|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-446 |
0e+00 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 845.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 1 MAYDMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQM 80
Cdd:PRK06189 1 MMYDLIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 81 MAAGGCTTYFDMPLNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIEDIRPMAEAGAIGFKAFLSKSGTDEFRS 160
Cdd:PRK06189 81 LAAGGCTTYFDMPLNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNLEHLRELAEAGVIGFKAFMSNSGTDEFRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 161 VDERTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHI 240
Cdd:PRK06189 161 SDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFVHI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 241 STAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSL 320
Cdd:PRK06189 241 SSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPCPPEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 321 KREDNMFLSWGGISGGQFTLLGMLELA-LEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSM-EPYTVTRE 398
Cdd:PRK06189 321 KEGDDFFLVWGGISGGQSTLLVMLTEGyIERGIPLETIARLLATNPAKRFGLPQKGRLEVGADADFVLVDLdETYTLTKE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16080294 399 SMFAKHKKSIYEGHTFPCSISATYSKGRCVYNDGEKVTEIDGALVVPS 446
Cdd:PRK06189 401 DLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVFPPPRGQLLRPS 448
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
4-444 |
0e+00 |
|
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: 743.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 4 DMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAA 83
Cdd:TIGR03178 1 DLIIRGGRVILPNGEREADVGVKGGKIAAIGPDILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 84 GGCTTYFDMPLNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIEDIRPMAEAGAIGFKAFLSKSGTDEFRSVDE 163
Cdd:TIGR03178 81 GGITTYIDMPLNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNLDDLRELDEAGVVGFKAFLSPSGDDEFPHVDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 164 RTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHISTA 243
Cdd:TIGR03178 161 WQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVHLSSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 244 KAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLKRE 323
Cdd:TIGR03178 241 EAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSPCTPDLKRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 324 DNMFLSWGGISGGQFTLLGMLELA-LEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSM-EPYTVTRESMF 401
Cdd:TIGR03178 321 GDFFKAWGGIAGLQSTLDVMFDEAvQKRGLPLEDIARLMATNPAKRFGLAQKGRIAPGKDADFVFVDPdESYTLTPDDLY 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 16080294 402 AKHKKSIYEGHTFPCSISATYSKGRCVYNDGEKVTEIDGALVV 444
Cdd:TIGR03178 401 YRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAPKGQLLL 443
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-444 |
0e+00 |
|
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: 672.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 4 DMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIE-ASGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMA 82
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIAnTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 83 AGGCTTYFDMPLNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIEDIRPMAEAGAIGFKAFLSKSGTDEFRSVD 162
Cdd:cd01315 81 AGGITTIIDMPLNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGFKCFLCPSGVDEFPAVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 163 ERTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHIST 242
Cdd:cd01315 161 DEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIVHLSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 243 AKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLK- 321
Cdd:cd01315 241 AEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSPCTPELKl 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 322 -REDNMFLSWGGISGGQFTLLGMLELALEHQI-PFETIAEWTAAAPAKRFGLQ-KKGRLEAGCDADFVLVSMEPYTVTRE 398
Cdd:cd01315 321 lGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGlSLEDIARLMCENPAKLFGLShQKGRIAVGYDADFVVWDPEEEFTVDA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16080294 399 SMFA-KHKKSIYEGHTFPCSISATYSKGRCVYNDGEKVTEIDGALVV 444
Cdd:cd01315 401 EDLYyKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEPLGQLLL 447
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
6-443 |
2.20e-173 |
|
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: 493.07 E-value: 2.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 6 VIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEA-SGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAG 84
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAApEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 85 GCTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPG---HIEDIRPMAEAGAIGFKAFLSkSGTDEFRsV 161
Cdd:COG0044 81 GVTTVVDMP-NTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGlgeNLAELGALAEAGAVAFKVFMG-SDDGNPV-L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 162 DERTLLKGMAEIAAAGKILALHAESDAITSYLQMvlaNKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHIS 241
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVM---NEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 242 TAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLK 321
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 322 REDnMFLSWGGISGGQfTLLGML--ELALEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSME-PYTVTRE 398
Cdd:COG0044 315 ELP-FAEAPNGIPGLE-TALPLLltELVHKGRLSLERLVELLSTNPARIFGLPRKGRIAVGADADLVLFDPDaEWTVTAE 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 16080294 399 SMFAKHKKSIYEGHTFPCSISATYSKGRCVYNDGEKVTEIDGALV 443
Cdd:COG0044 393 DLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEPRGRFL 437
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-430 |
4.35e-120 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 357.63 E-value: 4.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 1 MAYDMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIeASGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQM 80
Cdd:PRK08044 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDL-GDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 81 MAAGGCTTYFDMPLNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIEDIRPMAEAGAIGFKAFLSKSG----TD 156
Cdd:PRK08044 80 AAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGdrgiDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 157 EFRSVDERTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVH 236
Cdd:PRK08044 160 DFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 237 FVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPC 316
Cdd:PRK08044 240 VCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 317 RPSLKrEDNMFLSWGGISGGQFTLLGMLELALEHQ-IPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSME-PYT 394
Cdd:PRK08044 320 PPEMK-AGNIMEAWGGIAGLQNCMDVMFDEAVQKRgMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNsSYV 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 16080294 395 VTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYN 430
Cdd:PRK08044 399 LKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
|
|
| PLN02795 |
PLN02795 |
allantoinase |
6-445 |
8.98e-110 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 333.28 E-value: 8.98e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 6 VIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEASGT----EIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMM 81
Cdd:PLN02795 47 VLYSKRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKSqkkpHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 82 AAGGCTTYFDMPLNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIED---IRPMAEAGAIGFKAFLSKSGTDEF 158
Cdd:PLN02795 127 AAGGITTLVDMPLNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPENAHNasvLEELLDAGALGLKSFMCPSGINDF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 159 RSVDERTLLKGMAEIAAAGKILALHAEsdaitsyLQMVLANKGKVDADA-----YAASRPEEAEVEAVYRTIQYAKVT-- 231
Cdd:PLN02795 207 PMTTATHIKAALPVLAKYGRPLLVHAE-------VVSPVESDSRLDADPrsystYLKSRPPSWEQEAIRQLLEVAKDTrp 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 232 -----GCPVHFVHISTAK-AVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGD 305
Cdd:PLN02795 280 ggvaeGAHVHIVHLSDAEsSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 306 IDMVSSDHSPCRPSLK--REDNMFLSWGGISGGQFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDA 383
Cdd:PLN02795 360 IDMLSSDHSPSPPDLKllEEGNFLRAWGGISSLQFVLPATWTAGRAYGLTLEQLARWWSERPAKLAGLDSKGAIAPGKDA 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16080294 384 DFVLVSMEPYTVTRES--MFAKHKK-SIYEGHTFPCSISATYSKGRCVYNDGEKVTEIDGALVVP 445
Cdd:PLN02795 440 DIVVWDPEAEFVLDESypIYHKHKSlSPYLGTKLSGKVIATFVRGNLVFLEGKHAKQACGSPILA 504
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
4-440 |
3.80e-97 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 298.49 E-value: 3.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 4 DMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEASGTE-IIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMA 82
Cdd:PRK02382 3 DALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEeVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRSAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 83 AGGCTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGlVPGHIEDIRPMAEAGAIGF-KAFLSKSgTDEFrSV 161
Cdd:PRK02382 83 AGGVTTVVDQP-NTDPPTVDGESFDEKAELAARKSIVDFGINGG-VTGNWDPLESLWERGVFALgEIFMADS-TGGM-GI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 162 DERTLLKGMAEIAAAGKILALHAESDAItsYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHIS 241
Cdd:PRK02382 159 DEELFEEALAEAARLGVLATVHAEDEDL--FDELAKLLKGDADADAWSAYRPAAAEAAAVERALEVASETGARIHIAHIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 242 TAKAVRLIREAKqegldVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLK 321
Cdd:PRK02382 237 TPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAPHTREEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 322 REDnmflSWGGISG--GQFTLLG-MLELALEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSMEPYTVTRE 398
Cdd:PRK02382 312 DAD----IWDAPSGvpGVETMLPlLLAAVRKNRLPLERVRDVTAANPARIFGLDGKGRIAEGYDADLVLVDPDAAREIRG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16080294 399 SMFakHKKS---IYEGHT--FPcsiSATYSKGRCVYnDGEKVTEIDG 440
Cdd:PRK02382 388 DDL--HSKAgwtPFEGMEgvFP---ELTMVRGTVVW-DGDDINAKRG 428
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
49-425 |
2.70e-90 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 278.06 E-value: 2.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 49 GKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAGGCTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGlV 128
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMP-NTKPPTTTAEALYEKLRLAAAKSVVDYGLYFG-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 129 PGHiEDIRPMAEAGAIGFKAFLSKSGTDEFrsVDERTLlkgmAEIAAAGKIL-ALHAESDAitsylqMVLAN-KGKVDAD 206
Cdd:cd01318 79 TGS-EDLEELDKAPPAGYKIFMGDSTGDLL--DDEETL----ERIFAEGSVLvTFHAEDED------RLRENrKELKGES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 207 AYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHISTAKAVRLIREAKQeglDVSVETCPHYVLFSHDDLRQRGSVAKCAP 286
Cdd:cd01318 146 AHPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKP---GVTVEVTPHHLFLDVEDYDRLGTLGKVNP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 287 PLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLKREDNMFlSWGGISGGQFTLLGMLELALEHQIPFETIAEWTAAAPA 366
