|
Name |
Accession |
Description |
Interval |
E-value |
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-423 |
0e+00 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 694.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 1 MNYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAA 80
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 81 AKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASM 160
Cdd:PRK09357 81 AAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQDARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 161 MLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRV 240
Cdd:PRK09357 161 MRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 241 IRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERA 320
Cdd:PRK09357 241 IRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 321 PFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTP 400
Cdd:PRK09357 321 PFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTP 400
|
410 420
....*....|....*....|...
gi 1208968218 401 FAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK09357 401 FIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-422 |
0e+00 |
|
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: 605.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITA-DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAK 82
Cdd:COG0044 1 LIKNGRVVDPGGLERA-DVLIEDGRIAAIGPDLAApEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 83 GGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQaGSEMTDFETLKELGAFAF-----TDDGVGVQD 157
Cdd:COG0044 80 GGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAVAFkvfmgSDDGNPVLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 158 ASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGS 237
Cdd:COG0044 159 DGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 238 VRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGI 317
Cdd:COG0044 239 VELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKELPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 318 ERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLE-AGRLKEGRTADITIIDLEQEEEIDPTTFLSKG 396
Cdd:COG0044 319 AEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLPrKGRIAVGADADLVLFDPDAEWTVTAEDLHSKS 398
|
410 420
....*....|....*....|....*.
gi 1208968218 397 KNTPFAGWKCQGWPVMTIVGGKIAWQ 422
Cdd:COG0044 399 KNTPFEGRELTGRVVATIVRGRVVYE 424
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
40-413 |
0e+00 |
|
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: 514.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 40 NAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNV 119
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 120 LPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKH 199
Cdd:cd01317 81 LPIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 200 GLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPP 279
Cdd:cd01317 161 GLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 280 LRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPAD 359
Cdd:cd01317 241 LRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1208968218 360 TFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMT 413
Cdd:cd01317 321 ILGLPPGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
15-420 |
7.77e-179 |
|
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: 505.05 E-value: 7.77e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 15 GKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNT 94
Cdd:TIGR00857 1 GKETEVDILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 95 RPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFA--FTDDGVGVQDASMMLAAMKRAAKLN 172
Cdd:TIGR00857 81 KPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGrmFTDDGSEVQDILSMRRALEYAAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 173 MAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVT 252
Cdd:TIGR00857 161 VPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 253 AEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFP 332
Cdd:TIGR00857 241 AEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 333 LLYtNLVKKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPV 411
Cdd:TIGR00857 321 LLL-QLLVKGLISLKDLIRMLSINPARIFGLpDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPI 399
|
....*....
gi 1208968218 412 MTIVGGKIA 420
Cdd:TIGR00857 400 ATILRGKVV 408
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
21-418 |
1.06e-110 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 332.38 E-value: 1.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 21 DLLVQDGKIAKVAENITA----DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRP 96
Cdd:PRK09059 24 TVLIEDGVIVAAGKGAGNqgapEGAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 97 VPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVV 176
Cdd:PRK09059 104 VIDDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEEMTEFGLLRAAGAVAFTDGRRSVANTQVMRRALTYARDFDAVIV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 177 AHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVT 256
Cdd:PRK09059 184 HETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 257 PHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKaqgieRAPF-----GITGFETAF 331
Cdd:PRK09059 264 INHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTK-----RLPFseaaaGAIGLETLL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 332 PLLYtNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPV 411
Cdd:PRK09059 339 AAAL-RLYHNGEVPLLRLIEALSTRPAEIFGLPAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVV 417
|
....*..
gi 1208968218 412 MTIVGGK 418
Cdd:PRK09059 418 RTIVAGK 424
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
48-417 |
2.34e-105 |
|
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: 316.20 E-value: 2.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 48 GKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITv 127
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 128 rqagsemtDFETLKELGAFA------FTDDGVGvqDASMMLAAMKRAAKLNMAVVA-HCEENTLINKgcvHEGKFSEKHG 200
Cdd:cd01318 80 --------GSEDLEELDKAPpagykiFMGDSTG--DLLDDEETLERIFAEGSVLVTfHAEDEDRLRE---NRKELKGESA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 201 LNGIPS-VCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKragIKVTAEVTPHHLVLCEDDIPSADPNFKMNPP 279
Cdd:cd01318 147 HPRIRDaEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAK---PGVTVEVTPHHLFLDVEDYDRLGTLGKVNPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 280 LRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLyTNLVKKGIITLEQLIQFLTEKPAD 359
Cdd:cd01318 224 LRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLM-LTLVNKGILSLSRVVRLTSHNPAR 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1208968218 360 TFGLE-AGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGG 417
Cdd:cd01318 303 IFGIKnKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-425 |
4.57e-99 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 303.11 E-value: 4.57e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 1 MNYLFKNGRyMNEEGKIVATDLLVQDGKIAKVAENITADNAE-VIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA 79
Cdd:PRK02382 2 RDALLKDGR-VYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEeVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 80 AAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITvrqagSEMTDFETLKELGAFAF-------TDDG 152
Cdd:PRK02382 81 AAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVT-----GNWDPLESLWERGVFALgeifmadSTGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 153 VGVqDASMMLAAMKRAAKLNMAVVAHCEENTLINkgcvhEGKFSEKHGLNG------IPSVCESVHIARDILLAEAADCH 226
Cdd:PRK02382 156 MGI-DEELFEEALAEAARLGVLATVHAEDEDLFD-----ELAKLLKGDADAdawsayRPAAAEAAAVERALEVASETGAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 227 YHVCHVSTKGSVRVIRDAKragikVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHA 306
Cdd:PRK02382 230 IHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 307 PHTAEEKAQGIERAPFGITGFETAFPLLYTNlVKKGIITLEQLIQFLTEKPADTFGLEA-GRLKEGRTADITIIDLEQEE 385
Cdd:PRK02382 305 PHTREEKDADIWDAPSGVPGVETMLPLLLAA-VRKNRLPLERVRDVTAANPARIFGLDGkGRIAEGYDADLVLVDPDAAR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1208968218 386 EIDPTTFLSKGKNTPFAGWKCQgWPVMTIVGGKIAWQKES 425
Cdd:PRK02382 384 EIRGDDLHSKAGWTPFEGMEGV-FPELTMVRGTVVWDGDD 422
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
2-428 |
1.32e-94 |
|
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: 291.50 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 2 NYLFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENIT-ADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAA 80
Cdd:cd01315 1 DLVIKNGRVVTPDGVREA-DIAVKGGKIAAIGPDIAnTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 81 AKGGFTTICAMP-NTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAgsemTDFETLKELGAFAF--------TDD 151
Cdd:cd01315 80 AAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNL----DQLRPLDEAGVVGFkcflcpsgVDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 152 GVGVQDASMMLAaMKRAAKLNMAVVAHCEeNTLINKGCVHEGKFSEKHG----LNGIPSVCESVHIARDILLAEAADCHY 227
Cdd:cd01315 156 FPAVDDEQLEEA-MKELAKTGSVLAVHAE-NPEITEALQEQAKAKGKRDyrdyLASRPVFTEVEAIQRILLLAKETGCRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 228 HVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAP 307
Cdd:cd01315 234 HIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 308 HTAEEKAQGIE---RAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEA--GRLKEGRTADITIIDLE 382
Cdd:cd01315 314 CTPELKLLGKGdffKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHqkGRIAVGYDADFVVWDPE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1208968218 383 QEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKESALV 428
Cdd:cd01315 394 EEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVG 439
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
20-408 |
2.95e-91 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 281.87 E-value: 2.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 20 TDLLVQDGKIAKVAENI--TADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPV 97
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIdpIPPDTQIIDASGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 98 PDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDdGVGVQDASMMLAAMKRAAKLNMAVVA 177
Cdd:PRK07369 102 LDNPATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTELAELAAAGVVGFTD-GQPLENLALLRRLLEYLKPLGKPVAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 178 HCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTP 257
Cdd:PRK07369 181 WPCDRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 258 HHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTN 337
Cdd:PRK07369 261 MHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVAFAEAPPGAIGLELALPLLWQN 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208968218 338 LVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQG 408
Cdd:PRK07369 341 LVETGELSALQLWQALSTNPARCLGQEPPSLAPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKG 411
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
49-413 |
3.16e-91 |
|
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: 279.28 E-value: 3.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 49 KLIAPGLVDVHVHLREPG-GEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITV 127
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGgTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 128 RQAGSEMT-----DFETLKELGAFAFTDDgVGVQDASMMLAAMKrAAKLNMAVVAHCEentlinkgcvhegkfsekhgln 202
Cdd:cd01302 81 GDVTDELKklfdaGINSLKVFMNYYFGEL-FDVDDGTLMRTFLE-IASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 203 gipsvcesvhiaRDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRG 282
Cdd:cd01302 137 ------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPPLRS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 283 KEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQG--IERAPFGITGFETAFPLLYTNLVKKGIItLEQLIQFLTEKPADT 360
Cdd:cd01302 205 KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGkdIWKAPPGFPGLETRLPILLTEGVKRGLS-LETLVEILSENPARI 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1208968218 361 FGLEA-GRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMT 413
Cdd:cd01302 284 FGLYPkGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
1-422 |
1.98e-89 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 277.71 E-value: 1.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 1 MNYLFKNGRYMNEEGKIVAT-DLLVQDGKIA---KVAENITADNaeVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETG 76
Cdd:PRK07627 1 MKIHIKGGRLIDPAAGTDRQaDLYVAAGKIAaigQAPAGFNADK--TIDASGLIVCPGLVDLSARLREPGYEYKATLESE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 77 TLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDDGVGVQ 156
Cdd:PRK07627 79 MAAAVAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGFSQANVPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 157 DASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCHVSTKG 236
Cdd:PRK07627 159 DTQVLLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPVAAETIALHTIFELMRVTGARVHLARLSSAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 237 SVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQG 316
Cdd:PRK07627 239 GVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 317 IERAPFGITGFETAFPLLYTNLVKKGiITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKG 396
Cdd:PRK07627 319 FAEATPGATGLELLLPLTLKWADEAK-VPLARALARITSAPARVLGLPAGRLAEGAPADLCVFDPDAHWRVEPRALKSQG 397
|
410 420
....*....|....*....|....*.
