|
Name |
Accession |
Description |
Interval |
E-value |
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
1-577 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 1163.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 1 MTRLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRCGGPGLAGEEAVFGGGKVLRESMGQSRLTRAGGAPDTVITGAVI 80
Cdd:PRK13206 1 MTRLSRERYAALYGPTTGDRIRLADTDLLIEVTEDRSGGPGLAGDEAVFGGGKVIRESMGQGRATRAEGAPDTVITGAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 81 IDYWGIIKADIGIRDGRIVGIGKAGNPDIMDGVHPQLIVGPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEEAIGGGITT 160
Cdd:PRK13206 81 LDHWGIVKADVGIRDGRIVAIGKAGNPDIMDGVHPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICPQIVDEALAAGITT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 161 MIGGGTGPAEGSKATTVTPGAWHLGRMLQALDRWPVNVLLLGKGNTVNPESMWEQLRGGAAGFKLHEDWGTTPAVIDACL 240
Cdd:PRK13206 161 LIGGGTGPAEGSKATTVTPGAWHLARMLEALDGWPVNVALLGKGNTVSAEALWEQLRGGAGGFKLHEDWGSTPAAIDACL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 241 RVADEADVQVALHSDTLNETGFVEGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSSTNPTRPHTVNTLDEHL 320
Cdd:PRK13206 241 RVADAAGVQVALHSDTLNEAGFVEDTLAAIAGRSIHAYHTEGAGGGHAPDIITVASHPNVLPSSTNPTRPHTVNTLDEHL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 321 DMLMVCHHLNAAVPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEVVMRTWQTAHVMKKRRGALEGDPS 400
Cdd:PRK13206 321 DMLMVCHHLNPAVPEDLAFAESRIRPSTIAAEDVLHDMGAISMIGSDSQAMGRIGEVVLRTWQTAHVMKRRRGALPGDGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 401 gargNDNNRVRRYVAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRPHVVIKGGAIAWAAMGDANASIPTPQP 480
Cdd:PRK13206 401 ----ADNNRARRYVAKYTICPAVAHGIDHEIGSVEVGKLADLVLWEPAFFGVRPHAVLKGGAIAWAAMGDANASIPTPQP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 481 VLPRPMFGAMPNVAPGLAVHFVSPTAIEDDLAARLALRRRLVPTRDVRNRGKADLPLNDAMPDIRVDPDTFTVRIDGEVW 560
Cdd:PRK13206 477 VLPRPMFGAAPAAAAATSVHFVAPQAIEDGLADRLGLRRRLVPVADTRAVGKADMPLNDALPDIEVDPDTFTVRIDGEVW 556
|
570
....*....|....*..
gi 1093666480 561 QEQPATELPMAQRYFLF 577
Cdd:PRK13206 557 EPQPAAELPMAQRYFLF 573
|
|
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
1-577 |
0e+00 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 1117.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 1 MTRLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRCGGpglaGEEAVFGGGKVLRESMGQSRLTRAGGAPDTVITGAVI 80
Cdd:COG0804 1 MAKISRKAYADLYGPTTGDRVRLADTDLFIEVEKDLTTY----GDEVKFGGGKVIRDGMGQSQTTRAEGALDLVITNAVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 81 IDYWGIIKADIGIRDGRIVGIGKAGNPDIMDGVHPQLIVGPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEEAIGGGITT 160
Cdd:COG0804 77 LDHWGIVKADIGIKDGRIVGIGKAGNPDTMDGVDPDLVIGPGTEVIAGEGLILTAGGIDTHIHFICPQQIEEALASGITT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 161 MIGGGTGPAEGSKATTVTPGAWHLGRMLQALDRWPVNVLLLGKGNTVNPESMWEQLRGGAAGFKLHEDWGTTPAVIDACL 240
Cdd:COG0804 157 MIGGGTGPAEGTNATTCTPGPWNIARMLEAADALPMNIGFLGKGNASSPEALEEQIRAGACGLKLHEDWGATPAAIDACL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 241 RVADEADVQVALHSDTLNETGFVEGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSSTNPTRPHTVNTLDEHL 320
Cdd:COG0804 237 SVADEYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 321 DMLMVCHHLNAAVPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEVVMRTWQTAHVMKKRRGALEGDPS 400
Cdd:COG0804 317 DMLMVCHHLDPSIPEDVAFAESRIRPETIAAEDVLHDLGAISMMSSDSQAMGRVGEVITRTWQTAHKMKKQRGPLPGDSG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 401 garGNDNNRVRRYVAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRPHVVIKGGAIAWAAMGDANASIPTPQP 480
Cdd:COG0804 397 ---RNDNFRVKRYVAKYTINPAIAHGISHEVGSVEVGKLADLVLWDPAFFGVKPELVIKGGMIAWAQMGDPNASIPTPQP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 481 VLPRPMFGAMPNVAPGLAVHFVSPTAIEDDLAARLALRRRLVPTRDVRNRGKADLPLNDAMPDIRVDPDTFTVRIDGEVW 560
Cdd:COG0804 474 VHYRPMFGAYGKALAATSVTFVSQAALEAGIAERLGLRKRLLPVKNTRNIGKADMVLNDATPDIEVDPETYEVRVDGELL 553
|
570
....*....|....*..