Cdd:cd01318 223 PLRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA-APSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPA 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 367 KRFGLQKKGRLEAGCDADFVLVSMEPYTVTRESMFA-KHKKSIYEGHTFPCSISATYSKG 425
Cdd:cd01318 302 RIFGIKNKGRIAEGYDADLTVVDLKEERTIRAEEFHsKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
19-431 |
1.05e-89 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 278.56 E-value: 1.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 19 IEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAGGCTTYFDMPlNCIP 98
Cdd:TIGR00857 4 TEVDILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMP-NTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 99 STVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIEDIrpMAEAGAIGFKAFLSKSGTDEF-RSVDERTLLKGMAEIAAAG 177
Cdd:TIGR00857 83 PIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKE--LTEAYELKEAGAVGRMFTDDGsEVQDILSMRRALEYAAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 178 KILALHAESDAITSYLQMvlaNKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHISTAKAVRLIREAKQEGL 257
Cdd:TIGR00857 161 VPIALHAEDPDLIYGGVM---HEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 258 DVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLKREdNMFLSWGGISGGQ 337
Cdd:TIGR00857 238 KITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTK-EFAAAPPGIPGLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 338 FTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSMEP-YTVTRESMFAKHKKSIYEGHTFPC 416
Cdd:TIGR00857 317 TALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPDKGTLEEGNPADITVFDLKKeWTINAETFYSKAKNTPFEGMSLKG 396
|
410
....*....|....*
gi 16080294 417 SISATYSKGRCVYND 431
Cdd:TIGR00857 397 KPIATILRGKVVYED 411
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
5-437 |
1.13e-89 |
|
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: 279.49 E-value: 1.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 5 MVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEAS-GTEIIQADGKYVFPGVIDCHVHFNEP--GREDWEGFETGSQMM 81
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPgGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 82 AAGGCTTYFDMplnCIPSTvtAEHLLAKAELGRQ----KSAVDFALWGGLV---PGHIEDIRPMAEAGAIGFKAFLSKSG 154
Cdd:cd01314 81 AAGGTTTIIDF---AIPNK--GQSLLEAVEKWRGkadgKSVIDYGFHMIITdwtDSVIEELPELVKKGISSFKVFMAYKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 155 tdeFRSVDERTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCP 234
Cdd:cd01314 156 ---LLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 235 VHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQ---RGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSS 311
Cdd:cd01314 233 LYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWKdwfEGAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 312 DHSPCRPSLKR----------------EDNMFLSW-GGISGGQFTLLGMLELalehqipfetiaewTAAAPAKRFGL-QK 373
Cdd:cd01314 313 DHCPFNFAQKArgkddftkipngvpgvETRMPLLWsEGVAKGRITLEKFVEL--------------TSTNPAKIFGLyPR 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16080294 374 KGRLEAGCDADFVLVSME-PYTVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYNDGEKVTE 437
Cdd:cd01314 379 KGTIAVGSDADLVIWDPNaEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGE 443
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-431 |
3.73e-89 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 277.46 E-value: 3.73e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 5 MVIKGAKAVTPDGVIE-ADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAA 83
Cdd:PRK09357 3 ILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 84 GGCTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDF----ALWGGLVPGHIEDIRPMAEAGAIGFkaflsksgTDEFR 159
Cdd:PRK09357 83 GGFTTVVAMP-NTKPVIDTPEVVEYVLDRAKEAGLVDVlpvgAITKGLAGEELTEFGALKEAGVVAF--------SDDGI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 160 SVDERTLLKGMAEIAAA-GKILALHAESDAITSYLQMvlaNKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFV 238
Cdd:PRK09357 154 PVQDARLMRRALEYAKAlDLLIAQHCEDPSLTEGGVM---NEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHIC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 239 HISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSP--- 315
Cdd:PRK09357 231 HVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPhar 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 316 ---CRPSLKREdnmFlswgGISGGQFTL-LGMLELALEHQIPFETIAEWTAAAPAKRFGLqKKGRLEAGCDADFVLVSME 391
Cdd:PRK09357 311 eekECEFEAAP---F----GITGLETALsLLYTTLVKTGLLDLEQLLEKMTINPARILGL-PAGPLAEGEPADLVIFDPE 382
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16080294 392 P-YTVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYND 431
Cdd:PRK09357 383 AeWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
3-433 |
3.44e-80 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 255.48 E-value: 3.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 3 YDMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDieaSGTEIIQADGKYVFPGVIDCHVHFNEP--GREDWEGFETGSQM 80
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGAN---LGDEVIDATGKYVMPGGIDPHTHMEMPfgGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 81 MAAGGCTTYFDMplnCIPS-------TVTAEHllAKAElgrQKSAVDFALwgGLVPGHI-----EDIRPMAEAGAIGFKA 148
Cdd:PRK08323 78 AACGGTTTIIDF---ALQPkgqslreALEAWH--GKAA---GKAVIDYGF--HMIITDWnevvlDEMPELVEEGITSFKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 149 FLSKSGtdEFRsVDERTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYA 228
Cdd:PRK08323 148 FMAYKG--ALM-LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 229 KVTGCPVHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSV--AK--CAPPLRSRQSKETLIETLIAG 304
Cdd:PRK08323 225 ELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFegAKyvMSPPLRDKEHQDALWRGLQDG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 305 DIDMVSSDHSPCRPSLKR-----------------EDNMFLSWG-GISGGQFTLLGMLELalehqipfetiaewTAAAPA 366
Cdd:PRK08323 305 DLQVVATDHCPFCFEQKKqlgrgdftkipngtpgvEDRMPLLFSeGVMTGRITLNRFVEL--------------TSTNPA 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16080294 367 KRFGLQ-KKGRLEAGCDADFVLvsMEP---YTVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYNDGE 433
Cdd:PRK08323 371 KIFGLYpRKGTIAVGADADIVI--WDPnatKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGE 439
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
7-433 |
4.92e-78 |
|
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: 249.61 E-value: 4.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 7 IKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEASGT-EIIQADGKYVFPGVIDCHVHFNEP--GREDWEGFETGSQMMAA 83
Cdd:TIGR02033 3 IKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAvEVIDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 84 GGCTTYFDMplnCIPSTvtAEHLLAKAE----LGRQKSAVDFALWGGLVpgHI------EDIRPMAEAGAIGFKAFLSks 153
Cdd:TIGR02033 83 GGTTTIIDF---VVPEK--GSSLTEALEtwheKAEGKSVIDYGFHMDIT--HWndsvleEHIPEVKEEGINSFKVFMA-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 154 gTDEFRSVDERTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGC 233
Cdd:TIGR02033 154 -YKNLLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 234 PVHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQ---RGSVAKCAPPLRSRQSKETLIETLIAGDIDMVS 310
Cdd:TIGR02033 233 PLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKpgfEGAKYVCSPPLREPEDQDALWSALSSGALQTVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 311 SDHSPCRPSLKR-----------------EDNMFLSW-GGISGGQFTLLGMLELalehqipfetiaewTAAAPAKRFGLQ 372
Cdd:TIGR02033 313 SDHCTFNFAQKKaigkddftkipnggpgvEERMSLLFdEGVAKGRITLEKFVEV--------------TSTNPAKIFNLY 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16080294 373 -KKGRLEAGCDADFVLVsmEPYTVTreSMFAKHKKS-----IYEGHTFPCSISATYSKGRCVYNDGE 433
Cdd:TIGR02033 379 pRKGTIAVGSDADIVIW--DPNRTT--VISAETHHSnadynPFEGFKVRGAPVSVLSRGRVVVEDGQ 441
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
7-433 |
7.01e-75 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 240.93 E-value: 7.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 7 IKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEA-SGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAGG 85
Cdd:PRK09236 6 IKNARIVNEGKIFEGDVLIENGRIAKIASSISAkSADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESRAAVAGG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 86 CTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIEDIRPMAEAGAIGFKAFLSKSgTDEFRSVDERT 165
Cdd:PRK09236 86 ITSFMEMP-NTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLDEIKRLDPKRVCGVKVFMGAS-TGNMLVDNPET 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 166 LLKGMAEiaaAGKILALHAESDAitsylqMVLANKGK--------VDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHF 237
Cdd:PRK09236 164 LERIFRD---APTLIATHCEDTP------TIKANLAKykekygddIPAEMHPLIRSAEACYKSSSLAVSLAKKHGTRLHV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 238 VHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPcr 317
Cdd:PRK09236 235 LHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALADDRIDVIATDHAP-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 318 PSLKREDNMFLSwgGISGG---QFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSM-EPY 393
Cdd:PRK09236 313 HTWEEKQGPYFQ--APSGLplvQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDIKERGFIREGYWADLVLVDLnSPW 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16080294 394 TVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYNDGE 433
Cdd:PRK09236 391 TVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQ 430
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-440 |
9.11e-75 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 240.73 E-value: 9.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 1 MAYDMVIKGAKAVTPDG-VIEADIVVQNGVIAEIGSDIEASG-TEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGS 78
Cdd:PRK07575 1 MMMSLLIRNARILLPSGeLLLGDVLVEDGKIVAIAPEISATAvDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 79 QMMAAGGCTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIEDIRpmAEAGAIGFKAFLSKSGTDEF 158
Cdd:PRK07575 81 RACAKGGVTSFLEMP-NTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELL--TANPTCGIKIFMGSSHGPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 159 rsVDERTLLKgmaEIAAAGKIL-ALHAESDAitsylqMVLANK----GKVDADAYAASRPEEAEVEAVYRTIQYAKVTGC 233
Cdd:PRK07575 158 --VDEEAALE---RIFAEGTRLiAVHAEDQA------RIRARRaefaGISDPADHSQIQDEEAALLATRLALKLSKKYQR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 234 PVHFVHISTAKAVRLIREAKqeGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDH 313
Cdd:PRK07575 227 RLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIATDH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 314 SPCRPSLKRED--NmflSWGGISGGQFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSME 391
Cdd:PRK07575 305 APHTLEEKAQPypN---SPSGMPGVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGIPNKGRIAPGYDADLVLVDLN 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 16080294 392 PY-TVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYNDGEKVTEIDG 440
Cdd:PRK07575 382 TYrPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVNTEVRG 431
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
50-421 |
5.39e-72 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 230.36 E-value: 5.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 50 KYVFPGVIDCHVHFNEPG-REDWEGFETGSQMMAAGGCTTYFDMPLNCIPSTVTAEHLLAKaELGRQKSAVDFALWGGLV 128
