|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
118-567 |
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: 739.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 197
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 198 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKdHGVNSFLVYMAFKDRFQL 277
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 278 TDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVM 357
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 358 SKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSPDpTTPDFLNSLLSCGDLQVTGSAHCTF 437
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 438 NTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDS 517
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1820048643 518 VKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSG 567
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
118-572 |
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: 677.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 197
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 198 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQL 277
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 278 TDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVM 357
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 358 SKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTF 437
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 438 NTAQK-AVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPD 516
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820048643 517 SVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 572
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
117-576 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 585.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 117 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlivpGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKA 196
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 197 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVkDHGVNSFLVYMAFKDRFQ 276
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 277 LTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKV 356
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 357 MSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCT 436
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 437 FNTAQKA-VGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDP 515
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820048643 516 DSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 576
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
115-576 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 553.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 115 SDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGT 194
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 195 KAALAGGTTMIIDHVVPEPGtSLLAAFDQWREWADsKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDR 274
Cdd:PLN02942 84 AAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 275 FQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVT 354
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 355 KVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAH 434
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 435 CTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWD 514
Cdd:PLN02942 321 CPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820048643 515 PDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 576
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
119-572 |
2.70e-123 |
|
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: 373.27 E-value: 2.70e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 119 LIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAAL 198
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 199 AGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVkDHGVNSFLVYMAFKD-RFQL 277
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 278 TDSQIYEVLSVIRDIGAIAQVHAENGDIIAEeqqRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVM 357
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 358 SKSAAEVIAQARKKGTVVYGE--P----ITAS-LGTDGSHYwsknwakaaafVTSPPLsPDPTTPDFL-NSLLScGDLQV 429
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPL-RTEEDREALwEGLAD-GTIDV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 430 TGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDAD 509
Cdd:COG0044 302 IATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADAD 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820048643 510 LVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 572
Cdd:COG0044 378 LVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
118-572 |
2.53e-119 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 364.79 E-value: 2.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPD-QGMTSADDFFQGTKA 196
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 197 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGI-QEEMEALVKDhGVNSFLVYMAFkDRF 275
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 276 QLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTK 355
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 356 VMSKSAAEVIAQARKKGTVVYGEP------ITAS-LGTDGSHywsknwakAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQ 428
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 429 VTGSAHCTFN---TAQKAVGKDN--FTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIS 503
Cdd:PRK13404 313 VFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820048643 504 VGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 572
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
118-570 |
3.31e-63 |
|
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: 216.39 E-value: 3.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 197
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 198 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWH-KGIQEEMEALVKdhGVNSFLVYMAFKD 273
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNlDQLRPLDEAGVV--GFKCFLCPSGVDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 274 RFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYV 353
Cdd:cd01315 156 FPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 354 TKVMSKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWS-------KNwakAAAFVTSPPLSpDPTTPDFLNSLLSCGD 426
Cdd:cd01315 236 VHLSSAEAVPLIREARAEGVDVTVETCP--------HYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWEALENGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 427 LQVTGSAH--CTfnTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISV 504
Cdd:cd01315 304 IDMVVSDHspCT--PELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAV 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820048643 505 GSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTlHVTEGSGRYI 570
Cdd:cd01315 382 GYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
166-544 |
4.49e-60 |
|
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: 204.93 E-value: 4.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 166 VIPGGIDVHTRFQMPDQGMTSaDDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEw 245
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 246 hkGIQEEMEALVKDHGVNSFLVYMAFK--DRFQLTDSQIYEVLSVIRDIGAIAQVHAEngdiiaeeqqrildlgitgpeg 323
Cdd:cd01302 81 --GDVTDELKKLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 324 hvlsrpeeveaeavnRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGShYWSKNWAKaaaFV 403
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 404 TSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDnFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 483
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820048643 484 VTSTNAAKVFNLYPrKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSP 544
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
111-561 |
1.98e-51 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 184.52 E-value: 1.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 111 IYDqsdrLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDF 190
Cdd:PRK06189 2 MYD----LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 191 FQGTKAALAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKgiqEEMEALVkDHGVNSFLV 267
Cdd:PRK06189 75 ATGSAALAAGGCTTYFD--MPlnsIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL---EHLRELA-EAGVIGFKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 268 YMAFK--DRFQLTDSQ-IYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIA 344
