|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02303 |
PLN02303 |
urease |
1-838 |
0e+00 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 1728.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 1 MKLLPREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGDKSVAELMDIGRQLLGRRQVLPAVLHLLYT 80
Cdd:PLN02303 1 MKLSPREIDKLLLHQAGFLAQKRLARGLRLNYTEAVALIATQILEFIRDGDKSVAELMDLGKQLLGRRQVLPAVPHLLHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 81 VQVEGTFRDGTKLVTVHEPISLENGNLELALHGSFLPVPSLDKFPEVHEGVIiPGDMKYGDGSIIINHGRKAVVLKVVNT 160
Cdd:PLN02303 81 VQVEGTFPDGTKLVTVHDPISSEDGNLELALHGSFLPVPSLDKFPEDEEEPI-PGEIITGDGSIIINAGRKAVKLKVTNT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 161 GDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVVLVNIGGNKVIRGGNGIVDGLVDDVNWTVL 240
Cdd:PLN02303 160 GDRPIQVGSHYHFIETNPYLVFDRRKAYGMRLNIPAGTAVRFEPGETKTVTLVSIGGNKVIRGGNGIVDGPVDDSRLTKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 241 METMERRGFKHLEDIDASEGIAGEDPRFTTMISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLR 320
Cdd:PLN02303 240 MERVSSRGFGHVEEDDASEGVIGEDPDFTTTISREKYANMYGPTTGDKIRLGDTNLYAEIEKDFTVYGDECKFGGGKVLR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 321 EGMGQGIEQAEALSLDTVITNSVIIDYSGIYKADIGIKNGHIVGIGKAGNPDTMHGVQNNMLIGNKTEVIAGEGMIVTAG 400
Cdd:PLN02303 320 DGMGQATGYGAADSLDTVITNAVIIDYTGIYKADIGIKDGLIVGIGKAGNPDVMDGVTSNMIVGVNTEVIAGEGMIVTAG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 401 AIDCHVHFICPQLVYEAVSSGITTMVGGGTGPAYGTRATTCTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLELRHIV 480
Cdd:PLN02303 400 GIDCHVHFICPQLATEAIASGITTLVGGGTGPAHGTCATTCTPAPSHMKLMLQSTDDLPLNFGFTGKGNTAKPEGLHEII 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 481 EAGAMGLKLHEDWGTTPAAIDNCLAVAEEYDIQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCG 560
Cdd:PLN02303 480 KAGAMGLKLHEDWGTTPAAIDNCLDVAEEYDIQVTIHTDTLNESGCVEHSIAAFKGRTIHTYHSEGAGGGHAPDIIKVCG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 561 VKNVLPSSTNPTRPYTKNTVDEHLDMLMVCHHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGE 640
Cdd:PLN02303 560 VKNVLPSSTNPTRPYTKNTIDEHLDMLMVCHHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 641 VISRTWQTADKMKAQRGAIDPNMADDDNSRIKRYIAKYTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMIIK 720
Cdd:PLN02303 640 VITRTWQTAHKMKSQRGALEPRGADNDNFRIKRYIAKYTINPAIAHGMSHFVGSVEVGKLADLVLWKPAFFGAKPEMVIK 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 721 GGNIAWANMGDANASIPTPEPVISRPMFGAFGKAGSENSVAFVSKAALRKGVKELYGLKKRVVAVSNVRQLTKLDMKLND 800
Cdd:PLN02303 720 GGQIAWAQMGDPNASIPTPEPVIMRPMFGAFGKAGSSNSIAFVSKAALDAGVKQLYGLTKRVEAVGNVRGLTKLDMKLND 799
|
810 820 830
....*....|....*....|....*....|....*...
gi 15220459 801 ALPEITVDPETYVVTANGEVLTCAPADSVPLSRNYFLF 838
Cdd:PLN02303 800 ALPVITVDPETYEVTADGEVLTCAPATSVPLSRNYFLF 837
|
|
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
272-838 |
0e+00 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 1158.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 272 ISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLREGMGQGIEQAEALSLDTVITNSVIIDYSGIY 351
Cdd:COG0804 4 ISRKAYADLYGPTTGDRVRLADTDLFIEVEKDLTTYGDEVKFGGGKVIRDGMGQSQTTRAEGALDLVITNAVILDHWGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 352 KADIGIKNGHIVGIGKAGNPDTMHGVQNNMLIGNKTEVIAGEGMIVTAGAIDCHVHFICPQLVYEAVSSGITTMVGGGTG 431
Cdd:COG0804 84 KADIGIKDGRIVGIGKAGNPDTMDGVDPDLVIGPGTEVIAGEGLILTAGGIDTHIHFICPQQIEEALASGITTMIGGGTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 432 PAYGTRATTCTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLELRHIVEAGAMGLKLHEDWGTTPAAIDNCLAVAEEYD 511
Cdd:COG0804 164 PAEGTNATTCTPGPWNIARMLEAADALPMNIGFLGKGNASSPEALEEQIRAGACGLKLHEDWGATPAAIDACLSVADEYD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 512 IQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCGVKNVLPSSTNPTRPYTKNTVDEHLDMLMVCH 591
Cdd:COG0804 244 VQVAIHTDTLNESGFVEDTIAAIKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLMVCH 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 592 HLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVISRTWQTADKMKAQRGAIDPNMADDDNSRI 671
Cdd:COG0804 324 HLDPSIPEDVAFAESRIRPETIAAEDVLHDLGAISMMSSDSQAMGRVGEVITRTWQTAHKMKKQRGPLPGDSGRNDNFRV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 672 KRYIAKYTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMIIKGGNIAWANMGDANASIPTPEPVISRPMFGAF 751
Cdd:COG0804 404 KRYVAKYTINPAIAHGISHEVGSVEVGKLADLVLWDPAFFGVKPELVIKGGMIAWAQMGDPNASIPTPQPVHYRPMFGAY 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 752 GKAGSENSVAFVSKAALRKGVKELYGLKKRVVAVSNVRQLTKLDMKLNDALPEITVDPETYVVTANGEVLTCAPADSVPL 831
Cdd:COG0804 484 GKALAATSVTFVSQAALEAGIAERLGLRKRLLPVKNTRNIGKADMVLNDATPDIEVDPETYEVRVDGELLTCEPATELPL 563
|
....*..
gi 15220459 832 SRNYFLF 838
Cdd:COG0804 564 AQRYFLF 570
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
272-838 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 1132.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 272 ISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLREGMGQGIEQAEALSLDTVITNSVIIDYSGIY 351
Cdd:PRK13207 4 ISRRAYAEMYGPTTGDRVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQRARADGAVDTVITNALILDHWGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 352 KADIGIKNGHIVGIGKAGNPDTMHGVqnNMLIGNKTEVIAGEGMIVTAGAIDCHVHFICPQLVYEAVSSGITTMVGGGTG 431
Cdd:PRK13207 84 KADIGIKDGRIVAIGKAGNPDIQDGV--DIIIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQIEEALASGVTTMIGGGTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 432 PAYGTRATTCTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLELRHIVEAGAMGLKLHEDWGTTPAAIDNCLAVAEEYD 511
Cdd:PRK13207 162 PATGTNATTCTPGPWHIHRMLQAADAFPMNIGFLGKGNASLPEALEEQIEAGAIGLKLHEDWGATPAAIDNCLSVADEYD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 512 IQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCGVKNVLPSSTNPTRPYTKNTVDEHLDMLMVCH 591
Cdd:PRK13207 242 VQVAIHTDTLNESGFVEDTIAAFKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLMVCH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 592 HLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVISRTWQTADKMKAQRGAIDPNMADDDNSRI 671
Cdd:PRK13207 322 HLDPSIPEDVAFAESRIRRETIAAEDILHDLGAISMISSDSQAMGRVGEVIIRTWQTAHKMKVQRGPLPGDSGRNDNFRV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 672 KRYIAKYTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMIIKGGNIAWANMGDANASIPTPEPVISRPMFGAF 751
Cdd:PRK13207 402 KRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWKPAFFGVKPELVLKGGMIAWAPMGDPNASIPTPQPVHYRPMFGAY 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 752 GKAGSENSVAFVSKAALRKGVKELYGLKKRVVAVSNVRQLTKLDMKLNDALPEITVDPETYVVTANGEVLTCAPADSVPL 831
Cdd:PRK13207 482 GGALAATSVTFVSQAALDAGIPEKLGLKKRLVPVKNTRGITKADMKLNDATPKIEVDPETYEVRADGELLTCEPATVLPL 561
|
....*..