gi 1093666480 561 QEQPATELPMAQRYFLF 577
Cdd:COG0804 554 TCEPATELPLAQRYFLF 570
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
1-577 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 1018.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 1 MTRLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRCggpgLAGEEAVFGGGKVLRESMGQSRLTRAGGAPDTVITGAVI 80
Cdd:PRK13207 1 MAKISRRAYAEMYGPTTGDRVRLADTELWIEVEKDFT----TYGEEVKFGGGKVIRDGMGQSQRARADGAVDTVITNALI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 81 IDYWGIIKADIGIRDGRIVGIGKAGNPDIMDGVHpqLIVGPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEEAIGGGITT 160
Cdd:PRK13207 77 LDHWGIVKADIGIKDGRIVAIGKAGNPDIQDGVD--IIIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQIEEALASGVTT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 161 MIGGGTGPAEGSKATTVTPGAWHLGRMLQALDRWPVNVLLLGKGNTVNPESMWEQLRGGAAGFKLHEDWGTTPAVIDACL 240
Cdd:PRK13207 155 MIGGGTGPATGTNATTCTPGPWHIHRMLQAADAFPMNIGFLGKGNASLPEALEEQIEAGAIGLKLHEDWGATPAAIDNCL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 241 RVADEADVQVALHSDTLNETGFVEGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSSTNPTRPHTVNTLDEHL 320
Cdd:PRK13207 235 SVADEYDVQVAIHTDTLNESGFVEDTIAAFKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 321 DMLMVCHHLNAAVPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEVVMRTWQTAHVMKKRRGALEGDPS 400
Cdd:PRK13207 315 DMLMVCHHLDPSIPEDVAFAESRIRRETIAAEDILHDLGAISMISSDSQAMGRVGEVIIRTWQTAHKMKVQRGPLPGDSG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 401 garGNDNNRVRRYVAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRPHVVIKGGAIAWAAMGDANASIPTPQP 480
Cdd:PRK13207 395 ---RNDNFRVKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWKPAFFGVKPELVLKGGMIAWAPMGDPNASIPTPQP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 481 VLPRPMFGAMPNVAPGLAVHFVSPTAIEDDLAARLALRRRLVPTRDVRNRGKADLPLNDAMPDIRVDPDTFTVRIDGEVW 560
Cdd:PRK13207 472 VHYRPMFGAYGGALAATSVTFVSQAALDAGIPEKLGLKKRLVPVKNTRGITKADMKLNDATPKIEVDPETYEVRADGELL 551
|
570
....*....|....*..
gi 1093666480 561 QEQPATELPMAQRYFLF 577
Cdd:PRK13207 552 TCEPATVLPLAQRYFLF 568
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
3-576 |
0e+00 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 984.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 3 RLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRCggpgLAGEEAVFGGGKVLRESMGQSRLTRAGGAPDTVITGAVIID 82
Cdd:cd00375 1 KISREAYADMYGPTTGDKVRLGDTDLWIEVEKDYT----TYGDEVKFGGGKVLRDGMGQSSGYTREDVLDLVITNALIID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 83 YWGIIKADIGIRDGRIVGIGKAGNPDIMDGVHPQLIVGPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEEAIGGGITTMI 162
Cdd:cd00375 77 YTGIYKADIGIKDGRIVAIGKAGNPDIMDGVTPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIEEALASGITTMI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 163 GGGTGPAEGSKATTVTPGAWHLGRMLQALDRWPVNVLLLGKGNTVNPESMWEQLRGGAAGFKLHEDWGTTPAVIDACLRV 242
Cdd:cd00375 157 GGGTGPAAGTKATTCTPGPWNIKRMLQAADGLPVNIGFLGKGNGSSPDALAEQIEAGACGLKLHEDWGATPAAIDTCLSV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 243 ADEADVQVALHSDTLNETGFVEGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSSTNPTRPHTVNTLDEHLDM 322
Cdd:cd00375 237 ADEYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTYHTEGAGGGHAPDIIKVAGHPNVLPSSTNPTRPFTVNTLDEHLDM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 323 LMVCHHLNAAVPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEVVMRTWQTAHVMKKRRGALEGDPSga 402
Cdd:cd00375 317 LMVCHHLDPNIPEDVAFAESRIRAETIAAEDVLHDLGAISIMSSDSQAMGRVGEVILRTWQTAHKMKAQRGPLPEDSG-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 403 rGNDNNRVRRYVAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRPHVVIKGGAIAWAAMGDANASIPTPQPVL 482
Cdd:cd00375 395 -DADNFRVKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGVKPEMVLKGGFIAYAQMGDPNASIPTPQPVM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 483 PRPMFGAMPNVAPGLAVHFVSPTAIEDDLAARLALRRRLVPTRDVRNRGKADLPLNDAMPDIRVDPDTFTVRIDGEVWQE 562
Cdd:cd00375 474 MRPMFGAHGKAPAATSVTFVSQASLDAGIAEELGLRRRVVAVKNCRGVGKKDMKLNSATPDIEVDPETYEVRVDGELLTC 553
|
570
....*....|....