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGgTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKI-KLAEESSYVDFSFHAGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 129 PG-HIEDIRPMAEAGAIGFKAFLSKSGTDEFrSVDERTLLKGMAEIAAAGKILALHAEsdaitsylqmvlankgkvdada 207
Cdd:cd01302 80 PGdVTDELKKLFDAGINSLKVFMNYYFGELF-DVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 208 yaasrpeeaeveavyRTIQYAKVTGCPVHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPP 287
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 288 LRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLKREDNMF-LSWGGISGGQFTLLGMLELALEHQIPFETIAEWTAAAPA 366
Cdd:cd01302 202 LRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKDIwKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPA 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16080294 367 KRFGLQKKGRLEAGCDADFVLVSME-PYTVTRESMFAKHKKSIYEGHTFPCSISAT 421
Cdd:cd01302 282 RIFGLYPKGTIAVGYDADLVIVDPKkEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-443 |
2.04e-68 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 224.41 E-value: 2.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 1 MAYDMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQM 80
Cdd:PRK09060 3 QTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 81 MAAGGCTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIEDIRPM-AEAGAIGFKAFLSKSGTDEFR 159
Cdd:PRK09060 83 AVLGGVTAVFEMP-NTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELeRLPGCAGIKVFMGSSTGDLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 160 SVDErtllkGMAEIAAAG-KILALHAESDAitsylqMVLANKGKV---DADAYAASRPEEAEVEAVYRTIQYAKVTGCPV 235
Cdd:PRK09060 162 EDDE-----GLRRILRNGrRRAAFHSEDEY------RLRERKGLRvegDPSSHPVWRDEEAALLATRRLVRLARETGRRI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 236 HFVHISTAKAVRLIREAKqeglDV-SVETCPHYVLFSHDDLRQR-GSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDH 313
Cdd:PRK09060 231 HVLHVSTAEEIDFLADHK----DVaTVEVTPHHLTLAAPECYERlGTLAQMNPPIRDARHRDGLWRGVRQGVVDVLGSDH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 314 SP------CRPSLKrednmflSWGGISGGQFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVL 387
Cdd:PRK09060 307 APhtleekAKPYPA-------SPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAGKGRIAVGYDADFTI 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16080294 388 VSME-PYTVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYNDGEKVTEIDGALV 443
Cdd:PRK09060 380 VDLKrRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELVGPPTGEPV 436
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
43-421 |
8.22e-67 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 217.87 E-value: 8.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 43 EIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAGGCTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDFA 122
Cdd:cd01317 3 EVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMP-NTNPVIDNPAVVELLKNRAKDVGIVRVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 123 LWGGLVPG----HIEDIRPMAEAGAIGFkaflsksGTDEFRSVDERTLLKGMAEIAAAGKILALHAESDAITSYLQMvla 198
Cdd:cd01317 82 PIGALTKGlkgeELTEIGELLEAGAVGF-------SDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVM--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 199 NKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQR 278
Cdd:cd01317 152 NEGKVASRLGLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 279 GSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLKR---EDNMFlswgGISGgqftllgmLELAL------- 348
Cdd:cd01317 232 DTNAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDlpfAEAPP----GIIG--------LETALpllwtll 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16080294 349 --EHQIPFETIAEWTAAAPAKRFGLqKKGRLEAGCDADFVLVSM-EPYTVTRESMFAKHKKSIYEGHTFPCSISAT 421
Cdd:cd01317 300 vkGGLLTLPDLIRALSTNPAKILGL-PPGRLEVGAPADLVLFDPdAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1-437 |
6.85e-65 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 216.10 E-value: 6.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 1 MAYDMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIeASGTEIIQADGKYVFPGVIDCHVHFNEP---GREDWEGFETG 77
Cdd:PRK13404 2 MAFDLVIRGGTVVTATDTFQADIGIRGGRIAALGEGL-GPGAREIDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 78 SQMMAAGGCTTYfdMPLNC------IPSTVTAEHLLAKAelgrqKSAVDFALwgglvpgHI-----------EDIRPMAE 140
Cdd:PRK13404 81 TVSAAFGGTTTV--IPFAAqhrgqsLREAVEDYHRRAAG-----KAVIDYAF-------HLivadpteevltEELPALIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 141 AGAIGFKAFLsksgTDEFRSVDERTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEA 220
Cdd:PRK13404 147 QGYTSFKVFM----TYDDLKLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 221 VYRTIQYAKVTGCPVHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRG-SVAK--CAPPLRSRQSKETL 297
Cdd:PRK13404 223 THRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDRPGmEGAKyiCSPPPRDKANQEAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 298 IETLIAGDIDMVSSDHSPCR---PSLKRE--DNMFLSW--GGISGGQFTL-LGMLELALEHQIPFETIAEWTAAAPAKRF 369
Cdd:PRK13404 303 WNGLADGTFEVFSSDHAPFRfddTDGKLAagANPSFKAiaNGIPGIETRLpLLFSEGVVKGRISLNRFVALTSTNPAKLY 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 370 GLQ-KKGRLEAGCDADFVLVS-MEPYTVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYNDGEKVTE 437
Cdd:PRK13404 383 GLYpRKGAIAIGADADIAIWDpDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAE 452
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
6-440 |
1.88e-54 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 186.51 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 6 VIKGaKAVTPDGVIEADIVVQNGVIAEIGSDiEASGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAGG 85
Cdd:PRK04250 1 VLEG-KFLLKGRIVEGGIGIENGRISKISLR-DLKGKEVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 86 CTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDFALwGGLVPGHIEDIRPmaeAGAIGFKAFLSKSGTDEFrsvdert 165
Cdd:PRK04250 79 ITLVFDMP-NTKPPIMDEKTYEKRMRIAEKKSYADYAL-NFLIAGNCEKAEE---IKADFYKIFMGASTGGIF------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 166 lLKGMAE-IAAAGKILALHAES-DAITSYLQmvlankgkvdadayaasRPEEAEVEAVYRTIQYAKVTGCPVHFVHISTA 243
Cdd:PRK04250 147 -SENFEVdYACAPGIVSVHAEDpELIREFPE-----------------RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 244 KAVRLIREAKQEGldVSVETCPHYVLFSHDDLRqRGSVAKCAPPLRSRQSKETLIETLiaGDIDMVSSDHSPCRPSLKRE 323
Cdd:PRK04250 209 DGLKLILKSNLPW--VSFEVTPHHLFLTRKDYE-RNPLLKVYPPLRSEEDRKALWENF--SKIPIIASDHAPHTLEDKEA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 324 DNmflswGGISGGQFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLQKKGrLEAGCDADFVLVSM-EPYTVTRESMFA 402
Cdd:PRK04250 284 GA-----AGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNYG-IEEGNYANFAVFDMkKEWTIKAEELYT 357
|
410 420 430
....*....|....*....|....*....|....*...
gi 16080294 403 KHKKSIYEGHTFPCSISATYSKGRCVYNDGEKVTEIDG 440
Cdd:PRK04250 358 KAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKPRG 395
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1-430 |
9.45e-45 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 161.36 E-value: 9.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 1 MAYDMVIKGAKAVTP----DGVieADIVVQNGVIAEIGSDIEASG----TEIIQADGKYVFPGVIDCHVHFNEPGREDWE 72
Cdd:PRK09059 1 MMRPILLANARIIDPsrglDEI--GTVLIEDGVIVAAGKGAGNQGapegAEIVDCAGKAVAPGLVDARVFVGEPGAEHRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 73 GFETGSQMMAAGGCTTYFDMPLN--CIPSTVTAEHLLAKAelgRQKSAVDF----ALWGGLVPGHIEDIRPMAEAGAIGF 146
Cdd:PRK09059 79 TIASASRAAAAGGVTSIIMMPDTdpVIDDVALVEFVKRTA---RDTAIVNIhpaaAITKGLAGEEMTEFGLLRAAGAVAF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 147 kaflsksgTDEFRSV-DERTLLKGMAEIAAAGKILALHAESDAITSYLQMvlaNKGKVdadayaASR------PEEAEVE 219
Cdd:PRK09059 156 --------TDGRRSVaNTQVMRRALTYARDFDAVIVHETRDPDLGGNGVM---NEGLF------ASWlglsgiPREAEVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 220 AVYRTIQYAKVTGCPVHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIE 299
Cdd:PRK09059 219 PLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 300 TLIAGDIDMVSSDHSPCRPSLKRednmfLSWGGISGGQFTLLGMLELALE--H--QIPFETIAEWTAAAPAKRFGLqKKG 375
Cdd:PRK09059 299 AVASGTIDIIVSSHDPQDVDTKR-----LPFSEAAAGAIGLETLLAAALRlyHngEVPLLRLIEALSTRPAEIFGL-PAG 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16080294 376 RLEAGCDADFVLVSM-EPYTVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYN 430
Cdd:PRK09059 373 TLKPGAPADIIVIDLdEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
5-433 |
1.99e-40 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 150.76 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 5 MVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEA-SGTEIIQADGKYVFPGVIDCHVHFNEP--GREDWEGFETGSQMM 81
Cdd:PLN02942 7 ILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVpDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 82 AAGGCTTYFD--MPLNcipstvtaEHLLAKAELGR---QKSAVDFAL------WGGLVPGHIEDIrpMAEAGAIGFKAFL 150
Cdd:PLN02942 87 LAGGTTMHIDfvIPVN--------GNLLAGYEAYEkkaEKSCMDYGFhmaitkWDDTVSRDMETL--VKEKGINSFKFFM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 151 SKSGTdefRSVDERTLLKGMAEIAAAGKILALHAESDAITSYLQMVLANKGKVDADAYAASRPEEAEVEAVYRTIQYAKV 230
Cdd:PLN02942 157 AYKGS---LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 231 TGCPVHFVHISTAKAVRLIREAKQEGLDVSVE-TCPHYVLfshDDLRQRGSVAKCA------PPLRSRQSKETLIETLIA 303
Cdd:PLN02942 234 VNTPLYVVHVMSIDAMEEIARARKSGQRVIGEpVVSGLVL---DDSKLWDPDFTIAskyvmsPPIRPAGHGKALQAALSS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 304 GDIDMVSSDHSPCRPSLKR----------------EDNMFLSWG-GISGGQFTLLGMLELalehqipfetiaewTAAAPA 366
Cdd:PLN02942 311 GILQLVGTDHCPFNSTQKAfgkddfrkipngvngiEERMHLVWDtMVESGQISPTDYVRV--------------TSTECA 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16080294 367 KRFGL-QKKGRLEAGCDADFVLVSME-PYTVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVYNDGE 433
Cdd:PLN02942 377 KIFNIyPRKGAILAGSDADIIILNPNsTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGE 445
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
16-443 |
3.50e-40 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 148.47 E-value: 3.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 16 DGVIEADIVVQNGVIAEIGSDIEASGTeiIQADGKyVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAGGCTTYFDMPLN 95
Cdd:PRK01211 11 GKFDYLEIEVEDGKIKSIKKDAGNIGK--KELKGA-ILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 96 CIPSTvtaEHLLAKAELGR--QKSAVDFALWGGLVPGHIEDIrpmaEAGAIGFKAFLSKSGTDEFRSVDERTLLKgmaeI 173
Cdd:PRK01211 88 NIPIK---DYNAFSDKLGRvaPKAYVDFSLYSMETGNNALIL----DERSIGLKVYMGGTTNTNGTDIEGGEIKK----I 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 174 AAAGKILALHAESDAITSYLQMVLANkgkvdADAYAASRPEEAEVEAVYRTIQYAKVTgcpVHFVHISTAKAV-RLIREA 252
Cdd:PRK01211 157 NEANIPVFFHAELSECLRKHQFESKN-----LRDHDLARPIECEIKAVKYVKNLDLKT---KIIAHVSSIDVIgRFLREV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 253 KqegldvsvetcPHYvLFSHDDLrQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLKREdnMFLSWGG 332
Cdd:PRK01211 229 T-----------PHH-LLLNDDM-PLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQE--FEYAKSG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 333 ISGGQFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLqKKGRLEAGCDADFVLVSMEPYTVTRES-MFAKHKKSIYEG 411
Cdd:PRK01211 294 IIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGI-KKGKIEEGYDADFMAFDFTNIKKINDKrLHSKCPVSPFNG 372
|
410 420 430
....*....|....*....|....*....|....