Cdd:PRK06189 149 FMSNSgtDEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 345 NQTNCPLYVTKVMSKSAAEVIAQARKKGtvvygepITASLGTdGSHY--WSKN--WAKAAAFVTSPPLSpDPTTPDFLNS 420
Cdd:PRK06189 229 QETGCPLHFVHISSGKAVALIAEAKKRG-------VDVSVET-CPHYllFTEEdfERIGAVAKCAPPLR-SRSQKEELWR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 421 LLSCGDLQVTGSAH--CTFNTAQkavgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPR 498
Cdd:PRK06189 300 GLLAGEIDMISSDHspCPPELKE----GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQ 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820048643 499 KGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLH 561
Cdd:PRK06189 375 KGRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
118-573 |
6.30e-51 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 182.93 E-value: 6.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 197
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 198 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDIT-EWhkgiqEEMEALVkDHGVNSF-LVYMA----- 270
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgNW-----DPLESLW-ERGVFALgEIFMAdstgg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 271 ---FKDRFQltdsqiyEVLSVIRDIGAIAQVHAENGDIIaEEQQRILDlGITGPEGHVLSRPEEVEAEAVNRSITIANQT 347
Cdd:PRK02382 156 mgiDEELFE-------EALAEAARLGVLATVHAEDEDLF-DELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 348 NCPLYVTKVmskSAAEVIAQARKKGTVVYGEPITASLGTDgshywskNWAKAAAFV-TSPPLSPDPTTPDFLNSLLScGD 426
Cdd:PRK02382 227 GARIHIAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRREALWERLND-GT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 427 LQVTGSAHCTFNTAQKAVG-KDnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVG 505
Cdd:PRK02382 296 IDVVASDHAPHTREEKDADiWD----APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEG 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820048643 506 SDADLVIWDPDSVKTISAKTHNSALEYNIFEGMEcrGS-PLVVISQGKIVLEDGTLHVTEGSGRYIPRK 573
Cdd:PRK02382 370 YDADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
118-571 |
4.08e-49 |
|
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: 177.96 E-value: 4.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 197
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 198 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWH-KGIQEEMEALVkdHGVNSFLVYMAFKD 273
Cdd:TIGR03178 79 AAGGITTYID--MPlnsIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNlDDLRELDEAGV--VGFKAFLSPSGDDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 274 RFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYV 353
Cdd:TIGR03178 155 FPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 354 TKVMSKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAK----AAAFVTSPPLSpDPTTPDFLNSLLSCGDLQV 429
Cdd:TIGR03178 235 VHLSSAEAVELITEAKQEGLDVTVETCP--------HYLTLTAEEvpdgGTLAKCAPPIR-DLANQEGLWEALLNGLIDC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 430 TGSAHCTFNTAQKAvgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDAD 509
Cdd:TIGR03178 306 VVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDAD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820048643 510 LVIWDPDSVKTISakthNSALEY----NIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIP 571
Cdd:TIGR03178 383 FVFVDPDESYTLT----PDDLYYrhkvSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
134-557 |
2.19e-46 |
|
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: 169.55 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 134 ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIID--HVVP 211
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADmpNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 212 EPGTSllAAFDQWREWADSKSCCDYSLHVDITEWHKGiQEEMEAlvkdhgvnSFLVYMA-----FKDRFQ--LTDSQIYE 284
Cdd:TIGR00857 83 PIDTP--ETLEWKLQRLKKVSLVDVHLYGGVTQGNQG-KELTEA--------YELKEAGavgrmFTDDGSevQDILSMRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 285 VLSVIRDIGAIAQVHAENGDIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEV 364
Cdd:TIGR00857 152 ALEYAAIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 365 IAQARKkgtvvYGEPITAS------LGTDGSHYWSKNWAKaaafvTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFN 438
Cdd:TIGR00857 229 IVKAKS-----QGIKITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 439 TAQKAVgkdNFTLIPEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDPDSV 518
Cdd:TIGR00857 298 LEEKTK---EFAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKE 372
|
410 420 430
....*....|....*....|....*....|....*....
gi 1820048643 519 KTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLED 557
Cdd:TIGR00857 373 WTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
166-551 |
1.82e-35 |
|
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: 137.47 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 166 VIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEw 245
Cdd:cd01318 4 ILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 246 hkgiQEEMEALVKdHGVNSFLVYMAfkdrfQLTDS--QIYEVLSVI-RDIGAIAQVHAENGDIIAEEQQRILDLGItgpe 322
Cdd:cd01318 81 ----SEDLEELDK-APPAGYKIFMG-----DSTGDllDDEETLERIfAEGSVLVTFHAEDEDRLRENRKELKGESA---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 323 gHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVvygePITAS--LGTDGSHYWSKNWAKaa 400
Cdd:cd01318 147 -HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTV----EVTPHhlFLDVEDYDRLGTLGK-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 401 afvTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVI---WDKAVVTGKmd 477
Cdd:cd01318 220 ---VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNKGILSLS-- 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820048643 478 enQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQG 551
Cdd:cd01318 291 --RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
165-554 |
3.58e-33 |
|
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: 130.31 E-value: 3.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 165 MVIPGGIDVHTRFQM------PDQGMTSADDFFQGTKAALAGGTTMIIDHVV--PEPGTSLLAAFDQW----REWAdsKS 232
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgiPVPPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELplglRFLG--PG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 233 CC---DYSLHVDITEWHKGIQEEMEALVKDHGVnsFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDiiAEE 309
Cdd:pfam01979 79 CSldtDGELEGRKALREKLKAGAEFIKGMADGV--VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETK--GEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 310 QQRILDLGITGPEGHVLSRPEEVeaeAVNRSITIANQTNCPLYVTkvmskSAAEVIAQARKKGTVvygepitasLGTDGS 389
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESG---GLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 390 HYWSKNWAKAAAfvtspplspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkaVGKDNFTLIPEGTNGTEERmsviwdk 469
Cdd:pfam01979 218 SKLRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 470 AVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSvktisakthnsaleYNIFEGMECRGSPLVVIS 549
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDP--------------LAAFFGLKPDGNVKKVIV 329
|
....*
gi 1820048643 550 QGKIV 554
Cdd:pfam01979 330 KGKIV 334
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
155-545 |
1.26e-32 |
|
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: 129.66 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 155 GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTmiidHVVPEPGTsllaafdqwREWADSKSCC 234
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVIDNPAVV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 235 DYSLHVD-------------ITEWHKGIQ-EEMEALvKDHGVNSFlvymaFKDRFQLTDSQI-YEVLSVIRDIGAIAQVH 299
Cdd:cd01317 66 ELLKNRAkdvgivrvlpigaLTKGLKGEElTEIGEL-LEAGAVGF-----SDDGKPIQDAELlRRALEYAAMLDLPIIVH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 300 AENGDIIAEEQqrILDLGITGPEGhVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGtvvygEP 379
Cdd:cd01317 140 PEDPSLAGGGV--MNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 380 ITASLGtdgSHYWS------KNWAkaAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIP 453
Cdd:cd01317 212 VTAEVT---PHHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 454 EGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPrkGRISVGSDADLVIWDPDSVKTISAKTHNSALEYN 533
Cdd:cd01317 283 PGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNT 360
|
410
....*....|..
