|
Name |
Accession |
Description |
Interval |
E-value |
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
139-707 |
0e+00 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 1171.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 139 ALEISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSADLVITNAMIIDpV 218
Cdd:COG0804 1 MAKISRKAYADLYGPTTGDRVRLADTDLFIEVEKDLTTYGDEVKFGGGKVIRDGMGQSQTTRAEGALDLVITNAVILD-H 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 219 LGIIKADIGVKDGKILGVGNAGNPNVMDDVD--IVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIG 296
Cdd:COG0804 80 WGIVKADIGIKDGRIVGIGKAGNPDTMDGVDpdLVIGPGTEVIAGEGLILTAGGIDTHIHFICPQQIEEALASGITTMIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 297 GGTGPADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVA 376
Cdd:COG0804 160 GGTGPAEGTNATTCTPGPWNIARMLEAADALPMNIGFLGKGNASSPEALEEQIRAGACGLKLHEDWGATPAAIDACLSVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 377 DKTDTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMM 456
Cdd:COG0804 240 DEYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDML 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 457 MVCHHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEEND 536
Cdd:COG0804 320 MVCHHLDPSIPEDVAFAESRIRPETIAAEDVLHDLGAISMMSSDSQAMGRVGEVITRTWQTAHKMKKQRGPLPGDSGRND 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 537 NLRIKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPM 616
Cdd:COG0804 400 NFRVKRYVAKYTINPAIAHGISHEVGSVEVGKLADLVLWDPAFFGVKPELVIKGGMIAWAQMGDPNASIPTPQPVHYRPM 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 617 FGALGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAE 696
Cdd:COG0804 480 FGAYGKALAATSVTFVSQAALEAGIAERLGLRKRLLPVKNTRNIGKADMVLNDATPDIEVDPETYEVRVDGELLTCEPAT 559
|
570
....*....|.
gi 663535746 697 KLSLARLYCLY 707
Cdd:COG0804 560 ELPLAQRYFLF 570
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
141-707 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 1142.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSADLVITNAMIIDPvLG 220
Cdd:PRK13207 3 KISRRAYAEMYGPTTGDRVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQRARADGAVDTVITNALILDH-WG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 221 IIKADIGVKDGKILGVGNAGNPNVMDDVDIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGGGTG 300
Cdd:PRK13207 82 IVKADIGIKDGRIVAIGKAGNPDIQDGVDIIIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQIEEALASGVTTMIGGGTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 301 PADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVADKTD 380
Cdd:PRK13207 162 PATGTNATTCTPGPWHIHRMLQAADAFPMNIGFLGKGNASLPEALEEQIEAGAIGLKLHEDWGATPAAIDNCLSVADEYD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 381 TQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMMVCH 460
Cdd:PRK13207 242 VQVAIHTDTLNESGFVEDTIAAFKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLMVCH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 461 HLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEENDNLRI 540
Cdd:PRK13207 322 HLDPSIPEDVAFAESRIRRETIAAEDILHDLGAISMISSDSQAMGRVGEVIIRTWQTAHKMKVQRGPLPGDSGRNDNFRV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 541 KRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPMFGAL 620
Cdd:PRK13207 402 KRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWKPAFFGVKPELVLKGGMIAWAPMGDPNASIPTPQPVHYRPMFGAY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 621 GKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAEKLSL 700
Cdd:PRK13207 482 GGALAATSVTFVSQAALDAGIPEKLGLKKRLVPVKNTRGITKADMKLNDATPKIEVDPETYEVRADGELLTCEPATVLPL 561
|
....*..
gi 663535746 701 ARLYCLY 707
Cdd:PRK13207 562 AQRYFLF 568
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
141-706 |
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: 1028.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSADLVITNAMIIDPVlG 220
Cdd:cd00375 1 KISREAYADMYGPTTGDKVRLGDTDLWIEVEKDYTTYGDEVKFGGGKVLRDGMGQSSGYTREDVLDLVITNALIIDYT-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 221 IIKADIGVKDGKILGVGNAGNPNVMDDVD--IVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGGG 298
Cdd:cd00375 80 IYKADIGIKDGRIVAIGKAGNPDIMDGVTpnMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIEEALASGITTMIGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 299 TGPADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVADK 378
Cdd:cd00375 160 TGPAAGTKATTCTPGPWNIKRMLQAADGLPVNIGFLGKGNGSSPDALAEQIEAGACGLKLHEDWGATPAAIDTCLSVADE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 379 TDTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMMV 458
Cdd:cd00375 240 YDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTYHTEGAGGGHAPDIIKVAGHPNVLPSSTNPTRPFTVNTLDEHLDMLMV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 459 CHHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEENDNL 538
Cdd:cd00375 320 CHHLDPNIPEDVAFAESRIRAETIAAEDVLHDLGAISIMSSDSQAMGRVGEVILRTWQTAHKMKAQRGPLPEDSGDADNF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 539 RIKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPMFG 618
Cdd:cd00375 400 RVKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGVKPEMVLKGGFIAYAQMGDPNASIPTPQPVMMRPMFG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 619 ALGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAEKL 698
Cdd:cd00375 480 AHGKAPAATSVTFVSQASLDAGIAEELGLRRRVVAVKNCRGVGKKDMKLNSATPDIEVDPETYEVRVDGELLTCEPADEL 559
|
....*...
gi 663535746 699 SLARLYCL 706
Cdd:cd00375 560 PLAQRYFL 567
|
|
| urease_alph |
TIGR01792 |
urease, alpha subunit; This model describes the urease alpha subunit UreC (designated beta or ... |
141-707 |
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: 937.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLR-KDSADLVITNAMIIDPVl 219
Cdd:TIGR01792 1 KMSREQYASLYGPTTGDKVRLGDTDLFVEVEKDLTTYGDESKFGGGKVLRDGMGQNATLTRnAGVLDLVITNALILDWT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 220 GIIKADIGVKDGKILGVGNAGNPNVMDDVDIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGGGT 299
Cdd:TIGR01792 80 GIYKADIGIKNGRIVGIGKAGNPDTMDGVDMIVGASTEAISGEGKIVTAGGIDTHVHYISPQQVQAALDNGITTLIGGGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 300 GPADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVADKT 379
Cdd:TIGR01792 160 GPADGTNATTCTPGPWYLHRMLQAADGLPINFGFTGKGSGSGPAALIEQIEAGACGLKVHEDWGATPAAIDNALSVADEY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 380 DTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMMVC 459
Cdd:TIGR01792 240 DVQVAVHTDTLNESGFVEDTIAAFKGRTIHTYHTEGAGGGHAPDIIVVVGYNNILPSSTNPTLPYTVNTIDEHLDMLMVC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 460 HHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEENDNLR 539
Cdd:TIGR01792 320 HHLNPKIPEDVAFAESRIRKETIAAEDVLQDMGAISMISSDSQAMGRIGEVVTRCWQTADKMKKQRGPLPGDSPGNDNNR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 540 IKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPMFGA 619
Cdd:TIGR01792 400 VKRYVAKYTINPAITHGISDYIGSIEVGKLADLVLWEPAFFGVKPDMVLKGGLIAWAIMGDPNASIPTPQPVLYRPMFGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 620 LGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAEKLS 699
Cdd:TIGR01792 480 YGRALQSTSITFVSQAAYDKGIKERLGLQKLLLPVHNTRSIGKADMKLNSATPKIEVDPQTYDVKVDGVLITVEPADELP 559
|
....*...
gi 663535746 700 LARLYCLY 707
Cdd:TIGR01792 560 LTQRYFLF 567
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
267-594 |
1.56e-67 |
|
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: 225.46 E-value: 1.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 267 TPGTIDSHIHF---------ISPQQAIDAICNGVTTMIGGGTGPADGTNATTCTpgewNIHRMIEAVEEYPLNFGFLCK- 336
Cdd:pfam01979 3 LPGLIDAHVHLemgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTST----GIEALLEAAEELPLGLRFLGPg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 337 ------GNDSREEALLEQVKAGAC------------GLKLHEDWGTTPATINSALNVADKTDTQVAIHTdtLNECGYVDD 398
Cdd:pfam01979 79 csldtdGELEGRKALREKLKAGAEfikgmadgvvfvGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHA--LETKGEVED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 399 TINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTnptrpyTVNTLQEHLDMMMVCHhlnpsvpedVSFAESRIR 478
Cdd:pfam01979 157 AIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPT------EANLLAEHLKGAGVAH---------CPFSNSKLR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 479 AETIAAEDVLHDiGAISMMSSDSQAMGRVGEVttrnwqtadkMRKMKGSLPEETEENDNLRIKRYIAKITINPAITHGIS 558
Cdd:pfam01979 222 SGRIALRKALED-GVKVGLGTDGAGSGNSLNM----------LEELRLALELQFDPEGGLSPLEALRMATINPAKALGLD 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 663535746 559 TYVGSLEPGKIADIVVW----TPQFFGIKPKLIIKGGFIA 594
Cdd:pfam01979 291 DKVGSIEVGKDADLVVVdldpLAAFFGLKPDGNVKKVIVK 330
|
|
| UreB |
COG0832 |
Urease beta subunit [Amino acid transport and metabolism]; |
13-113 |
2.56e-58 |
|
Urease beta subunit [Amino acid transport and metabolism];
Pssm-ID: 440594 Cd Length: 101 Bit Score: 192.20 E-value: 2.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:COG0832 1 GEIIVADGDIELNAGRETITLTVANTGDRPIQVGSHYHFFEVNPALEFDREAARGMRLDIPAGTAVRFEPGQTREVELVP 80
|
90 100
....*....|....*....|.
gi 663535746 93 YGGSKTIFGFSGLVSGDLKSK 113
Cdd:COG0832 81 IGGARRVYGFNGLVNGPLDDE 101
|
|
| Urease_beta |
pfam00699 |
Urease beta subunit; This subunit is known as alpha in Heliobacter. |
13-109 |
8.40e-58 |
|
Urease beta subunit; This subunit is known as alpha in Heliobacter.