gi 1093666480 563 QPATELPMAQRYFL 576
Cdd:cd00375 554 EPADELPLAQRYFL 567
|
|
| urease_alph |
TIGR01792 |
urease, alpha subunit; This model describes the urease alpha subunit UreC (designated beta or ... |
3-577 |
0e+00 |
|
urease, alpha subunit; This model describes the urease alpha subunit UreC (designated beta or B chain, UreB in Helicobacter species). Accessory proteins for incorporation of the nickel cofactor are usually found in addition to the urease alpha, beta, and gamma subunits. The trusted cutoff is set above the scores of many reported fragments and of a putative second urease alpha chain in Streptomyces coelicolor. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 273810 [Multi-domain] Cd Length: 567 Bit Score: 842.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 3 RLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRCggpgLAGEEAVFGGGKVLRESMGQ-SRLTRAGGAPDTVITGAVII 81
Cdd:TIGR01792 1 KMSREQYASLYGPTTGDKVRLGDTDLFVEVEKDLT----TYGDESKFGGGKVLRDGMGQnATLTRNAGVLDLVITNALIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 82 DYWGIIKADIGIRDGRIVGIGKAGNPDIMDGVhpQLIVGPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEEAIGGGITTM 161
Cdd:TIGR01792 77 DWTGIYKADIGIKNGRIVGIGKAGNPDTMDGV--DMIVGASTEAISGEGKIVTAGGIDTHVHYISPQQVQAALDNGITTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 162 IGGGTGPAEGSKATTVTPGAWHLGRMLQALDRWPVNVLLLGKGNTVNPESMWEQLRGGAAGFKLHEDWGTTPAVIDACLR 241
Cdd:TIGR01792 155 IGGGTGPADGTNATTCTPGPWYLHRMLQAADGLPINFGFTGKGSGSGPAALIEQIEAGACGLKVHEDWGATPAAIDNALS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 242 VADEADVQVALHSDTLNETGFVEGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSSTNPTRPHTVNTLDEHLD 321
Cdd:TIGR01792 235 VADEYDVQVAVHTDTLNESGFVEDTIAAFKGRTIHTYHTEGAGGGHAPDIIVVVGYNNILPSSTNPTLPYTVNTIDEHLD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 322 MLMVCHHLNAAVPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEVVMRTWQTAHVMKKRRGALEGDpsg 401
Cdd:TIGR01792 315 MLMVCHHLNPKIPEDVAFAESRIRKETIAAEDVLQDMGAISMISSDSQAMGRIGEVVTRCWQTADKMKKQRGPLPGD--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 402 ARGNDNNRVRRYVAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRPHVVIKGGAIAWAAMGDANASIPTPQPV 481
Cdd:TIGR01792 392 SPGNDNNRVKRYVAKYTINPAITHGISDYIGSIEVGKLADLVLWEPAFFGVKPDMVLKGGLIAWAIMGDPNASIPTPQPV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 482 LPRPMFGAMPNVAPGLAVHFVSPTAIEDDLAARLALRRRLVPTRDVRNRGKADLPLNDAMPDIRVDPDTFTVRIDGEVWQ 561
Cdd:TIGR01792 472 LYRPMFGAYGRALQSTSITFVSQAAYDKGIKERLGLQKLLLPVHNTRSIGKADMKLNSATPKIEVDPQTYDVKVDGVLIT 551
|
570
....*....|....*.