gi 15220459 832 SRNYFLF 838
Cdd:PRK13207 562 AQRYFLF 568
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
272-837 |
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: 1101.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 272 ISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLREGMGQGIEQAEALSLDTVITNSVIIDYSGIY 351
Cdd:cd00375 2 ISREAYADMYGPTTGDKVRLGDTDLWIEVEKDYTTYGDEVKFGGGKVLRDGMGQSSGYTREDVLDLVITNALIIDYTGIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 352 KADIGIKNGHIVGIGKAGNPDTMHGVQNNMLIGNKTEVIAGEGMIVTAGAIDCHVHFICPQLVYEAVSSGITTMVGGGTG 431
Cdd:cd00375 82 KADIGIKDGRIVAIGKAGNPDIMDGVTPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIEEALASGITTMIGGGTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 432 PAYGTRATTCTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLELRHIVEAGAMGLKLHEDWGTTPAAIDNCLAVAEEYD 511
Cdd:cd00375 162 PAAGTKATTCTPGPWNIKRMLQAADGLPVNIGFLGKGNGSSPDALAEQIEAGACGLKLHEDWGATPAAIDTCLSVADEYD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 512 IQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCGVKNVLPSSTNPTRPYTKNTVDEHLDMLMVCH 591
Cdd:cd00375 242 VQVAIHTDTLNESGFVEDTIAAIKGRTIHTYHTEGAGGGHAPDIIKVAGHPNVLPSSTNPTRPFTVNTLDEHLDMLMVCH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 592 HLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVISRTWQTADKMKAQRGAIDPNMADDDNSRI 671
Cdd:cd00375 322 HLDPNIPEDVAFAESRIRAETIAAEDVLHDLGAISIMSSDSQAMGRVGEVILRTWQTAHKMKAQRGPLPEDSGDADNFRV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 672 KRYIAKYTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMIIKGGNIAWANMGDANASIPTPEPVISRPMFGAF 751
Cdd:cd00375 402 KRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGVKPEMVLKGGFIAYAQMGDPNASIPTPQPVMMRPMFGAH 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 752 GKAGSENSVAFVSKAALRKGVKELYGLKKRVVAVSNVRQLTKLDMKLNDALPEITVDPETYVVTANGEVLTCAPADSVPL 831
Cdd:cd00375 482 GKAPAATSVTFVSQASLDAGIAEELGLRRRVVAVKNCRGVGKKDMKLNSATPDIEVDPETYEVRVDGELLTCEPADELPL 561
|
....*.
gi 15220459 832 SRNYFL 837
Cdd:cd00375 562 AQRYFL 567
|
|
| urease_alph |
TIGR01792 |
urease, alpha subunit; This model describes the urease alpha subunit UreC (designated beta or ... |
272-838 |
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: 975.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 272 ISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLREGMGQG-IEQAEALSLDTVITNSVIIDYSGI 350
Cdd:TIGR01792 2 MSREQYASLYGPTTGDKVRLGDTDLFVEVEKDLTTYGDESKFGGGKVLRDGMGQNaTLTRNAGVLDLVITNALILDWTGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 351 YKADIGIKNGHIVGIGKAGNPDTMHGVqnNMLIGNKTEVIAGEGMIVTAGAIDCHVHFICPQLVYEAVSSGITTMVGGGT 430
Cdd:TIGR01792 82 YKADIGIKNGRIVGIGKAGNPDTMDGV--DMIVGASTEAISGEGKIVTAGGIDTHVHYISPQQVQAALDNGITTLIGGGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 431 GPAYGTRATTCTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLELRHIVEAGAMGLKLHEDWGTTPAAIDNCLAVAEEY 510
Cdd:TIGR01792 160 GPADGTNATTCTPGPWYLHRMLQAADGLPINFGFTGKGSGSGPAALIEQIEAGACGLKVHEDWGATPAAIDNALSVADEY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 511 DIQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCGVKNVLPSSTNPTRPYTKNTVDEHLDMLMVC 590
Cdd:TIGR01792 240 DVQVAVHTDTLNESGFVEDTIAAFKGRTIHTYHTEGAGGGHAPDIIVVVGYNNILPSSTNPTLPYTVNTIDEHLDMLMVC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 591 HHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVISRTWQTADKMKAQRGAIDPNMADDDNSR 670
Cdd:TIGR01792 320 HHLNPKIPEDVAFAESRIRKETIAAEDVLQDMGAISMISSDSQAMGRIGEVVTRCWQTADKMKKQRGPLPGDSPGNDNNR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 671 IKRYIAKYTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMIIKGGNIAWANMGDANASIPTPEPVISRPMFGA 750
Cdd:TIGR01792 400 VKRYVAKYTINPAITHGISDYIGSIEVGKLADLVLWEPAFFGVKPDMVLKGGLIAWAIMGDPNASIPTPQPVLYRPMFGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 751 FGKAGSENSVAFVSKAALRKGVKELYGLKKRVVAVSNVRQLTKLDMKLNDALPEITVDPETYVVTANGEVLTCAPADSVP 830
Cdd:TIGR01792 480 YGRALQSTSITFVSQAAYDKGIKERLGLQKLLLPVHNTRSIGKADMKLNSATPKIEVDPQTYDVKVDGVLITVEPADELP 559
|
....*...
gi 15220459 831 LSRNYFLF 838
Cdd:TIGR01792 560 LTQRYFLF 567
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
270-838 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 926.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 270 TMISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTV----YGDECVFGGGKVLREGMGQGIEQAEALSLDTVITNSVII 345
Cdd:PRK13206 2 TRLSRERYAALYGPTTGDRIRLADTDLLIEVTEDRSGgpglAGDEAVFGGGKVIRESMGQGRATRAEGAPDTVITGAVIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 346 DYSGIYKADIGIKNGHIVGIGKAGNPDTMHGVQNNMLIGNKTEVIAGEGMIVTAGAIDCHVHFICPQLVYEAVSSGITTM 425
Cdd:PRK13206 82 DHWGIVKADVGIRDGRIVAIGKAGNPDIMDGVHPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICPQIVDEALAAGITTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 426 VGGGTGPAYGTRATTCTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLELRHIVEAGAMGLKLHEDWGTTPAAIDNCLA 505
Cdd:PRK13206 162 IGGGTGPAEGSKATTVTPGAWHLARMLEALDGWPVNVALLGKGNTVSAEALWEQLRGGAGGFKLHEDWGSTPAAIDACLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 506 VAEEYDIQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCGVKNVLPSSTNPTRPYTKNTVDEHLD 585
Cdd:PRK13206 242 VADAAGVQVALHSDTLNEAGFVEDTLAAIAGRSIHAYHTEGAGGGHAPDIITVASHPNVLPSSTNPTRPHTVNTLDEHLD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 586 MLMVCHHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVISRTWQTADKMKAQRGAIDPNMAd 665
Cdd:PRK13206 322 MLMVCHHLNPAVPEDLAFAESRIRPSTIAAEDVLHDMGAISMIGSDSQAMGRIGEVVLRTWQTAHVMKRRRGALPGDGR- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 666 DDNSRIKRYIAKYTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMIIKGGNIAWANMGDANASIPTPEPVISR 745
Cdd:PRK13206 401 ADNNRARRYVAKYTICPAVAHGIDHEIGSVEVGKLADLVLWEPAFFGVRPHAVLKGGAIAWAAMGDANASIPTPQPVLPR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 746 PMFGAFGKAGSENSVAFVSKAALRKGVKELYGLKKRVVAVSNVRQLTKLDMKLNDALPEITVDPETYVVTANGEVLTCAP 825
Cdd:PRK13206 481 PMFGAAPAAAAATSVHFVAPQAIEDGLADRLGLRRRLVPVADTRAVGKADMPLNDALPDIEVDPDTFTVRIDGEVWEPQP 560
|
570
....*....|...