gi 1820048643 534 IFEGMECRGSPL 545
Cdd:cd01317 361 PFDGQKLKGRVL 372
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
117-557 |
1.15e-31 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 128.00 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 117 RLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPDQgmTSADDFFQGTK 195
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREPGQ--EDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 196 AALAGGTTMiidhVVPEPGT----SLLAAFDQWREWADSKSCCDysLHV--DITEWHKGIQE-EMEALvKDHGVnsflvy 268
Cdd:PRK09357 79 AAAAGGFTT----VVAMPNTkpviDTPEVVEYVLDRAKEAGLVD--VLPvgAITKGLAGEELtEFGAL-KEAGV------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 269 MAFK-DRFQLTDSQI-YEVLSVIRDIG-AIAQvHAE----------NGDIIAEEqqrildLGITGpeghvlsRPEEVEAE 335
Cdd:PRK09357 146 VAFSdDGIPVQDARLmRRALEYAKALDlLIAQ-HCEdpslteggvmNEGEVSAR------LGLPG-------IPAVAEEV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 336 AVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTvvygePITA------------SLGTDGSHYwsknwaKAAafv 403
Cdd:PRK09357 212 MIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY------KVN--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 404 tsPPLSPDPTTPDFLNSLLScGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVA 483
Cdd:PRK09357 278 --PPLRTEEDREALIEGLKD-GTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLE 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820048643 484 VTSTNAAKVFNLYPrkGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLED 557
Cdd:PRK09357 352 KMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
118-532 |
5.41e-29 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 120.73 E-value: 5.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 197
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 198 LAGGTTMIIDHvvpePGTSLLAAFDqwREWADSK-SCCDYSLHVDITEWHKGIQEEMEAL--VKDHGVNSFLVYMAF-KD 273
Cdd:PRK08044 81 AKGGITTMIEM----PLNQLPATVD--RASIELKfDAAKGKLTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 274 R-----FQ-LTDSQIYEVLSVIRDIGAIAQVHAENG---DIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRSITIA 344
Cdd:PRK08044 155 RgidndFRdVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKR---EGRVTAHDYVASRPVFTEVEAIRRVLYLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 345 NQTNCPLYVTKVMSKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAKAAAFVT----SPPLSPDPTTPDFLNS 420
Cdd:PRK08044 232 KVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 421 LLScGDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKG 500
Cdd:PRK08044 304 LFN-GEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKG 378
|
410 420 430
....*....|....*....|....*....|..
gi 1820048643 501 RISVGSDADLVIWDPDSvktiSAKTHNSALEY 532
Cdd:PRK08044 379 RIAPGKDADFVFIQPNS----SYVLKNEDLEY 406
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
115-558 |
1.17e-27 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 116.31 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 115 SDRLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQG 193
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 194 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITewhkgiQEEMEALVKDHGVNSFLVYMAFKD 273
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT------PDNLPELLTANPTCGIKIFMGSSH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 274 RFQLTDSQiyEVLSVI--RDIGAIAqVHAENGDIIAEEQQRILdlGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPL 351
Cdd:PRK07575 154 GPLLVDEE--AALERIfaEGTRLIA-VHAEDQARIRARRAEFA--GISDPADHSQIQDEEAALLATRLALKLSKKYQRRL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 352 YVTKVMSKSAAEVIAQArkKGTVVYGEPITASLGTDGSHYwsknwAKAAAFVT-SPPLSpDPTTPDFLNSLLSCGDLQVT 430
Cdd:PRK07575 229 HILHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAY-----ERIGTLAQmNPPLR-SPEDNEALWQALRDGVIDFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 431 GSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVIWDKAVvTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDADL 510
Cdd:PRK07575 301 ATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADL 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1820048643 511 VIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDG 558
Cdd:PRK07575 376 VLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
118-568 |
2.13e-26 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 112.71 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 197
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 198 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITewHKGIQE--EMEALVKDHGVNsflVYM--AFKD 273
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGT--RDNADElaELERLPGCAGIK---VFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 274 RFQLTDSQIYEVLSVIRDIGAiaqVHAENGDIIAEEQqrilDLGITG-PEGHVLSRPEEVEAEAVNRSITIANQTNCPLY 352
Cdd:PRK09060 159 LLVEDDEGLRRILRNGRRRAA---FHSEDEYRLRERK----GLRVEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 353 VTKVMSKSAAEVIAQARKKGTV--------VYGEPITASLGTdgshYWSKNwakaaafvtsPPLSpDPTTPDFLNSLLSC 424
