|
Name |
Accession |
Description |
Interval |
E-value |
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
2-571 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 1130.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 2 SFKMTQSQYTSLYGPTVGDSVRLGDTNLFARVERDYATYGDEAAFGGGKSIRDGMAQNPNVTRDDkqVADLVITNAMIID 81
Cdd:PRK13207 1 MAKISRRAYAEMYGPTTGDRVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQRARADG--AVDTVITNALILD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 82 YDKIVKADIGVKNGYIMKIGKAGNPDIMDNVDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQSQVALESGITTHIGG 161
Cdd:PRK13207 79 HWGIVKADIGIKDGRIVAIGKAGNPDIQDGVDIIIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQIEEALASGVTTMIGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 162 GTGASEGTKATTVTPGPWHLHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGATPSALDHALQVAD 241
Cdd:PRK13207 159 GTGPATGTNATTCTPGPWHIHRMLQAADAFPMNIGFLGKGNASLPEALEEQIEAGAIGLKLHEDWGATPAAIDNCLSVAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 242 DYDVQIALHADTLNEAGFMEETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTNPTLPYTVNTIDEHLDMVM 321
Cdd:PRK13207 239 EYDVQVAIHTDTLNESGFVEDTIAAFKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 322 ITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGLLDGDSEYNDN 401
Cdd:PRK13207 319 VCHHLDPSIPEDVAFAESRIRRETIAAEDILHDLGAISMISSDSQAMGRVGEVIIRTWQTAHKMKVQRGPLPGDSGRNDN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 402 NRIKRYIAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIVKGGLINAAINGDANGSIPTSEPLKYRKMY 481
Cdd:PRK13207 399 FRVKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWKPAFFGVKPELVLKGGMIAWAPMGDPNASIPTPQPVHYRPMF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 482 GQLGGNLQSTSMTFVSTTAYENDIGKLLGLKRKLRPVHNIRKLSKKDMKNNNATPDLDVDPQTYEVFVDGEKITSEPATE 561
Cdd:PRK13207 479 GAYGGALAATSVTFVSQAALDAGIPEKLGLKKRLVPVKNTRGITKADMKLNDATPKIEVDPETYEVRADGELLTCEPATV 558
|
570
....*....|
gi 1478526384 562 LPLTQRYFLF 571
Cdd:PRK13207 559 LPLAQRYFLF 568
|
|
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
2-571 |
0e+00 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 1114.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 2 SFKMTQSQYTSLYGPTVGDSVRLGDTNLFARVERDYATYGDEAAFGGGKSIRDGMAQNPNvTRDDkQVADLVITNAMIID 81
Cdd:COG0804 1 MAKISRKAYADLYGPTTGDRVRLADTDLFIEVEKDLTTYGDEVKFGGGKVIRDGMGQSQT-TRAE-GALDLVITNAVILD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 82 YDKIVKADIGVKNGYIMKIGKAGNPDIMDNVD--IIIGATTDIISAEGKIVTAGGIDTHVHFINPEQSQVALESGITTHI 159
Cdd:COG0804 79 HWGIVKADIGIKDGRIVGIGKAGNPDTMDGVDpdLVIGPGTEVIAGEGLILTAGGIDTHIHFICPQQIEEALASGITTMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 160 GGGTGASEGTKATTVTPGPWHLHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGATPSALDHALQV 239
Cdd:COG0804 159 GGGTGPAEGTNATTCTPGPWNIARMLEAADALPMNIGFLGKGNASSPEALEEQIRAGACGLKLHEDWGATPAAIDACLSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 240 ADDYDVQIALHADTLNEAGFMEETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTNPTLPYTVNTIDEHLDM 319
Cdd:COG0804 239 ADEYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 320 VMITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGLLDGDSEYN 399
Cdd:COG0804 319 LMVCHHLDPSIPEDVAFAESRIRPETIAAEDVLHDLGAISMMSSDSQAMGRVGEVITRTWQTAHKMKKQRGPLPGDSGRN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 400 DNNRIKRYIAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIVKGGLINAAINGDANGSIPTSEPLKYRK 479
Cdd:COG0804 399 DNFRVKRYVAKYTINPAIAHGISHEVGSVEVGKLADLVLWDPAFFGVKPELVIKGGMIAWAQMGDPNASIPTPQPVHYRP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 480 MYGQLGGNLQSTSMTFVSTTAYENDIGKLLGLKRKLRPVHNIRKLSKKDMKNNNATPDLDVDPQTYEVFVDGEKITSEPA 559
Cdd:COG0804 479 MFGAYGKALAATSVTFVSQAALEAGIAERLGLRKRLLPVKNTRNIGKADMVLNDATPDIEVDPETYEVRVDGELLTCEPA 558
|
570
....*....|..
gi 1478526384 560 TELPLTQRYFLF 571
Cdd:COG0804 559 TELPLAQRYFLF 570
|
|
| urease_alph |
TIGR01792 |
urease, alpha subunit; This model describes the urease alpha subunit UreC (designated beta or ... |
4-571 |
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: 1068.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 4 KMTQSQYTSLYGPTVGDSVRLGDTNLFARVERDYATYGDEAAFGGGKSIRDGMAQNPNVTRDdKQVADLVITNAMIIDYD 83
Cdd:TIGR01792 1 KMSREQYASLYGPTTGDKVRLGDTDLFVEVEKDLTTYGDESKFGGGKVLRDGMGQNATLTRN-AGVLDLVITNALILDWT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 84 KIVKADIGVKNGYIMKIGKAGNPDIMDNVDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQSQVALESGITTHIGGGT 163
Cdd:TIGR01792 80 GIYKADIGIKNGRIVGIGKAGNPDTMDGVDMIVGASTEAISGEGKIVTAGGIDTHVHYISPQQVQAALDNGITTLIGGGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 164 GASEGTKATTVTPGPWHLHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGATPSALDHALQVADDY 243
Cdd:TIGR01792 160 GPADGTNATTCTPGPWYLHRMLQAADGLPINFGFTGKGSGSGPAALIEQIEAGACGLKVHEDWGATPAAIDNALSVADEY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 244 DVQIALHADTLNEAGFMEETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTNPTLPYTVNTIDEHLDMVMIT 323
Cdd:TIGR01792 240 DVQVAVHTDTLNESGFVEDTIAAFKGRTIHTYHTEGAGGGHAPDIIVVVGYNNILPSSTNPTLPYTVNTIDEHLDMLMVC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 324 HHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGLLDGDSEYNDNNR 403
Cdd:TIGR01792 320 HHLNPKIPEDVAFAESRIRKETIAAEDVLQDMGAISMISSDSQAMGRIGEVVTRCWQTADKMKKQRGPLPGDSPGNDNNR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 404 IKRYIAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIVKGGLINAAINGDANGSIPTSEPLKYRKMYGQ 483
Cdd:TIGR01792 400 VKRYVAKYTINPAITHGISDYIGSIEVGKLADLVLWEPAFFGVKPDMVLKGGLIAWAIMGDPNASIPTPQPVLYRPMFGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 484 LGGNLQSTSMTFVSTTAYENDIGKLLGLKRKLRPVHNIRKLSKKDMKNNNATPDLDVDPQTYEVFVDGEKITSEPATELP 563
Cdd:TIGR01792 480 YGRALQSTSITFVSQAAYDKGIKERLGLQKLLLPVHNTRSIGKADMKLNSATPKIEVDPQTYDVKVDGVLITVEPADELP 559
|
....*...