Pssm-ID: 459909 Cd Length: 98 Bit Score: 190.67 E-value: 8.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:pfam00699 2 GEIITGDGDIELNAGRETITLTVTNTGDRPIQVGSHYHFFEVNPALEFDREAAYGMRLDIPAGTAVRFEPGDTKTVTLVP 81
|
90
....*....|....*..
gi 663535746 93 YGGSKTIFGFSGLVSGD 109
Cdd:pfam00699 82 IGGARVVYGFNGLVNGP 98
|
|
| Urease_beta |
cd00407 |
Urease beta-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
13-110 |
7.53e-53 |
|
Urease beta-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, archaea, 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 three subunits, alpha, beta and gamma, which can exist as separate proteins or can be fused on a single protein chain. The alpha-beta-gamma heterotrimer 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: 238238 Cd Length: 101 Bit Score: 177.33 E-value: 7.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:cd00407 4 GEIILKEGDIELNAGREAVTLKVKNTGDRPIQVGSHYHFFEVNPALKFDREKAYGMRLDIPAGTAVRFEPGEEKEVELVP 83
|
90
....*....|....*...
gi 663535746 93 YGGSKTIFGFSGLVSGDL 110
Cdd:cd00407 84 IGGKRRVYGFNGLVNGPL 101
|
|
| ureB |
PRK13203 |
urease subunit beta; Reviewed |
13-110 |
8.31e-50 |
|
urease subunit beta; Reviewed
Pssm-ID: 237303 Cd Length: 102 Bit Score: 169.24 E-value: 8.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:PRK13203 4 GEYITADGEIELNAGRETVTLTVANTGDRPIQVGSHYHFFEVNPALSFDREAARGMRLNIPAGTAVRFEPGQTREVELVP 83
|
90
....*....|....*...
gi 663535746 93 YGGSKTIFGFSGLVSGDL 110
Cdd:PRK13203 84 LAGARRVYGFRGKVMGKL 101
|
|
| urease_beta |
TIGR00192 |
urease, beta subunit; In a number of species, including B.subtilis, Synechocystis, and ... |
13-110 |
1.05e-42 |
|
urease, beta subunit; In a number of species, including B.subtilis, Synechocystis, and Haemophilus influenzae, urease subunits beta and gamma are encoded as separate polypeptides. In Helicobacter pylori UreA and in the fission yeast Schizosaccharomyces pombe, beta subunit-like sequence follows gamma subunit-like sequence in a single chain; the fission yeast protein contains additional C-terminal regions. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 129296 Cd Length: 101 Bit Score: 149.59 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:TIGR00192 4 GELQLAEGDITINEGRKTVSVKVKNTGDRPIQVGSHFHFFEVNRALDFDRELAFGMRLDIPSGTAVRFEPGEEKSVELVA 83
|
90
....*....|....*...
gi 663535746 93 YGGSKTIFGFSGLVSGDL 110
Cdd:TIGR00192 84 IGGNRRIYGFNGLVDGQL 101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
139-707 |
0e+00 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 1171.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 139 ALEISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSADLVITNAMIIDpV 218
Cdd:COG0804 1 MAKISRKAYADLYGPTTGDRVRLADTDLFIEVEKDLTTYGDEVKFGGGKVIRDGMGQSQTTRAEGALDLVITNAVILD-H 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 219 LGIIKADIGVKDGKILGVGNAGNPNVMDDVD--IVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIG 296
Cdd:COG0804 80 WGIVKADIGIKDGRIVGIGKAGNPDTMDGVDpdLVIGPGTEVIAGEGLILTAGGIDTHIHFICPQQIEEALASGITTMIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 297 GGTGPADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVA 376
Cdd:COG0804 160 GGTGPAEGTNATTCTPGPWNIARMLEAADALPMNIGFLGKGNASSPEALEEQIRAGACGLKLHEDWGATPAAIDACLSVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 377 DKTDTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMM 456
Cdd:COG0804 240 DEYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDML 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 457 MVCHHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEEND 536
Cdd:COG0804 320 MVCHHLDPSIPEDVAFAESRIRPETIAAEDVLHDLGAISMMSSDSQAMGRVGEVITRTWQTAHKMKKQRGPLPGDSGRND 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 537 NLRIKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPM 616
Cdd:COG0804 400 NFRVKRYVAKYTINPAIAHGISHEVGSVEVGKLADLVLWDPAFFGVKPELVIKGGMIAWAQMGDPNASIPTPQPVHYRPM 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 617 FGALGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAE 696
Cdd:COG0804 480 FGAYGKALAATSVTFVSQAALEAGIAERLGLRKRLLPVKNTRNIGKADMVLNDATPDIEVDPETYEVRVDGELLTCEPAT 559
|
570
....*....|.
gi 663535746 697 KLSLARLYCLY 707
Cdd:COG0804 560 ELPLAQRYFLF 570
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
141-707 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 1142.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSADLVITNAMIIDPvLG 220
Cdd:PRK13207 3 KISRRAYAEMYGPTTGDRVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQRARADGAVDTVITNALILDH-WG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 221 IIKADIGVKDGKILGVGNAGNPNVMDDVDIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGGGTG 300
Cdd:PRK13207 82 IVKADIGIKDGRIVAIGKAGNPDIQDGVDIIIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQIEEALASGVTTMIGGGTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 301 PADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVADKTD 380
Cdd:PRK13207 162 PATGTNATTCTPGPWHIHRMLQAADAFPMNIGFLGKGNASLPEALEEQIEAGAIGLKLHEDWGATPAAIDNCLSVADEYD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 381 TQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMMVCH 460
Cdd:PRK13207 242 VQVAIHTDTLNESGFVEDTIAAFKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLMVCH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 461 HLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEENDNLRI 540
Cdd:PRK13207 322 HLDPSIPEDVAFAESRIRRETIAAEDILHDLGAISMISSDSQAMGRVGEVIIRTWQTAHKMKVQRGPLPGDSGRNDNFRV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 541 KRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPMFGAL 620
Cdd:PRK13207 402 KRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWKPAFFGVKPELVLKGGMIAWAPMGDPNASIPTPQPVHYRPMFGAY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 621 GKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAEKLSL 700
Cdd:PRK13207 482 GGALAATSVTFVSQAALDAGIPEKLGLKKRLVPVKNTRGITKADMKLNDATPKIEVDPETYEVRADGELLTCEPATVLPL 561
|
....*..
gi 663535746 701 ARLYCLY 707
Cdd:PRK13207 562 AQRYFLF 568
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
141-706 |
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: 1028.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSADLVITNAMIIDPVlG 220
Cdd:cd00375 1 KISREAYADMYGPTTGDKVRLGDTDLWIEVEKDYTTYGDEVKFGGGKVLRDGMGQSSGYTREDVLDLVITNALIIDYT-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 221 IIKADIGVKDGKILGVGNAGNPNVMDDVD--IVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGGG 298
Cdd:cd00375 80 IYKADIGIKDGRIVAIGKAGNPDIMDGVTpnMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIEEALASGITTMIGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 299 TGPADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVADK 378
Cdd:cd00375 160 TGPAAGTKATTCTPGPWNIKRMLQAADGLPVNIGFLGKGNGSSPDALAEQIEAGACGLKLHEDWGATPAAIDTCLSVADE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 379 TDTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMMV 458
Cdd:cd00375 240 YDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTYHTEGAGGGHAPDIIKVAGHPNVLPSSTNPTRPFTVNTLDEHLDMLMV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 459 CHHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEENDNL 538
Cdd:cd00375 320 CHHLDPNIPEDVAFAESRIRAETIAAEDVLHDLGAISIMSSDSQAMGRVGEVILRTWQTAHKMKAQRGPLPEDSGDADNF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 539 RIKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPMFG 618
Cdd:cd00375 400 RVKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGVKPEMVLKGGFIAYAQMGDPNASIPTPQPVMMRPMFG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 619 ALGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAEKL 698
Cdd:cd00375 480 AHGKAPAATSVTFVSQASLDAGIAEELGLRRRVVAVKNCRGVGKKDMKLNSATPDIEVDPETYEVRVDGELLTCEPADEL 559
|
....*...
