|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
257-706 |
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: 757.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 257 ILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPFMGTVAIDDFYQGTKAA 336
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 337 LAGGTTMIIDHCLPQKGEPLLEAYEKWRGWADPKVCCDYSLHVGVTWWGDGVAEDIATLCqEKGVNSFKMFMAYKGVFML 416
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 417 SDDELYKSFSIIKENGALALMHAENGDIIDENTKKMQSLGITGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYIVHVM 496
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 497 SRSAADAIRKARSEGKVVFGEPIAASLGTDGSHYFcKDWRHAAAHVMGPPLRPDpTTPGYLMDLLANGDLQLTGTDNCTF 576
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 577 SSDQKALGKDDFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMYPRKGVIQVGADADIVIWDPEA 656
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1229162187 657 TRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELHVTQGAG 706
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
256-713 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 678.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 256 RILIKGGKVVNADHSFHADVYIEDGTIRQVGKDlitpGGAKVLDAKGKLIIPGGIDTHTHMQMPFMGTVAIDDFYQGTKA 335
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 336 ALAGGTTMIIDHCLPQKGEPLLEAYEKWRGWADPKVCCDYSLHVGVTWWGDGVAEDIATLCQEkGVNSFKMFMAYKGVFM 415
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 416 LSDDELYKSFSIIKENGALALMHAENGDIIDENTKKMQSLGITGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYIVHV 495
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 496 MSRSAADAIRKARSEGKVVFGEPIAASLGTDGSHYFCKDWRHAAAHVMGPPLRP----DPTTPGylmdlLANGDLQLTGT 571
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRDkehqDALWRG-----LQDGDLQVVAT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 572 DNCTFS-SDQKALGKDDFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMYPRKGVIQVGADADIV 650
Cdd:PRK08323 312 DHCPFCfEQKKQLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229162187 651 IWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELHVTQGAGRFIPRPL 713
Cdd:PRK08323 392 IWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKP 454
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
257-711 |
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: 654.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 257 ILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPFMGTVAIDDFYQGTKAA 336
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 337 LAGGTTMIIDHCLPQKGEPLLEAYEKWRGWADPKVCCDYSLHVGVTWWGDGVAEDIATLCQEKGVNSFKMFMAYKGVFML 416
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 417 SDDELYKSFSIIKENGALALMHAENGDIIDENTKKMQSLGITGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYIVHVM 496
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 497 SRSAADAIRKARSEGKVVFGEPIAASLGTDGSHYFcKDWRHAAAHVMGPPLRpDPTTPGYLMDLLANGDLQLTGTDNCTF 576
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 577 SSDQK-ALGKDDFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMYPRKGVIQVGADADIVIWDPE 655
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1229162187 656 ATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELHVTQGAGRFIPR 711
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
256-712 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 619.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 256 RILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPFMGTVAIDDFYQGTKA 335
Cdd:PLN02942 6 KILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 336 ALAGGTTMIIDHCLPQKGEpLLEAYEKWRGWADpKVCCDYSLHVGVTWWGDGVAEDIATLCQEKGVNSFKMFMAYKGVFM 415
Cdd:PLN02942 86 ALAGGTTMHIDFVIPVNGN-LLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGSLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 416 LSDDELYKSFSIIKENGALALMHAENGDIIDENTKKMQSLGITGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYIVHV 495
Cdd:PLN02942 164 VTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVVHV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 496 MSRSAADAIRKARSEGKVVFGEPIAASLGTDGSHYFCKDWRHAAAHVMGPPLRPdPTTPGYLMDLLANGDLQLTGTDNCT 575
Cdd:PLN02942 244 MSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDHCP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 576 FSSDQKALGKDDFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMYPRKGVIQVGADADIVIWDPE 655
Cdd:PLN02942 323 FNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILNPN 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1229162187 656 ATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELHVTQGAGRFIPRP 712
Cdd:PLN02942 403 STFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMP 459
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
258-711 |
7.48e-145 |
|
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: 433.36 E-value: 7.48e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 258 LIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPFMgtVAIDDFYQGTKAAL 337
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 338 AGGTTMIIDHCLPQKGEPLLEAYEKWRGWADPKVCCDYSLHVGVTWWGDGVAEDIATLcQEKGVNSFKMFMAYK-GVFML 416
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGAL-AEAGAVAFKVFMGSDdGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 417 SDDELYKSFSIIKENGALALMHAENGDIIDENTKKMqslGITGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYIVHVM 496
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNE---GKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 497 SRSAADAIRKARSEGKVVFGE--PiaaslgtdgsHYFC---KDW-RHAAAHVMGPPLRP--DPTTpgyLMDLLANGDLQL 568
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcP----------HHLTltdEDLeRYGTNFKVNPPLRTeeDREA---LWEGLADGTIDV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 569 TGTDNCTFSSDQKAlgkDDFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMyPRKGVIQVGADAD 648
Cdd:COG0044 302 IATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADAD 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229162187 649 IVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELhVTQGAGRFIPR 711
Cdd:COG0044 378 LVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
259-711 |
1.41e-128 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 392.91 E-value: 1.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 259 IKGGKVVNADHSFHADVYIEDGTIRQVGKDLitPGGAKVLDAKGKLIIPGGIDTHTHMQMPF-MGTVAIDDFYQGTKAAL 337
Cdd:PRK13404 8 IRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVSAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 338 AGGTTMIIDHCLPQKGEPLLEAYEKWRGWADPKVCCDYSLHVGVTWWGDGV-AEDIATLCqEKGVNSFKMFMAYKGVfML 416
Cdd:PRK13404 86 FGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALI-AQGYTSFKVFMTYDDL-KL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 417 SDDELYKSFSIIKENGALALMHAENGDIIDENTKKMQSLGITGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYIVHVM 496
Cdd:PRK13404 164 DDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 497 SRSAADAIRKARSEGKVVFGEP-------IAASLGTDGSHyfckdwrhAAAHVMGPPLRpDPTTPGYLMDLLANGDLQLT 569
Cdd:PRK13404 244 GREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFEVF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 570 GTDNCTF---SSDQKALGKDD--FSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMYPRKGVIQVG 644
Cdd:PRK13404 315 SSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229162187 645 ADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELHVTQGAGRFIPR 711
Cdd:PRK13404 395 ADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
258-709 |
4.34e-78 |
|
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: 259.53 E-value: 4.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 258 LIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAAL 337
Cdd:cd01315 3 VIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 338 AGGTTMIIDhcLPQKGEP---LLEAYEKWRGWADPKvccdysLHVGVTWWGDGV---AEDIATLcQEKGVNSFKMFMAYK 411
Cdd:cd01315 81 AGGITTIID--MPLNSIPpttTVENLEAKLEAAQGK------LHVDVGFWGGLVpgnLDQLRPL-DEAGVVGFKCFLCPS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 412 GV--F-MLSDDELYKSFSIIKENGALALMHAENGDIIDENTKKMQSLGITGPEGHLQSRPEDVEAEATTRSICIANQVNC 488
Cdd:cd01315 152 GVdeFpAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 489 PLYIVHVMSRSAADAIRKARSEGKVVFGEpiaaslgtDGSHYFCKDW----RHAAAHVMGPPLRpDPTTPGYLMDLLANG 564
Cdd:cd01315 232 RLHIVHLSSAEAVPLIREARAEGVDVTVE--------TCPHYLTFTAedvpDGGTEFKCAPPIR-DAANQEQLWEALENG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 565 DLQLTGTDNCTFSSDQKALGKDDFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMYPRKGVIQVG 644