gi 1478526384 564 LTQRYFLF 571
Cdd:TIGR01792 560 LTQRYFLF 567
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-570 |
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: 996.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 4 KMTQSQYTSLYGPTVGDSVRLGDTNLFARVERDYATYGDEAAFGGGKSIRDGMAQNPNVTRDDkqVADLVITNAMIIDYD 83
Cdd:cd00375 1 KISREAYADMYGPTTGDKVRLGDTDLWIEVEKDYTTYGDEVKFGGGKVLRDGMGQSSGYTRED--VLDLVITNALIIDYT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 84 KIVKADIGVKNGYIMKIGKAGNPDIMDNVD--IIIGATTDIISAEGKIVTAGGIDTHVHFINPEQSQVALESGITTHIGG 161
Cdd:cd00375 79 GIYKADIGIKDGRIVAIGKAGNPDIMDGVTpnMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIEEALASGITTMIGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 162 GTGASEGTKATTVTPGPWHLHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGATPSALDHALQVAD 241
Cdd:cd00375 159 GTGPAAGTKATTCTPGPWNIKRMLQAADGLPVNIGFLGKGNGSSPDALAEQIEAGACGLKLHEDWGATPAAIDTCLSVAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 242 DYDVQIALHADTLNEAGFMEETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTNPTLPYTVNTIDEHLDMVM 321
Cdd:cd00375 239 EYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTYHTEGAGGGHAPDIIKVAGHPNVLPSSTNPTRPFTVNTLDEHLDMLM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 322 ITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGLLDGDSEYNDN 401
Cdd:cd00375 319 VCHHLDPNIPEDVAFAESRIRAETIAAEDVLHDLGAISIMSSDSQAMGRVGEVILRTWQTAHKMKAQRGPLPEDSGDADN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 402 NRIKRYIAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIVKGGLINAAINGDANGSIPTSEPLKYRKMY 481
Cdd:cd00375 399 FRVKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGVKPEMVLKGGFIAYAQMGDPNASIPTPQPVMMRPMF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 482 GQLGGNLQSTSMTFVSTTAYENDIGKLLGLKRKLRPVHNIRKLSKKDMKNNNATPDLDVDPQTYEVFVDGEKITSEPATE 561
Cdd:cd00375 479 GAHGKAPAATSVTFVSQASLDAGIAEELGLRRRVVAVKNCRGVGKKDMKLNSATPDIEVDPETYEVRVDGELLTCEPADE 558
|
....*....
gi 1478526384 562 LPLTQRYFL 570
Cdd:cd00375 559 LPLAQRYFL 567
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
4-571 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 863.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 4 KMTQSQYTSLYGPTVGDSVRLGDTNLFARVERDY----ATYGDEAAFGGGKSIRDGMAQNpNVTRDDKqVADLVITNAMI 79
Cdd:PRK13206 3 RLSRERYAALYGPTTGDRIRLADTDLLIEVTEDRsggpGLAGDEAVFGGGKVIRESMGQG-RATRAEG-APDTVITGAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 80 IDYDKIVKADIGVKNGYIMKIGKAGNPDIMDNV--DIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQSQVALESGITT 157
Cdd:PRK13206 81 LDHWGIVKADVGIRDGRIVAIGKAGNPDIMDGVhpDLVIGPSTEIIAGNGRILTAGAIDCHVHFICPQIVDEALAAGITT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 158 HIGGGTGASEGTKATTVTPGPWHLHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGATPSALDHAL 237
Cdd:PRK13206 161 LIGGGTGPAEGSKATTVTPGAWHLARMLEALDGWPVNVALLGKGNTVSAEALWEQLRGGAGGFKLHEDWGSTPAAIDACL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 238 QVADDYDVQIALHADTLNEAGFMEETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTNPTLPYTVNTIDEHL 317
Cdd:PRK13206 241 RVADAAGVQVALHSDTLNEAGFVEDTLAAIAGRSIHAYHTEGAGGGHAPDIITVASHPNVLPSSTNPTRPHTVNTLDEHL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 318 DMVMITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGLLDGDSE 397
Cdd:PRK13206 321 DMLMVCHHLNPAVPEDLAFAESRIRPSTIAAEDVLHDMGAISMIGSDSQAMGRIGEVVLRTWQTAHVMKRRRGALPGDGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 398 yNDNNRIKRYIAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIVKGGLINAAINGDANGSIPTSEPLKY 477
Cdd:PRK13206 401 -ADNNRARRYVAKYTICPAVAHGIDHEIGSVEVGKLADLVLWEPAFFGVRPHAVLKGGAIAWAAMGDANASIPTPQPVLP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 478 RKMYGQLGGNLQSTSMTFVSTTAYENDIGKLLGLKRKLRPVHNIRKLSKKDMKNNNATPDLDVDPQTYEVFVDGEKITSE 557
Cdd:PRK13206 480 RPMFGAAPAAAAATSVHFVAPQAIEDGLADRLGLRRRLVPVADTRAVGKADMPLNDALPDIEVDPDTFTVRIDGEVWEPQ 559
|
570
....*....|....