gi 15220459 826 ADSVPLSRNYFLF 838
Cdd:PRK13206 561 AAELPMAQRYFLF 573
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
269-837 |
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 15220459 269 TTMISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLREGMG--QGIEQAEAlSLDTVITNSVIID 346
Cdd:PRK13308 1 MATIDRRAYAELYGPTTGDRVRLADTSLLAEVEHDHTVYGDECLFGGGKTLRDGMGmaPGVTSADG-ALDFVLCNVTVID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 347 -YSGIYKADIGIKNGHIVGIGKAGNPDTMHGVQNNMLIGNKTEVIAGEGMIVTAGAIDCHVHFICPQLVYEAVSSGITTM 425
Cdd:PRK13308 80 pVLGIVKGDIGIRDGRIVGIGKAGNPDIMDGVDPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQLVDHALASGITTM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 426 VGGGTGPAygtrATTCTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLELRHIVEAGAMGLKLHEDWGTTPAAIDNCLA 505
Cdd:PRK13308 160 LGGGLGPT----VGIDSGGPFNTGRMLQAAEAWPVNFGFLGRGNSSKPAALIEQVEAGACGLKIHEDWGAMPAAIDTCLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 506 VAEEYDIQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCGVKNVLPSSTNPTRPYTKNTVDEHLD 585
Cdd:PRK13308 236 VADEYDFQVQLHTDTLNESGFVEDTLAAIGGRTIHMYHTEGAGGGHAPDIIRVVGEPHCLPSSTNPTNPYTVNTFDEHLD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 586 MLMVCHHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVISRTWQTADKMKAQRGAIDPNM-A 664
Cdd:PRK13308 316 MTMVCHHLNPDVPEDVAFAESRIRAQTIAAEDVLHDIGAISMLGSDSQGMGRIAEVIARTWQLASKMKDQRGPLPEDRgT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 665 DDDNSRIKRYIAKYTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMIIKGGNIAWANMGDANASIPTPEPVIS 744
Cdd:PRK13308 396 FADNARIKRYIAKYTINPAITFGIDDHIGSLEPGKLADIVLWRPAFFGIKPELVIKGGFPAWAAMGDANGSLMTCEPMLQ 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 745 RPMFGAFGKAGSENSVAFVSKAALRKGVKELYGLKKRVVAVSNVRQLTKLDMKLNDALPEITVDPETYVVTANGEVLTCA 824
Cdd:PRK13308 476 RPQWGAFGRAKQALSVCFVSPLAIEAGLGERLGLRKRLLPVRGTRTLTKADMLHNDACPDIRVDPQTFEVFVDGELVTCE 555
|
570
....*....|...
gi 15220459 825 PADSVPLSRNYFL 837
Cdd:PRK13308 556 PATELPLAQRYML 568
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
272-838 |
0e+00 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 838.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 272 ISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLREGMGQGIEQAEAlSLDTVITNSVIIDYSGIY 351
Cdd:PRK13985 3 ISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYTIYGEELKFGGGKTLREGMSQSNNPSKE-ELDLIITNALIIDYTGIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 352 KADIGIKNGHIVGIGKAGNPDTMHGVQNNMLIGNKTEVIAGEGMIVTAGAIDCHVHFICPQLVYEAVSSGITTMVGGGTG 431
Cdd:PRK13985 82 KADIGIKDGKIAGIGKGGNKDMQDGVKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTAFASGVTTMIGGGTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 432 PAYGTRATTCTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLELRHIVEAGAMGLKLHEDWGTTPAAIDNCLAVAEEYD 511
Cdd:PRK13985 162 PADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLGKGNSSNDASLADQIEAGAIGFKIHEDWGTTPSAINHALDVADKYD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 512 IQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCGVKNVLPSSTNPTRPYTKNTVDEHLDMLMVCH 591
Cdd:PRK13985 242 VQVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGGHAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDMLMVCH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 592 HLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVISRTWQTADKMKAQRGAIDPNMADDDNSRI 671
Cdd:PRK13985 322 HLDKSIKEDVQFADSRIRPQTIAAEDTLHDMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKGDNDNFRI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 672 KRYIAKYTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMIIKGGNIAWANMGDANASIPTPEPVISRPMFGAF 751
Cdd:PRK13985 402 KRYLSKYTINPAIAHGISEYVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVYYREMFAHH 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 752 GKAGSENSVAFVSKAALRKGVKELYGLKKRVVAVSNVRQLTKLDMKLNDALPEITVDPETYVVTANGEVLTCAPADSVPL 831
Cdd:PRK13985 482 GKAKYDANITFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTSKPANKVSL 561
|
....*..
gi 15220459 832 SRNYFLF 838
Cdd:PRK13985 562 AQLFSIF 568
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
270-837 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 777.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 270 TMISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLREGMGQGIE-QAEALSLDTVITNSVIIDYS 348
Cdd:PRK13309 2 PQISRQEYAGLFGPTTGDKIRLGDTNLFIEIEKDLRGYGDESVYGGGKSLRDGMGANNNlTRDNGVLDLVITNVTIVDAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 349 -GIYKADIGIKNGHIVGIGKAGNPDTMHGVQNNMLIGNKTEVIAGEGMIVTAGAIDCHVHFICPQLVYEAVSSGITTMVG 427
Cdd:PRK13309 82 lGVIKADVGIRDGKIVGIGKSGNPSTMDGVTQGMVVGVSTDAISGEHLILTAAGIDTHIHLISPQQAYHALSNGVTTFFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 428 GGTGPAYGTRATTCTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLELRHIVEAGAMGLKLHEDWGTTPAAIDNCLAVA 507
Cdd:PRK13309 162 GGIGPTDGTNGTTVTPGPWNIRQMLRSIEGLPVNVGILGKGNSYGRGPLLEQAIAGVAGYKVHEDWGATAAALRHALRVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 508 EEYDIQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCGVKNVLPSSTNPTRPYTKNTVDEHLDML 587
Cdd:PRK13309 242 DEVDIQVAVHTDSLNECGYVEDTIDAFEGRTIHTFHTEGAGGGHAPDIIKVASQTNVLPSSTNPTLPYGVNSQAELFDMI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 588 MVCHHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVISRTWQTADKMKAQRGAIDPNMADDD 667
Cdd:PRK13309 322 MVCHNLNPNVPADVAFAESRVRPETIAAENVLHDMGVISMFSSDSQAMGRVGENWLRAIQTADAMKAARGKLPEDAAGND 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 668 NSRIKRYIAKYTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMIIKGGNIAWANMGDANASIPTPEPVISRPM 747
Cdd:PRK13309 402 NFRVLRYVAKITINPAITQGVSHVIGSVEVGKMADLVLWEPRFFGAKPKMVIKGGMINWAAMGDPNASLPTPQPVFYRPM 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 748 FGAFGKAGSENSVAFVSKAALRKGVKELYGLKKRVVAVSNVRQLTKLDMKLNDALPEITVDPETYVVTANGEVLTCAPAD 827
Cdd:PRK13309 482 FGAMGKTLQDTCVTFVSQAALDDGVKEKAGLDRQVIAVKNCRTISKRDLVRNSQTPNIEVDPETFAVKVDGVHATVKPIA 561
|
570
....*....|
gi 15220459 828 SVPLSRNYFL 837
Cdd:PRK13309 562 TASLNQRYFF 571
|
|
| PRK13192 |
PRK13192 |
bifunctional urease subunit gamma/beta; Reviewed |
1-230 |
3.79e-101 |
|
bifunctional urease subunit gamma/beta; Reviewed
Pssm-ID: 183886 [Multi-domain] Cd Length: 208 Bit Score: 311.92 E-value: 3.79e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 1 MKLLPREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGdKSVAELMDIGRQLLGRRQVLPAVLHLLYT 80
Cdd:PRK13192 1 MRLTPTELDRLLLFTAAELARKRRARGLKLNYPEAVALIADEVLEAARDG-RSVAELIDLGRTILTTDDVLPGVADMVPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 81 VQVEGTFRDGTKLVTVHEPISLENGNLELALhgsflpvpsldkfpevhegviIPGDMKYGDGSIIINHGRKAVVLKVVNT 160
Cdd:PRK13192 80 VQVEATFPDGTKLVTVHDPIRPAEGDLADAL---------------------YPGEILPGDGEIELNAGRPAVTLDVTNT 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 161 GDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVVLVNIGGNKVIRGGNGIVDG 230
Cdd:PRK13192 139 GDRPIQVGSHFHFFEVNRALRFDRAAAYGMRLDIPAGTAVRFEPGETKEVRLVPIGGARVVIGFNGLTNG 208
|
|
| PRK13986 |
PRK13986 |
urease subunit beta; |
1-251 |
2.29e-79 |
|
urease subunit beta;
Pssm-ID: 184439 [Multi-domain] Cd Length: 225 Bit Score: 255.52 E-value: 2.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 1 MKLLPREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGDKSVAELMDIGRQLLGRRQVLPAVLHLLYT 80
Cdd:PRK13986 1 MKLTPKELDKLMLHYAGELAKKRKEKGIKLNYVEAVALISAHIMEEARAGKKTVAELMQEGRTLLKPDDVMDGVASMIHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 81 VQVEGTFRDGTKLVTVHEPISlENGNLelalhgsflpvpsldkfpevhegviIPGDMKYGDGSIIINHGRKAVVLKVVNT 160
Cdd:PRK13986 81 VGIEAMFPDGTKLVTVHTPIE-ANGKL-------------------------VPGELFLKDEDITINAGKKAVSVKVKNV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 161 GDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVVLVNIGGNKVIRGGNGIVDGLVDDVNWTVL 240
Cdd:PRK13986 135 GDRPVQVGSHFHFFEVNRCLEFDREKAFGKRLDIASGTAVRFEPGEEKSVELIDIGGNRRIFGFNALVNRQADNESKKIA 214
|
250
....*....|.