Cdd:cd01315 303 DIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVG 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229162187 645 ADADIVIWDPEATRVISKN---THHQAvdfNIFEGMECHGVPVITISQGRIVWEDGElHVTQGAGRFI 709
Cdd:cd01315 383 YDADFVVWDPEEEFTVDAEdlyYKNKI---SPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
303-686 |
5.12e-67 |
|
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: 226.12 E-value: 5.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 303 KLIIPGGIDTHTHMQMPFMGTVAiDDFYQGTKAALAGGTTMIIDHCLPQKGEPLLEAYEKWRGWADPKVCCDYSLHVGVt 382
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 383 wWGDGVAEDIATLcQEKGVNSFKMFMAYKGVFML--SDDELYKSFSIIKENGALALMHAEngdiidentkkmqslgitgp 460
Cdd:cd01302 79 -GPGDVTDELKKL-FDAGINSLKVFMNYYFGELFdvDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 461 eghlqsrpedveaeattRSICIANQVNCPLYIVHVMSRSAADAIRKARSEGKVVFGEpiaaslgTDGSHYFC--KDWRHA 538
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCE-------VCPHHLFLdeSMLRLN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 539 AAH-VMGPPLRPdPTTPGYLMDLLANGDLQLTGTDNCTFSSDQKALGKDdFSRIPNGVNGVEDRMSVIWEKGVvTGKMDA 617
Cdd:cd01302 193 GAWgKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTEGV-KRGLSL 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229162187 618 NRFVAVTSTNAAKIFNMYPrKGVIQVGADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVIT 686
Cdd:cd01302 270 ETLVEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
257-710 |
2.64e-64 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 222.22 E-value: 2.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 257 ILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAA 336
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 337 LAGGTTMIIDHclPQKGEPLL--EAYEKWRGWADPKVCCDYSLHVGVTwwgdGVAEDIATLCqEKGVNSF-KMFMAYKGV 413
Cdd:PRK02382 82 AAGGVTTVVDQ--PNTDPPTVdgESFDEKAELAARKSIVDFGINGGVT----GNWDPLESLW-ERGVFALgEIFMADSTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 414 FMLSDDELYK-SFSIIKENGALALMHAENGDIIDENTKKMQslGITGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYI 492
Cdd:PRK02382 155 GMGIDEELFEeALAEAARLGVLATVHAEDEDLFDELAKLLK--GDADADAWSAYRPAAAEAAAVERALEVASETGARIHI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 493 VHVMSRSAADAIRKARsegkvvfgepiaASLGTDGSHYFC--KDWRHAAAHV-MGPPLRPDPTTPGyLMDLLANGDLQLT 569
Cdd:PRK02382 233 AHISTPEGVDAARREG------------ITCEVTPHHLFLsrRDWERLGTFGkMNPPLRSEKRREA-LWERLNDGTIDVV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 570 GTDNCTFSSDQKALgkdDFSRIPNGVNGVEDRMSVIWEkGVVTGKMDANRFVAVTSTNAAKIFNMyPRKGVIQVGADADI 649
Cdd:PRK02382 300 ASDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADL 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1229162187 650 VIWDPEATRVISKNTHHQAVDFNIFEGMEchGV-PVITISQGRIVWEDGELHVTQGAGRFIP 710
Cdd:PRK02382 375 VLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
257-710 |
2.51e-62 |
|
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: 216.48 E-value: 2.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 257 ILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGgAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAA 336
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPDILGPA-AKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 337 LAGGTTMIID---HCLPQKGEplLEAYEKWRGWADPKVCCDYSLhvgvtwWGDGVAEDIATL--CQEKGVNSFKMFMAYK 411
Cdd:TIGR03178 79 AAGGITTYIDmplNSIPATTT--RASLEAKFEAAKGKLAVDVGF------WGGLVPYNLDDLreLDEAGVVGFKAFLSPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 412 GV--FM-LSDDELYKSFSIIKENGALALMHAENGDIIDENTKKMQSLGITGPEGHLQSRPEDVEAEATTRSICIANQVNC 488
Cdd:TIGR03178 151 GDdeFPhVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 489 PLYIVHVMSRSAADAIRKARSEGKVVFGEPIaaslgtdgSHYF---CKDWRHAAAHVM-GPPLRpDPTTPGYLMDLLANG 564
Cdd:TIGR03178 231 RVHVVHLSSAEAVELITEAKQEGLDVTVETC--------PHYLtltAEEVPDGGTLAKcAPPIR-DLANQEGLWEALLNG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 565 DLQLTGTDNCTFSSDQKAlgKDDFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMyPRKGVIQVG 644
Cdd:TIGR03178 302 LIDCVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPG 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229162187 645 ADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELhVTQGAGRFIP 710
Cdd:TIGR03178 379 KDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
257-714 |
3.27e-59 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 208.40 E-value: 3.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 257 ILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGgAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAA 336
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPA-REIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 337 LAGGTTMIID---HCLPqkgePLL--EAYEKWRGWADPKVCCDYSLHVGVTwwgDGVAEDIATLCqEKGVNSFKMFMAYK 411
Cdd:PRK06189 82 AAGGCTTYFDmplNSIP----PTVtrEALDAKAELARQKSAVDFALWGGLV---PGNLEHLRELA-EAGVIGFKAFMSNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 412 GV--FMLSDDE-LYKSFSIIKENGALALMHAENGDIIDENTKKMQSLGITGPEGHLQSRPEDVEAEATTRSICIANQVNC 488
Cdd:PRK06189 154 GTdeFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 489 PLYIVHVMSRSAADAIRKARSEGkvvfgepIAASLGTdGSHYFC---KDW-RHAAAHVMGPPLRpDPTTPGYLMDLLANG 564
Cdd:PRK06189 234 PLHFVHISSGKAVALIAEAKKRG-------VDVSVET-CPHYLLfteEDFeRIGAVAKCAPPLR-SRSQKEELWRGLLAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 565 DLQLTGTDNCTFSSDQKAlgKDDFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMyPRKGVIQVG 644
Cdd:PRK06189 305 EIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVG 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 645 ADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELHvTQGAGRFIPRPLH 714
Cdd:PRK06189 382 ADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF-PPPRGQLLRPSVV 450
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
273-696 |
7.78e-51 |
|
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: 183.80 E-value: 7.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 273 ADVYIEDGTIRQVGKdLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAALAGGTTMIIDhcLPQK 352
Cdd:TIGR00857 6 VDILVEGGRIKKIGK-LRIPPDAEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVAD--MPNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 353 GEPLL--EAYEKWRGWADPKVCCDYSLHVGVTwWGDGVAEDiatlcqekgVNSFKMFMAYKGVFMLSDD--ELYKSFSII 428
Cdd:TIGR00857 81 KPPIDtpETLEWKLQRLKKVSLVDVHLYGGVT-QGNQGKEL---------TEAYELKEAGAVGRMFTDDgsEVQDILSMR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 429 K------ENGALALMHAENGDIIDENTKKmqsLGITGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYIVHVMSRSAAD 502
Cdd:TIGR00857 151 RaleyaaIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 503 AIRKARSEGKVVFGE--PiaaslgtdgSHYFCKDWRHAAAHVMG---PPLRPdPTTPGYLMDLLANGDLQLTGTDNCTFS 577
Cdd:TIGR00857 228 LIVKAKSQGIKITAEvtP---------HHLLLSEEDVARLDGNGkvnPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 578 SDQKALGkddFSRIPNGVNGVEDRMSVIWEkGVVTGKMDANRFVAVTSTNAAKIFNMyPRKGVIQVGADADIVIWDPEAT 657
Cdd:TIGR00857 298 LEEKTKE---FAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKE 372
|
410 420 430
....*....|....*....|....*....|....*....
gi 1229162187 658 RVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWED 696
Cdd:TIGR00857 373 WTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
302-690 |
3.48e-43 |
|
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: 160.58 E-value: 3.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 302 GKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAALAGGTTMIIDhcLPQKGEPLL--EAYEKWRGWADPKVCCDYSLHV 379
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMD--MPNTKPPTTtaEALYEKLRLAAAKSVVDYGLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 380 GVTwwGDGVAEDIATLcqekGVNSFKMFMAYKGVFMLSDDElyKSFSIIKENGALALMHAENGDIIDENTKKMQSLGItg 459
Cdd:cd01318 77 GVT--GSEDLEELDKA----PPAGYKIFMGDSTGDLLDDEE--TLERIFAEGSVLVTFHAEDEDRLRENRKELKGESA-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 460 pegHLQSRPEDVEAEATTRSICIANQVNCPLYIVHVMSRSAADAIRKARSEGKV-------VFGEPIAASLGTdgshyFC 532
Cdd:cd01318 147 ---HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT-----LG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 533 KdwrhaaahvMGPPLRpDPTTPGYLMDLLANGDLQLTGTDNCTFSSDQKALGKDDfsrIPNGVNGVEDRMSVI---WEKG 609
Cdd:cd01318 219 K---------VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNKG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 610 VVTGKmdanRFVAVTSTNAAKIFNMyPRKGVIQVGADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQ 689
Cdd:cd01318 286 ILSLS----RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVR 360
|
.