gi 663535746 699 SLARLYCL 706
Cdd:cd00375 560 PLAQRYFL 567
|
|
| PLN02303 |
PLN02303 |
urease |
8-707 |
0e+00 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 1021.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 8 EPPHVGEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKH 87
Cdd:PLN02303 129 EEPIPGEIITGDGSIIINAGRKAVKLKVTNTGDRPIQVGSHYHFIETNPYLVFDRRKAYGMRLNIPAGTAVRFEPGETKT 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 88 VEVVEYGGSKTIFGFSGLVSGDLKSKKQEAI-KNIHENNFKNISEN-------AEEESNALEISRSRYVALFGPTVGDKV 159
Cdd:PLN02303 209 VTLVSIGGNKVIRGGNGIVDGPVDDSRLTKImERVSSRGFGHVEEDdasegviGEDPDFTTTISREKYANMYGPTTGDKI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 160 RLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSADLVITNAMIIDpVLGIIKADIGVKDGKILGVGNA 239
Cdd:PLN02303 289 RLGDTNLYAEIEKDFTVYGDECKFGGGKVLRDGMGQATGYGAADSLDTVITNAVIID-YTGIYKADIGIKDGLIVGIGKA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 240 GNPNVMDDV--DIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGGGTGPADGTNATTCTPGEWNI 317
Cdd:PLN02303 368 GNPDVMDGVtsNMIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQLATEAIASGITTLVGGGTGPAHGTCATTCTPAPSHM 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 318 HRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVADKTDTQVAIHTDTLNECGYVD 397
Cdd:PLN02303 448 KLMLQSTDDLPLNFGFTGKGNTAKPEGLHEIIKAGAMGLKLHEDWGTTPAAIDNCLDVAEEYDIQVTIHTDTLNESGCVE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 398 DTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMMVCHHLNPSVPEDVSFAESRI 477
Cdd:PLN02303 528 HSIAAFKGRTIHTYHSEGAGGGHAPDIIKVCGVKNVLPSSTNPTRPYTKNTIDEHLDMLMVCHHLDKNIPEDVAFAESRI 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 478 RAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEENDNLRIKRYIAKITINPAITHGI 557
Cdd:PLN02303 608 RAETIAAEDILHDMGAISIISSDSQAMGRIGEVITRTWQTAHKMKSQRGALEPRGADNDNFRIKRYIAKYTINPAIAHGM 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 558 STYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPMFGALGKAKQTTSVTFTSQLAL 637
Cdd:PLN02303 688 SHFVGSVEVGKLADLVLWKPAFFGAKPEMVIKGGQIAWAQMGDPNASIPTPEPVIMRPMFGAFGKAGSSNSIAFVSKAAL 767
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 638 DNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAEKLSLARLYCLY 707
Cdd:PLN02303 768 DAGVKQLYGLTKRVEAVGNVRGLTKLDMKLNDALPVITVDPETYEVTADGEVLTCAPATSVPLSRNYFLF 837
|
|
| urease_alph |
TIGR01792 |
urease, alpha subunit; This model describes the urease alpha subunit UreC (designated beta or ... |
141-707 |
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: 937.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLR-KDSADLVITNAMIIDPVl 219
Cdd:TIGR01792 1 KMSREQYASLYGPTTGDKVRLGDTDLFVEVEKDLTTYGDESKFGGGKVLRDGMGQNATLTRnAGVLDLVITNALILDWT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 220 GIIKADIGVKDGKILGVGNAGNPNVMDDVDIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGGGT 299
Cdd:TIGR01792 80 GIYKADIGIKNGRIVGIGKAGNPDTMDGVDMIVGASTEAISGEGKIVTAGGIDTHVHYISPQQVQAALDNGITTLIGGGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 300 GPADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVADKT 379
Cdd:TIGR01792 160 GPADGTNATTCTPGPWYLHRMLQAADGLPINFGFTGKGSGSGPAALIEQIEAGACGLKVHEDWGATPAAIDNALSVADEY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 380 DTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMMVC 459
Cdd:TIGR01792 240 DVQVAVHTDTLNESGFVEDTIAAFKGRTIHTYHTEGAGGGHAPDIIVVVGYNNILPSSTNPTLPYTVNTIDEHLDMLMVC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 460 HHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEENDNLR 539
Cdd:TIGR01792 320 HHLNPKIPEDVAFAESRIRKETIAAEDVLQDMGAISMISSDSQAMGRIGEVVTRCWQTADKMKKQRGPLPGDSPGNDNNR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 540 IKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPMFGA 619
Cdd:TIGR01792 400 VKRYVAKYTINPAITHGISDYIGSIEVGKLADLVLWEPAFFGVKPDMVLKGGLIAWAIMGDPNASIPTPQPVLYRPMFGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 620 LGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAEKLS 699
Cdd:TIGR01792 480 YGRALQSTSITFVSQAAYDKGIKERLGLQKLLLPVHNTRSIGKADMKLNSATPKIEVDPQTYDVKVDGVLITVEPADELP 559
|
....*...
gi 663535746 700 LARLYCLY 707
Cdd:TIGR01792 560 LTQRYFLF 567
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
141-706 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 918.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSA-DLVITNAMIIDPVL 219
Cdd:PRK13308 3 TIDRRAYAELYGPTTGDRVRLADTSLLAEVEHDHTVYGDECLFGGGKTLRDGMGMAPGVTSADGAlDFVLCNVTVIDPVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 220 GIIKADIGVKDGKILGVGNAGNPNVMDDVD--IVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGG 297
Cdd:PRK13308 83 GIVKGDIGIRDGRIVGIGKAGNPDIMDGVDprLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQLVDHALASGITTMLGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 298 GTGPAdgtnATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVAD 377
Cdd:PRK13308 163 GLGPT----VGIDSGGPFNTGRMLQAAEAWPVNFGFLGRGNSSKPAALIEQVEAGACGLKIHEDWGAMPAAIDTCLEVAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 378 KTDTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMM 457
Cdd:PRK13308 239 EYDFQVQLHTDTLNESGFVEDTLAAIGGRTIHMYHTEGAGGGHAPDIIRVVGEPHCLPSSTNPTNPYTVNTFDEHLDMTM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 458 VCHHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEE-TEEND 536
Cdd:PRK13308 319 VCHHLNPDVPEDVAFAESRIRAQTIAAEDVLHDIGAISMLGSDSQGMGRIAEVIARTWQLASKMKDQRGPLPEDrGTFAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 537 NLRIKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPM 616
Cdd:PRK13308 399 NARIKRYIAKYTINPAITFGIDDHIGSLEPGKLADIVLWRPAFFGIKPELVIKGGFPAWAAMGDANGSLMTCEPMLQRPQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 617 FGALGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAE 696
Cdd:PRK13308 479 WGAFGRAKQALSVCFVSPLAIEAGLGERLGLRKRLLPVRGTRTLTKADMLHNDACPDIRVDPQTFEVFVDGELVTCEPAT 558
|
570
....*....|
gi 663535746 697 KLSLARLYCL 706
Cdd:PRK13308 559 ELPLAQRYML 568
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
141-707 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 903.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDM----IKYGDELVFGGGKSARDGLGQASGVLRKDSADLVITNAMIID 216
Cdd:PRK13206 3 RLSRERYAALYGPTTGDRIRLADTDLLIEVTEDRsggpGLAGDEAVFGGGKVIRESMGQGRATRAEGAPDTVITGAVILD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 217 PvLGIIKADIGVKDGKILGVGNAGNPNVMDDV--DIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTM 294
Cdd:PRK13206 83 H-WGIVKADVGIRDGRIVAIGKAGNPDIMDGVhpDLVIGPSTEIIAGNGRILTAGAIDCHVHFICPQIVDEALAAGITTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 295 IGGGTGPADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALN 374
Cdd:PRK13206 162 IGGGTGPAEGSKATTVTPGAWHLARMLEALDGWPVNVALLGKGNTVSAEALWEQLRGGAGGFKLHEDWGSTPAAIDACLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 375 VADKTDTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLD 454
Cdd:PRK13206 242 VADAAGVQVALHSDTLNEAGFVEDTLAAIAGRSIHAYHTEGAGGGHAPDIITVASHPNVLPSSTNPTRPHTVNTLDEHLD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 455 MMMVCHHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETeE 534
Cdd:PRK13206 322 MLMVCHHLNPAVPEDLAFAESRIRPSTIAAEDVLHDMGAISMIGSDSQAMGRIGEVVLRTWQTAHVMKRRRGALPGDG-R 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 535 NDNLRIKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYR 614
Cdd:PRK13206 401 ADNNRARRYVAKYTICPAVAHGIDHEIGSVEVGKLADLVLWEPAFFGVRPHAVLKGGAIAWAAMGDANASIPTPQPVLPR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 615 PMFGALGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDP 694
Cdd:PRK13206 481 PMFGAAPAAAAATSVHFVAPQAIEDGLADRLGLRRRLVPVADTRAVGKADMPLNDALPDIEVDPDTFTVRIDGEVWEPQP 560
|
570
....*....|...