Cdd:PRK09060 232 VLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT----LAQMN----------PPIR-DARHRDGLWRGVRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 425 GDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKaVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISV 504
Cdd:PRK09060 297 GVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAV 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820048643 505 GSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGR 568
Cdd:PRK09060 372 GYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
123-572 |
1.74e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 109.56 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 123 GKIVNDDQSFYADIYMEDGLIKQIGENLivpGGVKTIEAHSrMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGT 202
Cdd:PRK01211 5 GNFYYKGKFDYLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 203 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHvditewhkgiqeEME----ALVKDHGVNSFLVYMAFKDRFQLT 278
Cdd:PRK01211 79 TFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLY------------SMEtgnnALILDERSIGLKVYMGGTTNTNGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 279 DSQIYEVlSVIRDIGAIAQVHAENGDIIAEEQQRILDLgitgpEGHVLSRPEEVEAEAVNRSITIANQtncplyvTKVMS 358
Cdd:PRK01211 147 DIEGGEI-KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 359 -KSAAEVIAQARKKGT----VVYGEpitASLGTDGShywsknwakaaafvTSPPLSPDPTTPDFLNSLLScGDLQVTGSA 433
Cdd:PRK01211 214 hVSSIDVIGRFLREVTphhlLLNDD---MPLGSYGK--------------VNPPLRDRWTQERLLEEYIS-GRFDILSSD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 434 HCTFNTAQKAvgkdNFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLypRKGRISVGSDADLVIW 513
Cdd:PRK01211 276 HAPHTEEDKQ----EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAF 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820048643 514 DPDSVKTISAKTHNSALEYNIFEGMECRgSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 572
Cdd:PRK01211 349 DFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPK 405
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
123-570 |
3.69e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 108.32 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 123 GKIVNDDQSFYADIYMEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTRFQmpDQGMTSADDFFQGTKAALAGGT 202
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR--DFEESYKETIESGTKAALHGGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 203 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSflVYMAFKDRFQLTDSQI 282
Cdd:PRK04250 80 TLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGAS--TGGIFSENFEVDYACA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 283 YEVLSvirdigaiaqVHAENGDIIAEEqqrildlgitgPEghvlsRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAA 362
Cdd:PRK04250 158 PGIVS----------VHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTKDGL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 363 EVIAQARKKGTVVYGEPitaslgtdgSH--YWSKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDlqVTGSAHCTFNTA 440
Cdd:PRK04250 212 KLILKSNLPWVSFEVTP---------HHlfLTRKDYERNPLLKVYPPLR-SEEDRKALWENFSKIP--IIASDHAPHTLE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 441 QKAVGKdnftlipEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNlYPRKGrISVGSDADLVIWDPDSVKT 520
Cdd:PRK04250 280 DKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEWT 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1820048643 521 ISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYI 570
Cdd:PRK04250 350 IKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI-IGKPRGVRI 398
|
|
| PLN02795 |
PLN02795 |
allantoinase |
115-573 |
4.25e-24 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 106.40 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 115 SDRLLIKGGKIVNDdqsfyadIYMEDGLIKQIGENLIVPG---GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFF 191
Cdd:PLN02795 50 SKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 192 QGTKAALAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKsccdysLHVDITEWHKGIQE------EMEALVkDHGV 262
Cdd:PLN02795 121 TGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 263 ---NSFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLgiTGPEGHVLSRPEEVEAEAVNR 339
Cdd:PLN02795 192 lglKSFMCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADP--RSYSTYLKSRPPSWEQEAIRQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 340 SITIANQTN-------CPLYVTKVM-SKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWsknwAKAAA--------FV 403
Cdd:PLN02795 270 LLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 404 TSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGkMDENQFVA 483
Cdd:PLN02795 338 CAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLAR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 484 VTSTNAAKVFNLyPRKGRISVGSDADLVIWDP------DSVKTISAKTHN-SAleyniFEGMECRGSPLVVISQGKIVLE 556
Cdd:PLN02795 416 WWSERPAKLAGL-DSKGAIAPGKDADIVVWDPeaefvlDESYPIYHKHKSlSP-----YLGTKLSGKVIATFVRGNLVFL 489
|
490
....*....|....*..