gi 1093666480 562 EQPATELPMAQRYFLF 577
Cdd:TIGR01792 552 VEPADELPLTQRYFLF 567
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
1-576 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 837.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 1 MTRLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRcggpGLAGEEAVFGGGKVLRESMG-QSRLTRAGGAPDTVITGAV 79
Cdd:PRK13308 1 MATIDRRAYAELYGPTTGDRVRLADTSLLAEVEHDH----TVYGDECLFGGGKTLRDGMGmAPGVTSADGALDFVLCNVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 80 IID-YWGIIKADIGIRDGRIVGIGKAGNPDIMDGVHPQLIVGPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEEAIGGGI 158
Cdd:PRK13308 77 VIDpVLGIVKGDIGIRDGRIVGIGKAGNPDIMDGVDPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQLVDHALASGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 159 TTMIGGGTGPAegskATTVTPGAWHLGRMLQALDRWPVNVLLLGKGNTVNPESMWEQLRGGAAGFKLHEDWGTTPAVIDA 238
Cdd:PRK13308 157 TTMLGGGLGPT----VGIDSGGPFNTGRMLQAAEAWPVNFGFLGRGNSSKPAALIEQVEAGACGLKIHEDWGAMPAAIDT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 239 CLRVADEADVQVALHSDTLNETGFVEGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSSTNPTRPHTVNTLDE 318
Cdd:PRK13308 233 CLEVADEYDFQVQLHTDTLNESGFVEDTLAAIGGRTIHMYHTEGAGGGHAPDIIRVVGEPHCLPSSTNPTNPYTVNTFDE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 319 HLDMLMVCHHLNAAVPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEVVMRTWQTAHVMKKRRGALEGD 398
Cdd:PRK13308 313 HLDMTMVCHHLNPDVPEDVAFAESRIRAQTIAAEDVLHDIGAISMLGSDSQGMGRIAEVIARTWQLASKMKDQRGPLPED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 399 PSGarGNDNNRVRRYVAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRPHVVIKGGAIAWAAMGDANASIPTP 478
Cdd:PRK13308 393 RGT--FADNARIKRYIAKYTINPAITFGIDDHIGSLEPGKLADIVLWRPAFFGIKPELVIKGGFPAWAAMGDANGSLMTC 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 479 QPVLPRPMFGAMPNVAPGLAVHFVSPTAIEDDLAARLALRRRLVPTRDVRNRGKADLPLNDAMPDIRVDPDTFTVRIDGE 558
Cdd:PRK13308 471 EPMLQRPQWGAFGRAKQALSVCFVSPLAIEAGLGERLGLRKRLLPVRGTRTLTKADMLHNDACPDIRVDPQTFEVFVDGE 550
|
570
....*....|....*...
gi 1093666480 559 VWQEQPATELPMAQRYFL 576
Cdd:PRK13308 551 LVTCEPATELPLAQRYML 568
|
|
| PLN02303 |
PLN02303 |
urease |
2-577 |
0e+00 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 832.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 2 TRLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRCggpgLAGEEAVFGGGKVLRESMGQSRLTRAGGAPDTVITGAVII 81
Cdd:PLN02303 269 TTISREKYANMYGPTTGDKIRLGDTNLYAEIEKDFT----VYGDECKFGGGKVLRDGMGQATGYGAADSLDTVITNAVII 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 82 DYWGIIKADIGIRDGRIVGIGKAGNPDIMDGVHPQLIVGPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEEAIGGGITTM 161
Cdd:PLN02303 345 DYTGIYKADIGIKDGLIVGIGKAGNPDVMDGVTSNMIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQLATEAIASGITTL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 162 IGGGTGPAEGSKATTVTPGAWHLGRMLQALDRWPVNVLLLGKGNTVNPESMWEQLRGGAAGFKLHEDWGTTPAVIDACLR 241
Cdd:PLN02303 425 VGGGTGPAHGTCATTCTPAPSHMKLMLQSTDDLPLNFGFTGKGNTAKPEGLHEIIKAGAMGLKLHEDWGTTPAAIDNCLD 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 242 VADEADVQVALHSDTLNETGFVEGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSSTNPTRPHTVNTLDEHLD 321
Cdd:PLN02303 505 VAEEYDIQVTIHTDTLNESGCVEHSIAAFKGRTIHTYHSEGAGGGHAPDIIKVCGVKNVLPSSTNPTRPYTKNTIDEHLD 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 322 MLMVCHHLNAAVPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEVVMRTWQTAHVMKKRRGALEGDPSg 401
Cdd:PLN02303 585 MLMVCHHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVITRTWQTAHKMKSQRGALEPRGA- 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 402 arGNDNNRVRRYVAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRPHVVIKGGAIAWAAMGDANASIPTPQPV 481
Cdd:PLN02303 664 --DNDNFRIKRYIAKYTINPAIAHGMSHFVGSVEVGKLADLVLWKPAFFGAKPEMVIKGGQIAWAQMGDPNASIPTPEPV 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 482 LPRPMFGAMPNVAPGLAVHFVSPTAIEDDLAARLALRRRLVPTRDVRNRGKADLPLNDAMPDIRVDPDTFTVRIDGEVWQ 561
Cdd:PLN02303 742 IMRPMFGAFGKAGSSNSIAFVSKAALDAGVKQLYGLTKRVEAVGNVRGLTKLDMKLNDALPVITVDPETYEVTADGEVLT 821
|
570
....*....|....*.