gi 663535746 695 AEKLSLARLYCLY 707
Cdd:PRK13206 561 AAELPMAQRYFLF 573
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
140-707 |
0e+00 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 854.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 140 LEISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQaSGVLRKDSADLVITNAMIIDpVL 219
Cdd:PRK13985 1 KKISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYTIYGEELKFGGGKTLREGMSQ-SNNPSKEELDLIITNALIID-YT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 220 GIIKADIGVKDGKILGVGNAGNPNVMDDV--DIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGG 297
Cdd:PRK13985 79 GIYKADIGIKDGKIAGIGKGGNKDMQDGVknNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTAFASGVTTMIGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 298 GTGPADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVAD 377
Cdd:PRK13985 159 GTGPADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLGKGNSSNDASLADQIEAGAIGFKIHEDWGTTPSAINHALDVAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 378 KTDTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMM 457
Cdd:PRK13985 239 KYDVQVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGGHAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDMLM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 458 VCHHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEENDN 537
Cdd:PRK13985 319 VCHHLDKSIKEDVQFADSRIRPQTIAAEDTLHDMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKGDNDN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 538 LRIKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPMF 617
Cdd:PRK13985 399 FRIKRYLSKYTINPAIAHGISEYVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVYYREMF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 618 GALGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAEK 697
Cdd:PRK13985 479 AHHGKAKYDANITFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTSKPANK 558
|
570
....*....|
gi 663535746 698 LSLARLYCLY 707
Cdd:PRK13985 559 VSLAQLFSIF 568
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
141-704 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 824.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSA-DLVITNAMIIDPVL 219
Cdd:PRK13309 3 QISRQEYAGLFGPTTGDKIRLGDTNLFIEIEKDLRGYGDESVYGGGKSLRDGMGANNNLTRDNGVlDLVITNVTIVDARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 220 GIIKADIGVKDGKILGVGNAGNPNVMDDVD--IVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAIDAICNGVTTMIGG 297
Cdd:PRK13309 83 GVIKADVGIRDGKIVGIGKSGNPSTMDGVTqgMVVGVSTDAISGEHLILTAAGIDTHIHLISPQQAYHALSNGVTTFFGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 298 GTGPADGTNATTCTPGEWNIHRMIEAVEEYPLNFGFLCKGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNVAD 377
Cdd:PRK13309 163 GIGPTDGTNGTTVTPGPWNIRQMLRSIEGLPVNVGILGKGNSYGRGPLLEQAIAGVAGYKVHEDWGATAAALRHALRVAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 378 KTDTQVAIHTDTLNECGYVDDTINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNTLQEHLDMMM 457
Cdd:PRK13309 243 EVDIQVAVHTDSLNECGYVEDTIDAFEGRTIHTFHTEGAGGGHAPDIIKVASQTNVLPSSTNPTLPYGVNSQAELFDMIM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 458 VCHHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEVTTRNWQTADKMRKMKGSLPEETEENDN 537
Cdd:PRK13309 323 VCHNLNPNVPADVAFAESRVRPETIAAENVLHDMGVISMFSSDSQAMGRVGENWLRAIQTADAMKAARGKLPEDAAGNDN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 538 LRIKRYIAKITINPAITHGISTYVGSLEPGKIADIVVWTPQFFGIKPKLIIKGGFIAYALMGDPNASIPTTEPVYYRPMF 617
Cdd:PRK13309 403 FRVLRYVAKITINPAITQGVSHVIGSVEVGKMADLVLWEPRFFGAKPKMVIKGGMINWAAMGDPNASLPTPQPVFYRPMF 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 618 GALGKAKQTTSVTFTSQLALDNKLEEKLKIQKKLVPVKNCRNIGKKDMLYNDKTPKIEVDPETYEVKVDGEIATVDPAEK 697
Cdd:PRK13309 483 GAMGKTLQDTCVTFVSQAALDDGVKEKAGLDRQVIAVKNCRTISKRDLVRNSQTPNIEVDPETFAVKVDGVHATVKPIAT 562
|
....*..
gi 663535746 698 LSLARLY 704
Cdd:PRK13309 563 ASLNQRY 569
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
267-594 |
1.56e-67 |
|
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: 225.46 E-value: 1.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 267 TPGTIDSHIHF---------ISPQQAIDAICNGVTTMIGGGTGPADGTNATTCTpgewNIHRMIEAVEEYPLNFGFLCK- 336
Cdd:pfam01979 3 LPGLIDAHVHLemgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTST----GIEALLEAAEELPLGLRFLGPg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 337 ------GNDSREEALLEQVKAGAC------------GLKLHEDWGTTPATINSALNVADKTDTQVAIHTdtLNECGYVDD 398
Cdd:pfam01979 79 csldtdGELEGRKALREKLKAGAEfikgmadgvvfvGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHA--LETKGEVED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 399 TINAIAGRTIHTYHTEGAGGGHAPDIMKIAGEPNILPSSTnptrpyTVNTLQEHLDMMMVCHhlnpsvpedVSFAESRIR 478
Cdd:pfam01979 157 AIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPT------EANLLAEHLKGAGVAH---------CPFSNSKLR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 479 AETIAAEDVLHDiGAISMMSSDSQAMGRVGEVttrnwqtadkMRKMKGSLPEETEENDNLRIKRYIAKITINPAITHGIS 558
Cdd:pfam01979 222 SGRIALRKALED-GVKVGLGTDGAGSGNSLNM----------LEELRLALELQFDPEGGLSPLEALRMATINPAKALGLD 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 663535746 559 TYVGSLEPGKIADIVVW----TPQFFGIKPKLIIKGGFIA 594
Cdd:pfam01979 291 DKVGSIEVGKDADLVVVdldpLAAFFGLKPDGNVKKVIVK 330
|
|
| UreB |
COG0832 |
Urease beta subunit [Amino acid transport and metabolism]; |
13-113 |
2.56e-58 |
|
Urease beta subunit [Amino acid transport and metabolism];
Pssm-ID: 440594 Cd Length: 101 Bit Score: 192.20 E-value: 2.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:COG0832 1 GEIIVADGDIELNAGRETITLTVANTGDRPIQVGSHYHFFEVNPALEFDREAARGMRLDIPAGTAVRFEPGQTREVELVP 80
|
90 100
....*....|....*....|.
gi 663535746 93 YGGSKTIFGFSGLVSGDLKSK 113
Cdd:COG0832 81 IGGARRVYGFNGLVNGPLDDE 101
|
|
| Urease_alpha |
pfam00449 |
Urease alpha-subunit, N-terminal domain; The N-terminal domain is a composite domain and plays ... |
141-259 |
3.54e-58 |
|
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: 192.32 E-value: 3.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 141 EISRSRYVALFGPTVGDKVRLADTELIMEIEKDMIKYGDELVFGGGKSARDGLGQASGVLRKDSADLVITNAMIIDPvLG 220
Cdd:pfam00449 1 KISREAYADMYGPTTGDRIRLGDTDLFIEVEKDLTVYGDEVKFGGGKVIRDGMGQSQGRTRDDALDLVITNALILDY-TG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 663535746 221 IIKADIGVKDGKILGVGNAGNPNVMDDVD--IVVSSNTEII 259
Cdd:pfam00449 80 IVKADIGIKDGRIVGIGKAGNPDTMDGVTpgMVIGPSTEVI 120
|
|
| Urease_beta |
pfam00699 |
Urease beta subunit; This subunit is known as alpha in Heliobacter. |
13-109 |
8.40e-58 |
|
Urease beta subunit; This subunit is known as alpha in Heliobacter.