gi 1208968218 397 KNTPFAGWKCQGWPVMTIVGGKIAWQ 422
Cdd:PRK07627 398 KNTPFLGYELPGRVRATLVAGQVAFE 423
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-423 |
4.21e-89 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 277.33 E-value: 4.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 1 MNYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITA-DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA 79
Cdd:PRK07575 3 MSLLIRNARILLPSGELLLGDVLVEDGKIVAIAPEISAtAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 80 AAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNvlpYGAITVRQAgsemtdfETLKELGAFAFTDdGVGVQDAS 159
Cdd:PRK07575 83 CAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVN---YGFFIGATP-------DNLPELLTANPTC-GIKIFMGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 160 M---ML----AAMKRA-AKLNMAVVAHCEENTLINkgcvhegkfSEKHGLNGIPSVC--------ESVHIA--RDILLAE 221
Cdd:PRK07575 152 ShgpLLvdeeAALERIfAEGTRLIAVHAEDQARIR---------ARRAEFAGISDPAdhsqiqdeEAALLAtrLALKLSK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 222 AADCHYHVCHVSTKGSVRVIRDAKRAgiKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMI 301
Cdd:PRK07575 223 KYQRRLHILHLSTAIEAELLRQDKPS--WVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 302 ATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVkKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIID 380
Cdd:PRK07575 301 ATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGIpNKGRIAPGYDADLVLVD 379
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1208968218 381 LEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK07575 380 LNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDR 422
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
4-421 |
1.68e-87 |
|
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: 273.32 E-value: 1.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIvATDLLVQDGKIAKVAENITA-DNAEVIDVNGKLIAPGLVDVHVHLREP--GGEHKETIETGTLAA 80
Cdd:cd01314 2 IIKNGTIVTADGSF-KADILIEDGKIVAIGPNLEApGGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 81 AKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAhvnVLPYG---AIT--VRQAGSEMtdfETLKELGAFAF----TDD 151
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKS---VIDYGfhmIITdwTDSVIEEL---PELVKKGISSFkvfmAYK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 152 GVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGC---VHEGKFS-EKHGLNGiPSVCESVHIARDILLAEAADCHY 227
Cdd:cd01314 155 GLLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQkklLAQGKTGpEYHALSR-PPEVEAEATARAIRLAELAGAPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 228 HVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDI--PSADPN-FKMNPPLRGKEDHAALIEGLLDGTIDMIATD 304
Cdd:cd01314 234 YIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYwkDWFEGAkYVCSPPLRPKEDQEALWDGLSSGTLQTVGSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 305 HAPHTAEEKAQGIE---RAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL--EAGRLKEGRTADITII 379
Cdd:cd01314 314 HCPFNFAQKARGKDdftKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLypRKGTIAVGSDADLVIW 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1208968218 380 DLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAW 421
Cdd:cd01314 394 DPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVV 435
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
4-424 |
1.26e-84 |
|
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: 265.79 E-value: 1.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKG 83
Cdd:TIGR03178 3 IIRGGRVILPNGEREA-DVGVKGGKIAAIGPDILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 84 GFTTICAMP-NTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQagseMTDFETLKELGAFAF--------TDDGVG 154
Cdd:TIGR03178 82 GITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYN----LDDLRELDEAGVVGFkaflspsgDDEFPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 155 VqDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVH---EGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCH 231
Cdd:TIGR03178 158 V-DDWQLYKGMRELARLGQLLLVHAENPAITSALGEEappQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 232 VSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAE 311
Cdd:TIGR03178 237 LSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSPCTPD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 312 EKAQG-IERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEEEIDP 389
Cdd:TIGR03178 317 LKRAGdFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGLaQKGRIAPGKDADFVFVDPDESYTLTP 396
|
410 420 430
....*....|....*....|....*....|....*
gi 1208968218 390 TTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKE 424
Cdd:TIGR03178 397 DDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDE 431
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
4-424 |
2.70e-78 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 249.62 E-value: 2.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKG 83
Cdd:PRK06189 6 IIRGGKVVTPEGVYRA-DIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALAAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 84 GFTTICAMP-NTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQagseMTDFETLKELGAFAF--------TDDGVG 154
Cdd:PRK06189 85 GCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGN----LEHLRELAEAGVIGFkafmsnsgTDEFRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 155 VQDASMmLAAMKRAAKLNMAVVAHCEENTLINK---GCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCH 231
Cdd:PRK06189 161 SDDLTL-YEGMKEIAALGKILALHAESDALTRHlttQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFVH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 232 VSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAE 311
Cdd:PRK06189 240 ISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPCPPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 312 EKaqgiERAPF-----GITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEE 385
Cdd:PRK06189 320 LK----EGDDFflvwgGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGLpQKGRLEVGADADFVLVDLDETY 395
|
410 420 430
....*....|....*....|....*....|....*....
