRK07627 195 GAVASRlglsgvPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAE-----GLPVTCDVGVNHVHlidvdi 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 290 -YWSKNwakaaaFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIgkdNFTAIPEGTNGVEERMSVIWDK 368
Cdd:PRK07627 270 gYFDSQ------FRLDPPLR-SQRDREAIRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPLTLKW 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 369 AVATgKMDENQFVAVTSTNAAKIFNLypRKGRISVGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVIC 448
Cdd:PRK07627 340 ADEA-KVPLARALARITSAPARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLV 416
|
....*...
gi 1622947725 449 QGKIMLED 456
Cdd:PRK07627 417 AGQVAFER 424
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-128 |
8.43e-07 |
|
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: 51.48 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 12 ITSDRLLIKGGRIVnddqsfyaDIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH------FQMP------ 79
Cdd:cd01293 2 LRNARLADGGTALV--------DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHldktftGGRWpnnsgg 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 80 -----------YKGMTTVDDFFQ----GTKAALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 128
Cdd:cd01293 74 tlleaiiaweeRKLLLTAEDVKEraerALELAIAHGTTAIRTHVDVDPAAGLKaleallELREEWADLID 143
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
15-113 |
9.04e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 51.54 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 15 DRLLIKGGRIVNDDQSF----YADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVIPGGIDVHTH--------------- 75
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHRHtwqsvlrgigadwtl 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622947725 76 ---FQMPYKGMTTV---DDFFQGTKA----ALAGGTTMIID--HVVPEPE 113
Cdd:PRK08204 81 qtyFREIHGNLGPMfrpEDVYIANLLgaleALDAGVTTLLDwsHINNSPE 130
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
33-105 |
4.10e-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 [Multi-domain] Cd Length: 567 Bit Score: 49.63 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 33 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 100
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151
|
....*
gi 1622947725 101 TTMII 105
Cdd:cd00375 152 ITTMI 156
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
33-104 |
1.07e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 48.16 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 33 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 100
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155
|
....*
gi 1622947725 101 -TTMI 104
Cdd:PRK13308 156 iTTML 160
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
17-76 |
1.18e-05 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 48.26 E-value: 1.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947725 17 LLIKGGRI--VNDDQSFYADIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVIPGGIDVHTHF 76
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-74 |
1.29e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 47.48 E-value: 1.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947725 16 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvkTIEANGKMVIPGGIDVHT 74
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
17-78 |
1.32e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 47.87 E-value: 1.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947725 17 LLIKGGRIVNDD--QSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQM 78
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
381-415 |
1.40e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.40 E-value: 1.40e-05
10 20 30
....*....|....*....|....*....|....*
gi 1622947725 381 VAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPD 415
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
381-436 |
1.46e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.53 E-value: 1.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947725 381 VAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEG 436
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
17-93 |
1.89e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 47.19 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVIPGGIDVHTHFQMP-YKGM---TTVDDF 89
Cdd:PRK06380 3 ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTaSKGLfddVDLEEF 80
|
....
gi 1622947725 90 FQGT 93
Cdd:PRK06380 81 LMKT 84
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
19-75 |
2.09e-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 [Multi-domain] Cd Length: 541 Bit Score: 47.41 E-value: 2.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 19 IKGGRIVNDDQSFYA---DIYMEDGlikQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
33-441 |
5.36e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 45.75 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 33 ADIYMEDGLIKQIGDNLI-VPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMI------- 104
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVailpdtf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 105 --IDHvvPEPESSL-----TEAYEKWREWADgksccdyalhvdITHwNDSVKQ--EVQNLIKdKGVNSFMVYMAYKDLYQ 175
Cdd:PRK07369 100 ppLDN--PATLARLqqqaqQIPPVQLHFWGA------------LTL-GGQGKQltELAELAA-AGVVGFTDGQPLENLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 176 VSNTELYeiftcLGELGAIAQVHAEN----GDIIAQEQTRMLEMGITGpeghvlsRPEELEAEAVFRAITIASQTNCPLY 251
Cdd:PRK07369 164 LRRLLEY-----LKPLGKPVALWPCDrslaGNGVMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGTPVH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 252 VTKVMSKSAADLISQARKKGnvvfgEPITASlgidgTHYWSKNWAKAAAFVTSPPLSPDPT--TPDYINSLLA---SGDL 326
Cdd:PRK07369 232 LMRISTARSVELIAQAKARG-----LPITAS-----TTWMHLLLDTEALASYDPNLRLDPPlgNPSDRQALIEgvrTGVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 327 QLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRkgRISVGSD 406
Cdd:PRK07369 302 DAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SLAPGQP 376
|
410 420 430
....*....|....*....|....*....|....*
gi 1622947725 407 SDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRG 441
Cdd:PRK07369 377 AELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKG 411
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
17-76 |
1.00e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 44.93 E-value: 1.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947725 17 LLIKGGRIV-NDDQSFY---ADIYMEDGLIKQIGDNlivpGGVKT-------IEANGKMVIPGGIDVHTHF 76
Cdd:PRK07203 2 LLIGNGTAItRDPAKPViedGAIAIEGNVIVEIGTT----DELKAkypdaefIDAKGKLIMPGLINSHNHI 68
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
33-105 |
1.11e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 45.09 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 33 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 100
Cdd:PRK13206 89 ADVGIRDGRIVAIGkagnpdimdgvhPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICP-----------QIVDEALAAG 157
|
....*
gi 1622947725 101 TTMII 105
Cdd:PRK13206 158 ITTLI 162
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
5-101 |
1.55e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 44.50 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 5 GKKNIPRITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDV 72
Cdd:PRK13985 55 SQSNNPSKEELDLIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLSVGPATEALAGEGLIVTAGGIDT 134
|
90 100
....*....|....*....|....*....