gi 15220459 241 METMERRGFKH 251
Cdd:PRK13986 215 LHRAKERGFHG 225
|
|
| Urease_alpha |
pfam00449 |
Urease alpha-subunit, N-terminal domain; The N-terminal domain is a composite domain and plays ... |
271-390 |
4.48e-71 |
|
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: 228.92 E-value: 4.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 271 MISREKYANMYGPTTGDKLRLGDTNLYARIEKDYTVYGDECVFGGGKVLREGMGQGIEQAEALSLDTVITNSVIIDYSGI 350
Cdd:pfam00449 1 KISREAYADMYGPTTGDRIRLGDTDLFIEVEKDLTVYGDEVKFGGGKVIRDGMGQSQGRTRDDALDLVITNALILDYTGI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15220459 351 YKADIGIKNGHIVGIGKAGNPDTMHGVQNNMLIGNKTEVI 390
Cdd:pfam00449 81 VKADIGIKDGRIVGIGKAGNPDTMDGVTPGMVIGPSTEVI 120
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
396-722 |
2.59e-64 |
|
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: 218.91 E-value: 2.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 396 IVTAGAIDCHVHF---------ICPQLVYEAVSSGITTMVGGGTGPAYGTRATTCTPspfdMKLMLQSTDSLPLNFGFTG 466
Cdd:pfam01979 1 IVLPGLIDAHVHLemgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTG----IEALLEAAEELPLGLRFLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 467 K-------GNTAKPLELRHIVEAGA------------MGLKLHEDWGTTPAAIDNCLAVAEEYDIQVNIHTdtLNESGFV 527
Cdd:pfam01979 77 PgcsldtdGELEGRKALREKLKAGAefikgmadgvvfVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHA--LETKGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 528 EHTINAFRGRTIHTYHSEGAGGGHAPDIIRVCGVKNVLPSSTnptrpyTKNTVDEHLDMLMVCHhldknipedVAFAESR 607
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPT------EANLLAEHLKGAGVAH---------CPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 608 IRAETIAAEDILHDmGAISIISSDSQAMGRIGEVISRtwqTADKMKAQRGaidpnmaDDDNSRIKRYIAKYTINPAIANG 687
Cdd:pfam01979 220 LRSGRIALRKALED-GVKVGLGTDGAGSGNSLNMLEE---LRLALELQFD-------PEGGLSPLEALRMATINPAKALG 288
|
330 340 350
....*....|....*....|....*....|....*....
gi 15220459 688 FADLIGSVEVKKLADLVIW----QPAFFGAKPEMIIKGG 722
Cdd:pfam01979 289 LDDKVGSIEVGKDADLVVVdldpLAAFFGLKPDGNVKKV 327
|
|
| Urease_beta |
pfam00699 |
Urease beta subunit; This subunit is known as alpha in Heliobacter. |
134-230 |
2.00e-59 |
|
Urease beta subunit; This subunit is known as alpha in Heliobacter.
Pssm-ID: 459909 Cd Length: 98 Bit Score: 196.83 E-value: 2.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 134 PGDMKYGDGSIIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVVLV 213
Cdd:pfam00699 1 PGEIITGDGDIELNAGRETITLTVTNTGDRPIQVGSHYHFFEVNPALEFDREAAYGMRLDIPAGTAVRFEPGDTKTVTLV 80
|
90
....*....|....*..
gi 15220459 214 NIGGNKVIRGGNGIVDG 230
Cdd:pfam00699 81 PIGGARVVYGFNGLVNG 97
|
|
| Urease_gamma |
pfam00547 |
Urease, gamma subunit; Urease is a nickel-binding enzyme that catalyzes the hydrolysis of urea ... |
1-100 |
9.19e-58 |
|
Urease, gamma subunit; Urease is a nickel-binding enzyme that catalyzes the hydrolysis of urea to carbon dioxide and ammonia.
Pssm-ID: 459850 Cd Length: 99 Bit Score: 192.25 E-value: 9.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 1 MKLLPREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGdKSVAELMDIGRQLLGRRQVLPAVLHLLYT 80
Cdd:pfam00547 1 MHLTPREQDKLLLFVAGELARRRLARGLKLNYPEAVALIADELLEGARDG-KSVAELMQLGRTVLGRDDVMPGVPEMLPE 79
|
90 100
....*....|....*....|
gi 15220459 81 VQVEGTFRDGTKLVTVHEPI 100
Cdd:pfam00547 80 VQVEATFPDGTKLVTVHDPI 99
|
|
| Urease_beta |
cd00407 |
Urease beta-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
132-230 |
7.69e-56 |
|
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: 186.96 E-value: 7.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 132 IIPGDMKYGDGSIIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVV 211
Cdd:cd00407 1 MIPGEIILKEGDIELNAGREAVTLKVKNTGDRPIQVGSHYHFFEVNPALKFDREKAYGMRLDIPAGTAVRFEPGEEKEVE 80
|
90
....*....|....*....
gi 15220459 212 LVNIGGNKVIRGGNGIVDG 230
Cdd:cd00407 81 LVPIGGKRRVYGFNGLVNG 99
|
|
| UreB |
COG0832 |
Urease beta subunit [Amino acid transport and metabolism]; |
135-234 |
9.09e-54 |
|
Urease beta subunit [Amino acid transport and metabolism];
Pssm-ID: 440594 Cd Length: 101 Bit Score: 181.03 E-value: 9.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 135 GDMKYGDGSIIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVVLVN 214
Cdd:COG0832 1 GEIIVADGDIELNAGRETITLTVANTGDRPIQVGSHYHFFEVNPALEFDREAARGMRLDIPAGTAVRFEPGQTREVELVP 80
|
90 100
....*....|....*....|
gi 15220459 215 IGGNKVIRGGNGIVDGLVDD 234
Cdd:COG0832 81 IGGARRVYGFNGLVNGPLDD 100
|
|
| Urease_gamma |
cd00390 |
Urease gamma-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
5-100 |
5.22e-50 |
|
Urease gamma-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: 238229 Cd Length: 96 Bit Score: 170.46 E-value: 5.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 5 PREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGdKSVAELMDIGRQLLGRRQVLPAVLHLLYTVQVE 84
Cdd:cd00390 2 PRELEKLLIFTAAELARKRLARGLKLNYPEAVALIADEILEGARDG-KSVAELMSLGKTVLTRDDVMEGVPEMLHDVQVE 80
|
90
....*....|....*.
gi 15220459 85 GTFRDGTKLVTVHEPI 100
Cdd:cd00390 81 ATFPDGTKLVTVHDPI 96
|
|
| UreA |
COG0831 |
Urease gamma subunit [Amino acid transport and metabolism]; |
1-103 |
2.24e-46 |
|
Urease gamma subunit [Amino acid transport and metabolism];
Pssm-ID: 440593 Cd Length: 102 Bit Score: 160.68 E-value: 2.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 1 MKLLPREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGdKSVAELMDIGRQLLGRRQVLPAVLHLLYT 80
Cdd:COG0831 1 MHLTPREQEKLLIFTAAELARRRRARGLKLNYPEAVALISDEVLEGARDG-KSVAELMEEGRTVLTRDDVMPGVPEMIPE 79
|
90 100
....*....|....*....|...