Pssm-ID: 459909 Cd Length: 98 Bit Score: 190.67 E-value: 8.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:pfam00699 2 GEIITGDGDIELNAGRETITLTVTNTGDRPIQVGSHYHFFEVNPALEFDREAAYGMRLDIPAGTAVRFEPGDTKTVTLVP 81
|
90
....*....|....*..
gi 663535746 93 YGGSKTIFGFSGLVSGD 109
Cdd:pfam00699 82 IGGARVVYGFNGLVNGP 98
|
|
| Urease_beta |
cd00407 |
Urease beta-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
13-110 |
7.53e-53 |
|
Urease beta-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, archaea, 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 three subunits, alpha, beta and gamma, which can exist as separate proteins or can be fused on a single protein chain. The alpha-beta-gamma heterotrimer 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: 238238 Cd Length: 101 Bit Score: 177.33 E-value: 7.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:cd00407 4 GEIILKEGDIELNAGREAVTLKVKNTGDRPIQVGSHYHFFEVNPALKFDREKAYGMRLDIPAGTAVRFEPGEEKEVELVP 83
|
90
....*....|....*...
gi 663535746 93 YGGSKTIFGFSGLVSGDL 110
Cdd:cd00407 84 IGGKRRVYGFNGLVNGPL 101
|
|
| ureB |
PRK13203 |
urease subunit beta; Reviewed |
13-110 |
8.31e-50 |
|
urease subunit beta; Reviewed
Pssm-ID: 237303 Cd Length: 102 Bit Score: 169.24 E-value: 8.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:PRK13203 4 GEYITADGEIELNAGRETVTLTVANTGDRPIQVGSHYHFFEVNPALSFDREAARGMRLNIPAGTAVRFEPGQTREVELVP 83
|
90
....*....|....*...
gi 663535746 93 YGGSKTIFGFSGLVSGDL 110
Cdd:PRK13203 84 LAGARRVYGFRGKVMGKL 101
|
|
| PRK13192 |
PRK13192 |
bifunctional urease subunit gamma/beta; Reviewed |
13-108 |
6.78e-45 |
|
bifunctional urease subunit gamma/beta; Reviewed
Pssm-ID: 183886 [Multi-domain] Cd Length: 208 Bit Score: 159.76 E-value: 6.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:PRK13192 113 GEILPGDGEIELNAGRPAVTLDVTNTGDRPIQVGSHFHFFEVNRALRFDRAAAYGMRLDIPAGTAVRFEPGETKEVRLVP 192
|
90
....*....|....*.
gi 663535746 93 YGGSKTIFGFSGLVSG 108
Cdd:PRK13192 193 IGGARVVIGFNGLTNG 208
|
|
| urease_beta |
TIGR00192 |
urease, beta subunit; In a number of species, including B.subtilis, Synechocystis, and ... |
13-110 |
1.05e-42 |
|
urease, beta subunit; In a number of species, including B.subtilis, Synechocystis, and Haemophilus influenzae, urease subunits beta and gamma are encoded as separate polypeptides. In Helicobacter pylori UreA and in the fission yeast Schizosaccharomyces pombe, beta subunit-like sequence follows gamma subunit-like sequence in a single chain; the fission yeast protein contains additional C-terminal regions. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 129296 Cd Length: 101 Bit Score: 149.59 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:TIGR00192 4 GELQLAEGDITINEGRKTVSVKVKNTGDRPIQVGSHFHFFEVNRALDFDRELAFGMRLDIPSGTAVRFEPGEEKSVELVA 83
|
90
....*....|....*...
gi 663535746 93 YGGSKTIFGFSGLVSGDL 110
Cdd:TIGR00192 84 IGGNRRIYGFNGLVDGQL 101
|
|
| PRK13986 |
PRK13986 |
urease subunit beta; |
11-126 |
3.82e-42 |
|
urease subunit beta;
Pssm-ID: 184439 [Multi-domain] Cd Length: 225 Bit Score: 152.67 E-value: 3.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 11 HVGEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEV 90
Cdd:PRK13986 107 VPGELFLKDEDITINAGKKAVSVKVKNVGDRPVQVGSHFHFFEVNRCLEFDREKAFGKRLDIASGTAVRFEPGEEKSVEL 186
|
90 100 110
....*....|....*....|....*....|....*..
gi 663535746 91 VEYGGSKTIFGFSGLVSGDL-KSKKQEAIKNIHENNF 126
Cdd:PRK13986 187 IDIGGNRRIFGFNALVNRQAdNESKKIALHRAKERGF 223
|
|
| ureB |
PRK13201 |
urease subunit beta; Reviewed |
13-139 |
2.79e-37 |
|
urease subunit beta; Reviewed
Pssm-ID: 237302 [Multi-domain] Cd Length: 136 Bit Score: 135.73 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:PRK13201 4 GEIITKSTEVEINNHHPETVIEVENTGDRPIQVGSHFHFYEANAALDFEREMAYGKHLDIPAGAAVRFEPGDKKEVQLVE 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 663535746 93 YGGSKTIFGFSGLVSGDLKSKKQEAIKNIHENNFKNISENAEEESNA 139
Cdd:PRK13201 84 YAGKRKIFGFRGMVNGPIDESRVYRPTDENDAYAGVFGDNGAENVNK 130
|
|
| ureB |
PRK13198 |
urease subunit beta; Reviewed |
12-128 |
1.14e-32 |
|
urease subunit beta; Reviewed
Pssm-ID: 171897 [Multi-domain] Cd Length: 158 Bit Score: 123.64 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 12 VGEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVV 91
Cdd:PRK13198 31 LGGLVLAETPITFNENKPVTKVKVRNTGDRPIQVGSHFHFFEVNRALEFDRAAAYGKRLNISSTTAIRFEPGDETEVPLI 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 663535746 92 EYGGSKTIFGFSGLVSG---------DLKSKKQEAIKNIHENNFKN 128
Cdd:PRK13198 111 PFGGKQTLYGFNNLVDGwtgegvvpnSERPDKLAAIRLAAERGFKS 156
|
|
| ureB |
PRK13204 |
urease subunit beta; Reviewed |
12-108 |
5.29e-30 |
|
urease subunit beta; Reviewed
Pssm-ID: 171902 [Multi-domain] Cd Length: 159 Bit Score: 116.03 E-value: 5.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 12 VGEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVV 91
Cdd:PRK13204 26 VGGYVLAKDPIEINQGRPRTTLTVRNTGDRPIQIGSHFHFFEVNRYLEFDRSKAFGLRLDIPANTAVRFEPGDEKEVTLV 105
|
90
....*....|....*..
gi 663535746 92 EYGGSKTIFGFSGLVSG 108
Cdd:PRK13204 106 PFAGKRFIFGFNNLVDG 122
|
|
| ureB |
PRK13205 |
urease subunit beta; Reviewed |
13-114 |
9.79e-27 |
|
urease subunit beta; Reviewed
Pssm-ID: 106174 [Multi-domain] Cd Length: 162 Bit Score: 106.81 E-value: 9.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKTIKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVVE 92
Cdd:PRK13205 4 GEYILSSESLTGNVGREAKTIEIINTGDRPVQIGSHFHFAEVNPSISFDRSEGYGFRLDIPSGTAVRLEPGDARTVNLVA 83
|
90 100
....*....|....*....|..
gi 663535746 93 YGGSKTIFGFSGLVSGDLKSKK 114
Cdd:PRK13205 84 IGGDRIVAGFRDLVDGPLEDLK 105
|
|
| ureB |
PRK13202 |
urease subunit beta; Reviewed |
13-103 |
7.80e-19 |
|
urease subunit beta; Reviewed
Pssm-ID: 106171 Cd Length: 104 Bit Score: 82.05 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 13 GEYIPTDGKIIANKGKKT-IKLKVSNTGDRPIQVGSHTHFSEANKALEFDREKALGSHLNIPSGTSVRFEPGESKHVEVV 91
Cdd:PRK13202 4 GEIFYGSGDIEMNAAALSrLQMRIINAGDRPVQVGSHVHLPQANRALSFDRATAHGYRLDIPAATAVRFEPGIPQIVGLV 83
|
90
....*....|..