gi 1622947725 73 HTHFQMPYKGMTTvddFFQGTKAALAGGT 101
Cdd:PRK13985 135 HIHFISPQQIPTA---FASGVTTMIGGGT 160
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
17-455 |
1.74e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 44.26 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 17 LLIKGGRIVNDDQSF--YADIYMEDGLIKQIGD---NLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQ 91
Cdd:PRK09059 5 ILLANARIIDPSRGLdeIGTVLIEDGVIVAAGKgagNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 92 GTKAALAGGTTMIIdhVVPEPESSLTeayekwrewadgksccDYALhVDIthwndsvkqeVQNLIKDKG-VNSFMVYMAY 170
Cdd:PRK09059 83 ASRAAAAGGVTSII--MMPDTDPVID----------------DVAL-VEF----------VKRTARDTAiVNIHPAAAIT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 171 KDLYQVSNTElyeiFTCLGELGAIA-----------QV------HAENGDIIAQEQTRMLEMGITG--PEGHVLSR---- 227
Cdd:PRK09059 134 KGLAGEEMTE----FGLLRAAGAVAftdgrrsvantQVmrraltYARDFDAVIVHETRDPDLGGNGvmNEGLFASWlgls 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 228 --PEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKgnvvfGEPITASLGIdgtHYWSKNWAKAAAFVTSP 305
Cdd:PRK09059 210 giPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDR-----GLKVTAGVSI---NHLSLNENDIGEYRTFF 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 306 PLSPDPTTPDYINSL---LASGDLQLSGSAHCTFSTAQKAIgkdNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVA 382
Cdd:PRK09059 282 KLSPPLRTEDDRVAMveaVASGTIDIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLYHNGEVPLLRLIE 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947725 383 VTSTNAAKIFNLypRKGRISVGSDSDLVIWDPDAVKIISAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLE 455
Cdd:PRK09059 358 ALSTRPAEIFGL--PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
33-104 |
1.75e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 44.40 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 33 ADIYMEDGLIKQIG--------DNLIVPGGVKT--IEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG-T 101
Cdd:PRK13207 85 ADIGIKDGRIVAIGkagnpdiqDGVDIIIGPGTevIAGEGLIVTAGGIDTHIHFICP-----------QQIEEALASGvT 153
|
...
gi 1622947725 102 TMI 104
Cdd:PRK13207 154 TMI 156
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-76 |
2.22e-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: 2.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622947725 35 IYMEDGLIKQIGD----NLIVPGGVKTIEANGKMVIPGGIDVHTHF 76
Cdd:cd01296 1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-75 |
3.02e-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: 43.07 E-value: 3.02e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1622947725 39 DGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
33-128 |
3.41e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 43.00 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 33 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGM--------TTVDDFFQGTK---------- 94
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDpwypnepgPSLRERIANERrrraasghpa 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1622947725 95 ---------AALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 128
Cdd:PRK05985 97 aeralalarAAAAAGTTAMRSHVDVDPDAGLRhleavlAARETLRGLID 145
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
383-462 |
7.49e-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 [Multi-domain] Cd Length: 387 Bit Score: 41.99 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947725 383 VTSTNAAKIFNLYPrKGRISVGSDSDLVIWDPDavkiisaknhqsaaeYNIFEgmelrgaplvVICQGKIMLEDGNLHVT 462
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD---------------LDINS----------VIAKGQIMVRNGKLLVK 383
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
368-415 |
1.96e-03 |
|
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: 40.76 E-value: 1.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622947725 368 KAVATGKMDENQFVAVTStNAAKIFNLYPRKGRISVGSDSDLVIWDPD 415
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWNGD 340
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
33-75 |
2.00e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 40.74 E-value: 2.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622947725 33 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:PRK07583 41 VDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTH 83
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
16-76 |
3.38e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 40.22 E-value: 3.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947725 16 RLLIKGGRIV---NDDQSFYAD--IYMEDGLIKQIGDNLIVPG-GVKTIEANGKMVIPGGIDVHTHF 76
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHF 68
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
34-76 |
5.63e-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 phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 39.60 E-value: 5.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622947725 34 DIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVIPGGIDVHTHF 76
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
17-89 |
9.13e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 38.58 E-value: 9.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947725 17 LLIKGGRIVNDDQSFY--ADIYMEDGLIKQIGDNliVPGGVKT-IEANGKMVIPGGIDVHTHFQMP-YKGMTtvDDF 89
Cdd:PRK06038 4 IIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDADTvIDAKGSVVMPGLVNTHTHAAMTlFRGYA--DDL 76
|
|
| |