gi 1820048643 557 DGtLHVTEGSGRYIPRK 573
Cdd:PLN02795 490 EG-KHAKQACGSPILAK 505
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
116-239 |
1.24e-16 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 83.00 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 116 DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGID--VHTRfqmpDQGMTSADDFFQG 193
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDdqVHFR----EPGLTHKGDIASE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1820048643 194 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLH 239
Cdd:PRK09236 78 SRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFY 123
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
114-523 |
6.77e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 67.68 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 114 QSDRLLIKGGKIVNDDQSFY---ADIYMEDGLIKQIGEN--LIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPD------- 181
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGgravefe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 182 --QGMTSADDFFQGT----KAALAGGTTMIIDHvvpePGTSL----------LAAFDQWREWADSKSccdyslhVDITE- 244
Cdd:COG1228 86 agGGITPTVDLVNPAdkrlRRALAAGVTTVRDL----PGGPLglrdaiiageSKLLPGPRVLAAGPA-------LSLTGg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 245 WHKGIQEEMEALV---KDHGVNSFLVYMAFKDRfQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIaeeqQRILDLGITGP 321
Cdd:COG1228 155 AHARGPEEARAALrelLAEGADYIKVFAEGGAP-DFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 322 EgHVLSRPEeveaeavnrsitianqtncplyvtkvmsksaaEVIAQARKKGTVVYGePiTASLGTDGSHYWSKNWAKAAA 401
Cdd:COG1228 230 E-HGTYLDD--------------------------------EVADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKAR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 402 FVtspplspDPTTPDFLNSLLSCGdlqvtgsahCTFntaqkAVGKD-NFTLIPEGTNGTEERMsviwdkaVVTGKMDENQ 480
Cdd:COG1228 275 KV-------REAALANARRLHDAG---------VPV-----ALGTDaGVGVPPGRSLHRELAL-------AVEAGLTPEE 326
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1820048643 481 -FVAVTStNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISA 523
Cdd:COG1228 327 aLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
118-568 |
1.86e-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: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVndDQS----FYADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDF--- 190
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHY---DGQVFWDPDLrps 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 191 -FQGTKAALAG------------GTTMIIDHVVPEPGTSLLAAFDqWREWAD-------SKSCCDYSLHV---DITEWHK 247
Cdd:cd01297 76 sRQGVTTVVLGncgvspapanpdDLARLIMLMEGLVALGEGLPWG-WATFAEyldaleaRPPAVNVAALVghaALRRAVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 248 GI---------QEEMEALVKDH------GVNSFLVYMafkDRFQLTDSQIYEVLSVIRDIGAIAQVHaengdiIAEEQQR 312
Cdd:cd01297 155 GLdareateeeLAKMRELLREAleagalGISTGLAYA---PRLYAGTAELVALARVAARYGGVYQTH------VRYEGDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 313 ILdlgitgpeghvlsrpeeveaEAVNRSITIANQTNCPLYVT--KVMSKS-------AAEVIAQARKKGTVVYGE--PIT 381
Cdd:cd01297 226 IL--------------------EALDELLRLGRETGRPVHIShlKSAGAPnwgkidrLLALIEAARAEGLQVTADvyPYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 382 ASLGTDgshywsknwakAAAFVTSPPlspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkavgkdnftlipeGTNGTEE 461
Cdd:cd01297 286 AGSEDD-----------VRRIMAHPV-------------VMGGSDGGALGKPHP-------------------RSYGDFT 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 462 RMSVIWdkAVVTGKMDENQFVAVTSTNAAKVFNLYPRkGRISVGSDADLVIWDPDSVK---TISAKTHNSaleynifEGM 538
Cdd:cd01297 323 RVLGHY--VRERKLLSLEEAVRKMTGLPARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------EGI 392
|
490 500 510
....*....|....*....|....*....|
gi 1820048643 539 EcrgspLVVISqGKIVLEDGtLHVTEGSGR 568
Cdd:cd01297 393 E-----AVLVN-GVPVVRDG-AFTGARPGR 415
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
118-560 |
3.40e-10 |
|
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: 62.60 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQS---FYADIYMEDGLIKQIGENLIVPG--GVKTIEAHSRMVIPGGIDVHTRFQM------------- 179
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 180 --------PDQGMTSADDFFQGTKAALA----GGTTMIIDHVVPEPGTSLLAA-------------FDQWREWADSKS-C 233
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDAVAEAAeelgiravlgrgiMDLGTEDVEETEeA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 234 CDYSLHVdITEWHKGIQEEMEALVKDHGVNSflvymafkdrfqLTDSQIYEVLSVIRDIGAIAQVH-AENGDIIAEEQQR 312
Cdd:cd01298 161 LAEAERL-IREWHGAADGRIRVALAPHAPYT------------CSDELLREVAELAREYGVPLHIHlAETEDEVEESLEK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 313 --------ILDLGITGPE---GH-VLSRPEEVEaeavnrsitIANQTN-----CPlyvTKVMsKSAAEV--IAQARKKGt 373
Cdd:cd01298 228 ygkrpveyLEELGLLGPDvvlAHcVWLTDEEIE---------LLAETGtgvahNP---ASNM-KLASGIapVPEMLEAG- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 374 vvygepITASLGTDGShywsknwakaaafvtspplspdpttpdflnsllSCGD-LQVTGSAHCTFNTaQKAVGKDNFTLI 452
Cdd:cd01298 294 ------VNVGLGTDGA---------------------------------ASNNnLDMFEEMRLAALL-QKLAHGDPTALP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 453 PEgtngteermsviwdkavvtgkmdenQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEY 532
Cdd:cd01298 334 AE-------------------------EALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVY 387
|
490 500 510
....*....|....*....|....*....|
gi 1820048643 533 NifegmeCRGSP--LVVISqGKIVLEDGTL 560
Cdd:cd01298 388 S------ANGGDvdTVIVN-GRVVMEDGEL 410
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
167-567 |
8.45e-10 |
|
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: 60.93 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 167 IPGGIDVHTrfQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDIT--E 244
Cdd:cd01316 5 LPGLIDVHV--HLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATstN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 245 WHKGIQeemealVKDHGVNS-FLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAqVHAENGDIIAeeqqrILDLgitgpeg 323
Cdd:cd01316 83 AATVGE------LASEAVGLkFYLNETFSTLILDKITAWASHFNAWPSTKPIV-THAKSQTLAA-----VLLL------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 324 hvlsrpeeveAEAVNRSITIANqtncplyvtkVMSKSAAEVIAQARKKGTVVYGEPITASLgtdgshYWSKNWAKAAAFV 403