gi 1229162187 690 G 690
Cdd:cd01318 361 G 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
294-686 |
2.77e-38 |
|
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: 147.00 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 294 GAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAALAGGTTMIIdhCLPQKgEPLLEAYEKW-----RGWAD 368
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVV--CMPNT-NPVIDNPAVVellknRAKDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 369 PKVCCDyslhvgvtWWGDgvaedIATLCQEKGVNSFKMFMAYkGVFMLSDDE--------LYKSFSIIKENGALALMHAE 440
Cdd:cd01317 76 GIVRVL--------PIGA-----LTKGLKGEELTEIGELLEA-GAVGFSDDGkpiqdaelLRRALEYAAMLDLPIIVHPE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 441 NGDIIDE---NTKKMqslgiTGPEGhLQSRPEDVEAEATTRSICIANQVNCPLYIVHVMSRSAADAIRKARSEGkvvfgE 517
Cdd:cd01317 142 DPSLAGGgvmNEGKV-----ASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----L 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 518 PIAASLGtdgSHYF------CKDWRhAAAHVMgPPLRpDPTTPGYLMDLLANGDLQLTGTDNCTFSSDQKALgkdDFSRI 591
Cdd:cd01317 211 PVTAEVT---PHHLllddeaLESYD-TNAKVN-PPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDL---PFAEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 592 PNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMYPrkGVIQVGADADIVIWDPEATRVISKNTHHQAVDF 671
Cdd:cd01317 282 PPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKN 359
|
410
....*....|....*
gi 1229162187 672 NIFEGMECHGVPVIT 686
Cdd:cd01317 360 TPFDGQKLKGRVLAT 374
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
254-710 |
8.89e-38 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 147.31 E-value: 8.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 254 QARILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPggAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGT 333
Cdd:PRK08044 2 SFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDA--KEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 334 KAALAGGTTMIIDHCLPQ-----KGEPLLEAYEKWRGwadpkvccdySLHVGVTWWGDGVAEDIATLCQ--EKGVNSFKM 406
Cdd:PRK08044 78 RAAAKGGITTMIEMPLNQlpatvDRASIELKFDAAKG----------KLTIDAAQLGGLVSYNLDRLHEldEVGVVGFKC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 407 FMA------YKGVFMLSDD-ELYKSFSIIKENGALALMHAENGDIIDENTKKMQSLGITGPEGHLQSRPEDVEAEATTRS 479
Cdd:PRK08044 148 FVAtcgdrgIDNDFRDVNDwQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 480 ICIANQVNCPLYIVHVMSRSAADAIRKARSEGKVVFGEPIaaslgtdgSHYFC--KDWRHAAAHVM--GPPLRPDPTTPG 555
Cdd:PRK08044 228 LYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFVldTDQFEEIGTLAkcSPPIRDLENQKG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 556 yLMDLLANGDLQLTGTDNCTFSSDQKAlgkDDFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMy 635
Cdd:PRK08044 300 -MWEKLFNGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL- 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229162187 636 PRKGVIQVGADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELHVTQGAGRFIP 710
Cdd:PRK08044 375 QQKGRIAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFIL 449
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
256-696 |
1.17e-37 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 146.11 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 256 RILIKGGKVVNADHSFH-ADVYIEDGTIRQVGKDlITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTK 334
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGEN-IEAEGAEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 335 AALAGGTTMIidHCLPQKgEPLLEAYEkwrgwadpkvccdyslhvgvtwwgdgVAEDIATLCQEKGV------------- 401
Cdd:PRK09357 79 AAAAGGFTTV--VAMPNT-KPVIDTPE--------------------------VVEYVLDRAKEAGLvdvlpvgaitkgl 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 402 -----NSFKMfMAYKGVFMLSDD--------------ELYKSFsiikeNGALALmHAE-----NGDIIDEntkkmqslGI 457
Cdd:PRK09357 130 ageelTEFGA-LKEAGVVAFSDDgipvqdarlmrralEYAKAL-----DLLIAQ-HCEdpsltEGGVMNE--------GE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 458 TGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYIVHVMSRSAADAIRKARSEGKvvfgePIAA------------SLGT 525
Cdd:PRK09357 195 VSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLT 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 526 DGSHYfcKdwrhaaahvMGPPLRpDPTTPGYLMDLLANGDLQLTGTDNCTFSSDQKALgkdDFSRIPNGVNGVEDRMSVI 605
Cdd:PRK09357 270 YDPNY--K---------VNPPLR-TEEDREALIEGLKDGTIDAIATDHAPHAREEKEC---EFEAAPFGITGLETALSLL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 606 WEKGVVTGKMDANRFVAVTSTNAAKIFNMYPrkGVIQVGADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVI 685
Cdd:PRK09357 335 YTTLVKTGLLDLEQLLEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVY 412
|
490
....*....|.
gi 1229162187 686 TISQGRIVWED 696
Cdd:PRK09357 413 TIVDGKIVYQD 423
|
|
| PLN02795 |
PLN02795 |
allantoinase |
256-709 |
9.67e-34 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 136.44 E-value: 9.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 256 RILIKGGKVVNAdhsfhadVYIEDGTIRQVGKDLITPG---GAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQG 332
Cdd:PLN02795 52 RVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 333 TKAALAGGTTMIIDhcLPQKGEPLL---EAYEKWRGWADPKvccdysLHVGVTWWGDGVAEDI--ATLCQE---KGVNSF 404
Cdd:PLN02795 123 TKAAAAGGITTLVD--MPLNSFPSTtsvETLELKIEAAKGK------LYVDVGFWGGLVPENAhnASVLEElldAGALGL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 405 KMFMAYKGV--F-MLSDDELYKSFSIIKENGALALMHAENGDIIDENTKKMQSLgiTGPEGHLQSRPEDVEAEA------ 475
Cdd:PLN02795 195 KSFMCPSGIndFpMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADP--RSYSTYLKSRPPSWEQEAirqlle 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 476 ---TTRSICIANqvNCPLYIVHVM-SRSAADAIRKARSEGKVVFGEPIAASLGTDGSHYFCKDWRHAAAhvmgPPLRpDP 551
Cdd:PLN02795 273 vakDTRPGGVAE--GAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCA----PPIR-DA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 552 TTPGYLMDLLANGDLQLTGTDNCTFSSDQKALGKDDFSRIPNGVNGVEDRMSVIWEKGVVTGkMDANRFVAVTSTNAAKI 631
Cdd:PLN02795 346 ANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 632 FNMyPRKGVIQVGADADIVIWDPEATRVISKNT----HHQAVDfnIFEGMECHGVPVITISQGRIVWEDGElHVTQGAGR 707
Cdd:PLN02795 425 AGL-DSKGAIAPGKDADIVVWDPEAEFVLDESYpiyhKHKSLS--PYLGTKLSGKVIATFVRGNLVFLEGK-HAKQACGS 500
|
..
gi 1229162187 708 FI 709
Cdd:PLN02795 501 PI 502
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
255-699 |
1.55e-33 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 134.42 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 255 ARILIKGGKVVNADHSF-HADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGT 333
Cdd:PRK07575 3 MSLLIRNARILLPSGELlLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 334 KAALAGGTTMIIDhcLPQKgEPL---LEAYEKWRGWADPKVCCDYSLHVGVTwwgdgvAEDIATLCQEKGVNSFKMFM-A 409
Cdd:PRK07575 81 RACAKGGVTSFLE--MPNT-KPLtttQAALDDKLARAAEKCVVNYGFFIGAT------PDNLPELLTANPTCGIKIFMgS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 410 YKGVFMLSDDELYKsfSIIKENGALALMHAENGDIIDENTKKMQslGITGPEGHLQSRPEDVEAEATTRSICIANQVNCP 489
Cdd:PRK07575 152 SHGPLLVDEEAALE--RIFAEGTRLIAVHAEDQARIRARRAEFA--GISDPADHSQIQDEEAALLATRLALKLSKKYQRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 490 LYIVHVMSRSAADAIRKARseGKVVFGEPIAASLGTDGSHYFckdwRHAAAHVMGPPLRpDPTTPGYLMDLLANGDLQLT 569
Cdd:PRK07575 228 LHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTDAYE----RIGTLAQMNPPLR-SPEDNEALWQALRDGVIDFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 570 GTDNCTFSSDQKALGkddFSRIPNGVNGVEDRMSVIWEKgVVTGKMDANRFVAVTSTNAAKIFNMyPRKGVIQVGADADI 649