gi 16080294 412 HT--FPCSISAtysKGRCVYNDGEKVTEIDGALV 443
Cdd:PRK01211 373 FDaiFPSHVIM---RGEVVIDNYELISERTGKFV 403
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
7-429 |
1.09e-37 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 142.12 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 7 IKGAKAVTPDGVIE--ADIVVQNGVIAEIGS---DIEASGTeiIQADGKYVFPGVIDCHVHFNEPGREDWEGFEtgSQMM 81
Cdd:PRK07627 5 IKGGRLIDPAAGTDrqADLYVAAGKIAAIGQapaGFNADKT--IDASGLIVCPGLVDLSARLREPGYEYKATLE--SEMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 82 AA--GGCTTyfdmpLNCIPSTVT-------AEHLLAKAE-LGRQKSAVDFALWGGLVPGHIEDIRPMAEAGAIGFkaflS 151
Cdd:PRK07627 81 AAvaGGVTS-----LVCPPDTDPvldepglVEMLKFRARnLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGF----S 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 152 KSGTDefrSVDERTLLKGMAEIAAAGKILALHAEsDAITSylqmvlanKGKVDADAYAASR------PEEAEVEAVYRTI 225
Cdd:PRK07627 152 QANVP---VVDTQVLLRALQYASTFGFTVWLRPL-DAFLG--------RGGVAASGAVASRlglsgvPVAAETIALHTIF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 226 QYAKVTGCPVHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGD 305
Cdd:PRK07627 220 ELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 306 IDMVSSDHSPCrpslkREDNMFLSWG----GISGGQFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLqKKGRLEAGC 381
Cdd:PRK07627 300 IDAICSDHTPV-----DDDEKLLPFAeatpGATGLELLLPLTLKWADEAKVPLARALARITSAPARVLGL-PAGRLAEGA 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16080294 382 DADFVLVSMEPY-TVTRESMFAKHKKSIYEGHTFPCSISATYSKGRCVY 429
Cdd:PRK07627 374 PADLCVFDPDAHwRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAF 422
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
27-440 |
5.13e-31 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 122.95 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 27 NGVIAEIGSDIEASGTEI---IQAD-----GKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAGGCTTYFDMPlNCIP 98
Cdd:PRK00369 12 GKEIKEICINFDRRIKEIksrCKPDldlpqGTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMP-NTIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 99 STVTAEHLLAK-AELgRQKSAVDFALWGGlVPGHIEDIRPMAEAgaiGFKAF---LSKSGTdefrsvdERTLLKGMaeia 174
Cdd:PRK00369 91 PLNTPEAITEKlAEL-EYYSRVDYFVYSG-VTKDPEKVDKLPIA---GYKIFpedLEREET-------FRVLLKSR---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 175 aagKILALHAEsdaitsylqMVLANKGKvdadaYAASRPEEAEVEAVYRTIQYAKvtgcpVHFVHISTAKAVRLireAKQ 254
Cdd:PRK00369 155 ---KLKILHPE---------VPLALKSN-----RKLRRNCWYEIAALYYVKDYQN-----VHITHASNPRTVRL---AKE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 255 EGLdvSVETCPHYVLFshddLRQRGSVAKCAPPLRSRQSKETLIETLIagDIDMVSSDHSpcrPSLKREDNMFLSW--GG 332
Cdd:PRK00369 210 LGF--TVDITPHHLLV----NGEKDCLTKVNPPIRDINERLWLLQALS--EVDAIASDHA---PHSSFEKLQPYEVcpPG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 333 ISGGQFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLqKKGRLEAGCDADFVLVSMEPYTVTREsmFAKHKKSIYEGH 412
Cdd:PRK00369 279 IAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGI-PYGEIKEGYRANFTVIQFEDWRYSTK--YSKVIETPLDGF 355
|
410 420
....*....|....*....|....*...
gi 16080294 413 TFPCSISATYSKGRCVYNDGEkVTEIDG 440
Cdd:PRK00369 356 ELKASVYATIVQGKLAYLEGE-VFPVKG 382
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
21-400 |
4.01e-30 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 120.86 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 21 ADIVVQNGVIAEIGSDIEA--SGTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGFETGSQMMAAGGCTTYFDMPlNCIP 98
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDPipPDTQIIDASGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILP-DTFP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 99 STVTAEHLLAKAELGRQKSAVDFALWGGLVPG----HIEDIRPMAEAGAIGFkaflsksgTDEfRSVDERTLLKGMAE-I 173
Cdd:PRK07369 101 PLDNPATLARLQQQAQQIPPVQLHFWGALTLGgqgkQLTELAELAAAGVVGF--------TDG-QPLENLALLRRLLEyL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 174 AAAGKILALHAESDAitsylqmvLANKGkVDADAYAASR------PEEAEVEAVYRTIQYAKVTGCPVHFVHISTAKAVR 247
Cdd:PRK07369 172 KPLGKPVALWPCDRS--------LAGNG-VMREGLLALRlglpgdPASAETTALAALLELVAAIGTPVHLMRISTARSVE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 248 LIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPcrpsLKREDNMf 327
Cdd:PRK07369 243 LIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAP----YTYEEKT- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 328 LSW-----GGISggqftllgmLELALE--HQIPFETiAEWTA--------AAPAKRFGlQKKGRLEAGCDADFVLVS-ME 391
Cdd:PRK07369 318 VAFaeappGAIG---------LELALPllWQNLVET-GELSAlqlwqalsTNPARCLG-QEPPSLAPGQPAELILFDpQK 386
|
....*....
gi 16080294 392 PYTVTRESM 400
Cdd:PRK07369 387 TWTVSAQTL 395
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
23-429 |
2.51e-28 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 115.18 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 23 IVVQNGVIAEIGSDIEasGTEIIQADGKYVFPGVIDCHV--HFNEPGREDWEGFETGSqmmAAGGCTTYFDMPlNCIPSt 100
Cdd:PRK08417 1 IRIKDGKITEIGSDLK--GEEILDAKGKTLLPALVDLNVslKNDSLSSKNLKSLENEC---LKGGVGSIVLYP-DSTPA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 101 VTAEHLLAKAELGRQKSavdfalwgglvPGHIED-IRPMAEAGAIGFKAFLSKSGTD--EFRSVDERTLLKGMAEIAAAG 177
Cdd:PRK08417 74 IDNEIALELINSAQREL-----------PMQIFPsIRALDEDGKLSNIATLLKKGAKalELSSDLDANLLKVIAQYAKML 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 178 KI-LALHAESDAITSYLQMvlaNKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGCPVHFVHISTAKAVRLIREAKQEG 256
Cdd:PRK08417 143 DVpIFCRCEDSSFDDSGVM---NDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 257 LDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRSRQSKETLIETLIAGDIDMVSSDHSPCRPSLKreDNMF-LSWGGISG 335
Cdd:PRK08417 220 EKLLKEVSIHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKK--DLAFdEAAFGIDS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 336 --GQFTLLgMLELALEHQIPFETIAEWTAAAPAKRFGLQkKGRLEAGCDADFVLVSMEpytvtrESMFAKHKKSIYEGHT 413
Cdd:PRK08417 298 icEYFSLC-YTYLVKEGIITWSELSRFTSYNPAQFLGLN-SGEIEVGKEADLVLFDPN------ESTIIDDNFSLYSGDE 369
|
410
....*....|....*.
gi 16080294 414 FPCSISATYSKGRCVY 429
Cdd:PRK08417 370 LYGKIEAVIIKGKLYL 385
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-440 |
1.13e-19 |
|
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: 90.43 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 4 DMVIKGAKAVTPDGV--IEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVHFnepgreDWEGFETGSQMM 81
Cdd:cd01297 1 DLVIRNGTVVDGTGAppFTADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTHY------DGQVFWDPDLRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 82 AAG-GCTTYFDMplNCIPSTVTAEH--------LLAKAELGRQKSAVDFALWGGLVpGHIEDIRPMAEAGA-IGFKAFLS 151
Cdd:cd01297 75 SSRqGVTTVVLG--NCGVSPAPANPddlarlimLMEGLVALGEGLPWGWATFAEYL-DALEARPPAVNVAAlVGHAALRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 152 KSGTDEFR--SVDErtlLKGMAEIAA----AGKI---------LALHAESDAITSyLQMVLANKGKVdadAYAASRPE-E 215
Cdd:cd01297 152 AVMGLDAReaTEEE---LAKMRELLRealeAGALgistglayaPRLYAGTAELVA-LARVAARYGGV---YQTHVRYEgD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 216 AEVEAVYRTIQYAKVTGCPVHFVHISTAKAV---------RLIREAKQEGLDVSVETCPhYVLFSHDDLRQrgsvakcap 286
Cdd:cd01297 225 SILEALDELLRLGRETGRPVHISHLKSAGAPnwgkidrllALIEAARAEGLQVTADVYP-YGAGSEDDVRR--------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 287 plrsrqsketlietLIAGDIDMVSSDHSPCRPSLKRednmflSWGGisggqFTLLgmlelaLEHQ------IPFETIAEW 360
Cdd:cd01297 295 --------------IMAHPVVMGGSDGGALGKPHPR------SYGD-----FTRV------LGHYvrerklLSLEEAVRK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 361 TAAAPAKRFGLQKKGRLEAGCDADFVLVSMEpyTVTRESMFakhkksiYEGHTFPCSISATYSKGRCVYNDGEKVTEIDG 440
Cdd:cd01297 344 MTGLPARVFGLADRGRIAPGYRADIVVFDPD--TLADRATF-------TRPNQPAEGIEAVLVNGVPVVRDGAFTGARPG 414
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
54-315 |
5.83e-19 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 87.51 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 54 PGVIDCHVHFNEPGREDWEGFETGSQMMAAGGCTTYFDMPlNCIPSTVTAEHLLAKAELGRQKSAVDFALWGGLVPGHIE 133
Cdd:cd01316 6 PGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMP-NTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATSTNAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 134 DIRPMAEAgAIGFKAFLSKsgTDEFRSVDERTLLKGMAEIAAAGKILALHAESDAITSYLQMV-LANKGkvdadayaasr 212
Cdd:cd01316 85 TVGELASE-AVGLKFYLNE--TFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLAsLHNRS----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 213 peeaeveavyrtiqyakvtgcpVHFVHISTAKAVRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSvaKCAPPLRSRQ 292
Cdd:cd01316 151 ----------------------IHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQY--EVRPFLPTRE 206
|
250 260
....*....|....*....|...