gi 1208968218 386 EIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKE 424
Cdd:PRK06189 396 TLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDG 434
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
4-424 |
1.22e-77 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 247.53 E-value: 1.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKG 83
Cdd:PRK09060 8 ILKGGTVVNPDGEGRA-DIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 84 GFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGsemtDFETLKELGAFA----FTDDGVG---VQ 156
Cdd:PRK09060 87 GVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNAD----ELAELERLPGCAgikvFMGSSTGdllVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 157 DASMMLAAMKRAAKlNMAVvaHCEENTLIN--KGCVHEGKFSekhglngipsvceSVHIARD-----------ILLAEAA 223
Cdd:PRK09060 163 DDEGLRRILRNGRR-RAAF--HSEDEYRLRerKGLRVEGDPS-------------SHPVWRDeeaallatrrlVRLARET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 224 DCHYHVCHVSTKGSVRVIRDAKRAgikVTAEVTPHHLVLcedDIPSADPNFK----MNPPLRGKEDHAALIEGLLDGTID 299
Cdd:PRK09060 227 GRRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTL---AAPECYERLGtlaqMNPPIRDARHRDGLWRGVRQGVVD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 300 MIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNlVKKGIITLEQLIQFLTEKPADTFGLEA-GRLKEGRTADITI 378
Cdd:PRK09060 301 VLGSDHAPHTLEEKAKPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGIAGkGRIAVGYDADFTI 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1208968218 379 IDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIA-WQKE 424
Cdd:PRK09060 380 VDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVmWDGE 426
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-421 |
2.77e-76 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 244.70 E-value: 2.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 1 MNYLFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENitaDNAEVIDVNGKLIAPGLVDVHVHLREP-GGEH-KETIETGTL 78
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKA-DVLIEDGKIAAIGAN---LGDEVIDATGKYVMPGGIDPHTHMEMPfGGTVsSDDFETGTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 79 AAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAIT--VRQAGSEMtdfETLKELGAFAF----TDDG 152
Cdd:PRK08323 77 AAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITdwNEVVLDEM---PELVEEGITSFklfmAYKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 153 VGVQDASMMLAAMKRAAKLNMAVVAHCEENTLIN---KGCVHEGKFS-EKHGLNGiPSVCESVHIARDILLAEAADCHYH 228
Cdd:PRK08323 154 ALMLDDDELLRALQRAAELGALPMVHAENGDAIAylqAKLLAEGKTGpEYHALSR-PPEVEGEATNRAIMLAELAGAPLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 229 VCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPN----FKMNPPLRGKEDHAALIEGLLDGTIDMIATD 304
Cdd:PRK08323 233 IVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFegakYVMSPPLRDKEHQDALWRGLQDGDLQVVATD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 305 HAPHTAEEKAQGiERAPF-----GITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL--EAGRLKEGRTADIT 377
Cdd:PRK08323 313 HCPFCFEQKKQL-GRGDFtkipnGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLypRKGTIAVGADADIV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1208968218 378 IIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAW 421
Cdd:PRK08323 392 IWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVV 435
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
15-419 |
1.28e-75 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 241.21 E-value: 1.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 15 GKIVATDLLVQDGKIAKV-AENITADnaEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPN 93
Cdd:PRK04250 10 GRIVEGGIGIENGRISKIsLRDLKGK--EVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 94 TRPVPDCREHMEDLQKRIQEKAHV----NVLPYGaiTVRQAGSEMTDFETlkelgafAFTDDGVGVQDASMMLAAMKRAA 169
Cdd:PRK04250 88 TKPPIMDEKTYEKRMRIAEKKSYAdyalNFLIAG--NCEKAEEIKADFYK-------IFMGASTGGIFSENFEVDYACAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 170 KlnmAVVAHCEENTLINKgcvhegkFSEKhglngiPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRdaKRAGI 249
Cdd:PRK04250 159 G---IVSVHAEDPELIRE-------FPER------PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLIL--KSNLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 250 KVTAEVTPHHLVLCEDDIpSADPNFKMNPPLRGKEDHAALIEGLldGTIDMIATDHAPHTAEEKAQGierAPfGITGFET 329
Cdd:PRK04250 221 WVSFEVTPHHLFLTRKDY-ERNPLLKVYPPLRSEEDRKALWENF--SKIPIIASDHAPHTLEDKEAG---AA-GIPGLET 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 330 AFPLLYtNLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGW 409
Cdd:PRK04250 294 EVPLLL-DAANKGMISLFDIVEKMHDNPARIFGIKNYGIEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGK 372
|
410
....*....|
gi 1208968218 410 PVMTIVGGKI 419
Cdd:PRK04250 373 VIMTILRGEV 382
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-423 |
8.06e-73 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 235.15 E-value: 8.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 1 MNYLFKNGRYMNEeGKIVATDLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA 79
Cdd:PRK09236 2 KRILIKNARIVNE-GKIFEGDVLIENGRIAKIASSISAKSAdTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 80 AAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNvlpYGAITvrqaGSEMTDFETLKELGAfaftDDGVGVQ--- 156
Cdd:PRK09236 81 AVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLAN---YSFYF----GATNDNLDEIKRLDP----KRVCGVKvfm 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 157 ---------DASMMLAAMKRAAKlnMAVVAHCEENTLINKgcvHEGKFSEKHGlNGIP----------SVC-ESVHIArd 216
Cdd:PRK09236 150 gastgnmlvDNPETLERIFRDAP--TLIATHCEDTPTIKA---NLAKYKEKYG-DDIPaemhplirsaEACyKSSSLA-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 217 ILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDG 296
Cdd:PRK09236 222 VSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALADD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 297 TIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYtNLVKKGIITLEQLIQFLTEKPADTFGLEA-GRLKEGRTAD 375
Cdd:PRK09236 302 RIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALL-ELVHEGKLSLEKVVEKTSHAPAILFDIKErGFIREGYWAD 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1208968218 376 ITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK09236 381 LVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHN 428
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
4-423 |
2.01e-71 |
|
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: 231.89 E-value: 2.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITA-DNAEVIDVNGKLIAPGLVDVHVHLREP--GGEHKETIETGTLAA 80
Cdd:TIGR02033 2 LIKGGTVVNADDVFQA-DVLIEGGKIVAVGDNLIPpDAVEVIDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 81 AKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKA------HVNVLPYGAITVRQAGSEMTDfETLKELGAFAFTDDGVG 154
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSvidygfHMDITHWNDSVLEEHIPEVKE-EGINSFKVFMAYKNLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 155 VQDASMmLAAMKRAAKLNMAVVAHCEENTLIN---KGCVHEGKFS-EKHGLNGiPSVCESVHIARDILLAEAADCHYHVC 230
Cdd:TIGR02033 160 VDDEEL-FEILKRLKELGALLQVHAENGDIIAelqARMLAQGITGpEYHALSR-PPELEAEAVARAITLAALADAPLYVV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 231 HVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCED--DIPSADP-NFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAP 307
Cdd:TIGR02033 238 HVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDThyDKPGFEGaKYVCSPPLREPEDQDALWSALSSGALQTVGSDHCT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 308 HTAEEKAQG----IERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL--EAGRLKEGRTADITIIDL 381
Cdd:TIGR02033 318 FNFAQKKAIgkddFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLypRKGTIAVGSDADIVIWDP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1208968218 382 EQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:TIGR02033 398 NRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVED 439
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
22-419 |
7.86e-66 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 215.34 E-value: 7.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 22 LLVQDGKIAKVAENItaDNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKeTIETGTLAAAKGGFTTICAMPNTRPvPDCR 101
Cdd:PRK08417 1 IRIKDGKITEIGSDL--KGEEILDAKGKTLLPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTP-AIDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 102 EHMEDLQKRIQEKAHVNVLPygAITVRQAGSEMTDFETLKELGAFA-FTDDGVgvqDASMMLAAMKRAAKLNMAVVAHCE 180
Cdd:PRK08417 77 EIALELINSAQRELPMQIFP--SIRALDEDGKLSNIATLLKKGAKAlELSSDL---DANLLKVIAQYAKMLDVPIFCRCE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 181 ENTLINKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEaadcHYHV----CHVSTKGSVRVIRDAKRAGIKVTAEVT 256
Cdd:PRK08417 152 DSSFDDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAK----FYKNkvlfDTLALPRSLELLDKFKSEGEKLLKEVS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 257 PHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYT 336
Cdd:PRK08417 228 IHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 337 NLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPttflskgKNTPFAGWKCQGWPVMTIVG 416
Cdd:PRK08417 308 YLVKEGIITWSELSRFTSYNPAQFLGLNSGEIEVGKEADLVLFDPNESTIIDD-------NFSLYSGDELYGKIEAVIIK 380
|
...
gi 1208968218 417 GKI 419
Cdd:PRK08417 381 GKL 383
|
|
| PLN02795 |
PLN02795 |
allantoinase |
24-417 |
2.34e-61 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 206.94 E-value: 2.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 24 VQDGKIAKVAENITAD----NAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMP-NTRPVP 98
Cdd:PLN02795 66 VEGGRIVSVTKEEEAPksqkKPHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPST 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 99 DCREHMEDLQKRIQEKAHVNVLPYGAITVRQAGSEmTDFETLKELGAFAFTD-------DGVGVQDASMMLAAMKRAAKL 171
Cdd:PLN02795 146 TSVETLELKIEAAKGKLYVDVGFWGGLVPENAHNA-SVLEELLDAGALGLKSfmcpsgiNDFPMTTATHIKAALPVLAKY 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 172 NMAVVAHCEENTLINKGCVHEG--------------KFSEkhglNGIPSVCESVHIARDILLAEAAdcHYHVCHVS-TKG 236
Cdd:PLN02795 225 GRPLLVHAEVVSPVESDSRLDAdprsystylksrppSWEQ----EAIRQLLEVAKDTRPGGVAEGA--HVHIVHLSdAES 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 237 SVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAqg 316
Cdd:PLN02795 299 SLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKL-- 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 317 IE-----RAPFGITGFETAFPLLYTNLVKKGiITLEQLIQFLTEKPADTFGLEA-GRLKEGRTADITIIDLEQEEEIDPT 390
Cdd:PLN02795 377 LEegnflRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGLDSkGAIAPGKDADIVVWDPEAEFVLDES 455
|
410 420
....*....|....*....|....*....