Cdd:PRK07575 301 ATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADL 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1229162187 650 VIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGEL 699
Cdd:PRK07575 376 VLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
258-712 |
6.87e-33 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 132.74 E-value: 6.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 258 LIKGGKVVNADHSFHADVYIEDGTIRQVGkDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAAL 337
Cdd:PRK09060 8 ILKGGTVVNPDGEGRADIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 338 AGGTTMIIDhcLPQKGEPLL--EAYEKWRGWADPKVCCDYSLHVGVTwwgDGVAEDIATLCQEKGVNSFKMFM-AYKGVF 414
Cdd:PRK09060 85 LGGVTAVFE--MPNTNPLTTtaEALADKLARARHRMHCDFAFYVGGT---RDNADELAELERLPGCAGIKVFMgSSTGDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 415 MLSDDE-LYKSFSIIKENGALalmHAENGDIIDENtkkmQSLGITG-PEGHLQSRPEDVEAEATTRSICIANQVNCPLYI 492
Cdd:PRK09060 160 LVEDDEgLRRILRNGRRRAAF---HSEDEYRLRER----KGLRVEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 493 VHVMSRSAADAIRKARSEGKV--------VFGEPIAASLGTdgshyfckdwrHAaahVMGPPLRpDPTTPGYLMDLLANG 564
Cdd:PRK09060 233 LHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT-----------LA---QMNPPIR-DARHRDGLWRGVRQG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 565 DLQLTGTDNCTFSSDQKALgkdDFSRIPNGVNGVEDRMSVIWEKgVVTGKMDANRFVAVTSTNAAKIFNMyPRKGVIQVG 644
Cdd:PRK09060 298 VVDVLGSDHAPHTLEEKAK---PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVG 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229162187 645 ADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGELhVTQGAG---RFIPRP 712
Cdd:PRK09060 373 YDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGepvRFLETL 442
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
262-699 |
7.19e-27 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 113.71 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 262 GKVVNADHSFHADVYIEDGTIRQVGKDLITpgGAKVLDAKGKLIIPGGIDTHTHMQmpfmgtvaidDFYQ--------GT 333
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDLK--GKEVIKVKGGIILPGLIDVHVHLR----------DFEEsyketiesGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 334 KAALAGGTTMIIDhcLPQKGEPLL--EAYEKWRGWADPKVCCDYSLHVGVTwwgdGVAEDIatlcQEKGVNSFKMFM--A 409
Cdd:PRK04250 72 KAALHGGITLVFD--MPNTKPPIMdeKTYEKRMRIAEKKSYADYALNFLIA----GNCEKA----EEIKADFYKIFMgaS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 410 YKGVFMLSDDELYKSFSIIKEngalalMHAENGDIIDENtkkmqslgitgPEghlqsRPEDVEAEATTRSICIANQVNCP 489
Cdd:PRK04250 142 TGGIFSENFEVDYACAPGIVS------VHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 490 LYIVHVMSRSAADAIRKARSEGKVVFGEPiaaslgtdgSHYFC--KDWRHAAAHVMGPPLRPDpttpgylmdllangdlq 567
Cdd:PRK04250 200 LHICHISTKDGLKLILKSNLPWVSFEVTP---------HHLFLtrKDYERNPLLKVYPPLRSE----------------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 568 ltgtdnctfsSDQKALGKdDFSRIP------------------NGVNGVEDRMSVIWE---KGVVTgkmdANRFVAVTST 626
Cdd:PRK04250 254 ----------EDRKALWE-NFSKIPiiasdhaphtledkeagaAGIPGLETEVPLLLDaanKGMIS----LFDIVEKMHD 318
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229162187 627 NAAKIFNmYPRKGvIQVGADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGEL 699
Cdd:PRK04250 319 NPARIFG-IKNYG-IEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI 389
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
304-693 |
1.18e-26 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that 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: 111.82 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 304 LIIPGGIDTHTHMQMPFMGTVAIDDFY------QGTKAALAGGTTMIIDH--CLPQKGEPLLEAYEKwrgwadpkvccdy 375
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLDMgaTTSTGIEALLEAAEE------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 376 sLHVGVTWWG-------DGVAEDIATLCQE--KGVNSFKMF--------MAYKGVFMLSDDELYKSFSIIKENGALALMH 438
Cdd:pfam01979 68 -LPLGLRFLGpgcsldtDGELEGRKALREKlkAGAEFIKGMadgvvfvgLAPHGAPTFSDDELKAALEEAKKYGLPVAIH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 439 AENGDIIDENTKKmqSLGITGPEGHLQSRPEDVEAEATTRSICIANqvncplyiVHVMSRSAADAIRKARSEGKVvfgep 518
Cdd:pfam01979 147 ALETKGEVEDAIA--AFGGGIEHGTHLEVAESGGLLDIIKLILAHG--------VHLSPTEANLLAEHLKGAGVA----- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 519 iaasLGTDGSHYFCKDWRHAAahvmgpplrpdpttpgylmDLLANGDLQLTGTDNCtfssdqkaLGKDDFSRIPNGVNGV 598
Cdd:pfam01979 212 ----HCPFSNSKLRSGRIALR-------------------KALEDGVKVGLGTDGA--------GSGNSLNMLEELRLAL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 599 EDRmsviwekGVVTGKMDANRFVAVTSTNAAKIFNMYPRKGVIQVGADADIVIWDPEATrvisknthhqavdfNIFEGME 678
Cdd:pfam01979 261 ELQ-------FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLK 319
|
410
....*....|....*
gi 1229162187 679 CHGVPVITISQGRIV 693
Cdd:pfam01979 320 PDGNVKKVIVKGKIV 334
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
262-712 |
1.66e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 106.87 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 262 GKVVNADHSFHADVYIEDGTIRQVGKDLitpGGAKVLDAKGkLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAALAGGT 341
Cdd:PRK01211 5 GNFYYKGKFDYLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 342 TMIIDhcLPQKGEPL--LEAYEKWRGWADPKVCCDYSLHVGVTwwGDGvaediATLCQEKGVnSFKMFMA---YKGVFML 416
Cdd:PRK01211 79 TFIMD--MPNNNIPIkdYNAFSDKLGRVAPKAYVDFSLYSMET--GNN-----ALILDERSI-GLKVYMGgttNTNGTDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 417 SDDELYKsfsiIKENGALALMHAENGDIIDENTKKMQSLgitgpEGHLQSRPEDVEAEAT--TRSICIANQVncplyIVH 494
Cdd:PRK01211 149 EGGEIKK----INEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVkyVKNLDLKTKI-----IAH 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 495 VMS-RSAADAIRKARSEGKVVFGEpiaASLGTDGShyfckdwrhaaahvMGPPLRpDPTTPGYLMDLLANGDLQLTGTDN 573
Cdd:PRK01211 215 VSSiDVIGRFLREVTPHHLLLNDD---MPLGSYGK--------------VNPPLR-DRWTQERLLEEYISGRFDILSSDH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 574 CTFSSDQKAlgkdDFSRIPNGVNGVEDRMSVIWEKgVVTGKMDANRFVAVTSTNAAKIFNMypRKGVIQVGADADIVIWD 653
Cdd:PRK01211 277 APHTEEDKQ----EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFD 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229162187 654 PEATRVISKNTHHQAVDFNIFEGMECHgVPVITISQGRIVWEDGELhVTQGAGRFIPRP 712
Cdd:PRK01211 350 FTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPKG 406
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
256-700 |
7.79e-23 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 102.26 E-value: 7.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 256 RILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKA 335
Cdd:PRK09236 3 RILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 336 ALAGGTTMIID--HCLPQKG--EPLLEAYEKWRG--WAdpkvccDYSLHVGVTwwGDGVAEdIATLcQEKGVNSFKMFMA 409
Cdd:PRK09236 81 AVAGGITSFMEmpNTNPPTTtlEALEAKYQIAAQrsLA------NYSFYFGAT--NDNLDE-IKRL-DPKRVCGVKVFMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 410 YKGVFMLSDDE--LYKSFSiikENGALALMHAENGDIIDENTKKMQSL---GITgPEGHLQSRPEDVEAEATTRSICIAN 484
Cdd:PRK09236 151 ASTGNMLVDNPetLERIFR---DAPTLIATHCEDTPTIKANLAKYKEKygdDIP-AEMHPLIRSAEACYKSSSLAVSLAK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 485 QVNCPLYIVHVmsrSAADAI---RKARSEGKVVFGEPIAASL-------GTDGSHYFC----KDWRHAAAhvmgpplrpd 550