gi 16080294 293 SKETLIETLiaGDIDMVSSDHSP 315
Cdd:cd01316 207 DQEALWENL--DYIDCFATDHAP 227
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
3-402 |
1.77e-17 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 84.36 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 3 YDMVIKGAKAVTP----DGVieADIVVQNGVIAEIGSDIeASGTEIIQADGKYVFPGVIDCHVHFNEPGredwegfetGS 78
Cdd:PRK09061 19 YDLVIRNGRVVDPetglDAV--RDVGIKGGKIAAVGTAA-IEGDRTIDATGLVVAPGFIDLHAHGQSVA---------AY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 79 QMMAAGGCTTYFDMPLNCIPstVTAehllAKAELGRQKSAVDFALWGGLVPGHI-EDIRPMAEAGAIGF-KAFLSKSGTD 156
Cdd:PRK09061 87 RMQAFDGVTTALELEAGVLP--VAR----WYAEQAGEGRPLNYGASVGWTPARIaVLTGPQAEGTIADFgKALGDPRWQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 157 EFRSVDERT-----LLKGMAEIAAAGKILALHAESDAITSYLQMV-LANKGKVDAD---AYAASRPEEAEVEAVYRTIQY 227
Cdd:PRK09061 161 RAATPAELAeilelLEQGLDEGALGIGIGAGYAPGTGHKEYLELArLAARAGVPTYthvRYLSNVDPRSSVDAYQELIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 228 AKVTGCPVHFVHI-STAK-----AVRLIREAKQEGLDVSVETCPH--------YVLFSHDDLRQRGSVAKC--------- 284
Cdd:PRK09061 241 AAETGAHMHICHVnSTSLrdidrCLALVEKAQAQGLDVTTEAYPYgagstvvgAAFFDPGWLERMGLGYGSlqwvetger 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 285 ---APPLRSRQ------------------SKETLIETLIAGDIDMVSSDHSPCRPSlKREDNMFLSWGGISG-------- 335
Cdd:PRK09061 321 lltREELAKLRandpgglvlihfldednpRDRALLDRSVLFPGAAIASDAMPWTWS-DGTVYEGDAWPLPEDavshprsa 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 336 GQFT-----------LLGMLElALEH--QIPFETIAEWTAAAPAkrfglqkKGRLEAGCDADFVLvsMEPYTVTRESMFA 402
Cdd:PRK09061 400 GTFArflreyvrerkALSLLE-AIRKctLMPAQILEDSVPAMRR-------KGRLQAGADADIVV--FDPETITDRATFE 469
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-393 |
4.73e-17 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 82.32 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 1 MAYDMVIKGAKAVTPDG--VIE-ADIVVQNGVIAEIGSDIEAS---GTEIIQADGKYVFPGVIDCHVHFNEPGREDWEGF 74
Cdd:COG1228 6 QAGTLLITNATLVDGTGggVIEnGTVLVEDGKIAAVGPAADLAvpaGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 75 ETGS---------------QMMAAGGCTTYFDMPLNCIP-STVTAEHLLAKAELGR-QKSAVDFALWGGLVPGHIEDIRP 137
Cdd:COG1228 86 AGGGitptvdlvnpadkrlRRALAAGVTTVRDLPGGPLGlRDAIIAGESKLLPGPRvLAAGPALSLTGGAHARGPEEARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 138 M----AEAGAIGFKAFLSKSGTDefRSVDErtlLKGMAEIA-AAGKILALHAESdaitsylqmvlankgkvDADAYAAsr 212
Cdd:COG1228 166 AlrelLAEGADYIKVFAEGGAPD--FSLEE---LRAILEAAhALGLPVAAHAHQ-----------------ADDIRLA-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 213 peeaeVEAVYRTIqyakvtgcpVHFVHISTAkavrLIREAKQEGldvSVETCPhyVLFSHDDLRQRGSVAKCAPPLRSRQ 292
Cdd:COG1228 222 -----VEAGVDSI---------EHGTYLDDE----VADLLAEAG---TVVLVP--TLSLFLALLEGAAAPVAAKARKVRE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 293 SKETLIETLIAGDIDMV-SSDHspcrpslkredNMFLSWGgisggqFTLLGMLELALEHQI-PFETIAEWTaAAPAKRFG 370
Cdd:COG1228 279 AALANARRLHDAGVPVAlGTDA-----------GVGVPPG------RSLHRELALAVEAGLtPEEALRAAT-INAAKALG 340
|
410 420
....*....|....*....|....
gi 16080294 371 LQKK-GRLEAGCDADFVLVSMEPY 393
Cdd:COG1228 341 LDDDvGSLEPGKLADLVLLDGDPL 364
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
5-105 |
7.64e-14 |
|
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: 72.61 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 5 MVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEA-SGTEIIQADGKYVFPGVIDCHVH------FNEpgrEDWEGFETG 77
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELeEADEIIDLKGQYLVPGFIDIHIHggggadFMD---GTAEALKTI 77
|
90 100
....*....|....*....|....*...
gi 16080294 78 SQMMAAGGCTTYFdmplnciPSTVTAEH 105
Cdd:cd00854 78 AEALAKHGTTSFL-------PTTVTAPP 98
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-147 |
3.96e-13 |
|
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: 71.21 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 4 DMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSD-------------IEASGTEIIQADGKYVFPGVIDCHVHFNEPgRED 70
Cdd:cd00375 66 DLVITNALIIDYTGIYKADIGIKDGRIVAIGKAgnpdimdgvtpnmIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-QQI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 71 WEGFETGSQMM-------AAGGCTTyfdmplNCIPSTVTAEHLLAKAElgrqKSAVDFALWGGLVPGHIEDIRPMAEAGA 143
Cdd:cd00375 145 EEALASGITTMigggtgpAAGTKAT------TCTPGPWNIKRMLQAAD----GLPVNIGFLGKGNGSSPDALAEQIEAGA 214
|
....
gi 16080294 144 IGFK 147
Cdd:cd00375 215 CGLK 218
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
51-428 |
8.73e-12 |
|
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: 65.99 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 51 YVFPGVIDCHVHFN--------EPGREDWEGFETGSQMMAAGGCTTYFDMPLNcipsTVTAEHLLAKAELgrqKSAVDFA 122
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGAT----TSTGIEALLEAAE---ELPLGLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 123 LWGGLVPG-------HIEDIRPMAEAGAIGFKAFLSK----SGTDEFRSVDERTLLKGMAEIAA-AGKILALHA-ESDAI 189
Cdd:pfam01979 74 FLGPGCSLdtdgeleGRKALREKLKAGAEFIKGMADGvvfvGLAPHGAPTFSDDELKAALEEAKkYGLPVAIHAlETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 190 TSYLqmvlanKGKVDADAYAASRPEEAEVEAVYRTIQYAKVTGcpvhfVHISTAKAVRLIREAKqeglDVSVETCPhyvl 269
Cdd:pfam01979 154 VEDA------IAAFGGGIEHGTHLEVAESGGLLDIIKLILAHG-----VHLSPTEANLLAEHLK----GAGVAHCP---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 270 fshddlrqrgsvakcAPPLRSRQSKETLIETLIAGDIDMVSSDHspcrpslkrednmflswgGISGGQFTLLGMLELALE 349
Cdd:pfam01979 215 ---------------FSNSKLRSGRIALRKALEDGVKVGLGTDG------------------AGSGNSLNMLEELRLALE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 350 HQ------IPFETIAEWTAAAPAKRFGL-QKKGRLEAGCDADFVLvsmepytvtresmFAKHKKSIYEGHTFPCSISATY 422
Cdd:pfam01979 262 LQfdpeggLSPLEALRMATINPAKALGLdDKVGSIEVGKDADLVV-------------VDLDPLAAFFGLKPDGNVKKVI 328
|
....*.
gi 16080294 423 SKGRCV 428
Cdd:pfam01979 329 VKGKIV 334
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
2-147 |
1.55e-11 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 66.27 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 2 AYDMVIKGAKAVTP-DGVIEADIVVQNGVIAEIGSD-------------IEASGTEIIQADGKYVFPGVIDCHVHFNEPG 67
Cdd:PRK13308 67 ALDFVLCNVTVIDPvLGIVKGDIGIRDGRIVGIGKAgnpdimdgvdprlVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 68 REDwEGFETGSQMMAAGGCTTYFDMplnCIPSTVTAEHLLAKAElgrqKSAVDFALWGGLVPGHIEDIRPMAEAGAIGFK 147
Cdd:PRK13308 147 LVD-HALASGITTMLGGGLGPTVGI---DSGGPFNTGRMLQAAE----AWPVNFGFLGRGNSSKPAALIEQVEAGACGLK 218
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-77 |
2.64e-11 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 64.87 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 5 MVIKGAKAVTPDGVIEA--DIVVQNGVIAEIGSDIEAS-GTEIIQADGKYVFPGVIDCHVHFNePGREDWE------GFE 75
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSqAKKVIDLSGLYVSPGWIDLHVHVY-PGSTPYGdepdevGVR 79
|
..
