|
Name |
Accession |
Description |
Interval |
E-value |
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
3-399 |
3.20e-171 |
|
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: 485.17 E-value: 3.20e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 3 ILIKNVL----FNDRTI---DIYIEGKEIKQIGEGL---SFPADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLM 72
Cdd:cd01298 1 ILIRNGTivttDPRRVLedgDVLVEDGRIVAVGPALplpAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDLPLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 73 PWLEQKIWPNEAKMTREDVYWGAKLACLEMIKSGTTTFFDMYQRPR-VTADVTEEMGLRGIIAGVCFD--GFDKEEAEKC 149
Cdd:cd01298 81 EWLKDLIWPLERLLTEEDVYLGALLALAEMIRSGTTTFADMYFFYPdAVAEAAEELGIRAVLGRGIMDlgTEDVEETEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 150 KRHNERLIQDVDNYSK-RVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVRYLYKLG 228
Cdd:cd01298 161 LAEAERLIREWHGAADgRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEKYGKRPVEYLEELG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 229 VLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIhFKFKEMRQLGITVGLGTDGCSSSNNLDMIEAMKLAS 308
Cdd:cd01298 241 LLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGI-APVPEMLEAGVNVGLGTDGAASNNNLDMFEEMRLAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 309 LLGKAWRKDPEALTANEMLQAATAEGAAMFGLK-AGQIKEGYLADLCLIDLNTPAFTPNFNFVSNLVYAANGSCVDTVIC 387
Cdd:cd01298 320 LLQKLAHGDPTALPAEEALEMATIGGAKALGLDeIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYSANGGDVDTVIV 399
|
410
....*....|..
gi 496047653 388 DGKILMENKKVP 399
Cdd:cd01298 400 NGRVVMEDGELL 411
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-395 |
1.48e-170 |
|
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: 483.56 E-value: 1.48e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 2 SILIKNVLF----NDRTI----DIYIEGKEIKQIGEGLS----FPADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDM 69
Cdd:COG0402 1 DLLIRGAWVltmdPAGGVledgAVLVEDGRIAAVGPGAElparYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 70 PLMPWLEQKIWPNEAKMTREDVYWGAKLACLEMIKSGTTTFFDMY----QRPRVTADVTEEMGLRGIIAGVCFD----GF 141
Cdd:COG0402 81 PLLDWLEEYIWPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYyvhpESADALAEAAAEAGIRAVLGRGLMDrgfpDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 142 DKEEAEKCKRHNERLIQDVDNYSK-RVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGLTP 220
Cdd:COG0402 161 LREDADEGLADSERLIERWHGAADgRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYGKRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 221 VRYLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIhFKFKEMRQLGITVGLGTDGCSSSNNLDM 300
Cdd:COG0402 241 VEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGI-APVPRLLAAGVRVGLGTDGAASNNSLDM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 301 IEAMKLASLLGKAWRKDPEALTANEMLQAATAEGAAMFGL--KAGQIKEGYLADLCLIDLNTPAFTPNFNFVSNLVYAAN 378
Cdd:COG0402 320 FEEMRLAALLQRLRGGDPTALSAREALEMATLGGARALGLddEIGSLEPGKRADLVVLDLDAPHLAPLHDPLSALVYAAD 399
|
410
....*....|....*..