gi 15220459 81 VQVEGTFRDGTKLVTVHEPISLE 103
Cdd:COG0831 80 VQVEATFPDGTKLVTVHDPIRPA 102
|
|
| ureB |
PRK13203 |
urease subunit beta; Reviewed |
133-233 |
7.20e-46 |
|
urease subunit beta; Reviewed
Pssm-ID: 237303 Cd Length: 102 Bit Score: 159.22 E-value: 7.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 133 IPGDMKYGDGSIIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVVL 212
Cdd:PRK13203 2 IPGEYITADGEIELNAGRETVTLTVANTGDRPIQVGSHYHFFEVNPALSFDREAARGMRLNIPAGTAVRFEPGQTREVEL 81
|
90 100
....*....|....*....|.
gi 15220459 213 VNIGGNKVIRGGNGIVDGLVD 233
Cdd:PRK13203 82 VPLAGARRVYGFRGKVMGKLD 102
|
|
| urease_beta |
TIGR00192 |
urease, beta subunit; In a number of species, including B.subtilis, Synechocystis, and ... |
132-230 |
4.82e-43 |
|
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: 151.13 E-value: 4.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 132 IIPGDMKYGDGSIIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVV 211
Cdd:TIGR00192 1 MIPGELQLAEGDITINEGRKTVSVKVKNTGDRPIQVGSHFHFFEVNRALDFDRELAFGMRLDIPSGTAVRFEPGEEKSVE 80
|
90
....*....|....*....
gi 15220459 212 LVNIGGNKVIRGGNGIVDG 230
Cdd:TIGR00192 81 LVAIGGNRRIYGFNGLVDG 99
|
|
| ureA |
PRK13241 |
urease subunit gamma; Provisional |
1-100 |
1.03e-41 |
|
urease subunit gamma; Provisional
Pssm-ID: 183913 Cd Length: 100 Bit Score: 147.33 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 1 MKLLPREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGdKSVAELMDIGRQLLGRRQVLPAVLHLLYT 80
Cdd:PRK13241 1 MHLTPREKDKLLIFTAALLAERRKARGLKLNYPEAVALISDALLEGARDG-KTVAELMSYGRTVLTRDDVMEGVPEMIPD 79
|
90 100
....*....|....*....|
gi 15220459 81 VQVEGTFRDGTKLVTVHEPI 100
Cdd:PRK13241 80 VQVEATFPDGTKLVTVHDPI 99
|
|
| urease_gam |
TIGR00193 |
urease, gamma subunit; In a number of species, including B.subtilis, Synechocystis, and ... |
1-103 |
2.39e-33 |
|
urease, gamma 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. Nomenclature for the various subunits of urease in Helicobacter differs from nomenclature in most other species. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 272952 Cd Length: 102 Bit Score: 123.83 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 1 MKLLPREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGdKSVAELMDIGRQLLGRRQVLPAVLHLLYT 80
Cdd:TIGR00193 1 MKLTPKEQDKLMLFYAGELAKKRKARGVKLNYPEAVAYISAHIMEGARDG-KKVAELMQYGRTLLTPDDVMEGVAEMLHE 79
|
90 100
....*....|....*....|...
gi 15220459 81 VQVEGTFRDGTKLVTVHEPISLE 103
Cdd:TIGR00193 80 VQIEATFPDGTKLVTVHTPIRAN 102
|
|
| ureB |
PRK13201 |
urease subunit beta; Reviewed |
132-264 |
2.10e-32 |
|
urease subunit beta; Reviewed
Pssm-ID: 237302 [Multi-domain] Cd Length: 136 Bit Score: 122.25 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 132 IIPGDMKYGDGSIIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVV 211
Cdd:PRK13201 1 MIPGEIITKSTEVEINNHHPETVIEVENTGDRPIQVGSHFHFYEANAALDFEREMAYGKHLDIPAGAAVRFEPGDKKEVQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15220459 212 LVNIGGNKVIRGGNGIVDGLVDdvnwtvlmetmERRGFKHLEDIDASEGIAGE 264
Cdd:PRK13201 81 LVEYAGKRKIFGFRGMVNGPID-----------ESRVYRPTDENDAYAGVFGD 122
|
|
| ureB |
PRK13205 |
urease subunit beta; Reviewed |
132-239 |
4.35e-32 |
|
urease subunit beta; Reviewed
Pssm-ID: 106174 [Multi-domain] Cd Length: 162 Bit Score: 122.60 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 132 IIPGDMKYGDGSIIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVV 211
Cdd:PRK13205 1 MIPGEYILSSESLTGNVGREAKTIEIINTGDRPVQIGSHFHFAEVNPSISFDRSEGYGFRLDIPSGTAVRLEPGDARTVN 80
|
90 100
....*....|....*....|....*...
gi 15220459 212 LVNIGGNKVIRGGNGIVDGLVDDVNWTV 239
Cdd:PRK13205 81 LVAIGGDRIVAGFRDLVDGPLEDLKVNV 108
|
|
| ureB |
PRK13204 |
urease subunit beta; Reviewed |
144-250 |
5.13e-31 |
|
urease subunit beta; Reviewed
Pssm-ID: 171902 [Multi-domain] Cd Length: 159 Bit Score: 119.11 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 144 IIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSVVLVNIGGNKVIRG 223
Cdd:PRK13204 36 IEINQGRPRTTLTVRNTGDRPIQIGSHFHFFEVNRYLEFDRSKAFGLRLDIPANTAVRFEPGDEKEVTLVPFAGKRFIFG 115
|
90 100 110
....*....|....*....|....*....|....
gi 15220459 224 GNGIVDGLVDD-------VNWTVLMETMERRGFK 250
Cdd:PRK13204 116 FNNLVDGWSGDgptpdyqPNREIAAERAEKLGFK 149
|
|
| ureB |
PRK13198 |
urease subunit beta; Reviewed |
129-251 |
6.43e-29 |
|
urease subunit beta; Reviewed
Pssm-ID: 171897 [Multi-domain] Cd Length: 158 Bit Score: 113.24 E-value: 6.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 129 EGVIIPGDMKYGDGSIIINHGRKAVVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERK 208
Cdd:PRK13198 26 EQNTPLGGLVLAETPITFNENKPVTKVKVRNTGDRPIQVGSHFHFFEVNRALEFDRAAAYGKRLNISSTTAIRFEPGDET 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15220459 209 SVVLVNIGGNKVIRGGNGIVDG-----LVDDVNWTVLMETMER---RGFKH 251
Cdd:PRK13198 106 EVPLIPFGGKQTLYGFNNLVDGwtgegVVPNSERPDKLAAIRLaaeRGFKS 156
|
|
| ureB |
PRK13202 |
urease subunit beta; Reviewed |
132-223 |
4.54e-22 |
|
urease subunit beta; Reviewed
Pssm-ID: 106171 Cd Length: 104 Bit Score: 91.68 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 132 IIPGDMKYGDGSIIINHGRKA-VVLKVVNTGDRPVQVGSHYHFIEVNPLLVFDRRKALGMRLNIPAGTAVRFEPGERKSV 210
Cdd:PRK13202 1 MIPGEIFYGSGDIEMNAAALSrLQMRIINAGDRPVQVGSHVHLPQANRALSFDRATAHGYRLDIPAATAVRFEPGIPQIV 80
|
90
....*....|...
gi 15220459 211 VLVNIGGNKVIRG 223
Cdd:PRK13202 81 GLVPLGGRREVPG 93
|
|
| ureA |
PRK13242 |
urease subunit gamma; Provisional |
1-101 |
7.08e-19 |
|
urease subunit gamma; Provisional
Pssm-ID: 139420 Cd Length: 100 Bit Score: 82.43 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 1 MKLLPREIEKLELHQAGFLAQKRLARGIRLNYTEAVALIATQILEFIRDGdKSVAELMDIGRQLLGRRQVLPAVLHLLYT 80
Cdd:PRK13242 1 MHLTPREFDKLVIHMLSDVALKRKNKGLKLNHPEAVAVLSAYVLDGAREG-KTVEEVMDGARSVLKADDVMDGVPDLLPL 79
|
90 100
....*....|....*....|.