gi 1208968218 391 -TFLSKGKN-TPFAGWKCQGWPVMTIVGG 417
Cdd:PLN02795 456 yPIYHKHKSlSPYLGTKLSGKVIATFVRG 484
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
53-420 |
3.78e-60 |
|
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: 199.21 E-value: 3.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 53 PGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHV-----------NVLP 121
Cdd:cd01316 6 PGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCdyafsigatstNAAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 122 YGAITVRQAGSEMTDFETLKELgafaFTDDGVGVQDASMMLAAMKraaklnmAVVAHCEENTLinkgcvhegkfsekhgl 201
Cdd:cd01316 86 VGELASEAVGLKFYLNETFSTL----ILDKITAWASHFNAWPSTK-------PIVTHAKSQTL----------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 202 ngipsvcesvhiARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPsaDPNFKMNPPLR 281
Cdd:cd01316 138 ------------AAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLP--RGQYEVRPFLP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 282 GKEDHAALIEGLldGTIDMIATDHAPHTAEEKAQgiERAPFGITGFETAFPLLYTnLVKKGIITLEQLIQFLTEKPADTF 361
Cdd:cd01316 204 TREDQEALWENL--DYIDCFATDHAPHTLAEKTG--NKPPPGFPGVETSLPLLLT-AVHEGRLTIEDIVDRLHTNPKRIF 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 362 GLEAgrlkegrTADITI-IDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIA 420
Cdd:cd01316 279 NLPP-------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETA 331
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
4-424 |
9.44e-60 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 201.24 E-value: 9.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVaTDLLVQDGKIAKVAENItADNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKG 83
Cdd:PRK08044 6 IIKNGTVILENEARV-VDIAVKGGKIAAIGQDL-GDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 84 GFTTICAMP-NTRPVPDCREHMEDLQKRIQEKAHVNVLPYGAITvrqaGSEMTDFETLKELGAFAFT------------D 150
Cdd:PRK08044 84 GITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLV----SYNLDRLHELDEVGVVGFKcfvatcgdrgidN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 151 DGVGVQDASMmLAAMKRAAKLNMAVVAHCEeNTLI----NKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCH 226
Cdd:PRK08044 160 DFRDVNDWQF-YKGAQKLGELGQPVLVHCE-NALIcdelGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 227 YHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHA 306
Cdd:PRK08044 238 LHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 307 PHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEE 385
Cdd:PRK08044 318 PCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLqQKGRIAPGKDADFVFIQPNSSY 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 1208968218 386 EIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKE 424
Cdd:PRK08044 398 VLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIE 436
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
15-423 |
4.20e-54 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 186.83 E-value: 4.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 15 GKIVAT------DLLVQDGKIAKVAENITAdNAEVIDVNGKLIAPGLVDVHVHLREPGGE---HKETIETGTLAAAKGGF 85
Cdd:PRK13404 11 GTVVTAtdtfqaDIGIRGGRIAALGEGLGP-GAREIDATGRLVLPGGVDSHCHIDQPSGDgimMADDFYTGTVSAAFGGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 86 TTI---CAMPNTRPVPDCrehMEDLQKRIQEKAHVNVlPYGAItVRQAGSEMT--DFETLKELGAFAF----TDDGVGVQ 156
Cdd:PRK13404 90 TTVipfAAQHRGQSLREA---VEDYHRRAAGKAVIDY-AFHLI-VADPTEEVLteELPALIAQGYTSFkvfmTYDDLKLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 157 DASMM--LAAMKRAAKLNMAvvaHCEENTLI---NKGCVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAADCHYHVCH 231
Cdd:PRK13404 165 DRQILdvLAVARRHGAMVMV---HAENHDMIawlTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 232 VSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLCEDD--IPSAD-PNFKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPH 308
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDldRPGMEgAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 309 ----TAEEKAQGIERA----PFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGLEA--GRLKEGRTADITI 378
Cdd:PRK13404 322 rfddTDGKLAAGANPSfkaiANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPrkGAIAIGADADIAI 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1208968218 379 IDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQK 423
Cdd:PRK13404 402 WDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVED 446
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
15-419 |
5.97e-54 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 185.06 E-value: 5.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 15 GKIVATDLLVQDGKIAKVAENitADNAEVIDVNGkLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNT 94
Cdd:PRK01211 11 GKFDYLEIEVEDGKIKSIKKD--AGNIGKKELKG-AILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 95 RPVPDCREHMEDLQKRIQEKAHVNVLPYGAITvrQAGSEMTDFET--LKELGAFAFTDDGVGVQDASMmlaamKRAAKLN 172
Cdd:PRK01211 88 NIPIKDYNAFSDKLGRVAPKAYVDFSLYSMET--GNNALILDERSigLKVYMGGTTNTNGTDIEGGEI-----KKINEAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 173 MAVVAHCEENTLINKGcVHEGKFSEKHGLNGiPSVCEsvhIARDILLAEAADCHYHVCHVStkgSVRVIRDakragikVT 252
Cdd:PRK01211 161 IPVFFHAELSECLRKH-QFESKNLRDHDLAR-PIECE---IKAVKYVKNLDLKTKIIAHVS---SIDVIGR-------FL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 253 AEVTPHHLVLcEDDIPSADPNfKMNPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEEKAQgIERAPFGITGFETAFP 332
Cdd:PRK01211 226 REVTPHHLLL-NDDMPLGSYG-KVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQE-FEYAKSGIIGVETRVP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 333 LLYTnLVKKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQgWPVM 412
Cdd:PRK01211 303 LFLA-LVKKKILPLDVLYKTAIERPASLFGIKKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSH 380
|
....*..
gi 1208968218 413 TIVGGKI 419
Cdd:PRK01211 381 VIMRGEV 387
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
47-420 |
3.80e-51 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 176.88 E-value: 3.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 47 NGKLIAPGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCREhmedlqkRIQEKahvnvlpygait 126
Cdd:PRK00369 41 QGTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPE-------AITEK------------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 127 vrqagsemtdfetLKELGAFAFTDDGV--GVQD-----ASMMLAAMK-------------RAAKLNMAVVAHCEentlin 186
Cdd:PRK00369 102 -------------LAELEYYSRVDYFVysGVTKdpekvDKLPIAGYKifpedlereetfrVLLKSRKLKILHPE------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 187 kgcvhegkfsekhglngIPSVCESVHIARDILLAEAADCHY-------HVCHVSTKGSVRVirdAKRAGIkvTAEVTPHH 259
Cdd:PRK00369 163 -----------------VPLALKSNRKLRRNCWYEIAALYYvkdyqnvHITHASNPRTVRL---AKELGF--TVDITPHH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 260 LVLcedDIPSaDPNFKMNPPLRGKEDHAALIEGLLDgtIDMIATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTnLV 339
Cdd:PRK00369 221 LLV---NGEK-DCLTKVNPPIRDINERLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIYT-LV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 340 KKGIITLEQLIQFLTEKPADTFGLEAGRLKEGRTADITIIdleQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKI 419
Cdd:PRK00369 294 SKGILSIDRAVELISTNPARILGIPYGEIKEGYRANFTVI---QFEDWRYSTKYSKVIETPLDGFELKASVYATIVQGKL 370
|
.
gi 1208968218 420 A 420
Cdd:PRK00369 371 A 371
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
4-424 |
2.54e-42 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 155.39 E-value: 2.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENI-TADNAEVIDVNGKLIAPGLVDVHVHLREP--GGEHKETIETGTLAA 80
Cdd:PLN02942 8 LIKGGTVVNAHHQELA-DVYVEDGIIVAVAPNLkVPDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 81 AKGGFTTICAMPntrpVPDCREHMEDLQKrIQEKAHVNVLPYG---AITvRQAGSEMTDFETL-KELGAFAF----TDDG 152
Cdd:PLN02942 87 LAGGTTMHIDFV----IPVNGNLLAGYEA-YEKKAEKSCMDYGfhmAIT-KWDDTVSRDMETLvKEKGINSFkffmAYKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 153 VGVQDASMMLAAMKRAAKLNMAVVAHCEentliNKGCVHEGKFS---------EKHGLNGiPSVCESVHIARDILLAEAA 223
Cdd:PLN02942 161 SLMVTDELLLEGFKRCKSLGALAMVHAE-----NGDAVFEGQKRmielgitgpEGHALSR-PPLLEGEATARAIRLAKFV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 224 DCHYHVCHVSTKGSVRVIRDAKRAGIKVTAEVTPHHLVLceDDIPSADPNFK------MNPPLRGKEDHAALIEGLLDGT 297
Cdd:PLN02942 235 NTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVL--DDSKLWDPDFTiaskyvMSPPIRPAGHGKALQAALSSGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 298 IDMIATDHAPHTAEEKAQGIE---RAPFGITGFETAFPLLYTNLVKKGIITLEQLIQFLTEKPADTFGL--EAGRLKEGR 372
Cdd:PLN02942 313 LQLVGTDHCPFNSTQKAFGKDdfrKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIypRKGAILAGS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1208968218 373 TADITIIDLEQEEEIDPTTFLSKGKNTPFAGWKCQGWPVMTIVGGKIAWQKE 424
Cdd:PLN02942 393 DADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENG 444
|
|
| DHOase |
pfam12890 |
Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various ... |
48-237 |
6.56e-37 |
|
Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various bacteria.