gi 496047653 379 GSCVDTVICDGKILMEN 395
Cdd:COG0402 400 GRDVRTVWVAGRVVVRD 416
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
2-418 |
1.67e-146 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 423.39 E-value: 1.67e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 2 SILIKN--VLFND----RTIDIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLMPWL 75
Cdd:PRK06038 3 DIIIKNayVLTMDagdlKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 76 EQKIWPNEAKMTREDVYWGAKLACLEMIKSGTTTFFDMYQRPRVTADVTEEMGLRGIIAGVCFDGFDKEEAEKCKRHNER 155
Cdd:PRK06038 83 NDHIWPAEAKLTAEDVYAGSLLACLEMIKSGTTSFADMYFYMDEVAKAVEESGLRAALSYGMIDLGDDEKGEAELKEGKR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 156 LIQDVDNYSK-RVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVRYLYKLGVLSPRL 234
Cdd:PRK06038 163 FVKEWHGAADgRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQYGMCSVNYLDDIGFLGPDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 235 IIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIHfKFKEMRQLGITVGLGTDGCSSSNNLDMIEAMKLASLLGKAW 314
Cdd:PRK06038 243 LAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIA-PVPKLLERGVNVSLGTDGCASNNNLDMFEEMKTAALLHKVN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 315 RKDPEALTANEMLQAATAEGAAMFGLKAGQIKEGYLADLCLIDLNTPAFTPNFNFVSNLVYAANGSCVDTVICDGKILME 394
Cdd:PRK06038 322 TMDPTALPARQVLEMATVNGAKALGINTGMLKEGYLADIIIVDMNKPHLTPVRDVPSHLVYSASGSDVDTTIVDGRILME 401
|
410 420
....*....|....*....|....*.
gi 496047653 395 NKKVPGEDE--IMEKATEIAYNLMKR 418
Cdd:PRK06038 402 DYKVLCMDEqdVMEDAKKAAEELVSR 427
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-415 |
2.03e-146 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 422.67 E-value: 2.03e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 1 MSILIKN--VLFNDR----TIDIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLMPW 74
Cdd:PRK08393 1 MSILIKNgyVIYGENlkviRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTHSPMVLLRGLADDVPLMEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 75 LEQKIWPNEAKMTREDVYWGAKLACLEMIKSGTTTFFDMYQRPRVTADVTEEMGLRGIIAGVCFDGFDKEEAEKCKRHNE 154
Cdd:PRK08393 81 LQNYIWPRERKLKRKDIYWGAYLGLLEMIKSGTTTFVDMYFHMEEVAKATLEVGLRGYLSYGMVDLGDEEKREKEIKETE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 155 RLIQDVDNY-SKRVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVRYLYKLGVLSPR 233
Cdd:PRK08393 161 KLMEFIEKLnSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYGKSPVVLLDEIGFLNED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 234 LIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIhFKFKEMRQLGITVGLGTDGCSSSNNLDMIEAMKLASLLGKA 313
Cdd:PRK08393 241 VIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGV-MPLRKLLNAGVNVALGTDGAASNNNLDMLREMKLAALLHKV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 314 WRKDPEALTANEMLQAATAEGAAMFGLKAGQIKEGYLADLCLIDLNTPAFTPNFNFVSNLVYAANGSCVDTVICDGKILM 393
Cdd:PRK08393 320 HNLDPTIADAETVFRMATQNGAKALGLKAGVIKEGYLADIAVIDFNRPHLRPINNPISHLVYSANGNDVETTIVDGKIVM 399
|
410 420
....*....|....*....|....