gi 663535746 92 EYGGSKTIFGFS 103
Cdd:PRK13202 84 PLGGRREVPGLT 95
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
202-575 |
2.03e-17 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 84.63 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 202 KDSADLVITNAMIIDPVLGII--KADIGVKDGKILGVGNAGnpnvmddvDIVVSSNTEIISGEHTICTPGTIDSHIHF-- 277
Cdd:COG1228 5 AQAGTLLITNATLVDGTGGGVieNGTVLVEDGKIAAVGPAA--------DLAVPAGAEVIDATGKTVLPGLIDAHTHLgl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 278 -------------ISP---------QQAIDAICNGVTT---MIGGGTGPADGTNATTCT--PGEwnihRMIeaVEEYPLN 330
Cdd:COG1228 77 gggravefeagggITPtvdlvnpadKRLRRALAAGVTTvrdLPGGPLGLRDAIIAGESKllPGP----RVL--AAGPALS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 331 F--GFLCKGNDSREEALLEQVKAGACGLKLHEDWGT---TPATINSALNVADKTDTQVAIHTDTLnecgyvDDTINAI-A 404
Cdd:COG1228 151 LtgGAHARGPEEARAALRELLAEGADYIKVFAEGGApdfSLEELRAILEAAHALGLPVAAHAHQA------DDIRLAVeA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 405 G-RTI-HTYHT--EGAggghapDIMKIAGepnilPSSTNPTrpytvntlqehldmMMVCHHLNPSVPEDVSFAESRIRAE 480
Cdd:COG1228 225 GvDSIeHGTYLddEVA------DLLAEAG-----TVVLVPT--------------LSLFLALLEGAAAPVAAKARKVREA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 481 TIAAEDVLHDIGAISMMSSDSQAMGRVGevtTRNWQTADKMRKMKGSlPEETeendnlrikryIAKITINPAITHGISTY 560
Cdd:COG1228 280 ALANARRLHDAGVPVALGTDAGVGVPPG---RSLHRELALAVEAGLT-PEEA-----------LRAATINAAKALGLDDD 344
|
410
....*....|....*
gi 663535746 561 VGSLEPGKIADIVVW 575
Cdd:COG1228 345 VGSLEPGKLADLVLL 359
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
205-331 |
6.02e-12 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 68.59 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 205 ADLVITNAMIIDPVLG-IIKADIGVKDGKILGVGNAgnpnvmddvdivVSSNTEIISGEHTICTPGTIDSHIHF----IS 279
Cdd:COG1001 5 ADLVIKNGRLVNVFTGeILEGDIAIAGGRIAGVGDY------------IGEATEVIDAAGRYLVPGFIDGHVHIessmVT 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 280 PQQAIDAIC-NGVTTMIgggtgpADgtnattctP-------GEWNIHRMIEAVEEYPLNF 331
Cdd:COG1001 73 PAEFARAVLpHGTTTVI------AD--------PheianvlGLEGVRYMLEAAEGLPLDI 118
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
206-303 |
6.12e-12 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 67.88 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 206 DLVITNAMIIDPVLGI-IKADIGVKDGKILGVGNagnpnvmddvDIVVSSNTEIISGEHTICTPGTIDSHIHF------- 277
Cdd:COG3964 1 DLLIKGGRVIDPANGIdGVMDIAIKDGKIAAVAK----------DIDAAEAKKVIDASGLYVTPGLIDLHTHVfpggtdy 70
|
90 100
....*....|....*....|....*...
gi 663535746 278 -ISPQQAidAICNGVTTMI-GGGTGPAD 303
Cdd:COG3964 71 gVDPDGV--GVRSGVTTVVdAGSAGAAN 96
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
208-386 |
1.86e-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: 63.57 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 208 VITNAMIIDPVlGIIKADIGVKDGKILGVGNagnpnvmddvDIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQ----- 282
Cdd:COG0044 1 LIKNGRVVDPG-GLERADVLIEDGRIAAIGP----------DLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLehked 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 283 ------AidAICNGVTTMIgggtGPADgTNATTCTPGewNIHRMIEAVEEYPL-NFGF---LCKGNDSREEALLEQVKAG 352
Cdd:COG0044 70 ietgtrA--AAAGGVTTVV----DMPN-TNPVTDTPE--ALEFKLARAEEKALvDVGPhgaLTKGLGENLAELGALAEAG 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 663535746 353 ACGLKL-----HEDWGTTPATINSALNVADKTDTQVAIH 386
Cdd:COG0044 141 AVAFKVfmgsdDGNPVLDDGLLRRALEYAAEFGALVAVH 179
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
206-387 |
7.73e-10 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 61.31 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 206 DLVITNAMIIDPVLGI-IKADIGVKDGKILGVGNAGnpnvmddvdivVSSNTEIISGEHTICTPGTIDSHIHFISPQQAI 284
Cdd:PRK12394 4 DILITNGHIIDPARNInEINNLRIINDIIVDADKYP-----------VASETRIIHADGCIVTPGLIDYHAHVFYDGTEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 285 ----DAIC--NGVTTMIGG---GTGPADGTNATTCTPGEWNIHRMieaveeypLNFGFLCKGNDSREE------------ 343
Cdd:PRK12394 73 gvrpDMYMppNGVTTVVDAgsaGTANFDAFYRTVICASKVRIKAF--------LTVSPPGQTWSGYQEnydpdnidenki 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 663535746 344 -ALLEQVKAGACGLKLH------EDWGTTPATinSALNVADKTDTQVAIHT 387
Cdd:PRK12394 145 hALFRQYRNVLQGLKLRvqtediAEYGLKPLT--ETLRIANDLRCPVAVHS 193
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
206-411 |
4.36e-09 |
|
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: 59.23 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 206 DLVITNAMIIDPvLGIIKADIGVKDGKILGVGNagnpnvmddvDIVVSSNTEII-SGEHTIcTPGTIDSHIHFISP---- 280
Cdd:cd01315 1 DLVIKNGRVVTP-DGVREADIAVKGGKIAAIGP----------DIANTEAEEVIdAGGLVV-MPGLIDTHVHINEPgrte 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 281 -------QQAidAICNGVTTMIgggtgpaD-GTNATTCTPGEWNIHRMIEAVEEYPL-NFGFLCKGNDSREEALLEQVKA 351
Cdd:cd01315 69 wegfetgTKA--AAAGGITTII-------DmPLNSIPPTTTVENLEAKLEAAQGKLHvDVGFWGGLVPGNLDQLRPLDEA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663535746 352 GACGLK---LHEDWGTTPA----TINSALNVADKTDTQVAIHTDTLNECGYVDDTINAIAGRTIHTY 411
Cdd:cd01315 140 GVVGFKcflCPSGVDEFPAvddeQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDY 206
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
206-302 |
7.73e-09 |
|
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: 58.46 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 206 DLVITNAMIIDPVLGI-IKADIGVKDGKILGVGNAGNPnvmddvdivvsSNTEIISGEHTICTPGTIDSHIH----FISP 280
Cdd:cd01297 1 DLVIRNGTVVDGTGAPpFTADVGIRDGRIAAIGPILST-----------SAREVIDAAGLVVAPGFIDVHTHydgqVFWD 69
|
90 100
....*....|....*....|....
gi 663535746 281 QQAIDAICNGVTTMIGG--GTGPA 302
Cdd:cd01297 70 PDLRPSSRQGVTTVVLGncGVSPA 93
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
207-295 |
1.44e-08 |
|
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: 57.61 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 207 LVITNAMIIDPVlGIIKADIGVKDGKILGVGNagnpnvmddvDIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQAID- 285
Cdd:cd01314 1 LIIKNGTIVTAD-GSFKADILIEDGKIVAIGP----------NLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVt 69
|
90 100
....*....|....*....|
gi 663535746 286 ----------AICNGVTTMI 295
Cdd:cd01314 70 addfesgtraAAAGGTTTII 89
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
207-303 |
2.91e-08 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 56.40 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 207 LVITNAMIIDPVLGI-IKADIGVKDGKILGVGNagnpnvmddvDIVVSSNTEIISGEHTICTPGTIDSHIH--------F 277
Cdd:PRK09237 1 LLLRGGRVIDPANGIdGVIDIAIEDGKIAAVAG----------DIDGSQAKKVIDLSGLYVSPGWIDLHVHvypgstpyG 70
|
90 100
....*....|....*....|....*....
gi 663535746 278 ISPqqaiDAIC--NGVTTMI-GGGTGPAD 303
Cdd:PRK09237 71 DEP----DEVGvrSGVTTVVdAGSAGADN 95
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
200-279 |
8.44e-07 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 52.11 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 200 LRKDSADLVITNAMII--DPVLGIIKAdIGVKDGKILGVGNAgnpnvmDDVDIVVSSNTEIISGE-HTIcTPGTIDSHIH 276
Cdd:COG1574 3 LAAAAADLLLTNGRIYtmDPAQPVAEA-VAVRDGRIVAVGSD------AEVRALAGPATEVIDLGgKTV-LPGFIDAHVH 74
|
...