gi 1093666480 562 EQPATELPMAQRYFLF 577
Cdd:PLN02303 822 CAPATSVPLSRNYFLF 837
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
3-577 |
0e+00 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 710.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 3 RLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRCggpgLAGEEAVFGGGKVLRESMGQSRLTRAGGApDTVITGAVIID 82
Cdd:PRK13985 2 KISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYT----IYGEELKFGGGKTLREGMSQSNNPSKEEL-DLIITNALIID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 83 YWGIIKADIGIRDGRIVGIGKAGNPDIMDGVHPQLIVGPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEEAIGGGITTMI 162
Cdd:PRK13985 77 YTGIYKADIGIKDGKIAGIGKGGNKDMQDGVKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTAFASGVTTMI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 163 GGGTGPAEGSKATTVTPGAWHLGRMLQALDRWPVNVLLLGKGNTVNPESMWEQLRGGAAGFKLHEDWGTTPAVIDACLRV 242
Cdd:PRK13985 157 GGGTGPADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLGKGNSSNDASLADQIEAGAIGFKIHEDWGTTPSAINHALDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 243 ADEADVQVALHSDTLNETGFVEGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSSTNPTRPHTVNTLDEHLDM 322
Cdd:PRK13985 237 ADKYDVQVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGGHAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 323 LMVCHHLNAAVPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEVVMRTWQTAHVMKKRRGALEGDPSga 402
Cdd:PRK13985 317 LMVCHHLDKSIKEDVQFADSRIRPQTIAAEDTLHDMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKG-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 403 rGNDNNRVRRYVAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRPHVVIKGGAIAWAAMGDANASIPTPQPVL 482
Cdd:PRK13985 395 -DNDNFRIKRYLSKYTINPAIAHGISEYVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 483 PRPMFGAMPNVAPGLAVHFVSPTAIEDDLAARLALRRRLVPTRDVRNRGKADLPLNDAMPDIRVDPDTFTVRIDGEVWQE 562
Cdd:PRK13985 474 YREMFAHHGKAKYDANITFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTS 553
|
570
....*....|....*
gi 1093666480 563 QPATELPMAQRYFLF 577
Cdd:PRK13985 554 KPANKVSLAQLFSIF 568
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
1-576 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 703.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 1 MTRLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRCGgpglAGEEAVFGGGKVLRESMGQ-SRLTRAGGAPDTVITGAV 79
Cdd:PRK13309 1 MPQISRQEYAGLFGPTTGDKIRLGDTNLFIEIEKDLRG----YGDESVYGGGKSLRDGMGAnNNLTRDNGVLDLVITNVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 80 IID-YWGIIKADIGIRDGRIVGIGKAGNPDIMDGVHPQLIVGPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEEAIGGGI 158
Cdd:PRK13309 77 IVDaRLGVIKADVGIRDGKIVGIGKSGNPSTMDGVTQGMVVGVSTDAISGEHLILTAAGIDTHIHLISPQQAYHALSNGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 159 TTMIGGGTGPAEGSKATTVTPGAWHLGRMLQALDRWPVNVLLLGKGNTVNPESMWEQLRGGAAGFKLHEDWGTTPAVIDA 238
Cdd:PRK13309 157 TTFFGGGIGPTDGTNGTTVTPGPWNIRQMLRSIEGLPVNVGILGKGNSYGRGPLLEQAIAGVAGYKVHEDWGATAAALRH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 239 CLRVADEADVQVALHSDTLNETGFVEGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSSTNPTRPHTVNTLDE 318
Cdd:PRK13309 237 ALRVADEVDIQVAVHTDSLNECGYVEDTIDAFEGRTIHTFHTEGAGGGHAPDIIKVASQTNVLPSSTNPTLPYGVNSQAE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 319 HLDMLMVCHHLNAAVPEDLAFAESRIRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEVVMRTWQTAHVMKKRRGALegd 398
Cdd:PRK13309 317 LFDMIMVCHNLNPNVPADVAFAESRVRPETIAAENVLHDMGVISMFSSDSQAMGRVGENWLRAIQTADAMKAARGKL--- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 399 PSGARGNDNNRVRRYVAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRPHVVIKGGAIAWAAMGDANASIPTP 478
Cdd:PRK13309 394 PEDAAGNDNFRVLRYVAKITINPAITQGVSHVIGSVEVGKMADLVLWEPRFFGAKPKMVIKGGMINWAAMGDPNASLPTP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 479 QPVLPRPMFGAMPNVAPGLAVHFVSPTAIEDDLAARLALRRRLVPTRDVRNRGKADLPLNDAMPDIRVDPDTFTVRIDGE 558
Cdd:PRK13309 474 QPVFYRPMFGAMGKTLQDTCVTFVSQAALDDGVKEKAGLDRQVIAVKNCRTISKRDLVRNSQTPNIEVDPETFAVKVDGV 553
|
570
....*....|....*...
gi 1093666480 559 VWQEQPATELPMAQRYFL 576
Cdd:PRK13309 554 HATVKPIATASLNQRYFF 571
|
|
| Urease_alpha |
pfam00449 |
Urease alpha-subunit, N-terminal domain; The N-terminal domain is a composite domain and plays ... |
3-126 |
2.90e-68 |
|
Urease alpha-subunit, N-terminal domain; The N-terminal domain is a composite domain and plays a major trimer stabilising role by contacting the catalytic domain of the symmetry related alpha-subunit.