gi 1478526384 558 PATELPLTQRYFLF 571
Cdd:PRK13206 560 PAAELPMAQRYFLF 573
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
4-570 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 851.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 4 KMTQSQYTSLYGPTVGDSVRLGDTNLFARVERDYATYGDEAAFGGGKSIRDGMAQNPNVTRDDKqVADLVITNAMIID-Y 82
Cdd:PRK13308 3 TIDRRAYAELYGPTTGDRVRLADTSLLAEVEHDHTVYGDECLFGGGKTLRDGMGMAPGVTSADG-ALDFVLCNVTVIDpV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 83 DKIVKADIGVKNGYIMKIGKAGNPDIMDNVD--IIIGATTDIISAEGKIVTAGGIDTHVHFINPEQSQVALESGITTHIG 160
Cdd:PRK13308 82 LGIVKGDIGIRDGRIVGIGKAGNPDIMDGVDprLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQLVDHALASGITTMLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 161 GGTGASegtkATTVTPGPWHLHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGATPSALDHALQVA 240
Cdd:PRK13308 162 GGLGPT----VGIDSGGPFNTGRMLQAAEAWPVNFGFLGRGNSSKPAALIEQVEAGACGLKIHEDWGAMPAAIDTCLEVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 241 DDYDVQIALHADTLNEAGFMEETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTNPTLPYTVNTIDEHLDMV 320
Cdd:PRK13308 238 DEYDFQVQLHTDTLNESGFVEDTLAAIGGRTIHMYHTEGAGGGHAPDIIRVVGEPHCLPSSTNPTNPYTVNTFDEHLDMT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 321 MITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGLLDGDS-EYN 399
Cdd:PRK13308 318 MVCHHLNPDVPEDVAFAESRIRAQTIAAEDVLHDIGAISMLGSDSQGMGRIAEVIARTWQLASKMKDQRGPLPEDRgTFA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 400 DNNRIKRYIAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIVKGGLINAAINGDANGSIPTSEPLKYRK 479
Cdd:PRK13308 398 DNARIKRYIAKYTINPAITFGIDDHIGSLEPGKLADIVLWRPAFFGIKPELVIKGGFPAWAAMGDANGSLMTCEPMLQRP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 480 MYGQLGGNLQSTSMTFVSTTAYENDIGKLLGLKRKLRPVHNIRKLSKKDMKNNNATPDLDVDPQTYEVFVDGEKITSEPA 559
Cdd:PRK13308 478 QWGAFGRAKQALSVCFVSPLAIEAGLGERLGLRKRLLPVRGTRTLTKADMLHNDACPDIRVDPQTFEVFVDGELVTCEPA 557
|
570
....*....|.
gi 1478526384 560 TELPLTQRYFL 570
Cdd:PRK13308 558 TELPLAQRYML 568
|
|
| PLN02303 |
PLN02303 |
urease |
2-571 |
0e+00 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 847.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 2 SFKMTQSQYTSLYGPTVGDSVRLGDTNLFARVERDYATYGDEAAFGGGKSIRDGMAQNPNVTRDDkqVADLVITNAMIID 81
Cdd:PLN02303 268 TTTISREKYANMYGPTTGDKIRLGDTNLYAEIEKDFTVYGDECKFGGGKVLRDGMGQATGYGAAD--SLDTVITNAVIID 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 82 YDKIVKADIGVKNGYIMKIGKAGNPDIMDNV--DIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQSQVALESGITTHI 159
Cdd:PLN02303 346 YTGIYKADIGIKDGLIVGIGKAGNPDVMDGVtsNMIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQLATEAIASGITTLV 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 160 GGGTGASEGTKATTVTPGPWHLHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGATPSALDHALQV 239
Cdd:PLN02303 426 GGGTGPAHGTCATTCTPAPSHMKLMLQSTDDLPLNFGFTGKGNTAKPEGLHEIIKAGAMGLKLHEDWGTTPAAIDNCLDV 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 240 ADDYDVQIALHADTLNEAGFMEETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTNPTLPYTVNTIDEHLDM 319
Cdd:PLN02303 506 AEEYDIQVTIHTDTLNESGCVEHSIAAFKGRTIHTYHSEGAGGGHAPDIIKVCGVKNVLPSSTNPTRPYTKNTIDEHLDM 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 320 VMITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGLLDGDSEYN 399
Cdd:PLN02303 586 LMVCHHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVITRTWQTAHKMKSQRGALEPRGADN 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 400 DNNRIKRYIAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIVKGGLINAAINGDANGSIPTSEPLKYRK 479
Cdd:PLN02303 666 DNFRIKRYIAKYTINPAIAHGMSHFVGSVEVGKLADLVLWKPAFFGAKPEMVIKGGQIAWAQMGDPNASIPTPEPVIMRP 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 480 MYGQLGGNLQSTSMTFVSTTAYENDIGKLLGLKRKLRPVHNIRKLSKKDMKNNNATPDLDVDPQTYEVFVDGEKITSEPA 559
Cdd:PLN02303 746 MFGAFGKAGSSNSIAFVSKAALDAGVKQLYGLTKRVEAVGNVRGLTKLDMKLNDALPVITVDPETYEVTADGEVLTCAPA 825
|
570
....*....|..