gi 496047653 394 ENKKVPGEDE--IMEKATEIAYNL 415
Cdd:PRK08393 400 LDGEVLTLDEekILDKFLKVIEKL 423
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
33-410 |
5.75e-121 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 358.45 E-value: 5.75e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 33 FPADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLMPWLEQKIWPNEAKMTRED-VYWGAKLACLEMIKSGTTTFF 111
Cdd:PRK09045 51 YAAAETVELPDHVLIPGLINAHTHAAMSLLRGLADDLPLMTWLQDHIWPAEGAWVSEEfVRDGTLLAIAEMLRGGTTCFN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 112 DMYQRPRVTADVTEEMGLRGIIAGVCFDgFDKEEAEKCKRHNERLIQDVDNY--SKRVRFSIGPHAIYTVSGELLKWAHR 189
Cdd:PRK09045 131 DMYFFPEAAAEAAHQAGMRAQIGMPVLD-FPTAWASDADEYLAKGLELHDQWrhHPLISTAFAPHAPYTVSDENLERIRT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 190 FAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVRYLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLAS 269
Cdd:PRK09045 210 LAEQLDLPIHIHLHETAQEIADSLKQHGQRPLARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLAS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 270 GIHFKFKeMRQLGITVGLGTDGCSSSNNLDMIEAMKLASLLGKAWRKDPEALTANEMLQAATAEGAAMFGL--KAGQIKE 347
Cdd:PRK09045 290 GFCPVAK-LLQAGVNVALGTDGAASNNDLDLFGEMRTAALLAKAVAGDATALPAHTALRMATLNGARALGLddEIGSLEP 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496047653 348 GYLADLCLIDLNTPAFTPNFNFVSNLVYAANGSCVDTVICDGKILMENKKVPG--EDEIMEKATE 410
Cdd:PRK09045 369 GKQADLVAVDLSGLETQPVYDPVSQLVYAAGREQVSHVWVAGKQLLDDRELTTldEAELLARARQ 433
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-418 |
1.61e-107 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 324.26 E-value: 1.61e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 1 MSILIKN---VLFNDRTI----DIYIEGKEIKQIGEGLSFP-ADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLM 72
Cdd:PRK07228 1 MTILIKNagiVTMNAKREivdgDVLIEDDRIAAVGDRLDLEdYDDHIDATGKVVIPGLIQGHIHLCQTLFRGIADDLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 73 PWLEQKIWPNEAKMTREDVYWGAKLACLEMIKSGTTTFFDMyqrprVTADVTE-------EMGLRGIIAGVCFDGFD--- 142
Cdd:PRK07228 81 DWLKDRIWPLEAAHDAESMYYSALLGIGELIESGTTTIVDM-----ESVHHTDsafeaagESGIRAVLGKVMMDYGDdvp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 143 ---KEEAEKCKRHNERLIQDVDNYSK-RVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGL 218
Cdd:PRK07228 156 eglQEDTEASLAESVRLLEKWHGADNgRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEEETGM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 219 TPVRYLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIHfKFKEMRQLGITVGLGTDGCSSSNNL 298
Cdd:PRK07228 236 RNIHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIA-PVPDLLERGINVALGADGAPCNNTL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 299 DMIEAMKLASLLGKAWRKDPEALTANEMLQAATAEGAAMFGL--KAGQIKEGYLADLCLIDLNTPAFTPNF--NFVSNLV 374
Cdd:PRK07228 315 DPFTEMRQAALIQKVDRLGPTAMPARTVFEMATLGGAKAAGFedEIGSLEEGKKADLAILDLDGLHATPSHgvDVLSHLV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 496047653 375 YAANGSCVDTVICDGKILMENKKVPG--EDEIMEKATEIAYNLMKR 418
Cdd:PRK07228 395 YAAHGSDVETTMVDGKIVMEDGELTTidADAVRREANRSIKRLLKR 440
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-403 |
1.05e-103 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 313.74 E-value: 1.05e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 1 MSILIKNVLF----NDRTI---DIYIEGKEIKQIGEGLSFpADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLMP 73
Cdd:PRK06380 1 MSILIKNAWIvtqnEKREIlqgNVYIEGNKIVYVGDVNEE-ADYIIDATGKVVMPGLINTHAHVGMTASKGLFDDVDLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 74 WLEqKIWPNEAKMTREDVYWGAKLACLEMIKSGTTTFFDMYQRPRVTADVTEEMGLRGIIAGVCFDG-FDKEEAEKCKrH 152
Cdd:PRK06380 80 FLM-KTFKYDSKRTREGIYNSAKLGMYEMINSGITAFVDLYYSEDIIAKAAEELGIRAFLSWAVLDEeITTQKGDPLN-N 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 153 NERLIQDVDNySKRVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVRYLYKLGVLSP 232
Cdd:PRK06380 158 AENFIREHRN-EELVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEVYDHVKRTGERPVEHLEKIGFLNS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 233 RLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIHFKFKEMRQLGITVGLGTDGCSSSNNLDMIEAMKLASLLGK 312
Cdd:PRK06380 237 KLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGGSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALSVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 313 AWRKDPEALTANEMLQAATAEGAAMFGLKAGQIKEGYLADLCLIDLNTPAFTPNF--NFVSNLVYAANGSCVDTVICDGK 390
Cdd:PRK06380 317 NERWDASIIKAQEILDFATINAAKALELNAGSIEVGKLADLVILDARAPNMIPTRknNIVSNIVYSLNPLNVDHVIVNGK 396
|
410
....*....|...