gi 663535746 277 FIS 279
Cdd:COG1574 75 LLG 77
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
206-277 |
1.30e-06 |
|
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: 51.37 E-value: 1.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663535746 206 DLVITNAMII--DPVLGIIK-ADIGVKDGKILGVGNAGNPNVMDDVDivvssntEIISGEHTICTPGTIDSHIHF 277
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEdGAVLVEDGRIAAVGPGAELPARYPAA-------EVIDAGGKLVLPGLVNTHTHL 68
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
230-576 |
1.31e-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: 51.16 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 230 DGKILGVGNAgnpnvmddvdIVVSSNTEIISGEHTICTPGTIDSHIHF--------------------ISPQ-QAID--- 285
Cdd:cd01309 1 DGKIVAVGAE----------ITTPADAEVIDAKGKHVTPGLIDAHSHLgldeeggvretsdaneetdpVTPHvRAIDgin 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 286 --------AICNGVTT-MIG-GGTGPADGTNATTCTPGeWNIHRMIE--------AVEEYPLNFGflckGNDSREEA--- 344
Cdd:cd01309 71 pddeafkrARAGGVTTvQVLpGSANLIGGQGVVIKTDG-GTIEDMFIkapaglkmALGENPKRVY----GGKGKEPAtrm 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 345 --------LLEQVKAGACGLKLHEDWGTTPATIN----SALNVADKtDTQVAIHTDTlnecgyVDDTINAIA---GRTIH 409
Cdd:cd01309 146 gvaallrdAFIKAQEYGRKYDLGKNAKKDPPERDlkleALLPVLKG-EIPVRIHAHR------ADDILTAIRiakEFGIK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 410 TYHTEGAGGGHAPDIMKIAGEPNIL-PSSTNPTRPYTVNtlqehldmmmvchhlnpsvpeDVSFAESRIRAetiaAEDVl 488
Cdd:cd01309 219 ITIEHGAEGYKLADELAKHGIPVIYgPTLTLPKKVEEVN---------------------DAIDTNAYLLK----KGGV- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 489 hdigAISMMSSDSQAMGRvgevttRNWQTADKMrkMKGSLPEETEendnlrikryIAKITINPAITHGISTYVGSLEPGK 568
Cdd:cd01309 273 ----AFAISSDHPVLNIR------NLNLEAAKA--VKYGLSYEEA----------LKAITINPAKILGIEDRVGSLEPGK 330
|
....*...
gi 663535746 569 IADIVVWT 576
Cdd:cd01309 331 DADLVVWN 338
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
206-357 |
2.63e-06 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 50.47 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 206 DLVITNAMIIDPVlGIIKADIGVKDGKILGVGnagnpnvmDDVDivvSSNTEIISGEHTICTPGTIDSHIHFISPQQA-I 284
Cdd:PRK06189 4 DLIIRGGKVVTPE-GVYRADIGIKNGKIAEIA--------PEIS---SPAREIIDADGLYVFPGMIDVHVHFNEPGRThW 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663535746 285 DAICNGVTTMI-GGGTGPAD-GTNATTCTPGEWNIHRMIEAVEEYPL-NFGF---LCKGNDSREEALLEqvkAGACGLK 357
Cdd:PRK06189 72 EGFATGSAALAaGGCTTYFDmPLNSIPPTVTREALDAKAELARQKSAvDFALwggLVPGNLEHLRELAE---AGVIGFK 147
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
204-280 |
6.38e-06 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 49.15 E-value: 6.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663535746 204 SADLVITNAMIIDPVlGIIKADIGVKDGKILGVGnagnpnvmddvDIVVSSNTEII--SGEHTIctPGTIDSHIHFISP 280
Cdd:PRK09060 4 TFDLILKGGTVVNPD-GEGRADIGIRDGRIAAIG-----------DLSGASAGEVIdcRGLHVL--PGVIDSQVHFREP 68
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
193-295 |
6.47e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 49.31 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 193 LGQASGVLRKDSADLVITNAMIIDPVLGIIK-ADIGVKDGKILGVG-NAGNPN-VMDDVDIVVSsnteiisgehtictPG 269
Cdd:PRK09061 7 LSLLLMPASMAPYDLVIRNGRVVDPETGLDAvRDVGIKGGKIAAVGtAAIEGDrTIDATGLVVA--------------PG 72
|
90 100 110
....*....|....*....|....*....|
gi 663535746 270 TIDSHIHFISPQ----QAIDaicnGVTTMI 295
Cdd:PRK09061 73 FIDLHAHGQSVAayrmQAFD----GVTTAL 98
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
206-295 |
1.17e-05 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 48.54 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 206 DLVITNAMIIDPVlGIIKADIGVKDGKILGVGNAgnpnvmddvdivVSSNTEIISGEHTICTPGTIDSHIHFISP----- 280
Cdd:PRK13404 5 DLVIRGGTVVTAT-DTFQADIGIRGGRIAALGEG------------LGPGAREIDATGRLVLPGGVDSHCHIDQPsgdgi 71
|
90 100
....*....|....*....|..
gi 663535746 281 QQAID-------AICNGVTTMI 295
Cdd:PRK13404 72 MMADDfytgtvsAAFGGTTTVI 93
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
207-327 |
5.52e-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: 46.03 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 207 LVITNAMIIDPvLGIIKADIGVKDGKILGVGNAGNPNVMDdvdivvssntEIISGEHTICTPGTIDSHIH------FI-S 279
Cdd:cd00854 1 LIIKNARILTP-GGLEDGAVLVEDGKIVAIGPEDELEEAD----------EIIDLKGQYLVPGFIDIHIHggggadFMdG 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 663535746 280 PQQAIDAICN-----GVTTMIgggtgpadgtnATTCTPGEWNIHRMIEAVEEY 327
Cdd:cd00854 70 TAEALKTIAEalakhGTTSFL-----------PTTVTAPPEEIAKALAAIAEA 111
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
271-552 |
7.24e-05 |
|
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: 45.02 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 271 IDSHIHFISPQ--------------------------QAID-AICNGVTTMIGGGTGPADGTN-------ATTCTPGEWN 316
Cdd:cd01292 2 IDTHVHLDGSAlrgtrlnlelkeaeelspedlyedtlRALEaLLAGGVTTVVDMGSTPPPTTTkaaieavAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 317 IHRMIEAVEEYPLNFGFLckGNDSREEALLEQVKAGACGLKLHEDWGTTPATINSALNV---ADKTDTQVAIHTDTLNEC 393
Cdd:cd01292 82 RVVLGLGIPGVPAAVDED--AEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVleeARKLGLPVVIHAGELPDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 394 GYVDDTINAIAGRTIHTY--HtegaGGGHAPDIMKIAGEPNILPSSTNPTRPYTVNtlqehldmmmvchhlnpsvpedvs 471
Cdd:cd01292 160 TRALEDLVALLRLGGRVVigH----VSHLDPELLELLKEAGVSLEVCPLSNYLLGR------------------------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 472 faeSRIRAETIAAedvLHDIGAISMMSSDSQAMGRVGEVtTRNWQTADKMRKMKGSLPEeteendnlrikrYIAKITINP 551
Cdd:cd01292 212 ---DGEGAEALRR---LLELGIRVTLGTDGPPHPLGTDL-LALLRLLLKVLRLGLSLEE------------ALRLATINP 272
|
.
gi 663535746 552 A 552
Cdd:cd01292 273 A 273
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
207-296 |
7.28e-05 |
|
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: 45.84 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 207 LVITNAMIIDP-VLGiiKADIGVKDGKILGVGnagnpnvmDDVDIVVSSNTEIISGEHTICTPGTIDSHIHFI------- 278
Cdd:cd01308 2 TLIKNAEVYAPeYLG--KKDILIAGGKILAIE--------DQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIggggegg 71
|
90 100
....*....|....*....|...
gi 663535746 279 ----SPQQAI-DAICNGVTTMIG 296
Cdd:cd01308 72 pstrTPEVTLsDLTTAGVTTVVG 94
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
207-277 |
9.31e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 45.57 E-value: 9.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663535746 207 LVITNAMIIDPVLGIIKADIGVKDGKILGVGNAGNPNvmddvdivvssNTEIISGEHTICTPGTIDSHIHF 277
Cdd:PRK09357 3 ILIKNGRVIDPKGLDEVADVLIDDGKIAAIGENIEAE-----------GAEVIDATGLVVAPGLVDLHVHL 62
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
360-574 |
1.08e-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: 45.38 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 360 EDWGTTPATINSALNVADKTDTQVAIHT--DtlnecGYVDDTINAI------AGRTIHTYHTEgagggHA----PDIMKI 427
Cdd:cd01300 288 GLLLISPEELEELVRAADEAGLQVAIHAigD-----RAVDTVLDALeaalkdNPRADHRHRIE-----HAqlvsPDDIPR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 428 AGEPNILPSsTNPTRPYtvntlqEHLDMmmvchHLNPSVPEDVSFAESRIRAetiaaedvLHDIGAISMMSSDSqamgrv 507
Cdd:cd01300 358 FAKLGVIAS-VQPNHLY------SDGDA-----AEDRRLGEERAKRSYPFRS--------LLDAGVPVALGSDA------ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663535746 508 gEVTTRN-WQTADKM--RKMKGSLPEETEENdnlRIKRY--IAKITINPAITHGISTYVGSLEPGKIADIVV 574
Cdd:cd01300 412 -PVAPPDpLLGIWAAvtRKTPGGGVLGNPEE---RLSLEeaLRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
206-295 |
1.21e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 45.03 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 206 DLVITNAMIIDPVlGIIKADIGVKDGKILGVGNagnpnvmddvDIVVSSNTEIISGEHTICTPGTIDSHIHFISPQQ--- 282
Cdd:PRK02382 3 DALLKDGRVYYNN-SLQPRDVRIDGGKITAVGK----------DLDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYthk 71
|
90
....*....|....*....