Pssm-ID: 315550 [Multi-domain] Cd Length: 142 Bit Score: 131.53 E-value: 6.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 48 GKLIAPGLVDVHVHLREPGGEHKETIETgtlaaakggftTICAMPNTRPVPdcrehmedlqkriqekahvnvlpyGAITV 127
Cdd:pfam12890 1 GRLIVPGLAFLHVHLTAPSGEAQELKET-----------TWAAYGVTFKAP------------------------AGITV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 128 RQAGSEmtdfetlkelgAFAFTDDGVGVQDASMMLAAMKRAAkLNMAVVAHCEENTLINKGCVHEGKFSEKHGLNgIPSV 207
Cdd:pfam12890 46 EDDSEE-----------GFIFTNDTYYITIQLLEGEGMKKSE-LDQELKAIATDDEVTNQSAVQDFELPQFYGTQ-LKGN 112
|
170 180 190
....*....|....*....|....*....|
gi 1208968218 208 CESVHIARDILLAEAADCHYHVCHVSTKGS 237
Cdd:pfam12890 113 CETEHCVYSYLLAKAAGCGFYVSIIYTKEN 142
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
50-419 |
1.40e-32 |
|
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: 125.69 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 50 LIAPGLVDVHVHLR--------EPGGEHKETIETGTLAAAKGGFTTICAMPNTRP--VPDCREHMEDLQKRI-------- 111
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTStgIEALLEAAEELPLGLrflgpgcs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 112 --------QEKAHVNVLPYGAITVRQAGSEMTdFETLKELGAFAFTDDgvgvqdasMMLAAMKRAAKLNMAVVAHCEENT 183
Cdd:pfam01979 81 ldtdgeleGRKALREKLKAGAEFIKGMADGVV-FVGLAPHGAPTFSDD--------ELKAALEEAKKYGLPVAIHALETK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 184 LINKgcVHEGKFSEKHGLNGIPSVCESVHIARDILLAEAadchyHVCHVSTKGSVRVIRDAKRAGIkvtaevtphhlvlc 263
Cdd:pfam01979 152 GEVE--DAIAAFGGGIEHGTHLEVAESGGLLDIIKLILA-----HGVHLSPTEANLLAEHLKGAGV-------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 264 eDDIPSADpnfkmnppLRGKEDHAALIEGLLDGTIDMIATDHAPHTAEekAQGIERAPFgitgfetafpLLYTNLVKKGI 343
Cdd:pfam01979 211 -AHCPFSN--------SKLRSGRIALRKALEDGVKVGLGTDGAGSGNS--LNMLEELRL----------ALELQFDPEGG 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208968218 344 ITLEQLIQFLTEKPADTFGLE--AGRLKEGRTADITIIDLEqeeeidpttflskgKNTPFAGWKCQGWPVMTIVGGKI 419
Cdd:pfam01979 270 LSPLEALRMATINPAKALGLDdkVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-419 |
1.12e-15 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 78.08 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 3 YLFKNGRY--MNEEGKIVATDLLVQDGKIAKVAENITA---DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGT 77
Cdd:COG1228 10 LLITNATLvdGTGGGVIENGTVLVEDGKIAAVGPAADLavpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 78 LAAA---------------KGGFTTICAMPNTrPVPDCREHMEDLQKRIQE----KAHVNVLPYGAITVRQAGSEMTDFE 138
Cdd:COG1228 90 ITPTvdlvnpadkrlrralAAGVTTVRDLPGG-PLGLRDAIIAGESKLLPGprvlAAGPALSLTGGAHARGPEEARAALR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 139 TLKELGAFA---FTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEEntlinkgcvhegkfsekhglngipsvcesvhiAR 215
Cdd:COG1228 169 ELLAEGADYikvFAEGGAPDFSLEELRAILEAAHALGLPVAAHAHQ--------------------------------AD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 216 DILLA-EA-ADCHYHVCHVSTKgsvrVIRDAKRAGikvTAEVTPHHLVLceDDIPSADPNFKMNPPLRGKEDHAALIEGL 293
Cdd:COG1228 217 DIRLAvEAgVDSIEHGTYLDDE----VADLLAEAG---TVVLVPTLSLF--LALLEGAAAPVAAKARKVREAALANARRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 294 LDGTIDM-IATDHaphtaeekaqGIERAPFGITGFETAFpllytnLVKKGiITLEQLIQFLTEKPADTFGLEA--GRLKE 370
Cdd:COG1228 288 HDAGVPVaLGTDA----------GVGVPPGRSLHRELAL------AVEAG-LTPEEALRAATINAAKALGLDDdvGSLEP 350
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1208968218 371 GRTADITIIDleqeeeIDPTTFLSKGKNtpfagwkcqgwPVMTIVGGKI 419
Cdd:COG1228 351 GKLADLVLLD------GDPLEDIAYLED-----------VRAVMKDGRV 382
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
55-358 |
6.15e-13 |
|
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: 68.90 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 55 LVDVHVHLREPGGEH------------------KETIETGTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAH 116
Cdd:cd01292 1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 117 VNVLPYGAITVRQAGSEMTDFETLKEL----------GAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLin 186
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAEALLLELlrrglelgavGLKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHAGELPD-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 187 kgcvhegkfsekhglngipsvcESVHIARDILLAEaADCHYHVCHVSTkGSVRVIRDAKRAGIKVtaEVTPHHlvlcedd 266
Cdd:cd01292 159 ----------------------PTRALEDLVALLR-LGGRVVIGHVSH-LDPELLELLKEAGVSL--EVCPLS------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 267 ipsadpnfkmNPPLRGKEDHA-ALIEGLLDGTIDMIATDHAPHTaeekaqgierapfgitgFETAFPLLYTNLVKKGII- 344
Cdd:cd01292 206 ----------NYLLGRDGEGAeALRRLLELGIRVTLGTDGPPHP-----------------LGTDLLALLRLLLKVLRLg 258
|
330
....*....|....*
gi 1208968218 345 -TLEQLIQFLTEKPA 358
Cdd:cd01292 259 lSLEEALRLATINPA 273
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-380 |
1.15e-12 |
|
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: 68.76 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 3 YLFKNGRYMNEEGKIVAtDLLVQDGKIAKVAENITADN-AEVIDVNGKLIAPGLVDVHVHlrePGGEH------KETIET 75
Cdd:cd00854 1 LIIKNARILTPGGLEDG-AVLVEDGKIVAIGPEDELEEaDEIIDLKGQYLVPGFIDIHIH---GGGGAdfmdgtAEALKT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 76 GTLAAAKGGFTTICAMPNTRPVPDCREHMEDLQKRIQEKAHVNVL------PYgaITVRQAGSEmtDFETLKELGAFAFT 149
Cdd:cd00854 77 IAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILgihlegPF--ISPEKKGAH--PPEYLRAPDPEELK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 150 D-DGVGVQDASMM---------LAAMKRAAKLNMAV-VAHCE---ENTlinKGCVHEGKFSEKHGLNGIPSVcesVHiaR 215
Cdd:cd00854 153 KwLEAAGGLIKLVtlapeldgaLELIRYLVERGIIVsIGHSDatyEQA---VAAFEAGATHVTHLFNAMSPL---HH--R 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 216 DILLAEAADCHYHV--------CHVStKGSVRVIRDAKRagikvtaevtPHHLVLCEDDIPSA---DPNFKMNP-PLRGK 283
Cdd:cd00854 225 EPGVVGAALSDDDVyaeliadgIHVH-PAAVRLAYRAKG----------ADKIVLVTDAMAAAglpDGEYELGGqTVTVK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 284 EDHAALIEGLLDG-TIDMIatdhaphtaeekaQGIErapfgitgfetafpllytNLVKKGIITLEQLIQFLTEKPADTFG 362
Cdd:cd00854 294 DGVARLADGTLAGsTLTMD-------------QAVR------------------NMVKWGGCPLEEAVRMASLNPAKLLG 342
|
410 420
....*....|....*....|
gi 1208968218 363 LEA--GRLKEGRTADITIID 380
Cdd:cd00854 343 LDDrkGSLKPGKDADLVVLD 362
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
2-61 |