Cdd:PRK09236 227 KHGTRLHVLHI---STAKELslfENGPLAEKRITAEVCVHHLwfddsdyARLGNLIKCnpaiKTASDREA---------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 551 pttpgyLMDLLANGDLQLTGTDNCTFSSDQKALGkddFSRIPNGVNGVEDRMSVIWEKgVVTGKMDANRFVAVTSTNAAK 630
Cdd:PRK09236 294 ------LRQALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAI 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229162187 631 IFNMyPRKGVIQVGADADIVIWDPEATRVISKNthhqavdfNI--------FEGMECHGVPVITISQGRIVWEDGELH 700
Cdd:PRK09236 364 LFDI-KERGFIREGYWADLVLVDLNSPWTVTKE--------NIlykcgwspFEGRTFRSRVATTFVNGQLVYHNGQLV 432
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
250-676 |
2.06e-16 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 81.93 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 250 AATAQARILIKGGKVVNADHS---FHADVYIEDGTIRQVGK--DLITPGGAKVLDAKGKLIIPGGIDTHTHMqmpFMGTV 324
Cdd:COG1228 3 APAQAGTLLITNATLVDGTGGgviENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHL---GLGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 325 AIDDFYQGT----------------KAALAGGTTMIIDhcLPQKGEPLLEAYEK-----WRGW----ADPKVCCDYSLHv 379
Cdd:COG1228 80 RAVEFEAGGgitptvdlvnpadkrlRRALAAGVTTVRD--LPGGPLGLRDAIIAgesklLPGPrvlaAGPALSLTGGAH- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 380 gvtwwGDGVAEDIATLCQ--EKGVNSFKMFMAYkGVFMLSDDELYKsfsIIKENGALALM---HAENGDIIDENtkkmqs 454
Cdd:COG1228 157 -----ARGPEEARAALREllAEGADYIKVFAEG-GAPDFSLEELRA---ILEAAHALGLPvaaHAHQADDIRLA------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 455 lgitgpeghlqsrpedVEAEATTrsicianqvncplyIVHV--MSRSAADAIRKArseGKVVFGePiAASLGTDGSHYFC 532
Cdd:COG1228 222 ----------------VEAGVDS--------------IEHGtyLDDEVADLLAEA---GTVVLV-P-TLSLFLALLEGAA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 533 KDWRHAAAHVMGPPLRPdpttPGYLMDllANGDLqltgtdnctfssdqkALGKDDFSRIPNGVN-------GVEDRMSvi 605
Cdd:COG1228 267 APVAAKARKVREAALAN----ARRLHD--AGVPV---------------ALGTDAGVGVPPGRSlhrelalAVEAGLT-- 323
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229162187 606 wekgvvtgKMDAnrFVAVTStNAAKIFNMYPRKGVIQVGADADIVIWDPEATRVISkntHHQAVDFNIFEG 676
Cdd:COG1228 324 --------PEEA--LRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIA---YLEDVRAVMKDG 380
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
277-695 |
3.28e-15 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 78.21 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 277 IEDGTIRQVGKDLitpGGAKVLDAKGKLIIPGGIDTHTHmqmPFMGTVAIDDFYQGTKAALAGGTTMII--DHCLP---- 350
Cdd:PRK08417 3 IKDGKITEIGSDL---KGEEILDAKGKTLLPALVDLNVS---LKNDSLSSKNLKSLENECLKGGVGSIVlyPDSTPaidn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 351 ---------QKGEPLLEAYEKWRGWADpkvccdyslhvgvtwwgDGVAEDIATLcqekgvnsFKMfmAYKGVFMLSDDEL 421
Cdd:PRK08417 77 eialelinsAQRELPMQIFPSIRALDE-----------------DGKLSNIATL--------LKK--GAKALELSSDLDA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 422 YKSFSIIKengaLALM-------HAENGDIIDENTkkMQSlGITGPEGHLQSRPEDVEAEATTRSICIANQVNCPLYIVH 494
Cdd:PRK08417 130 NLLKVIAQ----YAKMldvpifcRCEDSSFDDSGV--MND-GELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDT 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 495 VMSRSAADAIRKARSEGKVVFGEPIAASLGTDGSHyfCKDWRHAAAhvMGPPLRpDPTTPGYLMDLLANGDLQLTGTDNC 574
Cdd:PRK08417 203 LALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSA--CENFNTAAK--LNPPLR-SKEDRLALLEALKEGKIDFLTSLHS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 575 TFSSDQKALGKDDFSripNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVTSTNAAKIFNMypRKGVIQVGADADIVIWDP 654
Cdd:PRK08417 278 AKSNSKKDLAFDEAA---FGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFDP 352
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1229162187 655 EATRVISKNthhqavdFNIFEGMECHGVPVITISQGRIVWE 695
Cdd:PRK08417 353 NESTIIDDN-------FSLYSGDELYGKIEAVIIKGKLYLE 386
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
256-362 |
9.96e-15 |
|
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: 77.17 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 256 RILIKGGKVVNADHSF----HADVYIEDGTIRQVGKDLITP---GGAKVLDAKGKLIIPGGIDTHTHMQMPFMGTVAID- 327
Cdd:COG0402 1 DLLIRGAWVLTMDPAGgvleDGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLADDl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229162187 328 --------------------DFYQGTKAA----LAGGTTMIIDHC--LPQKGEPLLEAYEK 362
Cdd:COG0402 81 plldwleeyiwplearldpeDVYAGALLAlaemLRSGTTTVADFYyvHPESADALAEAAAE 141
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
290-708 |
4.50e-14 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 74.80 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 290 ITPGGAKVLD-AKGKLIIPGGIDTHTHM---QMPFMGTVAiddfyQGTKAALAGGTTMIIDhcLPQKGEPL--------- 356
Cdd:PRK00369 29 IKSRCKPDLDlPQGTLILPGAIDLHVHLrglKLSYKEDVA-----SGTSEAAYGGVTLVAD--MPNTIPPLntpeaitek 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 357 ---LEAYEKwrgwadpkvcCDYSLHVGVTwwgdGVAEDIATLcqekGVNSFKMFMaykgvfmlSDDELYKSFSIIKENGA 433
Cdd:PRK00369 102 laeLEYYSR----------VDYFVYSGVT----KDPEKVDKL----PIAGYKIFP--------EDLEREETFRVLLKSRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 434 LALMHaengdiidentkkmqslgitgPEGHLQSRPEDVEAEATTRSICIANQVNcPLYIVHVMSRSAADAIRKARSEGKV 513
Cdd:PRK00369 156 LKILH---------------------PEVPLALKSNRKLRRNCWYEIAALYYVK-DYQNVHITHASNPRTVRLAKELGFT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 514 VFGEPiaaslgtdgSHYFCKDWRHAAAHVmGPPLRpDPTTPGYLMDLLANGDlqLTGTDNCTFSSDQKalgKDDFSRIPN 593
Cdd:PRK00369 214 VDITP---------HHLLVNGEKDCLTKV-NPPIR-DINERLWLLQALSEVD--AIASDHAPHSSFEK---LQPYEVCPP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 594 GVNGVEDRMSVIWEKgVVTGKMDANRFVAVTSTNAAKIFNMYPRKgvIQVGADADIVIWDPEATRVISKNThhqAVDFNI 673
Cdd:PRK00369 278 GIAALSFTPPFIYTL-VSKGILSIDRAVELISTNPARILGIPYGE--IKEGYRANFTVIQFEDWRYSTKYS---KVIETP 351
|
410 420 430
....*....|....*....|....*....|....*
gi 1229162187 674 FEGMECHGVPVITISQGRIVWEDGELHVTQGAGRF 708
Cdd:PRK00369 352 LDGFELKASVYATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
257-347 |
1.10e-12 |
|
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: 70.69 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 257 ILIKGGKVVNADHS---FHADVYIEDGTIRQVGKDLITPG--GAKVLDAKGKLIIPGGIDTHTHMQM------------- 318
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1229162187 319 --------PFMGTVAIDDFYQGTKAALA----GGTTMIIDH 347
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADM 121
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
257-315 |
5.49e-12 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 68.34 E-value: 5.49e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229162187 257 ILIKGGKVVNADHSFHA--DVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTH 315
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
249-714 |
1.55e-11 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 67.41 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 249 MAATAQARILIKGGKVVNADHSFHA--DVYIEDGTIRQVGKDLItpGGAKVLDAKGKLIIPGGIDTHTHMQMPfmgtvaI 326
Cdd:PRK09061 13 PASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAHGQSV------A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 327 DDFYQgtkaALAGGTTMIIDHC--LP-------QKGEPLLEAYEKWRGWA----------DPKVCCDYSLH-VGVTWWGD 386
Cdd:PRK09061 85 AYRMQ----AFDGVTTALELEAgvLPvarwyaeQAGEGRPLNYGASVGWTpariavltgpQAEGTIADFGKaLGDPRWQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 387 GVA-----EDIATLCQE---KGVNSFKMFMAYK-GVfmlSDDELYKSFSIIKENGALALMHAENGDIIDentkkmqslgi 457
Cdd:PRK09061 161 RAAtpaelAEILELLEQgldEGALGIGIGAGYApGT---GHKEYLELARLAARAGVPTYTHVRYLSNVD----------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 458 tgPEghlqsrpedVEAEATTRSICIANQVNCPLYIVHVMSRSAADA------IRKARSEGKVVFGE--PIAASLGTDGSH 529