gi 16080294 76 TG 77
Cdd:PRK09237 80 SG 81
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-431 |
5.45e-11 |
|
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: 64.08 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 4 DMVIKGAKAVTPD---GVIE-ADIVVQNGVIAEIGSDIEA----SGTEIIQADGKYVFPGVIDCHVHF---------NEP 66
Cdd:COG0402 1 DLLIRGAWVLTMDpagGVLEdGAVLVEDGRIAAVGPGAELparyPAAEVIDAGGKLVLPGLVNTHTHLpqtllrglaDDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 67 GREDW--------------EGFETGSQM----MAAGGCTTYFDMplncipstvtaehllakaelgrqksavdfalwGGLV 128
Cdd:COG0402 81 PLLDWleeyiwplearldpEDVYAGALLalaeMLRSGTTTVADF--------------------------------YYVH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 129 PGHIEDIrpMAEAGAIGFKAFLSKSGTD-EFRSVDERTLLKGMAEIAAAgkILALHAESDAITSYlqmvlankgkvdadA 207
Cdd:COG0402 129 PESADAL--AEAAAEAGIRAVLGRGLMDrGFPDGLREDADEGLADSERL--IERWHGAADGRIRV--------------A 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 208 YAASRPEEAEVEAVYRTIQYAKVTGCPVHfVHIS-TAKAVRLIRE----------AKQEGLDVSVeTCPHYVLFSHDD-- 274
Cdd:COG0402 191 LAPHAPYTVSPELLRAAAALARELGLPLH-THLAeTRDEVEWVLElygkrpveylDELGLLGPRT-LLAHCVHLTDEEia 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 275 -LRQRG-SVAKC----------APPLRSrqsketlietLIAGDIDM-VSSDHSPCRPSLkredNMFLSwggisggqftll 341
Cdd:COG0402 269 lLAETGaSVAHCptsnlklgsgIAPVPR----------LLAAGVRVgLGTDGAASNNSL----DMFEE------------ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 342 gMLELALEHQ--------IPFETIAEWTAAAPAKRFGLQKK-GRLEAGCDADFVLVSME-PYTVTRESMFAKHkksIYEG 411
Cdd:COG0402 323 -MRLAALLQRlrggdptaLSAREALEMATLGGARALGLDDEiGSLEPGKRADLVVLDLDaPHLAPLHDPLSAL---VYAA 398
|
490 500
....*....|....*....|
gi 16080294 412 HtfPCSISATYSKGRCVYND 431
Cdd:COG0402 399 D--GRDVRTVWVAGRVVVRD 416
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
4-60 |
1.61e-10 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 62.50 E-value: 1.61e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 16080294 4 DMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIeASGTEIIQADGKYVFPGVIDCH 60
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGA-SALPGAIDAEGDYLLPGLVDLH 58
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
2-147 |
3.27e-10 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 62.12 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 2 AYDMVIKGAKAVTPDGVIEADIVVQNGVIAEIGS----DIEA-------SGTEIIQADGKYVFPGVIDCHVHFNEPgRED 70
Cdd:PRK13207 66 AVDTVITNALILDHWGIVKADIGIKDGRIVAIGKagnpDIQDgvdiiigPGTEVIAGEGLIVTAGGIDTHIHFICP-QQI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 71 WEGFETGSQMMAAGG--------CTTyfdmplnCIPSTVTAEHLLAKAE--------LGRQKSAVDFALwgglvpghIED 134
Cdd:PRK13207 145 EEALASGVTTMIGGGtgpatgtnATT-------CTPGPWHIHRMLQAADafpmnigfLGKGNASLPEAL--------EEQ 209
|
170
....*....|...
gi 16080294 135 IrpmaEAGAIGFK 147
Cdd:PRK13207 210 I----EAGAIGLK 218
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
5-62 |
4.74e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 61.17 E-value: 4.74e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16080294 5 MVIKGAKAVTPDGVI----EADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVH 62
Cdd:PRK08204 4 TLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRH 65
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-63 |
6.48e-10 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 61.27 E-value: 6.48e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16080294 4 DMVIKGAKAVtpD----GVIEADIVVQNGVIAEIGsDIEASGTEIIQADGKYVFPGVIDCHVHF 63
Cdd:COG1001 6 DLVIKNGRLV--NvftgEILEGDIAIAGGRIAGVG-DYIGEATEVIDAAGRYLVPGFIDGHVHI 66
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
5-92 |
8.30e-10 |
|
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: 60.29 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 5 MVIKGAKAVT--PDGVIE-ADIVVQNGVIAEIGSDIEA---SGTEIIQADGKYVFPGVIDCHVHFNE-PGR--------E 69
Cdd:cd01298 1 ILIRNGTIVTtdPRRVLEdGDVLVEDGRIVAVGPALPLpayPADEVIDAKGKVVMPGLVNTHTHLAMtLLRgladdlplM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16080294 70 DW--------------EGFETGSQ----MMAAGGCTTYFDM 92
Cdd:cd01298 81 EWlkdliwplerllteEDVYLGALlalaEMIRSGTTTFADM 121
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
27-396 |
8.80e-10 |
|
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: 60.02 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 27 NGVIAEIGSDIEA-SGTEIIQADGKYVFPGVIDCHVH---FNEP-GREDWEGFETGSQMMA------------------- 82
Cdd:cd01309 1 DGKIVAVGAEITTpADAEVIDAKGKHVTPGLIDAHSHlglDEEGgVRETSDANEETDPVTPhvraidginpddeafkrar 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 83 AGGCTTYFDMP--LNCIpstvtaehllakaelGRQKSAVDFALWgglvpghieDIRPMAEAGAIGFKAFLsksGTDEFRS 160
Cdd:cd01309 81 AGGVTTVQVLPgsANLI---------------GGQGVVIKTDGG---------TIEDMFIKAPAGLKMAL---GENPKRV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 161 VDERTLLKG--MAEIAAAGKILALHAEsdaitsYLQmvLANKGKVDADAYAASRPE-EAEVEAVYRTIqyakvtgcPVHf 237
Cdd:cd01309 134 YGGKGKEPAtrMGVAALLRDAFIKAQE------YGR--KYDLGKNAKKDPPERDLKlEALLPVLKGEI--------PVR- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 238 VHISTAKAVR-LIREAKQEGLDVSVETCPH-YVLFSHddLRQRGSVAKCAPPLRSRQSKETLIETLiagDIDMVSSDHSP 315
Cdd:cd01309 197 IHAHRADDILtAIRIAKEFGIKITIEHGAEgYKLADE--LAKHGIPVIYGPTLTLPKKVEEVNDAI---DTNAYLLKKGG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 316 CRPSLKREDNmflswggISGGQFTLLgMLELALEHQIPFETIAEWTAAAPAKRFGL-QKKGRLEAGCDADFVLVSMEPYT 394
Cdd:cd01309 272 VAFAISSDHP-------VLNIRNLNL-EAAKAVKYGLSYEEALKAITINPAKILGIeDRVGSLEPGKDADLVVWNGDPLE 343
|
..
gi 16080294 395 VT 396
Cdd:cd01309 344 PT 345
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
57-367 |
5.24e-09 |
|
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: 56.96 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 57 IDCHVHF----NEPGREDWEG--------------FETGSQMMAAGGCTTYFDMPLNCIPSTvTAEHLLAKAELGRQKSA 118
Cdd:cd01292 2 IDTHVHLdgsaLRGTRLNLELkeaeelspedlyedTLRALEALLAGGVTTVVDMGSTPPPTT-TKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 119 VDFALWGGL-----------VPGHIEDIRPMAEAGAIGFKAFlsksGTDEFRSVDERTLLKGMAEIAAAGKILALHAESd 187
Cdd:cd01292 81 IRVVLGLGIpgvpaavdedaEALLLELLRRGLELGAVGLKLA----GPYTATGLSDESLRRVLEEARKLGLPVVIHAGE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 188 aitsylqmvlankgkvdadayaasrpEEAEVEAVYRTIQYAKVtGCPVHFVHIS--TAKAVRLIREAkqeglDVSVETCP 265
Cdd:cd01292 156 --------------------------LPDPTRALEDLVALLRL-GGRVVIGHVShlDPELLELLKEA-----GVSLEVCP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 266 HYVLFSHddlrqrgsvakcapplRSRQSKETLIETLIAGDIDMVSSDHSPcrpslkrednmflswGGISGGQFTLLGMLE 345
Cdd:cd01292 204 LSNYLLG----------------RDGEGAEALRRLLELGIRVTLGTDGPP---------------HPLGTDLLALLRLLL 252
|
330 340
....*....|....*....|..