gi 15220459 81 VQVEGTFRDGTKLVTVHEPIS 101
Cdd:PRK13242 80 IQVEAVFSDGSRLVSLHNPIT 100
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
333-488 |
1.08e-13 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 74.35 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 333 LSLDTVITNSVIIDYSGIYKADIGIKNGHIVGIGkagnPDTMhgvqnnmliGNKTEVIAGEGMIVTAGAIDCHVHFICP- 411
Cdd:PRK06189 1 MMYDLIIRGGKVVTPEGVYRADIGIKNGKIAEIA----PEIS---------SPAREIIDADGLYVFPGMIDVHVHFNEPg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 412 QLVYEAVSSGITTMVGGGtGPAYGTRATTCTPS-----PFDMKLMLQSTDSLpLNFGFTGkGNTAKPLE-LRHIVEAGAM 485
Cdd:PRK06189 68 RTHWEGFATGSAALAAGG-CTTYFDMPLNSIPPtvtreALDAKAELARQKSA-VDFALWG-GLVPGNLEhLRELAEAGVI 144
|
...
gi 15220459 486 GLK 488
Cdd:PRK06189 145 GFK 147
|
|
| Urease_linker |
pfam18473 |
Urease subunit beta-alpha linker domain; This domain is present in bacterial ureases and ... |
232-265 |
4.80e-13 |
|
Urease subunit beta-alpha linker domain; This domain is present in bacterial ureases and corresponds to the gap region between the C-terminus of the beta-chain Urease beta subunit pfam00699 and the N-terminus of the alpha-chain Urease alpha-subunit, N-terminal domain pfam00449. It is suggested that this region is required for the stability of the putative transmembrane beta-barrel, and might be the reason for bacterial urease (B. pasteurii) not being lethal to insects.
Pssm-ID: 408266 Cd Length: 34 Bit Score: 63.58 E-value: 4.80e-13
10 20 30
....*....|....*....|....*....|....
gi 15220459 232 VDDVNWTVLMETMERRGFKHLEDIDASEGIAGED 265
Cdd:pfam18473 1 VDDSNIEAVMEAVRRRGFGHLEEADASEGVTGED 34
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
338-517 |
1.42e-12 |
|
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: 70.51 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 338 VITNSVIIDYSGIYKADIGIKNGHIVGIGKAGNPDTmhgvqnnmlignKTEVIAGEGMIVTAGAIDCHVHFICPQLVYE- 416
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPE------------AAEVIDATGLLVLPGLIDLHVHLREPGLEHKe 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 417 --------AVSSGITTMVgggtGPAYgTRATTCTPSPFDMKLMLQSTDSLPlNFGFTG---KGNTAKPLELRHIVEAGAM 485
Cdd:COG0044 69 dietgtraAAAGGVTTVV----DMPN-TNPVTDTPEALEFKLARAEEKALV-DVGPHGaltKGLGENLAELGALAEAGAV 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 15220459 486 GLKL-----HEDWGTTPAAIDNCLAVAEEYDIQVNIH 517
Cdd:COG0044 143 AFKVfmgsdDGNPVLDDGLLRRALEYAAEFGALVAVH 179
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
336-724 |
1.29e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 64.21 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 336 DTVITNSVIIDYSG---IYKADIGIKNGHIVGIGKAGNPDTMHGvqnnmlignkTEVIAGEGMIVTAGAIDCHVHFI--- 409
Cdd:COG1228 9 TLLITNATLVDGTGggvIENGTVLVEDGKIAAVGPAADLAVPAG----------AEVIDATGKTVLPGLIDAHTHLGlgg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 410 ---------------------CPQLVYEAVSSGITT---MVGGGTGPAYGTRATTCTPSPFDMklMLQSTDSLPLNFGFT 465
Cdd:COG1228 79 gravefeagggitptvdlvnpADKRLRRALAAGVTTvrdLPGGPLGLRDAIIAGESKLLPGPR--VLAAGPALSLTGGAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 466 GKG-NTAKPLeLRHIVEAGAMGLKLHEDWGT---TPAAIDNCLAVAEEYDIQVNIHTDTLNEsgfVEHTInAFRGRTIHt 541
Cdd:COG1228 157 ARGpEEARAA-LRELLAEGADYIKVFAEGGApdfSLEELRAILEAAHALGLPVAAHAHQADD---IRLAV-EAGVDSIE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 542 yHSEGAggghAPDIIRVCGVKNvlPSSTNPTrpytkntvdehldmLMVCHHLDKNIPEDVAFAESRIRAETIAAEDILHD 621
Cdd:COG1228 231 -HGTYL----DDEVADLLAEAG--TVVLVPT--------------LSLFLALLEGAAAPVAAKARKVREAALANARRLHD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 622 MGAISIISSDSQAMGRIGEVISRTWQTA-----DKMKAQRGAidpnmadddnsrikryiakyTINPAIANGFADLIGSVE 696
Cdd:COG1228 290 AGVPVALGTDAGVGVPPGRSLHRELALAveaglTPEEALRAA--------------------TINAAKALGLDDDVGSLE 349
|
410 420 430
....*....|....*....|....*....|...
gi 15220459 697 VKKLADLVIWQ---PAFFGA--KPEMIIKGGNI 724
Cdd:COG1228 350 PGKLADLVLLDgdpLEDIAYleDVRAVMKDGRV 382
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
336-485 |
2.61e-10 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 63.47 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 336 DTVITNSVIIDYSG--IYKADIGIKNGHIVGIGKAGNPDTmhgvqnnmlignkTEVIAGEGMIVTAGAIDCHVH-----F 408
Cdd:cd01297 1 DLVIRNGTVVDGTGapPFTADVGIRDGRIAAIGPILSTSA-------------REVIDAAGLVVAPGFIDVHTHydgqvF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 409 ICPQLVyEAVSSGITTMVGG--GTGPAYGTRAttcTPSPFDMKLMLQSTDSLPLNFGFTGKGNTAKPLE-LRHIVEAGAM 485
Cdd:cd01297 68 WDPDLR-PSSRQGVTTVVLGncGVSPAPANPD---DLARLIMLMEGLVALGEGLPWGWATFAEYLDALEaRPPAVNVAAL 143
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
336-465 |
9.64e-10 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 62.04 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 336 DTVITNSVIID-YSG-IYKADIGIKNGHIVGIGKAgnpdtmhgvqnnmlIGNKTEVIAGEGMIVTAGAIDCHVHF----I 409
Cdd:COG1001 6 DLVIKNGRLVNvFTGeILEGDIAIAGGRIAGVGDY--------------IGEATEVIDAAGRYLVPGFIDGHVHIessmV 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220459 410 CPQLVYEAV-SSGITTMVgggTGP-----AYGTRAttctpspfdMKLMLQSTDSLPLNFGFT 465
Cdd:COG1001 72 TPAEFARAVlPHGTTTVI---ADPheianVLGLEG---------VRYMLEAAEGLPLDIFVM 121
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
387-724 |
7.33e-09 |
|
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: 58.48 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 387 TEVIAGEGMIVTAGAIDCHVH------------------------------FICPQ--LVYEAVSSGITTM--------V 426
Cdd:cd01309 17 AEVIDAKGKHVTPGLIDAHSHlgldeeggvretsdaneetdpvtphvraidGINPDdeAFKRARAGGVTTVqvlpgsanL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 427 GGGTGPAYGTRATTctpspFDMKLMLQSTDsLPLNFG-----FTGKGNT------AKPLELRHIVEAGAMGLKLHEDW-- 493
Cdd:cd01309 97 IGGQGVVIKTDGGT-----IEDMFIKAPAG-LKMALGenpkrVYGGKGKepatrmGVAALLRDAFIKAQEYGRKYDLGkn 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 494 -GTTPAAID---NCLAVAEEYDIQVNIHTDTLNESGFVEHTINAFRGRTIHTYHSEGAgggHAPDIIRVCGVKNVL-PSS 568
Cdd:cd01309 171 aKKDPPERDlklEALLPVLKGEIPVRIHAHRADDILTAIRIAKEFGIKITIEHGAEGY---KLADELAKHGIPVIYgPTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 569 TNPTRPYTKNtvdehldmlmvchHLDKNIPEdvafaesriraetiaaedILHDMGAISIISSDSQAMGrigevISRTWQT 648
Cdd:cd01309 248 TLPKKVEEVN-------------DAIDTNAY------------------LLKKGGVAFAISSDHPVLN-----IRNLNLE 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220459 649 AdkMKAQRGAIDPNMAdddnsrikryIAKYTINPAIANGFADLIGSVEVKKLADLVIW--QPAFFGAKPEMIIKGGNI 724
Cdd:cd01309 292 A--AKAVKYGLSYEEA----------LKAITINPAKILGIEDRVGSLEPGKDADLVVWngDPLEPTSKPEQVYIDGRL 357
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
336-488 |
2.19e-08 |
|
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: 57.30 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 336 DTVITNSVIIDYSGIYKADIGIKNGHIVGIGKAGnpdtmhgvqnnmLIGNKTEVIAGEGMIVTAGAIDCHVHFICP-QLV 414
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIGPDI------------ANTEAEEVIDAGGLVVMPGLIDTHVHINEPgRTE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 415 YE--------AVSSGITTMVgggTGPAYGTRATTcTPSPFDMKLMLQSTDSLpLNFGFTGKGNTAKPLELRHIVEAGAMG 486
Cdd:cd01315 69 WEgfetgtkaAAAGGITTII---DMPLNSIPPTT-TVENLEAKLEAAQGKLH-VDVGFWGGLVPGNLDQLRPLDEAGVVG 143
|
..