2.62e-12 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 67.88 E-value: 2.62e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208968218 2 NYLFKNGRYMNEEGKIVA-TDLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVH 61
Cdd:COG3964 1 DLLIKGGRVIDPANGIDGvMDIAIKDGKIAAVAKDIDAAEAkKVIDASGLYVTPGLIDLHTH 62
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
19-383 |
7.77e-12 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 66.55 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 19 ATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHlrepgGEHKETIETGTLAAAKGGFTTIcAMPN----T 94
Cdd:cd01297 19 TADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTH-----YDGQVFWDPDLRPSSRQGVTTV-VLGNcgvsP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 95 RPVPDcREHMEDLQKRIQEKAHVNVLPYGAITvrqagseMTDFetlkeLGAFAFTDDGVgvqDASMML--AAMKRAAKLN 172
Cdd:cd01297 93 APANP-DDLARLIMLMEGLVALGEGLPWGWAT-------FAEY-----LDALEARPPAV---NVAALVghAALRRAVMGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 173 MAVVAHCEENT----LINKGcVHEGKFSEKHGLNGIPSVC----ESVHIARdilLAEAADCHYHVcHVSTKGS------V 238
Cdd:cd01297 157 DAREATEEELAkmreLLREA-LEAGALGISTGLAYAPRLYagtaELVALAR---VAARYGGVYQT-HVRYEGDsilealD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 239 RVIRDAKRAGIKVTAEvtphHLVLCeddipsadpnfkMNPPLRGKEDHAALIEGLLDGTIDMIAtDHAPHTA--EEKAQG 316
Cdd:cd01297 232 ELLRLGRETGRPVHIS----HLKSA------------GAPNWGKIDRLLALIEAARAEGLQVTA-DVYPYGAgsEDDVRR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 317 IERAPFgiTGFET--------------AFPLLYTNLVK-KGIITLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIID 380
Cdd:cd01297 295 IMAHPV--VMGGSdggalgkphprsygDFTRVLGHYVReRKLLSLEEAVRKMTGLPARVFGLaDRGRIAPGYRADIVVFD 372
|
...
gi 1208968218 381 LEQ 383
Cdd:cd01297 373 PDT 375
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-61 |
7.93e-12 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 66.41 E-value: 7.93e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVA-TDLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVH 61
Cdd:PRK09237 2 LLRGGRVIDPANGIDGvIDIAIEDGKIAAVAGDIDGSQAkKVIDLSGLYVSPGWIDLHVH 61
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
21-397 |
1.74e-11 |
|
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: 65.49 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 21 DLLVQDGKIAKVAENITAD---NAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA---AAKGGFTTICAMPNT 94
Cdd:cd01308 19 DILIAGGKILAIEDQLNLPgyeNVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVTlsdLTTAGVTTVVGCLGT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 95 RPVpdCReHMEDLQKriqeKAHvnVLPYGAIT--VRQAGSEM---TDFETLKElgAFAFTDDGVGVQDASMmlaAMKRAA 169
Cdd:cd01308 99 DGI--SR-SMEDLLA----KAR--ALEEEGITcfVYTGSYEVptrTITGSIRK--DLLLIDKVIGVGEIAI---SDHRSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 170 KLNMAVVAHCEENTLI------NKGCVHEGKFSEKHGLNGIPSVCES----------VHIARDILLAEAAdchyhvchvs 233
Cdd:cd01308 165 QPTVEELARIAAEARVggllggKAGIVHIHLGDGKRALSPIFELIEEteipitqflpTHINRTAPLFEQG---------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 234 tkgsvrvIRDAKRAG-IKVTAevtphhlvlceddipSADPNFKMNPPLRGKEDHAALIE-GLLDGTIDMIATDHA--PHT 309
Cdd:cd01308 235 -------VEFAKMGGtIDLTS---------------SIDPQFRKEGEVRPSEALKRLLEqGVPLERITFSSDGNGslPKF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 310 AEEKA-QGIerapfGITGFETAFPLLyTNLVKKGIITLEQLIQFLTEKPADTFGLEA-GRLKEGRTADITIIDleqeEEI 387
Cdd:cd01308 293 DENGNlVGL-----GVGSVDTLLREV-REAVKCGDIPLEVALRVITSNVARILKLRKkGEIQPGFDADLVILD----KDL 362
|
410
....*....|
gi 1208968218 388 DPTTFLSKGK 397
Cdd:cd01308 363 DINSVIAKGQ 372
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
4-258 |
1.79e-11 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 65.87 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVAT-DLLVQDGKIAKVAEN-ITADnaEVIDVNGKLIAPGLVDVHVHLREPGGEHKET--------- 72
Cdd:PRK09061 22 VIRNGRVVDPETGLDAVrDVGIKGGKIAAVGTAaIEGD--RTIDATGLVVAPGFIDLHAHGQSVAAYRMQAfdgvttale 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 73 IETGTL--------AAAKG-----GFTT------ICAMPNTRPVPDcrehMEDLQKRIQEKAHVnvlpYGAITVRQAGSE 133
Cdd:PRK09061 100 LEAGVLpvarwyaeQAGEGrplnyGASVgwtparIAVLTGPQAEGT----IADFGKALGDPRWQ----ERAATPAELAEI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 134 MTDFETLKELGAFAFtddGVGVQ-----DASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGkfsekhglngipsvc 208
Cdd:PRK09061 172 LELLEQGLDEGALGI---GIGAGyapgtGHKEYLELARLAARAGVPTYTHVRYLSNVDPRSSVDA--------------- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1208968218 209 esvhIARDILLAEAADCHYHVCHV-STKGS-----VRVIRDAKRAGIKVTAEVTPH 258
Cdd:PRK09061 234 ----YQELIAAAAETGAHMHICHVnSTSLRdidrcLALVEKAQAQGLDVTTEAYPY 285
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
21-382 |
1.86e-11 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 65.58 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 21 DLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVH-----LREPGGEHKetietgtlaaAKGGFTTI----CAM 91
Cdd:COG3653 23 DVAIKGGRIVAVGDLAAAEAARVIDATGLVVAPGFIDIHTHydlqlLWDPRLEPS----------LRQGVTTVvmgnCGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 92 pntRPVPDCREHMEDLQKRIqekAHVNVLPYGaitvrqagsEMTDFETLKELGAfAFTDDGVGVQDASMM---------- 161
Cdd:COG3653 93 ---SFAPVRPEDRDRLIDLM---EGVEGIPEG---------LDWDWESFGEYLD-ALERRGLGVNVASLVghgtlrayvm 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 162 -----------LAAMKRAAKLNMAvvAHC-----------------EENTLINKGCVHEGKFSEKHGLNGIPSVCESVHI 213
Cdd:COG3653 157 glddrpptpeeLARMRALLREAME--AGAlglstgliyvpgtyastDELVALAKVVAEYGGVYQSHMRDEGDGLLEAVDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 214 ARDIllAEAADCHYHVCHVSTKG---------SVRVIRDAKRAGIKVTAEVTPH-----HLVLCeddIPS---ADPNFKM 276
Cdd:COG3653 235 LIRI--GREAGVPVHISHLKAAGkpnwgkadeVLALIEAARAEGLDVTADVYPYpagstGLGAL---LPPwaaAGGLDER 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 277 NPPLRGKEDHAALIEGLLDGTIDMIATDHAPHTAE-------EKAQGI-------ERapfGITGFETAFPLL-------- 334
Cdd:COG3653 310 LARLRDPATRARIRAEIEEGLPDNLLGRGGWDNILisdsppnEPLVGKslaeiaaER---GVDPADAALDLLleedgrvl 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 335 --YT-----NLVK-------------------------------------KGIITLEQLIQFLTEKPADTFGLE-AGRLK 369
Cdd:COG3653 387 ivYFimseeDVREllrhpwvmigsdgglggkahpraygtfprvlghyvreRGVLSLEEAVRKLTSLPADRLGLKdRGLLR 466
|
490
....*....|...