gi 1478526384 560 TELPLTQRYFLF 571
Cdd:PLN02303 826 TSVPLSRNYFLF 837
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
4-571 |
0e+00 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 799.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 4 KMTQSQYTSLYGPTVGDSVRLGDTNLFARVERDYATYGDEAAFGGGKSIRDGMAQNPNvtrDDKQVADLVITNAMIIDYD 83
Cdd:PRK13985 2 KISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYTIYGEELKFGGGKTLREGMSQSNN---PSKEELDLIITNALIIDYT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 84 KIVKADIGVKNGYIMKIGKAGNPDIMDNV--DIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQSQVALESGITTHIGG 161
Cdd:PRK13985 79 GIYKADIGIKDGKIAGIGKGGNKDMQDGVknNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTAFASGVTTMIGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 162 GTGASEGTKATTVTPGPWHLHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGATPSALDHALQVAD 241
Cdd:PRK13985 159 GTGPADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLGKGNSSNDASLADQIEAGAIGFKIHEDWGTTPSAINHALDVAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 242 DYDVQIALHADTLNEAGFMEETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTNPTLPYTVNTIDEHLDMVM 321
Cdd:PRK13985 239 KYDVQVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGGHAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDMLM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 322 ITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGLLDGDSEYNDN 401
Cdd:PRK13985 319 VCHHLDKSIKEDVQFADSRIRPQTIAAEDTLHDMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKGDNDN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 402 NRIKRYIAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIVKGGLINAAINGDANGSIPTSEPLKYRKMY 481
Cdd:PRK13985 399 FRIKRYLSKYTINPAIAHGISEYVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVYYREMF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 482 GQLGGNLQSTSMTFVSTTAYENDIGKLLGLKRKLRPVHNIRKLSKKDMKNNNATPDLDVDPQTYEVFVDGEKITSEPATE 561
Cdd:PRK13985 479 AHHGKAKYDANITFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTSKPANK 558
|
570
....*....|
gi 1478526384 562 LPLTQRYFLF 571
Cdd:PRK13985 559 VSLAQLFSIF 568
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
5-570 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 732.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 5 MTQSQYTSLYGPTVGDSVRLGDTNLFARVERDYATYGDEAAFGGGKSIRDGMAQNPNVTRDDKqVADLVITNAMIIDYDK 84
Cdd:PRK13309 4 ISRQEYAGLFGPTTGDKIRLGDTNLFIEIEKDLRGYGDESVYGGGKSLRDGMGANNNLTRDNG-VLDLVITNVTIVDARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 85 -IVKADIGVKNGYIMKIGKAGNPDIMDNVD--IIIGATTDIISAEGKIVTAGGIDTHVHFINPEQSQVALESGITTHIGG 161
Cdd:PRK13309 83 gVIKADVGIRDGKIVGIGKSGNPSTMDGVTqgMVVGVSTDAISGEHLILTAAGIDTHIHLISPQQAYHALSNGVTTFFGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 162 GTGASEGTKATTVTPGPWHLHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGATPSALDHALQVAD 241
Cdd:PRK13309 163 GIGPTDGTNGTTVTPGPWNIRQMLRSIEGLPVNVGILGKGNSYGRGPLLEQAIAGVAGYKVHEDWGATAAALRHALRVAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 242 DYDVQIALHADTLNEAGFMEETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTNPTLPYTVNTIDEHLDMVM 321
Cdd:PRK13309 243 EVDIQVAVHTDSLNECGYVEDTIDAFEGRTIHTFHTEGAGGGHAPDIIKVASQTNVLPSSTNPTLPYGVNSQAELFDMIM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 322 ITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGLLDGDSEYNDN 401
Cdd:PRK13309 323 VCHNLNPNVPADVAFAESRVRPETIAAENVLHDMGVISMFSSDSQAMGRVGENWLRAIQTADAMKAARGKLPEDAAGNDN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 402 NRIKRYIAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIVKGGLINAAINGDANGSIPTSEPLKYRKMY 481
Cdd:PRK13309 403 FRVLRYVAKITINPAITQGVSHVIGSVEVGKMADLVLWEPRFFGAKPKMVIKGGMINWAAMGDPNASLPTPQPVFYRPMF 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 482 GQLGGNLQSTSMTFVSTTAYENDIGKLLGLKRKLRPVHNIRKLSKKDMKNNNATPDLDVDPQTYEVFVDGEKITSEPATE 561
Cdd:PRK13309 483 GAMGKTLQDTCVTFVSQAALDDGVKEKAGLDRQVIAVKNCRTISKRDLVRNSQTPNIEVDPETFAVKVDGVHATVKPIAT 562
|
....*....
gi 1478526384 562 LPLTQRYFL 570
Cdd:PRK13309 563 ASLNQRYFF 571
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
129-458 |
2.05e-70 |
|
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: 229.70 E-value: 2.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 129 IVTAGGIDTHVHF---------INPEQSQVALESGITTHIGGGTGASEGTKATTVTpgpwHLHRMLLAAESLPLNIGFTG 199
Cdd:pfam01979 1 IVLPGLIDAHVHLemgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTST----GIEALLEAAEELPLGLRFLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 200 K-------GQAVNHTALVEQIHAGA------------IGLKVHEDWGATPSALDHALQVADDYDVQIALHAdtLNEAGFM 260
Cdd:pfam01979 77 PgcsldtdGELEGRKALREKLKAGAefikgmadgvvfVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHA--LETKGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 261 EETMAAVKDRVLHMYHTEGAGGGHAPDLIKSAAYANILPSSTnptlpyTVNTIDEHLDMVMITHhlnasipedIAFADSR 340
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPT------EANLLAEHLKGAGVAH---------CPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 341 IRKETIAAEDVLQDmGVFSMVSSDSQAMGRVGEVITRTwqvAHRMKEQrglldgdSEYNDNNRIKRYIAKYTINPAITHG 420
Cdd:pfam01979 220 LRSGRIALRKALED-GVKVGLGTDGAGSGNSLNMLEEL---RLALELQ-------FDPEGGLSPLEALRMATINPAKALG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1478526384 421 ISDYVGSIDEGKLADIILWE----PAFFGVKPDVIVKGGLIN 458
Cdd:pfam01979 289 LDDKVGSIEVGKDADLVVVDldplAAFFGLKPDGNVKKVIVK 330
|
|
| Urease_alpha |
pfam00449 |
Urease alpha-subunit, N-terminal domain; The N-terminal domain is a composite domain and plays ... |
4-123 |
8.09e-64 |
|
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: 204.65 E-value: 8.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 4 KMTQSQYTSLYGPTVGDSVRLGDTNLFARVERDYATYGDEAAFGGGKSIRDGMAQNPNVTRDDkqVADLVITNAMIIDYD 83
Cdd:pfam00449 1 KISREAYADMYGPTTGDRIRLGDTDLFIEVEKDLTVYGDEVKFGGGKVIRDGMGQSQGRTRDD--ALDLVITNALILDYT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1478526384 84 KIVKADIGVKNGYIMKIGKAGNPDIMDNVD--IIIGATTDII 123