Cdd:cd01316 144 ----------ASLHNRSIHICH----------VSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 404 TSPPLsPDPTTPDFLNSLLSCGDLQVTGSAHCTFntAQKAVGKdnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 483
Cdd:cd01316 198 VRPFL-PTREDQEALWENLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDIVD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 484 VTSTNAAKVFNLYPrkgrisvgsDADLVI-WDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHV 562
Cdd:cd01316 269 RLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 1820048643 563 TEGSG 567
Cdd:cd01316 340 PPGFG 344
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
136-556 |
4.68e-08 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 55.86 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 136 IYMEDGLIKQIGENLivpGGVKTIEAHSRMVIPGGIDVHTRfqMPDQGMtSADDFFQGTKAALAGGttmiIDHVVPEPGT 215
Cdd:PRK08417 1 IRIKDGKITEIGSDL---KGEEILDAKGKTLLPALVDLNVS--LKNDSL-SSKNLKSLENECLKGG----VGSIVLYPDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 216 SllaafdqwrewadsKSCCD-YSLhvditEWHKGIQEEMEalvkdhgVNSFLVYMAFKDRFQLTDsqiyevLSVIRDIGA 294
Cdd:PRK08417 71 T--------------PAIDNeIAL-----ELINSAQRELP-------MQIFPSIRALDEDGKLSN------IATLLKKGA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 295 IAqVHAE---NGDI---IAEEQQR------------------ILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCP 350
Cdd:PRK08417 119 KA-LELSsdlDANLlkvIAQYAKMldvpifcrcedssfddsgVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 351 LYVTKVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHywSKNWAKAAAFvtSPPLSpDPTTPDFLNSLLSCGDLQVT 430
Cdd:PRK08417 198 VLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSA--CENFNTAAKL--NPPLR-SKEDRLALLEALKEGKIDFL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 431 GSAHC-TFNTAQKAVgkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLypRKGRISVGSDAD 509
Cdd:PRK08417 273 TSLHSaKSNSKKDLA----FDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEAD 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1820048643 510 LVIWDPDSVKTISAKthnsaleYNIFEGMECRGSPLVVISQGKIVLE 556
Cdd:PRK08417 347 LVLFDPNESTIIDDN-------FSLYSGDELYGKIEAVIIKGKLYLE 386
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
118-516 |
6.32e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 55.28 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTrfqmpdqgmtsaddffQGtkaa 197
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHI----------------HG---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 198 lAGGttmiidhvvpepgtsllAAFDQWRewadsksccdyslhvditewHKGIQEEMEALVKdHGVNSFLVYMafkdrfqL 277
Cdd:cd00854 61 -GGG-----------------ADFMDGT--------------------AEALKTIAEALAK-HGTTSFLPTT-------V 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 278 TDS--QIYEVLSVIRD-----IGA-IAQVHAEnGDIIAEEQqrildlgiTG--PEGHVLS-RPEEVE-----AEAVNRSI 341
Cdd:cd00854 95 TAPpeEIAKALAAIAEaiaegQGAeILGIHLE-GPFISPEK--------KGahPPEYLRApDPEELKkwleaAGGLIKLV 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 342 TIANQTncplyvtkvmsKSAAEVIAQARKKGtvvygepITASLG-TDGSHYWSKNWAKAAA-FVTS-----PPLS---PD 411
Cdd:cd00854 166 TLAPEL-----------DGALELIRYLVERG-------IIVSIGhSDATYEQAVAAFEAGAtHVTHlfnamSPLHhrePG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 412 PTTPDFLNSLLSCG---DLQvtgsaHC---TFNTAQKAVGKDNFTLI---------PEGT---NGTEERM---------- 463
Cdd:cd00854 228 VVGAALSDDDVYAEliaDGI-----HVhpaAVRLAYRAKGADKIVLVtdamaaaglPDGEyelGGQTVTVkdgvarladg 302
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820048643 464 ----SVI-WDKAVVT----GKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPD 516
Cdd:cd00854 303 tlagSTLtMDQAVRNmvkwGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
117-321 |
3.01e-07 |
|
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: 53.29 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 117 RLLIKGGKIV--NDDQSFYAD--IYMEDGLIKQIGENLIVP---GGVKTIEAHSRMVIPGGIDVHTR-FQMPDQGMTSAD 188
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 189 DFFQ--------------------GTKAA----LAGGTTMIIDHvvpepGTSLLAAFDQWREWAD--------SKSCCDY 236
Cdd:COG0402 81 PLLDwleeyiwplearldpedvyaGALLAlaemLRSGTTTVADF-----YYVHPESADALAEAAAeagiravlGRGLMDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 237 SLHVDITEWHKGIQEEMEALVKD-HGVNSFLVYMAFKDRF--QLTDSQIYEVLSVIRDIGAIAQVH-----AENGDIIAE 308
Cdd:COG0402 156 GFPDGLREDADEGLADSERLIERwHGAADGRIRVALAPHApyTVSPELLRAAAALARELGLPLHTHlaetrDEVEWVLEL 235
|
250
....*....|....*..
gi 1820048643 309 EQQRILD----LGITGP 321
Cdd:COG0402 236 YGKRPVEyldeLGLLGP 252
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
482-516 |
8.06e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 51.64 E-value: 8.06e-07
10 20 30
....*....|....*....|....*....|....*
gi 1820048643 482 VAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPD 516
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
134-525 |
1.07e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 51.53 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 134 ADIYMEDGLIKQIGENLI-VPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTM--IIDHVV 210
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRvaILPDTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 211 P---EPGTslLAAFDQ---------WREWAD-SKSCCDYSLhvdiTEWhkgiQEEMEAlvkdhGVNSFlvymafkdrfql 277
Cdd:PRK07369 100 PpldNPAT--LARLQQqaqqippvqLHFWGAlTLGGQGKQL----TEL----AELAAA-----GVVGF------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 278 TDSQIYEVLSVIRDIGAIAQVH-------------AENGdiIAEEQQRILDLGITGpeghvlsRPEEVEAEAVNRSITIA 344
Cdd:PRK07369 153 TDGQPLENLALLRRLLEYLKPLgkpvalwpcdrslAGNG--VMREGLLALRLGLPG-------DPASAETTALAALLELV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 345 NQTNCPLYVTKVMSKSAAEVIAQARKKGTvvygePITAS-------LGT-DGSHYwSKNWAKAaafvtsPPLsPDPTTPD 416
Cdd:PRK07369 224 AAIGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD------PPL-GNPSDRQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 417 FLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLY 496
Cdd:PRK07369 291 ALIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQE 367
|
410 420
....*....|....*....|....*....