Cdd:PRK09061 227 --PR---------SSVDAYQELIAAAAETGAHMHICHVNSTSLRDIdrclalVEKAQAQGLDVTTEayPYGAGSTVVGAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 530 YFCKDWRHAaahvMGPP-------------------LRPDPTTPG------------------------YLMDLLANGDL 566
Cdd:PRK09061 296 FFDPGWLER----MGLGygslqwvetgerlltreelAKLRANDPGglvlihfldednprdralldrsvlFPGAAIASDAM 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 567 QLTGTDNCTFSSDQKALGKDDFSRiPNGvNGVEDRMSVIW--EKGVVTgKMDAnrfVAVTSTNAAKIFN----MYPRKGV 640
Cdd:PRK09061 372 PWTWSDGTVYEGDAWPLPEDAVSH-PRS-AGTFARFLREYvrERKALS-LLEA---IRKCTLMPAQILEdsvpAMRRKGR 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1229162187 641 IQVGADADIVIWDPEatRVISKNThhqavdfniFEGME--CHGVPVITISqGRIVWEDGELHVTQGAGRFIPRPLH 714
Cdd:PRK09061 446 LQAGADADIVVFDPE--TITDRAT---------FEDPNrpSEGVRHVLVN-GVPVVSNGELVRDARPGRPVRRPVK 509
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
271-695 |
8.52e-11 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 65.06 E-value: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 271 FHADVYIEDGTIRQVGKDLI---TPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAALAGGTTMIIdh 347
Cdd:PRK09059 21 EIGTVLIEDGVIVAAGKGAGnqgAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIASASRAAAAGGVTSII-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 348 CLPQKgEPLLeayekwrgwaDPKVCCDYSLHvgvtwwgdgVAEDIATlcqekgVNSFKMFMAYKGvfmLSDDELyKSFSI 427
Cdd:PRK09059 97 MMPDT-DPVI----------DDVALVEFVKR---------TARDTAI------VNIHPAAAITKG---LAGEEM-TEFGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 428 IKENGALA-----------------LMHAENGD--IIDENTKKmqSLGITG--PEGHLQSR------PEDVEA------- 473
Cdd:PRK09059 147 LRAAGAVAftdgrrsvantqvmrraLTYARDFDavIVHETRDP--DLGGNGvmNEGLFASWlglsgiPREAEViplerdl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 474 --EATTRSICIANQVNCPLyivhvmsrsAADAIRKARSEG-KVVFGEPIA-ASLG-TDGSHY--FCKdwrhaaahvMGPP 546
Cdd:PRK09059 225 rlAALTRGRYHAAQISCAE---------SAEALRRAKDRGlKVTAGVSINhLSLNeNDIGEYrtFFK---------LSPP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 547 LRPDPTTPGyLMDLLANGDLQLTGTDNCTFSSDQKALgkdDFSRIPNGVNGVEDRMSVIWeKGVVTGKMDANRFVAVTST 626
Cdd:PRK09059 287 LRTEDDRVA-MVEAVASGTIDIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLYHNGEVPLLRLIEALST 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229162187 627 NAAKIFNMypRKGVIQVGADADIVIWDPEATRVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWE 695
Cdd:PRK09059 362 RPAEIFGL--PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
257-707 |
2.12e-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: 63.47 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 257 ILIKGGKVV---NADhSFHADVYIEDGTIRQVGKDLITPGgAKVLDAKGKLIIPGGIDTHTHMQmpfmGTVAIDDFYqgT 333
Cdd:cd01297 2 LVIRNGTVVdgtGAP-PFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHYD----GQVFWDPDL--R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 334 KAALAGGTTMIIDHC---------------------LPQKGEPLLEAYEKWRGWAD--------PKVCCDY-----SLHV 379
Cdd:cd01297 74 PSSRQGVTTVVLGNCgvspapanpddlarlimlmegLVALGEGLPWGWATFAEYLDalearppaVNVAALVghaalRRAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 380 gvtwWGD----GVAEDIATLCQ--EKGVNSfkmfmaykGVFMLSDDELY--KSFSIIKENGALALMHAENGDIIdentkk 451
Cdd:cd01297 154 ----MGLdareATEEELAKMREllREALEA--------GALGISTGLAYapRLYAGTAELVALARVAARYGGVY------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 452 mqslgITGPEGHLQSRPEDVEaeattRSICIANQVNCPLYIVHVMSRSAA---------DAIRKARSEGKVVFGEpiaAS 522
Cdd:cd01297 216 -----QTHVRYEGDSILEALD-----ELLRLGRETGRPVHISHLKSAGAPnwgkidrllALIEAARAEGLQVTAD---VY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 523 LGTDGSHyfcKDWRHAAAHvmgpplrpdPTTPGyLMDLLANGDLQLTGtdNCTFSsdqKALGKddFSRipngvngvedrm 602
Cdd:cd01297 283 PYGAGSE---DDVRRIMAH---------PVVMG-GSDGGALGKPHPRS--YGDFT---RVLGH--YVR------------ 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 603 sviwEKGVVTgkmdANRFVAVTSTNAAKIFNMYPRkGVIQVGADADIVIWDPE--ATRVISKNTHHQAvdfnifEGMEch 680
Cdd:cd01297 331 ----ERKLLS----LEEAVRKMTGLPARVFGLADR-GRIAPGYRADIVVFDPDtlADRATFTRPNQPA------EGIE-- 393
|
490 500
....*....|....*....|....*..
gi 1229162187 681 gvpvITISQGRIVWEDGeLHVTQGAGR 707
Cdd:cd01297 394 ----AVLVNGVPVVRDG-AFTGARPGR 415
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
255-315 |
1.58e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 61.17 E-value: 1.58e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229162187 255 ARILIKGGKVVNADHSFH----ADVYIEDGTIRQVGKDlITPGGAKVLDAKGKLIIPGGIDTHTH 315
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIGdlprGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHRH 65
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
257-327 |
1.82e-09 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 60.58 E-value: 1.82e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229162187 257 ILIKGGKVVNADH--SFHADVYIEDGTIRQVGKDlITPGGAKVLDAKGKLIIPGGIDTHTHMQMPFMGTVAID 327
Cdd:PRK08393 3 ILIKNGYVIYGENlkVIRADVLIEGNKIVEVKRN-INKPADTVIDASGSVVSPGFINAHTHSPMVLLRGLADD 74
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
310-527 |
2.07e-09 |
|
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: 59.27 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 310 IDTHTHMQMPFMGTVAI----------------DDFYQGTKAALAGGTTMIIDHCLPQKGEPLLEAYEKWRGWADP---- 369
Cdd:cd01292 2 IDTHVHLDGSALRGTRLnlelkeaeelspedlyEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAsagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 370 -KVCCDYSLHVGVTWWGDGVAEDIATLCQ--EKGVNSFKMFMAYkGVFMLSDDELYKSFSIIKENGALALMHAENGDIID 446
Cdd:cd01292 82 rVVLGLGIPGVPAAVDEDAEALLLELLRRglELGAVGLKLAGPY-TATGLSDESLRRVLEEARKLGLPVVIHAGELPDPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 447 ENTKKMQSLGITGPEGHLQ--SRPEDVEAEATTR---SICIANQVNcplyIVHVMSRSAADAIRKARSEGKVVfgepiaa 521
Cdd:cd01292 161 RALEDLVALLRLGGRVVIGhvSHLDPELLELLKEagvSLEVCPLSN----YLLGRDGEGAEALRRLLELGIRV------- 229
|
....*.
gi 1229162187 522 SLGTDG 527
Cdd:cd01292 230 TLGTDG 235
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
255-329 |
2.95e-09 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 60.15 E-value: 2.95e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1229162187 255 ARILIKGGKVV--NADHSFHADVYIEDGTIRQVGKDliTPGGA-KVLDAKGKLIIPGGIDTHTHMQMPFMGTVAiDDF 329
Cdd:PRK06038 2 ADIIIKNAYVLtmDAGDLKKGSVVIEDGTITEVSES--TPGDAdTVIDAKGSVVMPGLVNTHTHAAMTLFRGYA-DDL 76
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
256-315 |
3.88e-09 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 59.63 E-value: 3.88e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229162187 256 RILIKGGKVVNADHS---FHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTH 315
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
258-315 |
4.77e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 58.96 E-value: 4.77e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229162187 258 LIKGGKVVNADHSFH-ADVYIEDGTIRQVGKDliTPGGAKVLDAKGKLIIPGGIDTHTH 315
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
255-346 |
6.49e-09 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 59.34 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 255 ARILIKGGKVVNAdHS---FHADVYIEDGTIRQVGkDLITPGgAKVLDAKGKLIIPGGIDTHTHM--QMpfmgtVAIDDF 329
Cdd:COG1001 5 ADLVIKNGRLVNV-FTgeiLEGDIAIAGGRIAGVG-DYIGEA-TEVIDAAGRYLVPGFIDGHVHIesSM-----VTPAEF 76
|
90
....*....|....*...