Cdd:pfam00449 79 GIVKADIGIKDGRIVGIGKAGNPDTMDGVTpgMVIGPSTEVI 120
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
63-440 |
2.63e-18 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 86.94 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 63 TRDDKQVADLVITNAMIIDYDK---IVKADIGVKNGYIMKIGKAGnpdimdnvDIIIGATTDIISAEGKIVTAGGIDTHV 139
Cdd:COG1228 1 KKAPAQAGTLLITNATLVDGTGggvIENGTVLVEDGKIAAVGPAA--------DLAVPAGAEVIDATGKTVLPGLIDAHT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 140 HF---------------INPEQSQV---------ALESGITT---HIGGGTGASEGTKATT--VTPGPwhlhRMLLAAES 190
Cdd:COG1228 73 HLglgggravefeagggITPTVDLVnpadkrlrrALAAGVTTvrdLPGGPLGLRDAIIAGEskLLPGP----RVLAAGPA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 191 LPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGA---TPSALDHALQVADDYDVQIALHADTLNEAgfmeetMAAV 267
Cdd:COG1228 149 LSLTGGAHARGPEEARAALRELLAEGADYIKVFAEGGApdfSLEELRAILEAAHALGLPVAAHAHQADDI------RLAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 268 KDRVLHMYHtegaGGGHAPDLIKSAAYANilPSSTNPTLPYTVNTIDEHldmvmithhlnasiPEDIAFADSRIRKETIA 347
Cdd:COG1228 223 EAGVDSIEH----GTYLDDEVADLLAEAG--TVVLVPTLSLFLALLEGA--------------AAPVAAKARKVREAALA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 348 AEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQ--VAHRMKEQRGLldgdseyndnnrikRYIakyTINPAITHGISDYV 425
Cdd:COG1228 283 NARRLHDAGVPVALGTDAGVGVPPGRSLHRELAlaVEAGLTPEEAL--------------RAA---TINAAKALGLDDDV 345
|
410
....*....|....*
gi 1478526384 426 GSIDEGKLADIILWE 440
Cdd:COG1228 346 GSLEPGKLADLVLLD 360
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
73-262 |
7.28e-16 |
|
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: 80.14 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 73 VITNAMIIDYDKIVKADIGVKNGYIMKIGKagnpdimdnvDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQ------ 146
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGP----------DLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLehkedi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 147 ---SQVALESGITTHIgggtgASEGTKATTVTPGPW-HLHRmlLAAESLPLNIGFTG---KGQAVNHTALVEQIHAGAIG 219
Cdd:COG0044 71 etgTRAAAAGGVTTVV-----DMPNTNPVTDTPEALeFKLA--RAEEKALVDVGPHGaltKGLGENLAELGALAEAGAVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1478526384 220 LKV-----HEDWGATPSALDHALQVADDYDVQIALHA--DTLNEAGFMEE 262
Cdd:COG0044 144 FKVfmgsdDGNPVLDDGLLRRALEYAAEFGALVAVHAedPDLIRGGVMNE 193
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
72-159 |
2.24e-11 |
|
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: 66.09 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 72 LVITNAMIIDYDKIVKADIGVKNGYIMKIGKagnpdimdnvDIIIGATTDIISAEGKIVTAGGIDTHVHFINP------- 144
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGP----------NLEAPGGVEVIDATGKYVLPGGIDPHTHLELPfmgtvta 70
|
90
....*....|....*....
gi 1478526384 145 ----EQSQVALESGITTHI 159
Cdd:cd01314 71 ddfeSGTRAAAAGGTTTII 89
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
67-198 |
1.44e-10 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 63.97 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 67 KQVADLVITNAMIIDY--DKIVKADIGVKNGYIMKIGKAgnpdimdnvdiiIGATTDIISAEGKIVTAGGIDTHVHF--- 141
Cdd:COG1001 2 REPADLVIKNGRLVNVftGEILEGDIAIAGGRIAGVGDY------------IGEATEVIDAAGRYLVPGFIDGHVHIess 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1478526384 142 -INPEQ-SQVALESGITT-----H-IGGGTGAsEGTKAttvtpgpwhlhrMLLAAESLPLNIGFT 198
Cdd:COG1001 70 mVTPAEfARAVLPHGTTTviadpHeIANVLGL-EGVRY------------MLEAAEGLPLDIFVM 121
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
71-251 |
1.73e-10 |
|
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: 63.08 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 71 DLVITNAMIIDYDKIVKADIGVKNGYIMKIGKagnpdimdnvDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQ---- 146
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIGP----------DIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRtewe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 147 -----SQVALESGITTHIGGGTGASEGTkaTTVTpgpwHLHRMLLAAE-SLPLNIGFTGKGQAVNHTALVEQIHAGAIGL 220
Cdd:cd01315 71 gfetgTKAAAAGGITTIIDMPLNSIPPT--TTVE----NLEAKLEAAQgKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGF 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 1478526384 221 K-------VHEDWGATPSALDHALQVADDYDVQIALHA 251
Cdd:cd01315 145 KcflcpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHA 182
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
72-241 |
2.63e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 59.09 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 72 LVITNAMIIDYDKIVKA--DIGVKNGYIMKIGKagnpdimdnvDIIIGATTDIISAEGKIVTAGGIDTHVH--------F 141
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAG----------DIDGSQAKKVIDLSGLYVSPGWIDLHVHvypgstpyG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 142 INPeqSQVALESGITTHI-GGGTGAS--EGTKATTVTPGPWHlhrmLLAAeslpLNIGFTGkGQAVNHTALVEQIHAGAI 218
Cdd:PRK09237 71 DEP--DEVGVRSGVTTVVdAGSAGADnfDDFRKLTIEASKTR----VLAF----LNISRIG-LLAQDELADLEDIDADAV 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1478526384 219 ------------GLKVHE------DWGATPsaLDHALQVAD 241
Cdd:PRK09237 140 aeavkrnpdfivGIKARMsssvvgDNGIEP--LELAKAIAA 178
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
71-221 |
3.70e-09 |
|
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: 58.93 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 71 DLVITNAMIIDYDKIVKADIGVKNGYIMKIGkagnpdimdnvDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQ---- 146
Cdd:TIGR03178 1 DLIIRGGRVILPNGEREADVGVKGGKIAAIG-----------PDILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRtewe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 147 -----SQVALESGITTHIGGGTGASEGTkaTTVTpgpwHLHRML-LAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGL 220
Cdd:TIGR03178 70 gfetgTRAAAAGGITTYIDMPLNSIPAT--TTRA----SLEAKFeAAKGKLAVDVGFWGGLVPYNLDDLRELDEAGVVGF 143
|
.