gi 496047653 391 ILMENKKVPGEDE 403
Cdd:PRK06380 397 ILKENGRLNGFNP 409
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
17-403 |
1.15e-91 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 283.49 E-value: 1.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 17 IYIEGKEIKQIGEG---LSFPADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLMPWLEQKIWPNEAKMTREDVYW 93
Cdd:PRK15493 25 IIVENDQIIDVNSGefaSDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFTPELAVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 94 GAKLACLEMIKSGTTTFFDMYQRPRVTADVTEEM----GLRGIIAGVCFDGFDKEEAEKCKRHNERLIQDVDNYSKRVRF 169
Cdd:PRK15493 105 STELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETvsrsGMRAAVSRTLFSFGTKEDEKKAIEEAEKYVKRYYNESGMLTT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 170 SIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVRYLYKLGVLSPRLIIAHGIYIDDDELRM 249
Cdd:PRK15493 185 MVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDNERAF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 250 LADHEVKVVHNPASNMKLASGIHfKFKEMRQLGITVGLGTDGCSSSNNLDMIEAMKLASLLGKAWRKDPEALTANEMLQA 329
Cdd:PRK15493 265 LAEHDVRVAHNPNSNLKLGSGIA-NVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLQKGIHQDATALPVETALTL 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496047653 330 ATAEGAAMFGLK-AGQIKEGYLADLCLID-LNTPAFTPNFNFVSNLVYAANGSCVDTVICDGKILMENKKVPGEDE 403
Cdd:PRK15493 344 ATKGAAEVIGMKqTGSLEVGKCADFITIDpSNKPHLQPADEVLSHLVYAASGKDISDVIINGKRVVWNGECKTLDE 419
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
16-418 |
5.27e-80 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 253.32 E-value: 5.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 16 DIYIEGKEIKQIG--EGLS--FPADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMP----LMPWLEQKIWPNEAKMT 87
Cdd:PRK07203 23 AIAIEGNVIVEIGttDELKakYPDAEFIDAKGKLIMPGLINSHNHIYSGLARGMMANIPpppdFISILKNLWWRLDRALT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 88 REDVYWGAKLACLEMIKSGTTTFFDMYQRPR-------VTADVTEEMGLRGIIagvCFDGFD---KEEAEKCKRHNERLI 157
Cdd:PRK07203 103 LEDVYYSALICSLEAIKNGVTTVFDHHASPNyiggslfTIADAAKKVGLRAML---CYETSDrdgEKELQEGVEENIRFI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 158 QDVD-NYSKRVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVRYLYKLGVLSPRLII 236
Cdd:PRK07203 180 KHIDeAKDDMVEAMFGLHASFTLSDATLEKCREAVKETGRGYHIHVAEGIYDVSDSHKKYGKDIVERLADFGLLGEKTLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 237 AHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIHFKFKEMRQlGITVGLGTDGCSSsnnlDMIEAMKLASLLGK---- 312
Cdd:PRK07203 260 AHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKN-GILLGLGTDGYTS----DMFESYKVANFKHKhagg 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 313 ----AWRKDPEALTANEMLQAataegAAMFGLKAGQIKEGYLADLCLIDLNTPafTP----NFNfvSNLVYAANGSCVDT 384
Cdd:PRK07203 335 dpnvGWPESPAMLFENNNKIA-----ERYFGAKFGILEEGAKADLIIVDYNPP--TPlnedNIN--GHILFGMNGGSVDT 405
|
410 420 430
....*....|....*....|....*....|....*.