Pssm-ID: 425689 [Multi-domain] Cd Length: 120 Bit Score: 216.59 E-value: 2.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 3 RLSREHYAKLYGPTTGDRIRLADTDLLIEITEDRcggpGLAGEEAVFGGGKVLRESMGQSRLTRAGGAPDTVITGAVIID 82
Cdd:pfam00449 1 KISREAYADMYGPTTGDRIRLGDTDLFIEVEKDL----TVYGDEVKFGGGKVIRDGMGQSQGRTRDDALDLVITNALILD 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1093666480 83 YWGIIKADIGIRDGRIVGIGKAGNPDIMDGVHPQLIVGPSTEII 126
Cdd:pfam00449 77 YTGIVKADIGIKDGRIVGIGKAGNPDTMDGVTPGMVIGPSTEVI 120
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
132-460 |
1.17e-51 |
|
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: 180.39 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 132 IVTAGGIDCHVHF---------ICPQLVEEAIGGGITTMIGGGTGPAEGSKATTVTPGAwhlgRMLQALDRWPVNVLLLG 202
Cdd:pfam01979 1 IVLPGLIDAHVHLemgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIE----ALLEAAEELPLGLRFLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 203 K-------GNTVNPESMWEQLRGGA------------AGFKLHEDWGTTPAVIDACLRVADEADVQVALHsdTLNETGFV 263
Cdd:pfam01979 77 PgcsldtdGELEGRKALREKLKAGAefikgmadgvvfVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIH--ALETKGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 264 EGTLEAIAGRAIHAYHTEGAGGGHAPDIITVASHPNVMPSstnptrPHTVNTLDEHLDMLMVCHhlnaavpedLAFAESR 343
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLS------PTEANLLAEHLKGAGVAH---------CPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 344 IRPSTIAAEDLLHDiGAISMIGSDSQAMGRIGEVVMRTwqtAHVMKKRRgalegdpsgaRGNDNNRVRRYVAKYTICPAI 423
Cdd:pfam01979 220 LRSGRIALRKALED-GVKVGLGTDGAGSGNSLNMLEEL---RLALELQF----------DPEGGLSPLEALRMATINPAK 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1093666480 424 THGIDHELGSVEVGKLADLVLWE----PAFFGVRP-----HVVIKG 460
Cdd:pfam01979 286 ALGLDDKVGSIEVGKDADLVVVDldplAAFFGLKPdgnvkKVIVKG 331
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
74-272 |
2.24e-10 |
|
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: 62.80 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 74 VITGAVIIDYWGIIKADIGIRDGRIVGIGKAGNPDimdgvhpqlivgPSTEIIAGNDRIVTAGGIDCHVHFICPQLVEea 153
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAP------------EAAEVIDATGLLVLPGLIDLHVHLREPGLEH-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 154 igggittmigggtgpAE----GSKA------TTV-----------TPGAWhlgRMLQAL--DRWPVNVLLLG---KGNTV 207
Cdd:COG0044 67 ---------------KEdietGTRAaaaggvTTVvdmpntnpvtdTPEAL---EFKLARaeEKALVDVGPHGaltKGLGE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093666480 208 NPESMWEQLRGGAAGFKL-----HEDWGTTPAVIDACLRVADEADVQVALHS--DTLNETGFV-EGTLEAIAG 272
Cdd:COG0044 129 NLAELGALAEAGAVAFKVfmgsdDGNPVLDDGLLRRALEYAAEFGALVAVHAedPDLIRGGVMnEGKTSPRLG 201
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
73-144 |
1.58e-09 |
|
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: 60.31 E-value: 1.58e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093666480 73 TVITGAVIIDYWGIIKADIGIRDGRIVGIGkagnpdimdgvhPQLIVGPSTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIG------------PNLEAPGGVEVIDATGKYVLPGGIDPHTHL 60
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
72-144 |
9.07e-09 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 57.79 E-value: 9.07e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093666480 72 DTVITGAVIIDYWGIIKADIGIRDGRIVGIGKAgnpdimdgvhpqliVGPSTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:PRK13404 5 DLVIRGGTVVTATDTFQADIGIRGGRIAALGEG--------------LGPGAREIDATGRLVLPGGVDSHCHI 63
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
71-144 |
8.32e-08 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 55.11 E-value: 8.32e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093666480 71 PDTVITGAVIID-YWG-IIKADIGIRDGRIVGIGKAgnpdimdgvhpqliVGPSTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:COG1001 5 ADLVIKNGRLVNvFTGeILEGDIAIAGGRIAGVGDY--------------IGEATEVIDAAGRYLVPGFIDGHVHI 66
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
65-463 |
1.54e-07 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 53.81 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 65 TRAGGAPDTVITGAVIIDYWG---IIKADIGIRDGRIVGIGKAGnpdimdgvhpQLIVGPSTEIIAGNDRIVTAGGIDCH 141
Cdd:COG1228 2 KAPAQAGTLLITNATLVDGTGggvIENGTVLVEDGKIAAVGPAA----------DLAVPAGAEVIDATGKTVLPGLIDAH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 142 VHFicpqlveeaiGGGITTMIGGGTGPAEGSKATTVTPGAWHLGRMLQ--------------ALDRWPV---NVLLLGK- 203
Cdd:COG1228 72 THL----------GLGGGRAVEFEAGGGITPTVDLVNPADKRLRRALAagvttvrdlpggplGLRDAIIageSKLLPGPr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 204 -------------GNTVNPESMW----EQLRGGAAGFKLHEDWGT---TPAVIDACLRVADEADVQVALHSDTLnetgfv 263