gi 1820048643 497 PRkgRISVGSDADLVIWDPDSVKTISAKT 525
Cdd:PRK07369 368 PP--SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
118-190 |
1.13e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.39 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVNDDQSFYA--DIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT--------RFQMP------- 180
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVhvypgstpYGDEPdevgvrs 80
|
90
....*....|....*.
gi 1820048643 181 ------DQGMTSADDF 190
Cdd:PRK09237 81 gvttvvDAGSAGADNF 96
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
99-575 |
1.92e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 50.85 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 99 IRRASGKEALQNIYDQSDRLLIKGGKIVNDDQSFYA--DIYMEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTr 176
Cdd:PRK09061 2 AKVAVLSLLLMPASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 177 fqmpdQGMTSADDFFQgtkaALAGGTTMIidhvVPEPGTSLLAAFdqWREWADSKSCCDYSLHVDiteWHKGIQEEMEAL 256
Cdd:PRK09061 79 -----HGQSVAAYRMQ----AFDGVTTAL----ELEAGVLPVARW--YAEQAGEGRPLNYGASVG---WTPARIAVLTGP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 257 VKDHGVNSFLVYMaFKDRFQ---LTDSQIYEVLSVIR---DIGAIAqVHAENGDIIAEEQQRILDLG-ITGPEG-----H 324
Cdd:PRK09061 141 QAEGTIADFGKAL-GDPRWQeraATPAELAEILELLEqglDEGALG-IGIGAGYAPGTGHKEYLELArLAARAGvptytH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 325 V--LSRPE-EVEAEAVNRSITIANQTNCPLYVTKVMSKS------AAEVIAQARKKGTVV------YGEPITAsLGTD-- 387
Cdd:PRK09061 219 VryLSNVDpRSSVDAYQELIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVtteaypYGAGSTV-VGAAff 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 388 --------GSHYWSKNW----------AKAAAFVTSPPLSP---------DPTTPDFLNSLLSCGDLQVTGSAHCTFNTA 440
Cdd:PRK09061 298 dpgwlermGLGYGSLQWvetgerlltrEELAKLRANDPGGLvlihfldedNPRDRALLDRSVLFPGAAIASDAMPWTWSD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 441 QKAVGKDNFTLIPEG-----TNGT---------EERMSVIWDKAVvtGKMdenqfvavtSTNAAKVFNLY----PRKGRI 502
Cdd:PRK09061 378 GTVYEGDAWPLPEDAvshprSAGTfarflreyvRERKALSLLEAI--RKC---------TLMPAQILEDSvpamRRKGRL 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820048643 503 SVGSDADLVIWDPDSVK---TISAKTHNSaleynifEGMEcrgsplVVISQGKIVLEDGTLHVTEGSGRYIpRKPF 575
Cdd:PRK09061 447 QAGADADIVVFDPETITdraTFEDPNRPS-------EGVR------HVLVNGVPVVSNGELVRDARPGRPV-RRPV 508
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
119-175 |
3.53e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 46.63 E-value: 3.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820048643 119 LIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENliVPGGVKTIEAHSRMVIPGGIDVHT 175
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHV 56
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
482-537 |
7.13e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.99 E-value: 7.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820048643 482 VAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEG 537
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
117-214 |
1.07e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 45.05 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 117 RLLIKGGKIVN-----DDQsfyADIYMEDGLIKQIGEnliVPGGV---KTIEAHSRMVIPGGIDVHTRFQMPdqGMTSAD 188
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90 100 110
....*....|....*....|....*....|.
gi 1820048643 189 DFFQGTKAALAGGTTMII-----DHVVPEPG 214
Cdd:PRK07627 74 TLESEMAAAVAGGVTSLVcppdtDPVLDEPG 104
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
118-175 |
1.41e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 44.80 E-value: 1.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820048643 118 LLIKGGKI------VNDDQsfyADIYMEDGlikQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 175
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHT 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
117-204 |
2.93e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 43.63 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 117 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvkTIEAHSRMVIPGGIDVHT----RFQMP--------DQGM 184
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHTdnleKHLAPrpgvdwpaDAAL 80
|
90 100
....*....|....*....|
gi 1820048643 185 TSADdffqgTKAALAGGTTM 204
Cdd:PRK15446 81 AAHD-----AQLAAAGITTV 95
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
484-524 |
3.51e-04 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 43.53 E-value: 3.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1820048643 484 VTSTNAAKVFNLYPrKGRISVGSDADLVIWDPD-SVKTISAK 524
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKDlDINSVIAK 370
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
457-517 |
3.93e-04 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 43.40 E-value: 3.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820048643 457 NGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDS 517
Cdd:cd01296 291 SSPTSSMPLVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPS 351
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
120-202 |
4.06e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 43.35 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 120 IKGGKIVNDDQSFYADiyMEDGlikqIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSaddFFQGTKAALA 199
Cdd:PRK13985 87 IKDGKIAGIGKGGNKD--MQDG----VKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTA---FASGVTTMIG 157
|
...