gi 663535746 283 ------AIDAICNGVTTMI 295
Cdd:PRK02382 72 etwytgSRSAAAGGVTTVV 90
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
208-327 |
1.80e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 44.32 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 208 VITNAMIIDPVLGIIKADIGVKDGKILGVGNAGNPNVmddvdivvssntEIISGEHTICTPGTIDSHIH------FISP- 280
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDA------------EVIDLGGGYLAPGFIDLHVHggggvdFMDGt 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 663535746 281 QQAIDAIC-----NGVTTMIgggtgpadgtnATTCTPGEWNIHRMIEAVEEY 327
Cdd:COG1820 69 PEALRTIAraharHGTTSFL-----------PTTITAPPEDLLRALAAIAEA 109
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
548-579 |
2.12e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 44.32 E-value: 2.12e-04
10 20 30
....*....|....*....|....*....|..
gi 663535746 548 TINPAITHGISTYVGSLEPGKIADIVVWTPQF 579
Cdd:COG1820 332 SLNPARALGLDDRKGSIAPGKDADLVVLDDDL 363
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
206-295 |
2.43e-04 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 44.01 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 206 DLVITNAMIIDPvLGIIKADIGVKDGKILGVGNAGNPNVMDdvdivvssnteiISGEHTIctPGTIDSHIHFISP---QQ 282
Cdd:PRK08323 2 STLIKNGTVVTA-DDTYKADVLIEDGKIAAIGANLGDEVID------------ATGKYVM--PGGIDPHTHMEMPfggTV 66
|
90 100
....*....|....*....|.
gi 663535746 283 AID--------AICNGVTTMI 295
Cdd:PRK08323 67 SSDdfetgtraAACGGTTTII 87
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
351-595 |
5.46e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 42.90 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 351 AGACGLKLHEDwgttpATINSALNVADKTDTQVAIHTDTLNEcgyVDDTINAIAGRTIHTYHTEGAGGGHApdimkiage 430
Cdd:pfam07969 239 APGTGWPDFED-----EALAELVAAARERGLDVAIHAIGDAT---IDTALDAFEAVAEKLGNQGRVRIEHA--------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 431 pnilpSSTNPTRPYTVNTLQEHLDMMMVCHHLNPSVPEDVSFAESRIRAETIAAEDVLHDIGAISMMSSDSQAMGRVGEV 510
Cdd:pfam07969 302 -----QGVVPYTYSQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 511 TTRNWQTADKMRKMKGSLPEETeendnLRIKRYIAKITINPAITHGISTYVGSLEPGKIADIVVW--------TPQFFGI 582
Cdd:pfam07969 377 RIGAAVMRQTAGGGEVLGPDEE-----LSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLdddpltvdPPAIADI 451
|
250
....*....|...
gi 663535746 583 KPKLIIKGGFIAY 595
Cdd:pfam07969 452 RVRLTVVDGRVVY 464
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
225-279 |
5.88e-04 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 43.07 E-value: 5.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 663535746 225 DIGVKDGKILGVGNAgnpnvmDDVDIVVSSNTEIIS-GEHTIcTPGTIDSHIHFIS 279
Cdd:cd01300 1 AVAVRDGRIVAVGSD------AEAKALKGPATEVIDlKGKTV-LPGFIDSHSHLLL 49
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
207-277 |
7.34e-04 |
|
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: 42.57 E-value: 7.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663535746 207 LVITNAMII--DPVLGIIKADIGVKDGKILGVGNAGNPNVMDDVdivvssntEIISGEHTICTPGTIDSHIHF 277
Cdd:cd01298 1 ILIRNGTIVttDPRRVLEDGDVLVEDGRIVAVGPALPLPAYPAD--------EVIDAKGKVVMPGLVNTHTHL 65
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
547-575 |
1.31e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 42.09 E-value: 1.31e-03
10 20
....*....|....*....|....*....
gi 663535746 547 ITINPAITHGISTYVGSLEPGKIADIVVW 575
Cdd:COG1574 476 YTIGAAYAAFEEDEKGSLEPGKLADFVVL 504
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
203-295 |
2.59e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 40.79 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 203 DSADLVITNAMIIDPVLGIIKA-DIGVKDGKIL----GVGNAGNPNvmddvdivvssNTEIISGEHTICTPGTIDSHIH- 276
Cdd:PRK09059 1 MMRPILLANARIIDPSRGLDEIgTVLIEDGVIVaagkGAGNQGAPE-----------GAEIVDCAGKAVAPGLVDARVFv 69
|
90 100
....*....|....*....|....*....
gi 663535746 277 ----------FISPQQAidAICNGVTTMI 295
Cdd:PRK09059 70 gepgaehretIASASRA--AAAGGVTSII 96
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
226-298 |
2.72e-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: 40.70 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 226 IGVKDGKILGVGNAgnpnvmDDVDIVVSSNTEIISGEHTICTPGTIDSHIHFI---SPQQAIDAICNGVTTMI----GGG 298
Cdd:cd01296 1 IAIRDGRIAAVGPA------ASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVfagDRVDEFAARLAGASYEEilaaGGG 74
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
544-591 |
3.30e-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: 40.32 E-value: 3.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 663535746 544 IAKITINPAITHGISTYVGSLEPGKIADIVVWT-------PQFFGIKP-KLIIKGG 591
Cdd:cd01296 316 LTAATINAAAALGLGETVGSLEVGKQADLVILDapsyehlAYRFGVNLvEYVIKNG 371
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
204-295 |
3.64e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 40.22 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 204 SADLVITNAMIIDPVlGIIKADIGVKDGKILGVG-NAGNP-NVMDDVDIVVSsnteiisgehtictPGTIDSHIHFISPQ 281
Cdd:PRK08044 2 SFDLIIKNGTVILEN-EARVVDIAVKGGKIAAIGqDLGDAkEVMDASGLVVS--------------PGMVDAHTHISEPG 66
|
90 100
....*....|....*....|...
gi 663535746 282 QAI---------DAICNGVTTMI 295
Cdd:PRK08044 67 RSHwegyetgtrAAAKGGITTMI 89
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
225-386 |
3.92e-03 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 40.00 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 225 DIGVKDGKILGVGNagnpnvmddvDIVVSSNTEIISGEHTICTPGTIDSHIH--------FISPQQAidAICNGVTTMIG 296
Cdd:cd01307 1 DVAIENGKIAAVGA----------ALAAPAATQIVDAGGCYVSPGWIDLHVHvyqggtryGDRPDMI--GVKSGVTTVVD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 297 GGtgpadgtnattcTPGEWNI----HRMIE--AVEEYP-LNFGF--LCKGNDSREEALLEQVKAGAC---------GLKL 358
Cdd:cd01307 69 AG------------SAGADNIdgfrYTVIErsATRVYAfLNISRvgLVAQDELPDPDNIDEDAVVAAareypdvivGLKA 136
|
170 180 190
....*....|....*....|....*....|....
gi 663535746 359 HE------DWGTTPATInsALNVADKTDTQVAIH 386
Cdd:cd01307 137 RAsksvvgEWGIKPLEL--AKKIAKEADLPLMVH 168
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
204-280 |
4.52e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 40.04 E-value: 4.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663535746 204 SADLVITNAMIIDPVLGIIKADIGVKDGKILGVgnagnpnvmdDVDIVVSSNTEIISGEHTICTPGTIDSHIHFISP 280
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLLGDVLVEDGKIVAI----------APEISATAVDTVIDAEGLTLLPGVIDPQVHFREP 68
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
187-279 |
4.78e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 40.20 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663535746 187 KSARDGLGQASGVLRKDS-ADLVITNAMIIDPVLG-IIKADIGVKDGKILGVGNAgnpnvmddvdIVVSSNTEIISGEHT 264
Cdd:PRK10027 11 HISRAEYQELLAVSRGDAvADYIIDNVSILDLINGgEISGPIVIKGRYIAGVGAE----------YADAPALQRIDARGA 80
|
90
....*....|....*
gi 663535746 265 ICTPGTIDSHIHFIS 279
Cdd:PRK10027 81 TAVPGFIDAHLHIES 95
|
|
| |