gi 1229162187 330 YqgtKAALAGGTT-MIID 346
Cdd:COG1001 77 A---RAVLPHGTTtVIAD 91
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
273-393 |
7.25e-09 |
|
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: 58.80 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 273 ADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQ-----------MPFMGTVAIDDFYQGTKA------ 335
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDktftggrwpnnSGGTLLEAIIAWEERKLLltaedv 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229162187 336 ----------ALAGGTTMIIDHC--LPQKG----EPLLEAYEKWRGWADPKVCCDYSLHVGVTWWGDGVAEDIA 393
Cdd:cd01293 95 keraeralelAIAHGTTAIRTHVdvDPAAGlkalEALLELREEWADLIDLQIVAFPQHGLLSTPGGEELMREAL 168
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
257-315 |
1.02e-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: 57.97 E-value: 1.02e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1229162187 257 ILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTH 315
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
254-666 |
2.18e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 57.30 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 254 QARILikgGKVVNADHsfHADVYIEDGTIRQVGKDLI-TPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmGTVAIDDFYQG 332
Cdd:PRK07369 8 QVRVL---DPVSNTDR--IADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 333 TKAALAGGTTM--IIDHCLPQKGEPLLEAYEKWRGWADPKVCCDY--SLHVGV-----TWWGDGVAEDIATLCQEKGVNS 403
Cdd:PRK07369 81 AAAAAAGGFTRvaILPDTFPPLDNPATLARLQQQAQQIPPVQLHFwgALTLGGqgkqlTELAELAAAGVVGFTDGQPLEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 404 FKM---FMAYKGVfmlsddeLYKSFSIIKENGALAlmhaENGdIIDENTKKMQsLGITGpeghlqsRPEDVEAEATTRSI 480
Cdd:PRK07369 161 LALlrrLLEYLKP-------LGKPVALWPCDRSLA----GNG-VMREGLLALR-LGLPG-------DPASAETTALAALL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 481 CIANQVNCPlyiVHVMSRSAADA---IRKARSEGKvvfgePIAASLgtdgshyfckDWRH------AAAHvMGPPLRPDP 551
Cdd:PRK07369 221 ELVAAIGTP---VHLMRISTARSvelIAQAKARGL-----PITAST----------TWMHllldteALAS-YDPNLRLDP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 552 ttP-GYLMDLLA------NGDLQLTGTDNCTFSSDQKALGkddFSRIPNGVNGVEDRMSVIWEKGVVTGKMDANRFVAVT 624
Cdd:PRK07369 282 --PlGNPSDRQAliegvrTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQAL 356
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1229162187 625 STNAAKIFNMYPRKgvIQVGADADIVIWDPEATRVISKNTHH 666
Cdd:PRK07369 357 STNPARCLGQEPPS--LAPGQPAELILFDPQKTWTVSAQTLH 396
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
274-315 |
2.66e-08 |
|
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: 56.57 E-value: 2.66e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1229162187 274 DVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTH 315
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVH 42
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
257-318 |
5.34e-08 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 56.05 E-value: 5.34e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229162187 257 ILIKGGKVVNADHS---FHADVYIEDGTIRQVGKDliTPGGAKVLDAKGKLIIPGGIDTHTHMQM 318
Cdd:PRK06380 3 ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYVGDV--NEEADYIIDATGKVVMPGLINTHAHVGM 65
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
257-315 |
5.94e-08 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 56.35 E-value: 5.94e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229162187 257 ILIKGGKV------VNADHsfhADVYIEDGTIrqVgKDLITPGGAKVLDAKGKLIIPGGIDTHTH 315
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDGKI--V-EEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
257-712 |
6.68e-08 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 55.95 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 257 ILIKGGKVV----NAdhSFHADVYIEDGTIRQVGkDLITPGGAKVLDAKGKLIIPGGIDTHTHMQmpfmGTVAIDDF--- 329
Cdd:COG3653 4 LLIRGGTVVdgtgAP--PFRADVAIKGGRIVAVG-DLAAAEAARVIDATGLVVAPGFIDIHTHYD----LQLLWDPRlep 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 330 --YQGTkaalaggTTMIIDHC-------LPQKGEPLLEAYEKWRGWADpkvccdyslhvGVTWWGDGVAEDIATLC-QEK 399
Cdd:COG3653 77 slRQGV-------TTVVMGNCgvsfapvRPEDRDRLIDLMEGVEGIPE-----------GLDWDWESFGEYLDALErRGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 400 GVNsFKMFMAYKGVFML---------SDDELYKSFSIIKE---NGALAL---------MHAENGDIIdENTKKMQSLGit 458
Cdd:COG3653 139 GVN-VASLVGHGTLRAYvmglddrppTPEELARMRALLREameAGALGLstgliyvpgTYASTDELV-ALAKVVAEYG-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 459 gpeGHLQS--RPE-DVEAEATTRSICIANQVNCPLYIVHV---------MSRSAADAIRKARSEGKVVFGE--------- 517
Cdd:COG3653 215 ---GVYQShmRDEgDGLLEAVDELIRIGREAGVPVHISHLkaagkpnwgKADEVLALIEAARAEGLDVTADvypypagst 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 518 -------PIAASLGTD------------------------GSHYFCKDWRHAAahVMGPPlrPDPTTPG----------- 555
Cdd:COG3653 292 glgallpPWAAAGGLDerlarlrdpatrariraeieeglpDNLLGRGGWDNIL--ISDSP--PNEPLVGkslaeiaaerg 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 556 -----YLMDLLANGDLQLTGT---------------DNCTFSSDQKALGK------DDFSRIPNGVngVEDR--MSViwE 607
Cdd:COG3653 368 vdpadAALDLLLEEDGRVLIVyfimseedvrellrhPWVMIGSDGGLGGKahprayGTFPRVLGHY--VRERgvLSL--E 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 608 KGV--VTGKmdanrfvavtstnAAKIFNMYPRkGVIQVGADADIVIWDPEatRVISKNTH---HQAVDfnifeGMEChgv 682
Cdd:COG3653 444 EAVrkLTSL-------------PADRLGLKDR-GLLRPGYRADLVVFDPA--TLADRATFdlpAQRAD-----GIRA--- 499
|
570 580 590
....*....|....*....|....*....|
gi 1229162187 683 pviTISQGRIVWEDGElHVTQGAGRFIPRP 712
Cdd:COG3653 500 ---VIVNGVVVVEDGK-PTGARPGRVLRGG 525
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
250-316 |
1.25e-07 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 55.19 E-value: 1.25e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229162187 250 AATAQARILIKGGKV--VNADHSFHADVYIEDGTIRQVGKD-----LITPGgAKVLDAKGKLIIPGGIDTHTHM 316
Cdd:COG1574 3 LAAAAADLLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaevraLAGPA-TEVIDLGGKTVLPGFIDAHVHL 75
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
305-706 |
1.84e-07 |
|
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: 53.99 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 305 IIPGGIDTHTHMQMPfmGTVAIDDFYQGTKAALAGGTTMIidHCLPQKGEPLL--EAYEKWRGWADPKVCCDYSLHVGVT 382
Cdd:cd01316 4 RLPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 383 wwgdgvAEDIATLCQEKGvnsfkmfmaykgvfmlsddelyksfsiiKENGALALMHAENGDIIDENTKKMQSLGITGPEg 462
Cdd:cd01316 80 ------STNAATVGELAS----------------------------EAVGLKFYLNETFSTLILDKITAWASHFNAWPS- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 463 hlqSRPEDVEAEATTRS--ICIANQVNCPLYIVHVMSRSAADAIRKARSEGKVVFGEPIAASLgtdgshYFCKDWRHAAA 540
Cdd:cd01316 125 ---TKPIVTHAKSQTLAavLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 541 HvmgpPLRPDPTTPGYLMDLLANGDlqltgTDNCtFSSDQ--KALGKDDFSRIPNGVNGVEDRMSVIWeKGVVTGKMDAN 618
Cdd:cd01316 196 Y----EVRPFLPTREDQEALWENLD-----YIDC-FATDHapHTLAEKTGNKPPPGFPGVETSLPLLL-TAVHEGRLTIE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 619 RFVAVTSTNAAKIFNMYPRKGViQVGADADiVIWdpeatrVISKNTHHQAVDFNIFEGMECHGVPVITISQGRIVWEDGE 698
Cdd:cd01316 265 DIVDRLHTNPKRIFNLPPQSDT-YVEVDLD-EEW------TIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGE 336
|
....*...
gi 1229162187 699 LHVTQGAG 706
Cdd:cd01316 337 IVAPPGFG 344
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
257-315 |
3.82e-07 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 53.40 E-value: 3.82e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1229162187 257 ILIKGGKVVNADHSFH----ADVYIEDGTIRQVGKdliTPG------GAKVLDAKGKLIIPGGIDTHTH 315
Cdd:PRK07203 2 LLIGNGTAITRDPAKPviedGAIAIEGNVIVEIGT---TDElkakypDAEFIDAKGKLIMPGLINSHNH 67
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
256-343 |
1.17e-06 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 51.72 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 256 RILIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAkvLDAKGKLIIPGGIDTHT-----HMQ------MPFMGTV 324
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVDLHTdnlekHLAprpgvdWPADAAL 80
|
90
....*....|....*....
gi 1229162187 325 AIDDfyqgTKAALAGGTTM 343
Cdd:PRK15446 81 AAHD----AQLAAAGITTV 95
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
292-693 |
1.50e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 51.38 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 292 PGGAKVLDAKGKliIPGGI---DTHTHMQMpfmgtVAIDDFYQGTKAALAG----GTTMIIDHCLPQKGEPLLEAY---- 360
Cdd:pfam07969 116 PGGEIARDANGE--GLTGLlreGAYALPPL-----LAREAEAAAVAAALAAlpgfGITSVDGGGGNVHSLDDYEPLrelt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 361 ---------EKWRGWadPKVCCDYSLHVG-VTWWGDGVAediatlcqekGVNSFKMFMAY-----KGVFMLSDDELYKSF 425
Cdd:pfam07969 189 aaeklkellDAPERL--GLPHSIYELRIGaMKLFADGVL----------GSRTAALTEPYfdapgTGWPDFEDEALAELV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 426 SIIKENGALALMHAENGDIIDENTKKMQSLGITGPeghLQSRPEDVEAEattrsicianqvncplyivhVMSRSAADAIR 505
Cdd:pfam07969 257 AAARERGLDVAIHAIGDATIDTALDAFEAVAEKLG---NQGRVRIEHAQ--------------------GVVPYTYSQIE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 506 KARSEGkvvfgepIAASLgtdgSHYFCKDWRHAAAHVMGPPlRPDPTTPgyLMDLLANGDlqltgtdNCTFSSDQKALGK 585
Cdd:pfam07969 314 RVAALG-------GAAGV----QPVFDPLWGDWLQDRLGAE-RARGLTP--VKELLNAGV-------KVALGSDAPVGPF 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 586 DDFSRIPNGVngvedrMSVIWEKGVVTG---KMDANRFVAVTSTNAAKIFNMYPRKGVIQVGADADIVIWDPEATRVisk 662
Cdd:pfam07969 373 DPWPRIGAAV------MRQTAGGGEVLGpdeELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTV--- 443
|
410 420 430
....*....|....*....|....*....|.