gi 1478526384 221 K 221
Cdd:TIGR03178 144 K 144
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
71-157 |
7.14e-09 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 58.12 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 71 DLVITNAMIIDYDKIVKADIGVKNGYIMKIGKAGNPDIMDNVdiiigattdiISAEGKIVTAGGIDTHVHFINPEQ---- 146
Cdd:PRK02382 3 DALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEV----------IDARGMLLLPGGIDVHVHFREPGYthke 72
|
90
....*....|....*.
gi 1478526384 147 -----SQVALESGITT 157
Cdd:PRK02382 73 twytgSRSAAAGGVTT 88
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
71-176 |
1.28e-08 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 57.40 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 71 DLVITNAMIIDYDKIVKADIGVKNGYIMKIGKAgnpdimdnvdiiIGATTDIISAEGKIVTAGGIDTHVHFINP--EQSQ 148
Cdd:PRK13404 5 DLVIRGGTVVTATDTFQADIGIRGGRIAALGEG------------LGPGAREIDATGRLVLPGGVDSHCHIDQPsgDGIM 72
|
90 100 110
....*....|....*....|....*....|
gi 1478526384 149 VA--LESGITTHIGGGTgasegtkaTTVTP 176
Cdd:PRK13404 73 MAddFYTGTVSAAFGGT--------TTVIP 94
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
71-144 |
2.21e-08 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 56.63 E-value: 2.21e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1478526384 71 DLVITNAMIIDYDKIVKADIGVKNGYIMKIGkagnPDIMdnvdiiiGATTDIISAEGKIVTAGGIDTHVHFINP 144
Cdd:PRK06189 4 DLIIRGGKVVTPEGVYRADIGIKNGKIAEIA----PEIS-------SPAREIIDADGLYVFPGMIDVHVHFNEP 66
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
71-325 |
2.98e-08 |
|
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: 56.15 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 71 DLVITNAMIID------YdkivKADIGVKNGYIMKIGKAGNPDimdnvdiiiGATTdiISAEGKIVTAGGIDTHVH---- 140
Cdd:cd01297 1 DLVIRNGTVVDgtgappF----TADVGIRDGRIAAIGPILSTS---------AREV--IDAAGLVVAPGFIDVHTHydgq 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 141 -FINPEqsqvALES---GITTHIGGGTGASeGTKATTVTPGPWHLHRMLLAAESLPLNIGF----------TGKGQAVNH 206
Cdd:cd01297 66 vFWDPD----LRPSsrqGVTTVVLGNCGVS-PAPANPDDLARLIMLMEGLVALGEGLPWGWatfaeyldalEARPPAVNV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 207 TALV------------------------------EQIHAGAIG----LKVHEDWGATPSALDHALQVADDYDVQIALHAD 252
Cdd:cd01297 141 AALVghaalrravmgldareateeelakmrellrEALEAGALGistgLAYAPRLYAGTAELVALARVAARYGGVYQTHVR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 253 TLNEAGF--MEE--TMAAVKDRVLHMYHTEGAGGGHAP------DLIKSAAYANIlpSSTNPTLPYTVNTiDEHLdMVMI 322
Cdd:cd01297 221 YEGDSILeaLDEllRLGRETGRPVHISHLKSAGAPNWGkidrllALIEAARAEGL--QVTADVYPYGAGS-EDDV-RRIM 296
|
...
gi 1478526384 323 THH 325
Cdd:cd01297 297 AHP 299
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
89-250 |
4.93e-08 |
|
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: 55.03 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 89 DIGVKNGYIMKIGKAGNPDimdnvdiiigATTDIISAEGKIVTAGGIDTHVH--------FINPeqSQVALESGITTHI- 159
Cdd:cd01307 1 DVAIENGKIAAVGAALAAP----------AATQIVDAGGCYVSPGWIDLHVHvyqggtryGDRP--DMIGVKSGVTTVVd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 160 GGGTGASEgtkattvTPGPWHlHRMLLAAESLP--LNIGFTGkGQAVNHTALVEQIHAGAI------------GLKVHE- 224
Cdd:cd01307 69 AGSAGADN-------IDGFRY-TVIERSATRVYafLNISRVG-LVAQDELPDPDNIDEDAVvaaareypdvivGLKARAs 139
|
170 180 190
....*....|....*....|....*....|.
gi 1478526384 225 -----DWGATPsaLDHALQVADDYDVQIALH 250
Cdd:cd01307 140 ksvvgEWGIKP--LELAKKIAKEADLPLMVH 168
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
71-141 |
1.08e-07 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 54.41 E-value: 1.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1478526384 71 DLVITNAMIIDYDKIVKADIGVKNGYIMKIGKAGNpdimdnvdiiigatTDIISAEGKIVTAGGIDTHVHF 141
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGANLG--------------DEVIDATGKYVMPGGIDPHTHM 58
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
68-176 |
5.49e-07 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 52.23 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 68 QVADLVITNAMIIDYDKIVKADIGVKNGYIMKIGKAGnpdimdnvdiiiGATTD-IISAEGKIVTAGGIDTHVHFINPEQ 146
Cdd:PRK09060 3 QTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLS------------GASAGeVIDCRGLHVLPGVIDSQVHFREPGL 70
|
90 100 110
....*....|....*....|....*....|....