gi 16080294 346 LALEHQIPFETIAEWTAAAPAK 367
Cdd:cd01292 253 KVLRLGLSLEEALRLATINPAR 274
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-63 |
9.76e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 57.50 E-value: 9.76e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080294 4 DMVIKGAKAVTPDG---VIEAdIVVQNGVIAEIGSDIEA-----SGTEIIQADGKYVFPGVIDCHVHF 63
Cdd:COG1574 9 DLLLTNGRIYTMDPaqpVAEA-VAVRDGRIVAVGSDAEVralagPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
22-91 |
1.09e-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: 56.57 E-value: 1.09e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16080294 22 DIVVQNGVIAEIGSDIEAS-GTEIIQADGKYVFPGVIDCHVHFNepgredWEGFETG---SQMMAAGGCTTYFD 91
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPaATQIVDAGGCYVSPGWIDLHVHVY------QGGTRYGdrpDMIGVKSGVTTVVD 68
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
22-83 |
2.73e-08 |
|
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: 55.78 E-value: 2.73e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16080294 22 DIVVQNGVIAEIGSDIEA-----SGTEIIQADGKYVFPGVIDCHVHFNEPGRE----DWEGFETGSQMMAA 83
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAkalkgPATEVIDLKGKTVLPGFIDSHSHLLLGGLSllwlDLSGVTSKEEALAR 71
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
6-411 |
3.10e-08 |
|
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: 55.47 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 6 VIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEASG---TEIIQADGKYVFPGVIDCHVHFNEPGREdwEGFETG----- 77
Cdd:cd01308 3 LIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGyenVTVVDLHGKILVPGFIDQHVHIIGGGGE--GGPSTRtpevt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 78 -SQMMAAGGCTTyfdmpLNCIPS---TVTAEHLLAKAELGRQKSAVDFALWGGL-VP-----GHIE-DIrpmaeagaigf 146
Cdd:cd01308 81 lSDLTTAGVTTV-----VGCLGTdgiSRSMEDLLAKARALEEEGITCFVYTGSYeVPtrtitGSIRkDL----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 147 kAFLSKS-GTDEFRSVDERT---LLKGMAEIAAAGKILALHAESDAITsYLQMVLANKGkvdadayaasrpeeaeVEAVY 222
Cdd:cd01308 145 -LLIDKViGVGEIAISDHRSsqpTVEELARIAAEARVGGLLGGKAGIV-HIHLGDGKRA----------------LSPIF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 223 RTIQyakVTGCPV-HFVHISTAKAVRL----IREAKQEG-LDVSVETCPhyvlFSHDDlrqrgsvakcaPPLRSRQSKET 296
Cdd:cd01308 207 ELIE---ETEIPItQFLPTHINRTAPLfeqgVEFAKMGGtIDLTSSIDP----QFRKE-----------GEVRPSEALKR 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 297 LIETLIAGDIDMVSSDHSPCRPSLKREDNmfLSWGGISGGQFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLQKKGR 376
Cdd:cd01308 269 LLEQGVPLERITFSSDGNGSLPKFDENGN--LVGLGVGSVDTLLREVREAVKCGDIPLEVALRVITSNVARILKLRKKGE 346
|
410 420 430
....*....|....*....|....*....|....*
gi 16080294 377 LEAGCDADFVLVSMEpytVTRESMFAKHKKSIYEG 411
Cdd:cd01308 347 IQPGFDADLVILDKD---LDINSVIAKGQIMVRNG 378
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-429 |
3.33e-08 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 55.15 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 1 MAYDMVIKGAKAVTPDG--VIEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVHFNEPGRedwEGFETGS 78
Cdd:PRK12394 1 MKNDILITNGHIIDPARniNEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAHVFYDGT---EGGVRPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 79 QMMAAGGCTTYFDM-PLNCIPSTVTAEHLLAKAELgRQKSAVDFALWGGLVPGHIEDIRPmaeagaigfkaflsksgtde 157
Cdd:PRK12394 78 MYMPPNGVTTVVDAgSAGTANFDAFYRTVICASKV-RIKAFLTVSPPGQTWSGYQENYDP-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 158 fRSVDERtllkgmaeiaaagKILALHAEsdaitsYLQMVLANKGKVDADAYA--ASRPEEaeveavyRTIQYAKVTGCP- 234
Cdd:PRK12394 137 -DNIDEN-------------KIHALFRQ------YRNVLQGLKLRVQTEDIAeyGLKPLT-------ETLRIANDLRCPv 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 235 -VHFVH--ISTAKAVRLIREAK-----QEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPlRSRQSKETLIETLIAGDI 306
Cdd:PRK12394 190 aVHSTHpvLPMKELVSLLRRGDiiahaFHGKGSTILTEEGAVLAEVRQARERGVIFDAANG-RSHFDMNVARRAIANGFL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 307 -DMVSSDHSpcrPSLKREDNMflswggisggqFTLLGMLELALEHQIPFETIAEWTAAAPAKRFGLQKK-GRLEAGCDAD 384
Cdd:PRK12394 269 pDIISSDLS---TITKLAWPV-----------YSLPWVLSKYLALGMALEDVINACTHTPAVLMGMAAEiGTLAPGAFAD 334
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16080294 385 FVLVSMepytVTRESMFAKHKKSIYEGHTF--PCsisATYSKGRCVY 429
Cdd:PRK12394 335 IAIFKL----KNRHVEFADIHGETLTGTHVlvPQ---MTIKSGEILY 374
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
2-147 |
7.86e-08 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 54.72 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 2 AYDMVIKGAKAVTPDGVIEADIVVQNGVIAEIGS----DIE---------ASGTEIIQADGKYVFPGVIDCHVHFNEPGR 68
Cdd:PRK13206 70 APDTVITGAVILDHWGIVKADVGIRDGRIVAIGKagnpDIMdgvhpdlviGPSTEIIAGNGRILTAGAIDCHVHFICPQI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 69 EDwEGFETGSQMMAAGGCTtyfdmplnciPS------TVT--AEHllakaeLGRQKSAVD-----FALWG-GLVPGHiED 134
Cdd:PRK13206 150 VD-EALAAGITTLIGGGTG----------PAegskatTVTpgAWH------LARMLEALDgwpvnVALLGkGNTVSA-EA 211
|
170
....*....|...
gi 16080294 135 IRPMAEAGAIGFK 147
Cdd:PRK13206 212 LWEQLRGGAGGFK 224
|
|
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
2-147 |
1.04e-07 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 53.99 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 2 AYDMVIKGAKAVTPDGVIEADIVVQNGVIAEIGS----DIEA---------SGTEIIQADGKYVFPGVIDCHVHFNEPgR 68
Cdd:COG0804 66 ALDLVITNAVILDHWGIVKADIGIKDGRIVGIGKagnpDTMDgvdpdlvigPGTEVIAGEGLILTAGGIDTHIHFICP-Q 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 69 EDWEGFETGSQMMAAGG--------CTTyfdmplnCIPSTVTAEHLLAKAE--------LGRQKSAVDFALWgglvpghi 132
Cdd:COG0804 145 QIEEALASGITTMIGGGtgpaegtnATT-------CTPGPWNIARMLEAADalpmnigfLGKGNASSPEALE-------- 209
|
170
....*....|....*
gi 16080294 133 EDIRpmaeAGAIGFK 147
Cdd:COG0804 210 EQIR----AGACGLK 220
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
4-62 |
3.01e-07 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 52.33 E-value: 3.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 16080294 4 DMVIKGAKavTPDGVIEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVH 62
Cdd:PRK07572 3 DLIVRNAN--LPDGRTGIDIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFH 59
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
74-429 |
2.61e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 49.45 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 74 FETGSQMMAAGGCTTYFDMPLNcIPSTVTAEHLLAKAelgrqksavdFALWGGLVPG--HIEDIRPMAEAGAIGFKAFLS 151
Cdd:pfam07969 181 YEPLRELTAAEKLKELLDAPER-LGLPHSIYELRIGA----------MKLFADGVLGsrTAALTEPYFDAPGTGWPDFED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 152 KSGTDEFRSVDERTLLkgmaeiaaagkiLALHAESDAITSYLQMVLANKGKVDADaYAASRPEEAEVEAVYRTiqyakvt 231
Cdd:pfam07969 250 EALAELVAAARERGLD------------VAIHAIGDATIDTALDAFEAVAEKLGN-QGRVRIEHAQGVVPYTY------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 232 gcpvhfvhistakavRLIREAKQEGLDVSVETCPHYVLFSHDDLRQRGSVAKCAPPLRsrqsketliETLIAGDIDMVSS 311
Cdd:pfam07969 310 ---------------SQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVK---------ELLNAGVKVALGS 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 312 DHSPCRPSlkrednmflSWGGISGGqFTL--LGMLELALEHQ-IPFETIAEWTAAAPAKRFGL-QKKGRLEAGCDADFVL 387
Cdd:pfam07969 366 DAPVGPFD---------PWPRIGAA-VMRqtAGGGEVLGPDEeLSLEEALALYTSGPAKALGLeDRKGTLGVGKDADLVV 435
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16080294 388 VSMEPYTVTRESMFAKhkksiyeghtfpcSISATYSKGRCVY 429
Cdd:pfam07969 436 LDDDPLTVDPPAIADI-------------RVRLTVVDGRVVY 464
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
5-62 |
6.92e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 48.26 E-value: 6.92e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 5 MVIKGAKAVTPDG--VIEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVH 62
Cdd:PRK08393 3 ILIKNGYVIYGENlkVIRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTH 62
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
4-62 |
7.07e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 48.07 E-value: 7.07e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16080294 4 DMVIKGAKAVTPDG---VIEADIVVQNGVIAEIGSDIEASGT-EIIQADGKYVFPGVIDCHVH 62
Cdd:PRK07228 2 TILIKNAGIVTMNAkreIVDGDVLIEDDRIAAVGDRLDLEDYdDHIDATGKVVIPGLIQGHIH 64
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
4-62 |
1.36e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 47.05 E-value: 1.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16080294 4 DMVIKGAKAVTPD--GVIEADIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVH 62
Cdd:PRK06038 3 DIIIKNAYVLTMDagDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTH 63
|
|
| PLN02303 |
PLN02303 |
urease |
4-147 |
1.49e-05 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 47.44 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 4 DMVIKGAKAVTPDGVIEADIVVQNGVIAEIGSD-------------IEASGTEIIQADGKYVFPGVIDCHVHFNEPGRED 70
Cdd:PLN02303 335 DTVITNAVIIDYTGIYKADIGIKDGLIVGIGKAgnpdvmdgvtsnmIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQLAT 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 71 wEGFETGSQMMAAGG-------CTTyfdmplNCIPSTVTAEHLLAKAElgrqKSAVDFALWGGLVPGHIEDIRPMAEAGA 143
Cdd:PLN02303 415 -EAIASGITTLVGGGtgpahgtCAT------TCTPAPSHMKLMLQSTD----DLPLNFGFTGKGNTAKPEGLHEIIKAGA 483
|
....