Cdd:COG1228 142 vlaagpalsltggAHARGPEEARaalrELLAEGADYIKVFAEGGApdfSLEELRAILEAAHALGLPVAAHAHQA------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 264 EGTLEAIAGRAIHAYHTEGAGgghAPDIITVASHPNVmpsSTNPTrphtvntldehldmLMVCHHLNAAVPEDLAFAESR 343
Cdd:COG1228 216 DDIRLAVEAGVDSIEHGTYLD---DEVADLLAEAGTV---VLVPT--------------LSLFLALLEGAAAPVAAKARK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 344 IRPSTIAAEDLLHDIGAISMIGSDSQAMGRIGEvvmRTWQTAHVMKKR--------RGAlegdpsgargndnnrvrryva 415
Cdd:COG1228 276 VREAALANARRLHDAGVPVALGTDAGVGVPPGR---SLHRELALAVEAgltpeealRAA--------------------- 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1093666480 416 kyTICPAITHGIDHELGSVEVGKLADLVLWE---PAFFGV--RPHVVIKGGAI 463
Cdd:COG1228 332 --TINAAKALGLDDDVGSLEPGKLADLVLLDgdpLEDIAYleDVRAVMKDGRV 382
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
72-144 |
1.81e-07 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 53.94 E-value: 1.81e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093666480 72 DTVITGAVIIDYWGIIKADIGIRDGRIVGIGkagnPDIMdgvhpqlivGPSTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:PRK06189 4 DLIIRGGKVVTPEGVYRADIGIKNGKIAEIA----PEIS---------SPAREIIDADGLYVFPGMIDVHVHF 63
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
72-144 |
5.75e-07 |
|
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: 52.00 E-value: 5.75e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093666480 72 DTVITGAVIIDYWGIIKADIGIRDGRIVGIGkagnpdimdgvhpQLIVGPSTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:TIGR03178 1 DLIIRGGRVILPNGEREADVGVKGGKIAAIG-------------PDILGPAAKIIDAGGLVVFPGVVDTHVHI 60
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
72-144 |
1.31e-06 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 50.94 E-value: 1.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093666480 72 DTVITGAVIIDYWGIIKADIGIRDGRIVGIGKAGNpdimdgvhpqlivgpsTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGANLG----------------DEVIDATGKYVMPGGIDPHTHM 58
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
72-144 |
1.23e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 47.99 E-value: 1.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093666480 72 DTVITGAVIIDYWGIIKADIGIRDGRIVGIGKAGNPDimdgvhpqlivgpSTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:PRK09060 6 DLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGAS-------------AGEVIDCRGLHVLPGVIDSQVHF 65
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
72-147 |
6.07e-05 |
|
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: 45.74 E-value: 6.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093666480 72 DTVITGAVIIDYWGIIKADIGIRDGRIVGIGkagnpdimdgvhPQLIVGPSTEIIAGNDRIVTAGGIDCHVHFICP 147
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIG------------PDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP 64
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
73-144 |
7.59e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 45.19 E-value: 7.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093666480 73 TVITGAVIIDYWGI-IKADIGIRDGRIVGIGKAGNPDImdgvhpqlivgpsTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:PRK09357 3 ILIKNGRVIDPKGLdEVADVLIDDGKIAAIGENIEAEG-------------AEVIDATGLVVAPGLVDLHVHL 62
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
382-446 |
8.35e-05 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 45.56 E-value: 8.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093666480 382 WQTAHVMKKRRgalegDPSGARGNDNNRVRRYVA--KYTICPAITHGIDHELGSVEVGKLADLVLWE 446
Cdd:COG1574 444 LLGIYAAVTRR-----TPSGRGLGPEERLTVEEAlrAYTIGAAYAAFEEDEKGSLEPGKLADFVVLD 505
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
73-143 |
8.84e-05 |
|
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: 44.88 E-value: 8.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093666480 73 TVITGAVIIDYWGIIKADIGIRDGRIVGIGKAGNPDIMDgvhpqlivgpstEIIAGNDRIVTAGGIDCHVH 143
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEAD------------EIIDLKGQYLVPGFIDIHIH 59
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
382-444 |
2.08e-04 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 44.22 E-value: 2.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093666480 382 WQTAHVMKKRRGalegdPSG-ARGNDNNRVRRYVA--KYTICPAITHGIDHELGSVEVGKLADLVL 444
Cdd:cd01300 419 LLGIWAAVTRKT-----PGGgVLGNPEERLSLEEAlrAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
356-445 |
2.66e-04 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 43.45 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 356 HDIGAIsmIGSDSQAMGRIGEVVMRTWQTAHVMKKR--RGALEGDPSGARGNDNNRVRRYVAKY-----------TICPA 422
Cdd:cd01309 237 HGIPVI--YGPTLTLPKKVEEVNDAIDTNAYLLKKGgvAFAISSDHPVLNIRNLNLEAAKAVKYglsyeealkaiTINPA 314
|
90 100
....*....|....*....|...