gi 1478526384 147 SQVA-LESGITTHIGGG-TGASE--GTKATTVTP 176
Cdd:PRK09060 71 EHKEdLETGSRAAVLGGvTAVFEmpNTNPLTTTA 104
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
72-266 |
1.92e-06 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 50.58 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 72 LVITNAMIID-YDKIVKADIGVKNGYIMKIGKAGNPDImdnvdiiigatTDIISAEGKIVTAGGIDTHVHFINPeqsqva 150
Cdd:PRK09357 3 ILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENIEAEG-----------AEVIDATGLVVAPGLVDLHVHLREP------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 151 lesgitthigGGTGAS---EGTKA------TTV-----------TPGpwHLHRMLLAAESLPL---------NIGFTGKg 201
Cdd:PRK09357 66 ----------GQEDKEtieTGSRAaaaggfTTVvampntkpvidTPE--VVEYVLDRAKEAGLvdvlpvgaiTKGLAGE- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1478526384 202 qavNHTALVEQIHAGAI-----GLKVHedwgaTPSALDHALQVADDYDVQIALHA--DTLNEAGFMEETMAA 266
Cdd:PRK09357 133 ---ELTEFGALKEAGVVafsddGIPVQ-----DARLMRRALEYAKALDLLIAQHCedPSLTEGGVMNEGEVS 196
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
72-185 |
4.99e-06 |
|
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: 49.11 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 72 LVITNAMIIDYDKIVKADIGVKNGYIMKIGKAGNPDIMDnvdiiigattDIISAEGKIVTAGGIDTHVHFIN----PEQS 147
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEAD----------EIIDLKGQYLVPGFIDIHIHGGGgadfMDGT 70
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1478526384 148 QVALESGITTHigggtgASEGTK---ATTVTPGPWHLHRML 185
Cdd:cd00854 71 AEALKTIAEAL------AKHGTTsflPTTVTAPPEEIAKAL 105
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
72-157 |
7.91e-06 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 48.33 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 72 LVITNAMIIDYDKIVKADIGVKNGYIMKIGKagnpdimdnvDIIIGATTDIISAEGKIVTAGGIDTHVHFINP------- 144
Cdd:PRK09236 4 ILIKNARIVNEGKIFEGDVLIENGRIAKIAS----------SISAKSADTVIDAAGRYLLPGMIDDQVHFREPglthkgd 73
|
90
....*....|....*
gi 1478526384 145 --EQSQVALESGITT 157
Cdd:PRK09236 74 iaSESRAAVAGGITS 88
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
71-163 |
3.85e-05 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 46.29 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 71 DLVITNAMIID--YDKIVKADIGVKNGYIMKIGKAGNpdimdnvdiiIGATTdIISAEGKIVTAGGIDTHVHF------- 141
Cdd:PRK12394 4 DILITNGHIIDpaRNINEINNLRIINDIIVDADKYPV----------ASETR-IIHADGCIVTPGLIDYHAHVfydgteg 72
|
90 100
....*....|....*....|...
gi 1478526384 142 -INPEqsQVALESGITTHIGGGT 163
Cdd:PRK12394 73 gVRPD--MYMPPNGVTTVVDAGS 93
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
94-439 |
6.29e-05 |
|
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: 45.38 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 94 NGYIMKIGKAgnpdimdnvdIIIGATTDIISAEGKIVTAGGIDTHVH------------------------------FIN 143
Cdd:cd01309 1 DGKIVAVGAE----------ITTPADAEVIDAKGKHVTPGLIDAHSHlgldeeggvretsdaneetdpvtphvraidGIN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 144 P--EQSQVALESGITT-HIGGGTGASEGTKATTVTPGPWHLHRMLLAAES-LPLNIG-----FTGKGQAVNHTALVEQIH 214
Cdd:cd01309 71 PddEAFKRARAGGVTTvQVLPGSANLIGGQGVVIKTDGGTIEDMFIKAPAgLKMALGenpkrVYGGKGKEPATRMGVAAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 215 AGAIGLKV------HEDW---GATPSALD---HALQVADDYDVQIALHADTLNEagfMEETMAAVKDRVLHMYHTEGAGG 282
Cdd:cd01309 151 LRDAFIKAqeygrkYDLGknaKKDPPERDlklEALLPVLKGEIPVRIHAHRADD---ILTAIRIAKEFGIKITIEHGAEG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 283 GHAPDLIKsaayANILPSSTNPTLpytvntidehldmvmithhlnaSIPEDIAFADSRIrkeTIAAEdVLQDMGVFSMVS 362
Cdd:cd01309 228 YKLADELA----KHGIPVIYGPTL----------------------TLPKKVEEVNDAI---DTNAY-LLKKGGVAFAIS 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1478526384 363 SDSQamgrvgEVITR--TWQVAHRMKEqrGLldgdseyndnnRIKRYIAKYTINPAITHGISDYVGSIDEGKLADIILW 439
Cdd:cd01309 278 SDHP------VLNIRnlNLEAAKAVKY--GL-----------SYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVW 337
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
67-198 |
8.57e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 45.46 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 67 KQVADLVITNAMIID----YDKIvkADIGVKNGYIMKIGKagnpdimdnvDIIIGATTdiISAEGKIVTAGGIDTHVHFI 142
Cdd:PRK09061 16 MAPYDLVIRNGRVVDpetgLDAV--RDVGIKGGKIAAVGT----------AAIEGDRT--IDATGLVVAPGFIDLHAHGQ 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1478526384 143 NPEQSQVALESGITTHIGGGTGASEGTKattvtpgpWHLHRmllAAESLPLNIGFT 198
Cdd:PRK09061 82 SVAAYRMQAFDGVTTALELEAGVLPVAR--------WYAEQ---AGEGRPLNYGAS 126
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
70-159 |
1.01e-04 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 44.85 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 70 ADLVITNAMIIDYDKIVKADIGVKNGYIMKIGKAgnpdimdnvdiiIGATTDIISAEGKIVTAGGIDTHVHFINPEQS-- 147
Cdd:PRK08044 3 FDLIIKNGTVILENEARVVDIAVKGGKIAAIGQD------------LGDAKEVMDASGLVVSPGMVDAHTHISEPGRShw 70
|
90
....*....|....*....
gi 1478526384 148 -------QVALESGITTHI 159
Cdd:PRK08044 71 egyetgtRAAAKGGITTMI 89
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
72-141 |
1.13e-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: 44.89 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1478526384 72 LVITNAMII---DYDKIVKADIGVKNGYIMKIGKAGNPDIMDNVDIIigattdiiSAEGKIVTAGGIDTHVHF 141
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPALPLPAYPADEVI--------DAKGKVVMPGLVNTHTHL 65
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
389-438 |
1.17e-04 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 44.99 E-value: 1.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1478526384 389 RGLLDGDSEYNDNNRIKRY--IAKYTINPAITHGISDYVGSIDEGKLADIIL 438
Cdd:cd01300 428 RKTPGGGVLGNPEERLSLEeaLRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
84-162 |
1.24e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 44.76 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 84 KIVKADIGVKNGYIMKIGKAGNPDimDNVdiiigattdiISAEGKIVTAGGIDTHVHFINPEQS-QVALESGITTHIGGG 162
Cdd:PRK04250 11 RIVEGGIGIENGRISKISLRDLKG--KEV----------IKVKGGIILPGLIDVHVHLRDFEESyKETIESGTKAALHGG 78
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
64-142 |
1.28e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 44.79 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 64 RDDKQVADLVITNAMII--DYDKIVKADIGVKNGYIMKIGkaGNPDIMDnvdiIIGATTDIISAEGKIVTAGGIDTHVHF 141
Cdd:COG1574 2 KLAAAAADLLLTNGRIYtmDPAQPVAEAVAVRDGRIVAVG--SDAEVRA----LAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
.