gi 1229162187 663 nthHQAVDFNIfegmechgVPVITISQGRIV 693
Cdd:pfam07969 444 ---DPPAIADI--------RVRLTVVDGRVV 463
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
256-316 |
2.57e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 50.62 E-value: 2.57e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229162187 256 RILIKGGKVV---NADHSFHAD--VYIEDGTIRQVGKDLITPG-GAKVLDAKGKLIIPGGIDTHTHM 316
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHF 68
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
275-345 |
1.94e-05 |
|
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: 47.64 E-value: 1.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229162187 275 VYIEDGTIRQVGK--DLITPGGA--KVLDAKGKLIIPGGIDTHTHMQmpFMGTVAiDDFYqgtkAALAGGTTMII 345
Cdd:cd01296 1 IAIRDGRIAAVGPaaSLPAPGPAaaEEIDAGGRAVTPGLVDCHTHLV--FAGDRV-DEFA----ARLAGASYEEI 68
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
259-315 |
2.73e-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: 47.79 E-value: 2.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 259 IKGGKVVNADHSFHA---DVYIEDGTIRQVGKDlitPGGAKVLDAKGKLIIPGGIDTHTH 315
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDGKIVESSSG---AKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
273-322 |
2.87e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 47.23 E-value: 2.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1229162187 273 ADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPFMG 322
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWG 66
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
279-342 |
3.00e-05 |
|
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: 46.92 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 279 DGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPFMGTV------------------AIDDFY---QGTKAAL 337
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLDEEGGVretsdaneetdpvtphvrAIDGINpddEAFKRAR 80
|
....*
gi 1229162187 338 AGGTT 342
Cdd:cd01309 81 AGGVT 85
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
256-358 |
1.14e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 45.44 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 256 RILIKGGKVVNADHSF--HADVYIEDGTIRQVGKDlitPGG---AKVLDAKGKLIIPGGIDTHTHMQMP---FMGTVAID 327
Cdd:PRK07627 2 KIHIKGGRLIDPAAGTdrQADLYVAAGKIAAIGQA---PAGfnaDKTIDASGLIVCPGLVDLSARLREPgyeYKATLESE 78
|
90 100 110
....*....|....*....|....*....|.
gi 1229162187 328 dfyqgTKAALAGGTTMIIdhCLPQKGEPLLE 358
Cdd:PRK07627 79 -----MAAAVAGGVTSLV--CPPDTDPVLDE 102
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
221-345 |
1.32e-04 |
|
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: 45.40 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 221 GGTIPRD-MTMSMVPVDEDAeslCDMdsemaataqariLIKGGKVVNADHSFHADVYIEDGTIRQVGK-------DLITP 292
Cdd:cd00375 45 GGKVLRDgMGQSSGYTREDV---LDL------------VITNALIIDYTGIYKADIGIKDGRIVAIGKagnpdimDGVTP 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1229162187 293 G-----GAKVLDAKGKLIIPGGIDTHTHMQMPfmgtvaiddfyQGTKAALAGGTTMII 345
Cdd:cd00375 110 NmivgpSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASGITTMI 156
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
272-323 |
1.59e-04 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 44.96 E-value: 1.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1229162187 272 HADVYIEDGTIRQVGKDLI-----------TPGGAKVLDAKGKLIIPGGIDTHTHM-QMPFMGT 323
Cdd:cd01303 19 DALRVVEDGLIVVVDGNIIaagaaetlkraAKPGARVIDSPNQFILPGFIDTHIHApQYANIGS 82
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
271-315 |
1.72e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 44.80 E-value: 1.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1229162187 271 FHAD--VYIEDGTIRQVGK--DLIT--PGGAKVLDAKGKLIIPGGIDTHTH 315
Cdd:PRK09228 28 YIEDglLLVEDGRIVAAGPyaELRAqlPADAEVTDYRGKLILPGFIDTHIH 78
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
254-341 |
3.60e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 44.12 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 254 QARILIKGGKVVNADHSFHADvyIEDGtirqVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPFMGTVAiddFYQGT 333
Cdd:PRK13985 82 KADIGIKDGKIAGIGKGGNKD--MQDG----VKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTA---FASGV 152
|
....*...
gi 1229162187 334 KAALAGGT 341
Cdd:PRK13985 153 TTMIGGGT 160
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
273-363 |
4.25e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 43.93 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 273 ADVYIEDGTIRQVGK------------DLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmgtvaiddfyQGTKAALAGG 340
Cdd:PRK13308 87 GDIGIRDGRIVGIGKagnpdimdgvdpRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155
|
90 100 110
....*....|....*....|....*....|...
gi 1229162187 341 -TTMI---------IDHCLPQKGEPLLEAYEKW 363
Cdd:PRK13308 156 iTTMLggglgptvgIDSGGPFNTGRMLQAAEAW 188
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
273-344 |
5.23e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 43.63 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 273 ADVYIEDGTIRQVGK----------DLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmgtvaiddfyQGTKAALAGG-T 341
Cdd:PRK13207 85 ADIGIKDGRIVAIGKagnpdiqdgvDIIIGPGTEVIAGEGLIVTAGGIDTHIHFICP-----------QQIEEALASGvT 153
|
...
gi 1229162187 342 TMI 344
Cdd:PRK13207 154 TMI 156
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
273-345 |
5.65e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 43.54 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 273 ADVYIEDGTIRQVGK------------DLITPGGAKVLDAKGKLIIPGGIDTHTHMQMPfmgtvaiddfyQGTKAALAGG 340
Cdd:PRK13206 89 ADVGIRDGRIVAIGKagnpdimdgvhpDLVIGPSTEIIAGNGRILTAGAIDCHVHFICP-----------QIVDEALAAG 157
|
....*
gi 1229162187 341 TTMII 345
Cdd:PRK13206 158 ITTLI 162
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
274-316 |
6.05e-04 |
|
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: 43.07 E-value: 6.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1229162187 274 DVYIEDGTIRQVG-----KDLITPGgAKVLDAKGKLIIPGGIDTHTHM 316
Cdd:cd01300 1 AVAVRDGRIVAVGsdaeaKALKGPA-TEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
271-365 |
1.07e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 42.28 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 271 FHADVYIEDGTIRQVGKDLITPGGAKVLDAKGKLIIPGGIDTHTHMQ----MP--------FMG---TVAID-------- 327
Cdd:PRK07583 39 VLVDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHLDkghiWPrspnpdgtFPGaldAVTADreahwsae 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1229162187 328 DFYQ----GTKAALAGGTTMIIDH--CLPQKGEPLLEAY----EKWRG 365
Cdd:PRK07583 119 DLYRrmefGLRCAYAHGTSAIRTHldSFAPQAAISWEVFaelrEAWAG 166
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
572-675 |
1.57e-03 |
|
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: 41.61 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 572 DNCTFSSD-QKALGKDDFSR--IPNGVNGVEDRMSVIWEkGVVTGKMDANRFVAVTSTNAAKIFNMYPrKGVIQVGADAD 648
Cdd:cd01308 277 ERITFSSDgNGSLPKFDENGnlVGLGVGSVDTLLREVRE-AVKCGDIPLEVALRVITSNVARILKLRK-KGEIQPGFDAD 354
|
90 100 110
....*....|....*....|....*....|...
gi 1229162187 649 IVIWDPEAT--RVISKNTH----HQAVDFNIFE 675
Cdd:cd01308 355 LVILDKDLDinSVIAKGQImvrnGKLLVKGTFE 387
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
623-727 |
5.23e-03 |
|
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: 40.09 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229162187 623 VTSTNAAKIFNMyPRKGVIQVGADADIVIWDPEAtrvisknthhQAVDFNIFEGME-CHGVPVITISQGRIVWEDGELhV 701
Cdd:cd01304 435 MTRAGPAKLLGL-SDKGHLGVGADADIAIYDDDP----------DQVDPSDYEKVEkAFSRAAYVLKDGEIVVKDGEV-V 502
|
90 100
....*....|....*....|....*.
gi 1229162187 702 TQGAGRFIPRPLHAPEAYNRILIRDR 727
Cdd:cd01304 503 AEPWGRTYWVDVEVPSLDEEVEKDLE 528
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
258-316 |
7.28e-03 |
|
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: 39.68 E-value: 7.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1229162187 258 LIKGGKVVNADHSFHADVYIEDGTIRQVGKDLITPGGAK--VLDAKGKLIIPGGIDTHTHM 316
Cdd:cd01308 3 LIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENvtVVDLHGKILVPGFIDQHVHI 63
|
|
| |