gi 1208968218 370 EGRTADITIIDLE 382
Cdd:COG3653 467 PGYRADLVVFDPA 479
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
49-364 |
2.52e-11 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 64.61 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 49 KLIAPGlvDVHVHLREpgGEHKETIeTGTLAAakgGFTTICAMPNTRP----VPDCREHMEDLQKRIQEKahvNVLPYGA 124
Cdd:cd01294 2 TIPRPD--DMHLHLRD--GAMLKLV-LPYTAR---GFSRAIVMPNLKPpvttTADALAYRERILAADPGP---NFTPLMT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 125 ITVR--------QAGSEMTDFETLKELGAFAFTDDGVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFs 196
Cdd:cd01294 71 LYLTenttpeelREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKF- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 197 ekhglngIPsVCESVHI---ARDILLAeaadchyhvcHVSTKGSVRVIrdaKRAGIKVTAEVTPHHLVLCEDDI--PSAD 271
Cdd:cd01294 150 -------IP-VLEPLAQrfpKLKIVLE----------HITTADAVEYV---KSCNENVAATITPHHLLLTRDDLlgGGLN 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 272 PNFKMNPPLRGKEDHAALIEGLLDGTID-MIATDHAPHTAEEK-----AQGIERAPFgitgfetAFPLLYTNLVKKGIit 345
Cdd:cd01294 209 PHLYCKPVAKRPEDREALRKAATSGHPKfFLGSDSAPHPKSNKesscgCAGIFSAPI-------ALPYLAEVFEEHNA-- 279
|
330
....*....|....*....
gi 1208968218 346 LEQLIQFLTEKPADTFGLE 364
Cdd:cd01294 280 LDKLEAFASDNGPNFYGLP 298
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
21-387 |
5.05e-11 |
|
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: 63.50 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 21 DLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVHLRE---PGGEHKETIetgtlaAAKGGFTTI--CAMPNT 94
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAAtQIVDAGGCYVSPGWIDLHVHVYQggtRYGDRPDMI------GVKSGVTTVvdAGSAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 95 RPVPDCREH-MEDLQKRIqeKAHVNVLPYGAItvrqAGSEMTDFETLkelgafaftddgvgvqDASMMLAAMKRAAKLNM 173
Cdd:cd01307 75 DNIDGFRYTvIERSATRV--YAFLNISRVGLV----AQDELPDPDNI----------------DEDAVVAAAREYPDVIV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 174 AVVAHCEentlinKGCVhegkfsekhGLNGIpsvcESVHIARDIllAEAADCHYHVcHVstkGSVRVIRDakragikvta 253
Cdd:cd01307 133 GLKARAS------KSVV---------GEWGI----KPLELAKKI--AKEADLPLMV-HI---GSPPPILD---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 254 EVTPhhlVLCEDDIPSADPNFKMNPPLRGKED-----HAALIEGL-LD---GTID--------MIATDHAPHTAEEKAQG 316
Cdd:cd01307 178 EVVP---LLRRGDVLTHCFNGKPNGIVDEEGEvlplvRRARERGViFDvghGTASfsfrvaraAIAAGLLPDTISSDIHG 254
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208968218 317 IERAPFGI-TGFETAFPLLYTNLvkkgiiTLEQLIQFLTEKPADTFGL-EAGRLKEGRTADITIIDLEQEEEI 387
Cdd:cd01307 255 RNRTNGPVyALATTLSKLLALGM------PLEEVIEAVTANPARMLGLaEIGTLAVGYDADLTVFDLKDGRVE 321
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
3-62 |
8.11e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 63.48 E-value: 8.11e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208968218 3 YLFKNGRYMNEE---GKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK08204 4 TLIRGGTVLTMDpaiGDLPRGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRHT 66
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-90 |
1.43e-10 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 62.42 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADnAEVIDVNGKLIAPGLVDVHVHlrepGG-------EHKETIETG 76
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPD-AEVIDLGGGYLAPGFIDLHVH----GGggvdfmdGTPEALRTI 75
|
90
....*....|....
gi 1208968218 77 TLAAAKGGFTTICA 90
Cdd:COG1820 76 ARAHARHGTTSFLP 89
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
4-176 |
2.27e-10 |
|
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: 61.88 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEGKIVatDLLVQDGKIAKVAENIT-ADNAEVIDVNGKLIAPGLVDVHVHLREP--GGEHKETIETGTLAA 80
Cdd:cd01293 1 LLRNARLADGGTALV--DIAIEDGRIAAIGPALAvPPDAEEVDAKGRLVLPAFVDPHIHLDKTftGGRWPNNSGGTLLEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 81 AKGGFTTIcampNTRPVPDCREHMEDLQKRIQE------KAHVNVLPYGAITVRQAGSEMtdFETLK---ELGAFAFTDD 151
Cdd:cd01293 79 IIAWEERK----LLLTAEDVKERAERALELAIAhgttaiRTHVDVDPAAGLKALEALLEL--REEWAdliDLQIVAFPQH 152
|
170 180
....*....|....*....|....*
gi 1208968218 152 GVGVQDASMMLaaMKRAAKLNMAVV 176
Cdd:cd01293 153 GLLSTPGGEEL--MREALKMGADVV 175
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-62 |
2.34e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 59.04 E-value: 2.34e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208968218 4 LFKNGR-YMNEEGKIVATDLLVQDGKIAKV-----AENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:COG1574 11 LLTNGRiYTMDPAQPVAEAVAVRDGRIVAVgsdaeVRALAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-61 |
1.18e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 56.73 E-value: 1.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208968218 1 MNYLFKNGRYM-NEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:PRK08393 1 MSILIKNGYVIyGENLKVIRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTH 62
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
11-62 |
2.49e-08 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 55.78 E-value: 2.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1208968218 11 MNEEGKIVATDLLVQDGKIAKVAENITADNA-EVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK07228 13 MNAKREIVDGDVLIEDDRIAAVGDRLDLEDYdDHIDATGKVVIPGLIQGHIHL 65
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-62 |
3.93e-08 |
|
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: 55.22 E-value: 3.93e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208968218 3 YLFKNGR--YMNEEGKIVAT-DLLVQDGKIAKVAENITA----DNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:COG0402 2 LLIRGAWvlTMDPAGGVLEDgAVLVEDGRIAAVGPGAELparyPAAEVIDAGGKLVLPGLVNTHTHL 68
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
2-62 |
1.19e-07 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 53.48 E-value: 1.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208968218 2 NYLFKNGR----YMNEEGKIVAT-----DLLVQDGKIAKVAENITA--DNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK06846 5 HYWLTNVRletgFDYENGVIVQTetalcTLEIQDGKIVAIRPNKQVpdATLPTYDANGLLMLPAFREMHIHL 76
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-61 |
1.26e-07 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 53.57 E-value: 1.26e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1208968218 4 LFKNGRYMN-EEGKIVATDLLVQDGKIAKVAENItADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:COG1001 8 VIKNGRLVNvFTGEILEGDIAIAGGRIAGVGDYI-GEATEVIDAAGRYLVPGFIDGHVH 65
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
21-62 |
3.46e-07 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 51.94 E-value: 3.46e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1208968218 21 DLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK07572 19 DIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
4-62 |
6.56e-07 |
|
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: 51.05 E-value: 6.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208968218 4 LFKNGRY--MNEEGKIVATDLLVQDGKIAKVAENITA---DNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:cd01298 2 LIRNGTIvtTDPRRVLEDGDVLVEDGRIVAVGPALPLpayPADEVIDAKGKVVMPGLVNTHTHL 65
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
4-62 |
8.26e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 50.70 E-value: 8.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMNEEgkivATDLLVQDGKIAKVAENITAD-NAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK05985 5 LFRNVRPAGGA----AVDILIRDGRIAAIGPALAAPpGAEVEDGGGALALPGLVDGHIHL 60
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
21-107 |
9.17e-07 |
|
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 131030 Cd Length: 389 Bit Score: 50.55 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 21 DLLVQDGKIAKVAENITA-----DNAEVIDVNGKLIAPGLVDVHVHLREPGGEHKETIETGTLA---AAKGGFTTICAMP 92
Cdd:TIGR01975 19 DILIANDKIIAIADEIPStkdfvPNCVVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPELTlsdITKGGVTTVVGLL 98
|
90
....*....|....*
gi 1208968218 93 NTRPVpdCReHMEDL 107
Cdd:TIGR01975 99 GTDGI--TR-HMESL 110
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
1-61 |
2.44e-06 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 49.81 E-value: 2.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208968218 1 MNYLFKNGR-Y--MNE-EGKIVatDLLVQDGKIakVAENITADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:COG1229 1 MELIIKNGRvYdpANGiDGEVM--DIAIKDGKI--VEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
26-419 |
3.10e-06 |
|
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: 48.85 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 26 DGKIAKVAENITAD-NAEVIDVNGKLIAPGLVDVHVHL-REPGGEHKETIETGTLAAAkggftticAMPNTRPVpDCREH 103
Cdd:cd01309 1 DGKIVAVGAEITTPaDAEVIDAKGKHVTPGLIDAHSHLgLDEEGGVRETSDANEETDP--------VTPHVRAI-DGINP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 104 MEDLQKRIQEKA--HVNVLPYGAITVRQAGSEMTDFETLkelgafafTDDGVGVQDASMMLA----------AMKRAAKL 171
Cdd:cd01309 72 DDEAFKRARAGGvtTVQVLPGSANLIGGQGVVIKTDGGT--------IEDMFIKAPAGLKMAlgenpkrvygGKGKEPAT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 172 NMAVVAHcEENTLINKGCVHEGKFSEKHGLNGIPsvcesvhiARDI---LLAEAADCHYHV-CHVSTKGSVR-VIRDAKR 246
Cdd:cd01309 144 RMGVAAL-LRDAFIKAQEYGRKYDLGKNAKKDPP--------ERDLkleALLPVLKGEIPVrIHAHRADDILtAIRIAKE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 247 AGIKVTAEvtpHHL-------VLCEDDIPSADP----NFKMNPPLRGKEDHAALIeglldgtidmiatdhaphtaeEKAQ 315
Cdd:cd01309 215 FGIKITIE---HGAegykladELAKHGIPVIYGptltLPKKVEEVNDAIDTNAYL---------------------LKKG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 316 GIeraPFGITGFETAFPLLYTNL-----VKKGiITLEQLIQFLTEKPADTFGLE--AGRLKEGRTADITIIDleqEEEID 388
Cdd:cd01309 271 GV---AFAISSDHPVLNIRNLNLeaakaVKYG-LSYEEALKAITINPAKILGIEdrVGSLEPGKDADLVVWN---GDPLE 343
|
410 420 430
....*....|....*....|....*....|.