gi 1478526384 142 I 142
Cdd:COG1574 76 L 76
|
|
| PLN02795 |
PLN02795 |
allantoinase |
60-274 |
1.39e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 44.77 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 60 PNVTRDDKQVA---DLVITNAMIIDYDKIVKADIGVKNGYIMKI-------GKAGNPDIMDnvdiiIGATtdiisaegkI 129
Cdd:PLN02795 31 PLQGRDRCSLLpwpHFVLYSKRVVTPAGVIPGAVEVEGGRIVSVtkeeeapKSQKKPHVLD-----YGNA---------V 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 130 VTAGGIDTHVHfINpEQSQVALEsGITThiggGTGASEGTKATTV----------TPGPWHLHRMLLAAE-SLPLNIGFT 198
Cdd:PLN02795 97 VMPGLIDVHVH-LN-EPGRTEWE-GFPT----GTKAAAAGGITTLvdmplnsfpsTTSVETLELKIEAAKgKLYVDVGFW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 199 GK---GQAVNHTALVEQIHAGAIGLKVH------EDWGAT-PSALDHALQVADDYDVQIALHADTLNEAGFMEETMAAVK 268
Cdd:PLN02795 170 GGlvpENAHNASVLEELLDAGALGLKSFmcpsgiNDFPMTtATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADPR 249
|
....*.
gi 1478526384 269 DRVLHM 274
Cdd:PLN02795 250 SYSTYL 255
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
408-452 |
2.26e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 44.06 E-value: 2.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1478526384 408 IAKYTINPAITHGISDYVGSIDEGKLADIILWEPAFFGVKPDVIV 452
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIA 449
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
73-140 |
3.11e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 43.16 E-value: 3.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1478526384 73 VITNAMIIDYDKIVK-ADIGVKNGYIMKIGKAGNPDImdnvdiiigattDIISAEGKIVTAGGIDTHVH 140
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPGAEPDA------------EVIDLGGGYLAPGFIDLHVH 57
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
72-159 |
4.35e-04 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 43.14 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 72 LVITNAMIIDYDKIVKADIGVKNGYIMKIGKagnpdimdnvDIIIGATTDIISAEGKIVTAGGIDTHVHFINP------- 144
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGD----------NLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPfggttta 70
|
90
....*....|....*....
gi 1478526384 145 ----EQSQVALESGITTHI 159
Cdd:TIGR02033 71 ddffTGTKAAAAGGTTTII 89
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
72-163 |
9.63e-04 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 41.75 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 72 LVITNAMIIDYDKIVKADIGVKNGYIMKIGKagNPDIMDNVDIIigattdiiSAEGKIVTAGGIDTHVHFINPEQSQVAL 151
Cdd:PLN02942 7 ILIKGGTVVNAHHQELADVYVEDGIIVAVAP--NLKVPDDVRVI--------DATGKFVMPGGIDPHTHLAMPFMGTETI 76
|
90
....*....|....*
gi 1478526384 152 E---SGITTHIGGGT 163
Cdd:PLN02942 77 DdffSGQAAALAGGT 91
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
72-160 |
1.27e-03 |
|
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: 41.22 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 72 LVITNAMIIDYDKIVKADIGVKNGYIMKIGkagnpdimDNVDIIIGATTDIISAEGKIVTAGGIDTHVHFI--------- 142
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIE--------DQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIggggeggps 73
|
90 100
....*....|....*....|.
gi 1478526384 143 --NPE-QSQVALESGITTHIG 160
Cdd:cd01308 74 trTPEvTLSDLTTAGVTTVVG 94
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
135-309 |
1.84e-03 |
|
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: 40.39 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 135 IDTHVHFINPEQSQV---------------------------ALESGITT-------HIGGGTGASEGTKATTVTPGPWh 180
Cdd:cd01292 2 IDTHVHLDGSALRGTrlnlelkeaeelspedlyedtlraleaLLAGGVTTvvdmgstPPPTTTKAAIEAVAEAARASAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478526384 181 lHRMLLAAESLPLNIGFTGKGQAVNHTALVEQIHAGAIGLKVHEDWGAT---PSALDHALQVADDYDVQIALHA-DTLNE 256
Cdd:cd01292 81 -IRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATglsDESLRRVLEEARKLGLPVVIHAgELPDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1478526384 257 AGFMEETMAAVK-DRVLHMYHtegaGGGHAPDLIKSAAYANILPSSTNPTLPYT 309
Cdd:cd01292 160 TRALEDLVALLRlGGRVVIGH----VSHLDPELLELLKEAGVSLEVCPLSNYLL 209
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
412-454 |
2.72e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 40.08 E-value: 2.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1478526384 412 TINPAITHGISDYVGSIDEGKLADIILWEPAfFGVKpDVIVKG 454
Cdd:COG1820 332 SLNPARALGLDDRKGSIAPGKDADLVVLDDD-LNVR-ATWVGG 372
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
90-142 |
3.56e-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: 39.93 E-value: 3.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1478526384 90 IGVKNGYIMKIGKAgnpdimDNVDIIIGATTDIISAEGKIVTAGGIDTHVHFI 142
Cdd:cd01296 1 IAIRDGRIAAVGPA------ASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLV 47
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
71-141 |
4.80e-03 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 39.42 E-value: 4.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1478526384 71 DLVITNAMIIDYDK----IVKADIGVKNGYIMKIGKAGNPDIMDNVDiiigattDIISAEGKIVTAGGIDTHVHF 141
Cdd:COG0402 1 DLLIRGAWVLTMDPaggvLEDGAVLVEDGRIAAVGPGAELPARYPAA-------EVIDAGGKLVLPGLVNTHTHL 68
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
411-440 |
5.28e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 39.40 E-value: 5.28e-03
10 20 30
....*....|....*....|....*....|
gi 1478526384 411 YTINPAITHGISDYVGSIDEGKLADIILWE 440
Cdd:COG1574 476 YTIGAAYAAFEEDEKGSLEPGKLADFVVLD 505
|
|
| |