gi 15220459 487 LK 488
Cdd:cd01315 144 FK 145
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
337-424 |
7.99e-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: 55.69 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 337 TVITNSVIIDYSGIYKADIGIKNGHIVGIGkagnpdtmhgvqNNMLIGNKTEVIAGEGMIVTAGAIDCHVHFicpqlvyE 416
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIG------------PNLEAPGGVEVIDATGKYVLPGGIDPHTHL-------E 61
|
....*...
gi 15220459 417 AVSSGITT 424
Cdd:cd01314 62 LPFMGTVT 69
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
336-408 |
1.03e-07 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 55.47 E-value: 1.03e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220459 336 DTVITNSVIIDYSGIYKADIGIKNGHIVGIGKAgnpdtmhgvqnnmlIGNKTEVIAGEGMIVTAGAIDCHVHF 408
Cdd:PRK13404 5 DLVIRGGTVVTATDTFQADIGIRGGRIAALGEG--------------LGPGAREIDATGRLVLPGGVDSHCHI 63
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
335-408 |
2.98e-07 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 53.64 E-value: 2.98e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220459 335 LDTVITNSVIIDYSGIYKADIGIKNGHIVGIGKAGNpdtmhgvqnnmlignkTEVIAGEGMIVTAGAIDCHVHF 408
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGANLG----------------DEVIDATGKYVMPGGIDPHTHM 58
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
336-488 |
4.12e-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: 53.16 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 336 DTVITNSVIIDYSGIYKADIGIKNGHIVGIGkagnPDTmhgvqnnmlIGNKTEVIAGEGMIVTAGAIDCHVHFICP-QLV 414
Cdd:TIGR03178 1 DLIIRGGRVILPNGEREADVGVKGGKIAAIG----PDI---------LGPAAKIIDAGGLVVFPGVVDTHVHINEPgRTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 415 YEAVSSGITTMVGGGTG-----PAYGTRATTcTPSPFDMKLMLQStDSLPLNFGFTGkGNTAKPL-ELRHIVEAGAMGLK 488
Cdd:TIGR03178 68 WEGFETGTRAAAAGGITtyidmPLNSIPATT-TRASLEAKFEAAK-GKLAVDVGFWG-GLVPYNLdDLRELDEAGVVGFK 144
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
352-444 |
1.95e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.00 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 352 KADIGIKNGHIVGIGKAGNPdtmhgvqnnmliGNKTEVIAGEGMIVTAGAIDCHVH--------FICPQLVyeAVSSGIT 423
Cdd:PRK09237 18 VIDIAIEDGKIAAVAGDIDG------------SQAKKVIDLSGLYVSPGWIDLHVHvypgstpyGDEPDEV--GVRSGVT 83
|
90 100
....*....|....*....|....
gi 15220459 424 TMV-GGGTGPAY--GTRATTCTPS 444
Cdd:PRK09237 84 TVVdAGSAGADNfdDFRKLTIEAS 107
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
333-546 |
4.18e-06 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 49.76 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 333 LSLDTVITNSVIID-YSGIY-KADIGIKNGHIVGIGKAGNpdtmhgvqnnmliGNKTEVIAGEGMIVTAGAIDCHVHF-- 408
Cdd:PRK12394 1 MKNDILITNGHIIDpARNINeINNLRIINDIIVDADKYPV-------------ASETRIIHADGCIVTPGLIDYHAHVfy 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 409 ------ICPQLVYEAvsSGITTMVGGGTG-----PAYgtRATTCTPSPFDMKLML------QSTDSLPLNFG-------- 463
Cdd:PRK12394 68 dgteggVRPDMYMPP--NGVTTVVDAGSAgtanfDAF--YRTVICASKVRIKAFLtvsppgQTWSGYQENYDpdnidenk 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 464 ----FTGKGNTAKPLELRHIVE-AGAMGLKlhedwgttpaAIDNCLAVAEEYDIQVNIH-TDTLNEsgfVEHTINAFRGR 537
Cdd:PRK12394 144 ihalFRQYRNVLQGLKLRVQTEdIAEYGLK----------PLTETLRIANDLRCPVAVHsTHPVLP---MKELVSLLRRG 210
|
250
....*....|.
gi 15220459 538 TI--HTYHSEG 546
Cdd:PRK12394 211 DIiaHAFHGKG 221
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
337-408 |
1.06e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 48.65 E-value: 1.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220459 337 TVITNSVIIDYSGI-YKADIGIKNGHIVGIGKAGNPDTmhgvqnnmlignkTEVIAGEGMIVTAGAIDCHVHF 408
Cdd:PRK09357 3 ILIKNGRVIDPKGLdEVADVLIDDGKIAAIGENIEAEG-------------AEVIDATGLVVAPGLVDLHVHL 62
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
337-427 |
1.17e-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: 48.54 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 337 TVITNSVIIDYSGIYKADIGIKNGHIVGIGKAGNPDTMHGVqnnmlignktEVIAGEGMIVTAGAIDCHVHFI------- 409
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENV----------TVVDLHGKILVPGFIDQHVHIIggggegg 71
|
90 100
....*....|....*....|...
gi 15220459 410 ----CPQL-VYEAVSSGITTMVG 427
Cdd:cd01308 72 pstrTPEVtLSDLTTAGVTTVVG 94
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
332-424 |
1.51e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 48.38 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 332 ALSLDTVITNSVIIDYSGIYKADIGIKNGHIVGIGKAGNPDTmhgvqnnmlignkTEVIAGEGMIVTAGAIDCHVHFICP 411
Cdd:PRK09060 2 TQTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASA-------------GEVIDCRGLHVLPGVIDSQVHFREP 68
|
90 100
....*....|....*....|..
gi 15220459 412 QLVYE---------AVSSGITT 424
Cdd:PRK09060 69 GLEHKedletgsraAVLGGVTA 90
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
333-426 |
8.04e-05 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 46.00 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 333 LSLDTVITNSVIIDYSGIYKADIGIKNGHIVGIGKAgnpdtmhgvqnnmlIGNKTEVIAGEGMIVTAGAIDCHVHFICPQ 412
Cdd:PRK08044 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQD--------------LGDAKEVMDASGLVVSPGMVDAHTHISEPG 66
|
90 100
....*....|....*....|...