gi 16080294 144 IGFK 147
Cdd:PLN02303 484 MGLK 487
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
7-388 |
1.54e-05 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 46.86 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 7 IKGAKAVTPDGVIeADIVVQNGVIAEIGSDIEASGT-EIIQADGKYVFPGVIDCHVHFNEpgredwegfetgsqmmaagg 85
Cdd:cd01293 2 LRNARLADGGTAL-VDIAIEDGRIAAIGPALAVPPDaEEVDAKGRLVLPAFVDPHIHLDK-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 86 cTTYFDMPLNCIPSTVTAEHLL-AKAELGRQKsavdfalwgglvpghiEDIRPMAEAGAigfkAFLSKSGTDEFRS---V 161
Cdd:cd01293 61 -TFTGGRWPNNSGGTLLEAIIAwEERKLLLTA----------------EDVKERAERAL----ELAIAHGTTAIRThvdV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 162 DER---TLLKGMAEIAAAGKilalhaesDAITsyLQMV-------LANKGKVD-----ADAYAA-------SRPEEAEVE 219
Cdd:cd01293 120 DPAaglKALEALLELREEWA--------DLID--LQIVafpqhglLSTPGGEElmreaLKMGADvvggippAEIDEDGEE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 220 AVYRTIQYAKVTGCPV--HfVHISTAKAVR----LIREAKQEGLDVSVeTCPHyvLFSHDDLrqrgsvakcapplrSRQS 293
Cdd:cd01293 190 SLDTLFELAQEHGLDIdlH-LDETDDPGSRtleeLAEEAERRGMQGRV-TCSH--ATALGSL--------------PEAE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 294 KETLIETLIAGDIDMVSS-----------DHSPCRPSLKR--------------EDNMFLSWGgiSGGQFTLLGMLELAL 348
Cdd:cd01293 252 VSRLADLLAEAGISVVSLppinlylqgreDTTPKRRGVTPvkelraagvnvalgSDNVRDPWY--PFGSGDMLEVANLAA 329
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 16080294 349 E-HQI--PFETIAEWTAAAPAKRFGL-QKKGRLEAGCDADFVLV 388
Cdd:cd01293 330 HiAQLgtPEDLALALDLITGNAARALgLEDYGIKVGCPADLVLL 373
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
4-147 |
1.91e-05 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 46.81 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 4 DMVIKGAKAVTPDGVIEADIVVQNGVIAEIGS----DIEAS---------GTEIIQADGKYVFPGVIDCHVHFNEPgRED 70
Cdd:PRK13985 66 DLIITNALIIDYTGIYKADIGIKDGKIAGIGKggnkDMQDGvknnlsvgpATEALAGEGLIVTAGGIDTHIHFISP-QQI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 71 WEGFETGSQMMAAGG--------CTTyfdmplnCIPSTVTAEHLLAKAElgrqKSAVDFALWGGLVPGHIEDIRPMAEAG 142
Cdd:PRK13985 145 PTAFASGVTTMIGGGtgpadgtnATT-------ITPGRRNLKWMLRAAE----EYSMNLGFLGKGNSSNDASLADQIEAG 213
|
....*
gi 16080294 143 AIGFK 147
Cdd:PRK13985 214 AIGFK 218
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
23-393 |
2.00e-05 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 46.48 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 23 IVVQNGVIAEIGS-----DIEASGTEIIQADGKYVFPGVIDCHVH--FNEPGREDWEGFETG---SQMMAAGGcttyfdm 92
Cdd:cd01296 1 IAIRDGRIAAVGPaaslpAPGPAAAEEIDAGGRAVTPGLVDCHTHlvFAGDRVDEFAARLAGasyEEILAAGG------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 93 plnCIPSTVTA------EHLLAKAelgrqksavdfalwgglvpghIEDIRPMAEAGAIGFKAflsKSG----TDefrsvD 162
Cdd:cd01296 74 ---GILSTVRAtraaseDELFASA---------------------LRRLARMLRHGTTTVEV---KSGygldLE-----T 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 163 ERTLLKGMAEIAAAGKI------LALHA---ESDAITSYLQMV-------LANKGKVD-ADAYAasrpEEA--EVEAVYR 223
Cdd:cd01296 122 ELKMLRVIRRLKEEGPVdlvstfLGAHAvppEYKGREEYIDLVieevlpaVAEENLADfCDVFC----EKGafSLEQSRR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 224 TIQYAKVTGCPV--HFVHISTAKAVRLIREAKQegldVSVEtcpHYVLFSHDD---LRQRGSVAK---------CAPPLR 289
Cdd:cd01296 198 ILEAAKEAGLPVkiHADELSNIGGAELAAELGA----LSAD---HLEHTSDEGiaaLAEAGTVAVllpgtafslRETYPP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 290 SRQsketLIEtliAGDIDMVSSDHSPcrpslkreDNMFLSwggisggqfTLLGMLELA--LEHQIPFETIAEWTAAApAK 367
Cdd:cd01296 271 ARK----LID---AGVPVALGTDFNP--------GSSPTS---------SMPLVMHLAcrLMRMTPEEALTAATINA-AA 325
|
410 420
....*....|....*....|....*..
gi 16080294 368 RFGLQKK-GRLEAGCDADFVLVSMEPY 393
Cdd:cd01296 326 ALGLGETvGSLEVGKQADLVILDAPSY 352
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
5-63 |
8.62e-05 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 44.54 E-value: 8.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16080294 5 MVIKGAKAVTPD---GVIE-ADIVVQNGVIAEIGSDIEASGT----EIIQADGKYVFPGVIDCHVHF 63
Cdd:PRK07203 2 LLIGNGTAITRDpakPVIEdGAIAIEGNVIVEIGTTDELKAKypdaEFIDAKGKLIMPGLINSHNHI 68
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
12-62 |
8.74e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 44.59 E-value: 8.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 16080294 12 AVTPDGVIEADIVVQNGVIAEIG-SDIEASGTEIIQADGKYVFPGVIDCHVH 62
Cdd:PRK07583 32 GDTLEGLVLVDIEIADGKIAAILpAGGAPDELPAVDLKGRMVWPCFVDMHTH 83
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
357-441 |
1.71e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 44.03 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 357 IAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSMEPYTVT---RESMFAKHKksiyegHTFpcsisatysK-GRCVYNDG 432
Cdd:COG1229 434 IAIMTRAGPAKALGLADRGHLGVGADADIAIYDINPDDKDyedIEKMFSKPA------YVI---------KdGEVVVKDG 498
|
....*....
gi 16080294 433 EKVTEIDGA 441
Cdd:COG1229 499 EIVATPQGR 507
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
6-110 |
2.75e-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: 42.85 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 6 VIKGAKAVTPDGVIEADIVVQNGVIAEIGSDIEASG-----TEIIQADGKYVFPGVIDCHVHFNEPGREDweGFETGSQM 80
Cdd:TIGR01975 3 LLKGAEVYAPEYIGKKDILIANDKIIAIADEIPSTKdfvpnCVVVGLEGMIAVPGFIDQHVHIIGGGGEG--GPTTRTPE 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 16080294 81 MA-----AGGCTTYfdmpLNCIPS---TVTAEHLLAKA 110
Cdd:TIGR01975 81 LTlsditKGGVTTV----VGLLGTdgiTRHMESLLAKA 114
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
14-63 |
3.96e-04 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 42.65 E-value: 3.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16080294 14 TPDGVIEAD--IVVQNGVIAEIGSDIEASG------------TEIIQADGKYVFPGVIDCHVHF 63
Cdd:cd01303 11 LPELELVEDalRVVEDGLIVVVDGNIIAAGaaetlkraakpgARVIDSPNQFILPGFIDTHIHA 74
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
4-62 |
1.16e-03 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 41.21 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16080294 4 DMVIKGAKAVTPDGVIEA------DIVVQNGVIAEIGSDIEASGTEIIQADGKYVFPGVIDCHVH 62
Cdd:PRK12393 3 SLLIRNAAAIMTGLPGDAarlggpDIRIRDGRIAAIGALTPLPGERVIDATDCVVYPGWVNTHHH 67
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
6-63 |
1.24e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 40.99 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16080294 6 VIKGAKAVTPDG----VIEADIVVQNGVIAEIG--SDIEASGTEIIQADGKYVFPGVIDCHVHF 63
Cdd:PRK08203 5 IKNPLAIVTMDAarreIADGGLVVEGGRIVEVGpgGALPQPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
15-63 |
1.29e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 40.94 E-value: 1.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 16080294 15 PDGVIeadiVVQNGVIAEIGS--DIEAS---GTEIIQADGKYVFPGVIDCHVHF 63
Cdd:PRK09228 30 EDGLL----LVEDGRIVAAGPyaELRAQlpaDAEVTDYRGKLILPGFIDTHIHY 79
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
347-443 |
1.88e-03 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 40.47 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 347 ALEHQIPFETIAEWTAAAPAKRFGLQKKGRLEAGCDADFVLVSMEPYTVtresmfakhKKSIYEghtfpcSISATYSKGR 426
Cdd:cd01304 422 GIDREYSLYEIAIMTRAGPAKLLGLSDKGHLGVGADADIAIYDDDPDQV---------DPSDYE------KVEKAFSRAA 486
|
90
....*....|....*..
gi 16080294 427 CVYNDGEKVTEiDGALV 443
Cdd:cd01304 487 YVLKDGEIVVK-DGEVV 502
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
5-62 |
2.19e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 40.25 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16080294 5 MVIKGAKAVTPDG---VIEADIVVQNGVIAEIGsDIEASGTEIIQADGKYVFPGVIDCHVH 62
Cdd:PRK06380 3 ILIKNAWIVTQNEkreILQGNVYIEGNKIVYVG-DVNEEADYIIDATGKVVMPGLINTHAH 62
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
298-390 |
2.40e-03 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 39.96 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 298 IETLIAGDIDMVSSDHSPcrPSLkrednmflswggisggqftLLGMLELALEHQIPFETIAEWTAAAPAKRFGLQKKGRL 377
Cdd:cd01306 240 RELAAHGLLDILSSDYVP--ASL-------------------LHAAFRLADLGGWSLPEAVALVSANPARAVGLTDRGSI 298
|
90
....*....|...
gi 16080294 378 EAGCDADFVLVSM 390
Cdd:cd01306 299 APGKRADLILVDD 311
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
17-387 |
6.53e-03 |
|
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: 38.83 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 17 GVIEADIVVQNGVIaeigsDIEASGteiiQADGKYVFPGVIDCHVHFNEPGREDW-EGFETGSQMMAAGGCTTYFDMPLN 95
Cdd:cd01300 136 GITRDTPDPPGGEI-----VRDADG----EPTGVLVEAAAALVLEAVPPPTPEERrAALRAAARELASLGVTTVHDAGGG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 96 cIPSTVTAEHLLAKAELGRQKSAV-------DFALWGGLVPGHIEDIRPMAEAGAI---------GFKAFLSKSGTD--- 156
Cdd:cd01300 207 -AADDIEAYRRLAAAGELTLRVRValyvsplAEDLLEELGARKNGAGDDRLRLGGVklfadgslgSRTAALSEPYLDspg 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 157 --EFRSVDERTLLKGMAEIAAAGKILALHAESDAITSylqMVLankgkvdaDAYAASRPEEAEVEAVYRtiqyakvtgcp 234
Cdd:cd01300 286 tgGLLLISPEELEELVRAADEAGLQVAIHAIGDRAVD---TVL--------DALEAALKDNPRADHRHR----------- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16080294 235 vhFVHISTAKAvRLIREAKQEGLDVSVEtcPHYVLF---SHDDLRQRGSVAKCAPPLRSRQSKetliETLIAGdidmvSS 311
Cdd:cd01300 344 --IEHAQLVSP-DDIPRFAKLGVIASVQ--PNHLYSdgdAAEDRRLGEERAKRSYPFRSLLDA----GVPVAL-----GS 409
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16080294 312 DHSPCRPslkreDNMFLSWGGISGGQftlLGMLELALEHQ-IPFET-IAEWTAAAPAKRFGLQKKGRLEAGCDADFVL 387
Cdd:cd01300 410 DAPVAPP-----DPLLGIWAAVTRKT---PGGGVLGNPEErLSLEEaLRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| |