gi 1093666480 423 ITHGIDHELGSVEVGKLADLVLW 445
Cdd:cd01309 315 KILGIEDRVGSLEPGKDADLVVW 337
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
72-143 |
3.43e-04 |
|
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: 43.05 E-value: 3.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093666480 72 DTVITGAVIIDYWG--IIKADIGIRDGRIVGIGKAGNPdimdgvhpqlivgPSTEIIAGNDRIVTAGGIDCHVH 143
Cdd:cd01297 1 DLVIRNGTVVDGTGapPFTADVGIRDGRIAAIGPILST-------------SAREVIDAAGLVVAPGFIDVHTH 61
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
65-145 |
5.83e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 42.86 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093666480 65 TRAGGAPDTVITGAVII--DYWGIIKADIGIRDGRIVGIGkaGNPDIMDgvhpqlIVGPSTEIIAGNDRIVTAGGIDCHV 142
Cdd:COG1574 2 KLAAAAADLLLTNGRIYtmDPAQPVAEAVAVRDGRIVAVG--SDAEVRA------LAGPATEVIDLGGKTVLPGFIDAHV 73
|
...
gi 1093666480 143 HFI 145
Cdd:COG1574 74 HLL 76
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
71-144 |
1.04e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 41.95 E-value: 1.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093666480 71 PDTVITGAVIIDYWGIIKADIGIRDGRIVGIGKAgnpdiMDGVHPQlivgpstEIIAGNDRIVTAGGIDCHVHF 144
Cdd:PRK02382 2 RDALLKDGRVYYNNSLQPRDVRIDGGKITAVGKD-----LDGSSSE-------EVIDARGMLLLPGGIDVHVHF 63
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
384-454 |
1.14e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 41.75 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093666480 384 TAHVMKKRRGAlegdpsGARGNDNNRVRRY--VAKYTICPAITHGIDHELGSVEVGKLADLVLWEPAFFGVRP 454
Cdd:pfam07969 379 GAAVMRQTAGG------GEVLGPDEELSLEeaLALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDP 445
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
91-145 |
1.38e-03 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 41.09 E-value: 1.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1093666480 91 IGIRDGRIVGIGKAgnPDImdgvhpQLIVGPSTEIIAGNDRIVTAGGIDCHVHFI 145
Cdd:cd01296 1 IAIRDGRIAAVGPA--ASL------PAPGPAAAEEIDAGGRAVTPGLVDCHTHLV 47
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
72-144 |
1.67e-03 |
|
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: 40.97 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093666480 72 DTVITGAVIIDYW---GIIK-ADIGIRDGRIVGIGKAGNPdimdgvhpqLIVGPSTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:COG0402 1 DLLIRGAWVLTMDpagGVLEdGAVLVEDGRIAAVGPGAEL---------PARYPAAEVIDAGGKLVLPGLVNTHTHL 68
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
74-143 |
2.65e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 40.22 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093666480 74 VITGAVIIDYWGIIKA--DIGIRDGRIVGIGKAGNPdimdgvhpqlivGPSTEIIAGNDRIVTAGGIDCHVH 143
Cdd:PRK09237 2 LLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDG------------SQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
73-143 |
2.80e-03 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 40.56 E-value: 2.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093666480 73 TVITGAVIID-YWGII--KADIGIRDGRIVgigkagnpdimdgvhPQLIVGPSTEIIAGNDRIVTAGGIDCHVH 143
Cdd:COG1229 3 LIIKNGRVYDpANGIDgeVMDIAIKDGKIV---------------EEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
93-149 |
4.87e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 39.40 E-value: 4.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1093666480 93 IRDGRIVGIGKAgnpdimDGVHPQLivGPSTEIIAGNDRIVTAGGIDCHVHFicPQL 149
Cdd:PRK09228 36 VEDGRIVAAGPY------AELRAQL--PADAEVTDYRGKLILPGFIDTHIHY--PQT 82
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
73-144 |
5.84e-03 |
|
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: 39.49 E-value: 5.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093666480 73 TVITGAVII---DYWGIIKADIGIRDGRIVGIGKAGnpdimdgvhpQLIVGPSTEIIAGNDRIVTAGGIDCHVHF 144
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPAL----------PLPAYPADEVIDAKGKVVMPGLVNTHTHL 65
|
|
| |