gi 15220459 413 LVY---------EAVSSGITTMV 426
Cdd:PRK08044 67 RSHwegyetgtrAAAKGGITTMI 89
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
336-517 |
9.58e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 45.80 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 336 DTVITNSVIIDYSGIYKADIGIKNGHIVGIGKAGNPDTMHgvqnnmlignktEVIAGEGMIVTAGAIDCHVHFICPQLVY 415
Cdd:PRK02382 3 DALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSE------------EVIDARGMLLLPGGIDVHVHFREPGYTH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 416 E---------AVSSGITTMVGG-GTGPaygtraTTCTPSPFDMKLMLQSTDSLpLNFGFTGkGNTAKPLELRHIVEAGAM 485
Cdd:PRK02382 71 KetwytgsrsAAAGGVTTVVDQpNTDP------PTVDGESFDEKAELAARKSI-VDFGING-GVTGNWDPLESLWERGVF 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 15220459 486 GL------KLHEDWGTTPAAIDNCLAVAEEYDIQVNIH 517
Cdd:PRK02382 143 ALgeifmaDSTGGMGIDEELFEEALAEAARLGVLATVH 180
|
|
| PLN02795 |
PLN02795 |
allantoinase |
337-517 |
2.58e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 44.38 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 337 TVITNSVIIDYSGIYKADIGIKNGHIVGIGKAgnpDTMHGVQNnmlignKTEVIAGEGMIVTAGAIDCHVHFICPQLV-Y 415
Cdd:PLN02795 46 FVLYSKRVVTPAGVIPGAVEVEGGRIVSVTKE---EEAPKSQK------KPHVLDYGNAVVMPGLIDVHVHLNEPGRTeW 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 416 E--------AVSSGITTMVGggtgPAYGTRATTCTPSPFDMKLMLqSTDSLPLNFGFTGK---GNTAKPLELRHIVEAGA 484
Cdd:PLN02795 117 EgfptgtkaAAAGGITTLVD----MPLNSFPSTTSVETLELKIEA-AKGKLYVDVGFWGGlvpENAHNASVLEELLDAGA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15220459 485 MGLK--LH----EDWG-TTPAAIDNCLAVAEEYDIQVNIH 517
Cdd:PLN02795 192 LGLKsfMCpsgiNDFPmTTATHIKAALPVLAKYGRPLLVH 231
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
337-407 |
3.58e-04 |
|
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: 43.72 E-value: 3.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220459 337 TVITNSVIIDYSGIYKADIGIKNGHIVGIGKAGNPDTMHgvqnnmlignktEVIAGEGMIVTAGAIDCHVH 407
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEAD------------EIIDLKGQYLVPGFIDIHIH 59
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
337-427 |
3.61e-04 |
|
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 131030 Cd Length: 389 Bit Score: 43.62 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 337 TVITNSVIIDYSGIYKADIGIKNGHIVGIGKAGNPDTMhgvqnnmlIGNKTEVIAGEGMIVTAGAIDCHVHFI------- 409
Cdd:TIGR01975 2 TLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPSTKD--------FVPNCVVVGLEGMIAVPGFIDQHVHIIggggegg 73
|
90 100
....*....|....*....|...
gi 15220459 410 ----CPQL-VYEAVSSGITTMVG 427
Cdd:TIGR01975 74 pttrTPELtLSDITKGGVTTVVG 96
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
336-547 |
3.83e-04 |
|
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: 43.66 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 336 DTVITNSVIIDYSG----IYKADIGIKNGHIVGIGKAGNPDTMHGVqnnmlignkTEVIAGEGMIVTAGAIDCHVHF--- 408
Cdd:COG0402 1 DLLIRGAWVLTMDPaggvLEDGAVLVEDGRIAAVGPGAELPARYPA---------AEVIDAGGKLVLPGLVNTHTHLpqt 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 409 -------------------------ICPQLVYEAVSSGITTMVGGGTgpaygtraTT----CTPSPFDMKLMLQSTDSLP 459
Cdd:COG0402 72 llrgladdlplldwleeyiwplearLDPEDVYAGALLALAEMLRSGT--------TTvadfYYVHPESADALAEAAAEAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 460 LNfGFTGKG--NTAKPLELRHIVEAG-AMGLKLHEDWG------------------TTPAAIDNCLAVAEEYDIQVNIHt 518
Cdd:COG0402 144 IR-AVLGRGlmDRGFPDGLREDADEGlADSERLIERWHgaadgrirvalaphapytVSPELLRAAAALARELGLPLHTH- 221
|
250 260 270
....*....|....*....|....*....|
gi 15220459 519 dtLNES-GFVEHTINAFRGRTIHTYHSEGA 547
Cdd:COG0402 222 --LAETrDEVEWVLELYGKRPVEYLDELGL 249
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
678-727 |
5.75e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 43.25 E-value: 5.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220459 678 YTINPAIANGFADLIGSVEVKKLADLVIWQPAFFGAKPEMI--------IKGGNIAWA 727
Cdd:COG1574 476 YTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIkdikvlltVVGGRVVYE 533
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
333-464 |
6.06e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 43.12 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 333 LSLDTVITNSVIIDYSG-IYKADIGIKNGHIVGIGKAGNPDTMhgvqnnmlignkTEVIAGEGMIVTAGAIDCHVHFICP 411
Cdd:PRK07575 1 MMMSLLIRNARILLPSGeLLLGDVLVEDGKIVAIAPEISATAV------------DTVIDAEGLTLLPGVIDPQVHFREP 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15220459 412 QLVY-EAVSSGITTMVGGGTG-----PayGTRATTCTPSPFDMKLMLQSTDSLpLNFGF 464
Cdd:PRK07575 69 GLEHkEDLFTASRACAKGGVTsflemP--NTKPLTTTQAALDDKLARAAEKCV-VNYGF 124
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
354-431 |
1.39e-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: 41.93 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 354 DIGIKNGHIVGIGKAGNPDTmhgvqnnmlignKTEVIAGEGMIVTAGAIDCHVHficpqlVYE------------AVSSG 421
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPA------------ATQIVDAGGCYVSPGWIDLHVH------VYQggtrygdrpdmiGVKSG 62
|
90
....*....|.
gi 15220459 422 ITTMV-GGGTG 431
Cdd:cd01307 63 VTTVVdAGSAG 73
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
336-409 |
2.19e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 41.32 E-value: 2.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220459 336 DTVITNSVII--DYSGIYKADIGIKNGHIVGIGKAgnpdtmHGVQNnmLIGNKTEVIAGEGMIVTAGAIDCHVHFI 409
Cdd:COG1574 9 DLLLTNGRIYtmDPAQPVAEAVAVRDGRIVAVGSD------AEVRA--LAGPATEVIDLGGKTVLPGFIDAHVHLL 76
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
675-724 |
2.44e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 41.36 E-value: 2.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15220459 675 IAKYTINPAIANGFADLIGSVEVKKLADLVIW--------QPAFFGAKPEMIIKGGNI 724
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLdddpltvdPPAIADIRVRLTVVDGRV 462
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
679-722 |
3.69e-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: 3.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15220459 679 TINPAIANGFADLIGSVEVKKLADLVIWQ-------PAFFGAKP-EMIIKGG 722
Cdd:cd01296 320 TINAAAALGLGETVGSLEVGKQADLVILDapsyehlAYRFGVNLvEYVIKNG 371
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
337-408 |
5.93e-03 |
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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: 39.88 E-value: 5.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220459 337 TVITNSVII---DYSGIYKADIGIKNGHIVGIGKAGNPDTMHGVqnnmlignktEVIAGEGMIVTAGAIDCHVHF 408
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPALPLPAYPAD----------EVIDAKGKVVMPGLVNTHTHL 65
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| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
355-409 |
9.18e-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: 39.16 E-value: 9.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15220459 355 IGIKNGHIVGIGKAgnpdtmHGVQNNMliGNKTEVIAGEGMIVTAGAIDCHVHFI 409
Cdd:cd01296 1 IAIRDGRIAAVGPA------ASLPAPG--PAAAEEIDAGGRAVTPGLVDCHTHLV 47
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| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
337-424 |
9.84e-03 |
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dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 39.47 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220459 337 TVITNSVIIDYSGIYKADIGIKNGHIVGIgkAGNPDTMHGvqnnmlignkTEVIAGEGMIVTAGAIDCHVHFICPQLVYE 416
Cdd:PRK09236 4 ILIKNARIVNEGKIFEGDVLIENGRIAKI--ASSISAKSA----------DTVIDAAGRYLLPGMIDDQVHFREPGLTHK 71
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90
....*....|....*..
gi 15220459 417 ---------AVSSGITT 424
Cdd:PRK09236 72 gdiasesraAVAGGITS 88
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