gi 1208968218 389 PTTflskgkntpfagwkcqgWPVMTIVGGKI 419
Cdd:cd01309 344 PTS-----------------KPEQVYIDGRL 357
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
4-62 |
6.41e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 48.21 E-value: 6.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 4 LFKNGRYMN-EEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK06038 5 IIKNAYVLTmDAGDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTHA 64
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
22-61 |
1.29e-05 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 47.11 E-value: 1.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1208968218 22 LLVQDGKIAKV--AENITA---DNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:PRK09228 34 LLVEDGRIVAAgpYAELRAqlpADAEVTDYRGKLILPGFIDTHIH 78
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-59 |
1.97e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 46.33 E-value: 1.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1208968218 1 MNYLFKNGRYMNEEGkIVATDLLVQDGKIAKVAENiTADNAEVIDVNGKLIAPGLVDVH 59
Cdd:PRK15446 2 MEMILSNARLVLPDE-VVDGSLLIEDGRIAAIDPG-ASALPGAIDAEGDYLLPGLVDLH 58
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
21-62 |
3.67e-05 |
|
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: 45.76 E-value: 3.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1208968218 21 DLLVQDGKIAKV-----AENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:cd01300 1 AVAVRDGRIVAVgsdaeAKALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
22-62 |
4.34e-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: 45.33 E-value: 4.34e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1208968218 22 LLVQDGKIAKV-----AENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:cd01296 1 IAIRDGRIAAVgpaasLPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
18-62 |
5.06e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 45.36 E-value: 5.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1208968218 18 VATDLLVQDGKIAKVA-ENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK07583 39 VLVDIEIADGKIAAILpAGGAPDELPAVDLKGRMVWPCFVDMHTHL 84
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
21-61 |
5.45e-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: 45.48 E-value: 5.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1208968218 21 DLLVQDGKIakVAENITADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:cd01304 19 DIFIRDGKI--VESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
344-419 |
1.08e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 44.44 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208968218 344 ITLEQLIQFLTEKPADTFGLE--AGRLKEGRTADITIIDLEqEEEIDPTTFLSKGkntpfagwkcqgwPVMTIVGGKI 419
Cdd:pfam07969 399 LSLEEALALYTSGPAKALGLEdrKGTLGVGKDADLVVLDDD-PLTVDPPAIADIR-------------VRLTVVDGRV 462
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
41-153 |
6.08e-04 |
|
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 41.51 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 41 AEVIDVNGKLIAPGLVDVHVHL--REPGGEHKETIETG--TLAAAK-------GGFTTicampntrpVPDC-REHMEDLQ 108
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLgsDPGDLPLDLALPVEyrTIRATRqaraalrAGFTT---------VRDAgGADYGLLR 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1208968218 109 KRIQEKAHV--NVLPYG-AITVRQAGSEMTDFETLKELGAFAFTDDGV 153
Cdd:cd01299 72 DAIDAGLIPgpRVFASGrALSQTGGHGDPRGLSGLFPAGGLAAVVDGV 119
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
13-61 |
8.24e-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: 41.49 E-value: 8.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1208968218 13 EEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVH 61
Cdd:cd01303 25 EDGLIVVVDGNIIAAGAAETLKRAAKPGARVIDSPNQFILPGFIDTHIH 73
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
347-384 |
3.29e-03 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 39.57 E-value: 3.29e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1208968218 347 EQLIQFLTEKPADTFGLEAGRLKEGRTADITIIDLEQE 384
Cdd:PRK08418 342 KILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEE 379
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
17-85 |
3.40e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 39.69 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 17 IVATDLLVQDGKIAKV--AEN-----------ITADNAEVIDVNGKLIAPGLVDVHVHLREPgGEHKETIETGTLAAAKG 83
Cdd:PRK13308 84 IVKGDIGIRDGRIVGIgkAGNpdimdgvdprlVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-QLVDHALASGITTMLGG 162
|
..
gi 1208968218 84 GF 85
Cdd:PRK13308 163 GL 164
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-62 |
3.48e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 39.48 E-value: 3.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208968218 1 MNYLFKNGRYM--NEEGKIVATDLLVQDGKIAKVAEnITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK06380 1 MSILIKNAWIVtqNEKREILQGNVYIEGNKIVYVGD-VNEEADYIIDATGKVVMPGLINTHAHV 63
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-68 |
5.44e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 38.97 E-value: 5.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208968218 1 MNYLFKNGRYMN-EEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLIAPGLVDVHVHLREPGGE 68
Cdd:PRK12394 3 NDILITNGHIIDpARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAHVFYDGTE 71
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
21-62 |
6.09e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 38.68 E-value: 6.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1208968218 21 DLLVQDGKIAKV--AENITADNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK08203 25 GLVVEGGRIVEVgpGGALPQPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
3-62 |
7.74e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 38.38 E-value: 7.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208968218 3 YLFKNGRYM-NEEGKIVATD--LLVQDGKIAKV--AENITA--DNAEVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK07203 2 LLIGNGTAItRDPAKPVIEDgaIAIEGNVIVEIgtTDELKAkyPDAEFIDAKGKLIMPGLINSHNHI 68
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
344-421 |
7.86e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 38.20 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968218 344 ITLEQLIQFLTEKPADTFGLEA--GRLKEGRTADITIIDLeqeeeidpttflsKGKNTPFA---GWKCQGW----PVMTI 414
Cdd:PRK12394 301 MALEDVINACTHTPAVLMGMAAeiGTLAPGAFADIAIFKL-------------KNRHVEFAdihGETLTGThvlvPQMTI 367
|
....*..
gi 1208968218 415 VGGKIAW 421
Cdd:PRK12394 368 KSGEILY 374
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
2-62 |
9.72e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 38.14 E-value: 9.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208968218 2 NYLFKNGRYMNEEGkivATDLLVQDGKIAKVAENITADNA--EVIDVNGKLIAPGLVDVHVHL 62
Cdd:PRK09230 5 LMTIKNARLPGKEG---LWQITIEDGKISAIEPQSEASLEagEVLDAEGGLAIPPFIEPHIHL 64
|
|
|