gi 1820048643 200 GGT 202
Cdd:PRK13985 158 GGT 160
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
118-179 |
4.70e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 43.25 E-value: 4.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820048643 118 LLIKGGKIVNDD--QSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQM 179
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
116-213 |
7.61e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 42.30 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 116 DRLLIKGGKIVNDDQSF----YADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVH-------TRFQMPD--- 181
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHrhtwqsvLRGIGADwtl 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1820048643 182 -----------QGMTSADDFFQGTKA----ALAGGTTMIID--HVVPEP 213
Cdd:PRK08204 81 qtyfreihgnlGPMFRPEDVYIANLLgaleALDAGVTTLLDwsHINNSP 129
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
134-206 |
1.66e-03 |
|
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: 41.55 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 134 ADIYMEDGLIKQIG------------ENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGG 201
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQ-----------IEEALASG 151
|
....*
gi 1820048643 202 TTMII 206
Cdd:cd00375 152 ITTMI 156
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
140-516 |
2.17e-03 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 40.76 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 140 DGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT---------RFQMPDQGMTSAD--------DFFQ----GTKAAL 198
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHShlgldeeggVRETSDANEETDPvtphvraiDGINpddeAFKRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 199 AGGTTmiidHVVPEPGTSLLAAfdqwREWADSKSccdyslhvditewhKGIQEEMEALVKDHGVNSFLVYMAFK--DRFQ 276
Cdd:cd01309 81 AGGVT----TVQVLPGSANLIG----GQGVVIKT--------------DGGTIEDMFIKAPAGLKMALGENPKRvyGGKG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 277 LTDSQIYEVLSVIRDIGAIAQvhaengdiiaeEQQRILDLGITGPEGHVLSRPE-EVEAEAVNRSITIanqtncplyvtK 355
Cdd:cd01309 139 KEPATRMGVAALLRDAFIKAQ-----------EYGRKYDLGKNAKKDPPERDLKlEALLPVLKGEIPV-----------R 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 356 VMSKSAAE---VIAQARKkgtvvYGEPITASLGTDGsHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLlscgdlqvtgs 432
Cdd:cd01309 197 IHAHRADDiltAIRIAKE-----FGIKITIEHGAEG-YKLADELAKHGIPVIYGPTLTLPKKVEEVNDA----------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 433 ahcTFNTAQ-KAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTStNAAKVFNLYPRKGRISVGSDADLV 511
Cdd:cd01309 260 ---IDTNAYlLKKGGVAFAISSDHPVLNIRNLNLEAAKAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLV 335
|
....*
gi 1820048643 512 IWDPD 516
Cdd:cd01309 336 VWNGD 340
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
431-514 |
2.34e-03 |
|
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: 40.77 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 431 GSAHCTFNTAQKAVGKDnftLIPEgTNGTE----ERMSV-IWDKAVVTGK-----MDENQFVAVTSTNAAKVFNLyPRKG 500
Cdd:cd01307 226 GTASFSFRVARAAIAAG---LLPD-TISSDihgrNRTNGpVYALATTLSKllalgMPLEEVIEAVTANPARMLGL-AEIG 300
|
90
....*....|....
gi 1820048643 501 RISVGSDADLVIWD 514
Cdd:cd01307 301 TLAVGYDADLTVFD 314
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
134-175 |
2.68e-03 |
|
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: 40.69 E-value: 2.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1820048643 134 ADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 175
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHI 56
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
484-568 |
2.74e-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: 40.86 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 484 VTSTNAAKVFNLyPRKGRISVGSDADLVIW--DPDSVKTISAKTHNSALEYnifegmecrgsPLVVISQGKIVLEDGTLh 561
Cdd:cd01304 435 MTRAGPAKLLGL-SDKGHLGVGADADIAIYddDPDQVDPSDYEKVEKAFSR-----------AAYVLKDGEIVVKDGEV- 501
|
....*..
gi 1820048643 562 VTEGSGR 568
Cdd:cd01304 502 VAEPWGR 508
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
118-207 |
3.19e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.47 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 118 LLIKGGKIVN--DDQSFYADIYMEDGLIKQIGEnlIVPGGVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDFfqgTK 195
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHI---ESSMVTPAEF---AR 78
|
90
....*....|...
gi 1820048643 196 AALAGGTT-MIID 207
Cdd:COG1001 79 AVLPHGTTtVIAD 91
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
134-205 |
3.97e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 40.46 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 134 ADIYMEDGLIKQIG------------ENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGG 201
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQL-----------VDHALASG 155
|
....*
gi 1820048643 202 -TTMI 205
Cdd:PRK13308 156 iTTML 160
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
489-574 |
4.16e-03 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 40.16 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820048643 489 AAKVFNLYPRkGRISVGSDADLVIWDPDSVKtiSAKTHNSALEYNifEGMECrgsplVVISqGKIVLEDGTlHVTEGSGR 568
Cdd:COG3653 453 PADRLGLKDR-GLLRPGYRADLVVFDPATLA--DRATFDLPAQRA--DGIRA-----VIVN-GVVVVEDGK-PTGARPGR 520
|
....*.
gi 1820048643 569 YIPRKP 574
Cdd:COG3653 521 VLRGGG 526
|
|
| |