gi 496047653 385 VICDGKILMENKKVPG--EDEIMEKATEIAYNLMKR 418
Cdd:PRK07203 406 TIVNGKVVMEDRKFLNfdEESIYARARKAAAKLWKR 441
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
35-398 |
3.64e-75 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 240.29 E-value: 3.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 35 ADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLMPWLEQKIWPNEAKMTREDVYWGAKLACLEMIKSGTTTFFDMY 114
Cdd:PRK06687 45 AEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAESEFTPDMTTNAVKEALTEMLQSGTTTFNDMY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 115 QRPRVTAD----VTEEMGLRGIIAGVCFDGfDKEEAEKCKRHNERLIQDVDNY-SKRVRFSIGPHAIYTVSGELLKWAHR 189
Cdd:PRK06687 125 NPNGVDIQqiyqVVKTSKMRCYFSPTLFSS-ETETTAETISRTRSIIDEILKYkNPNFKVMVAPHSPYSCSRDLLEASLE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 190 FAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVRYLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLAS 269
Cdd:PRK06687 204 MAKELNIPLHVHVAETKEESGIILKRYGKRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLAS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 270 GIHfKFKEMRQLGITVGLGTDGCSSSNNLDMIEAMKLASLLGKAWRKDPEALTANEMLQAATAEGAAMFGL--KAGQIKE 347
Cdd:PRK06687 284 GIA-PIIQLQKAGVAVGIATDSVASNNNLDMFEEGRTAALLQKMKSGDASQFPIETALKVLTIEGAKALGMenQIGSLEV 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 496047653 348 GYLADLCLIDlntPA----FTPNFNFVSNLVYAANGSCVDTVICDGKILMENKKV 398
Cdd:PRK06687 363 GKQADFLVIQ---PQgkihLQPQENMLSHLVYAVKSSDVDDVYIAGEQVVKQGQV 414
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
1-418 |
3.40e-67 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 220.49 E-value: 3.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 1 MSILIKNVLF---------NDRTIDIYIEGKEIKQIGEGLSFP--ADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGD-- 67
Cdd:PRK08203 1 TTLWIKNPLAivtmdaarrEIADGGLVVEGGRIVEVGPGGALPqpADEVFDARGHVVTPGLVNTHHHFYQTLTRALPAaq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 68 DMPLMPWLEQ--KIWpneAKMTREDVYWGAKLACLEMIKSGTTTFFD-MYQRPR-------VTADVTEEMGLRGIIAGVC 137
Cdd:PRK08203 81 DAELFPWLTTlyPVW---ARLTPEMVRVATQTALAELLLSGCTTSSDhHYLFPNglrdaldDQIEAAREIGMRFHATRGS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 138 FD-GFDK---------EEAEKCKRHNERLIQ---DVDNYSkRVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAE 204
Cdd:PRK08203 158 MSlGESDgglppdsvvEDEDAILADSQRLIDryhDPGPGA-MLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 205 TEGEVKDSLDRFGLTPVRYLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIHfKFKEMRQLGIT 284
Cdd:PRK08203 237 TLDEEAFCLERFGMRPVDYLEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIA-PVRELRAAGVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 285 VGLGTDGCSSSNNLDMIEAMKLASLLGKAwRKDPEALTANEMLQAATAEGAAMFGLK-AGQIKEGYLADLCLIDLNTPAF 363
Cdd:PRK08203 316 VGLGVDGSASNDGSNLIGEARQALLLQRL-RYGPDAMTAREALEWATLGGARVLGRDdIGSLAPGKLADLALFDLDELRF 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 496047653 364 TPNFNFVSNLVYAANGScVDTVICDGKILMENKKVPG--EDEIMEKATEIAYNLMKR 418
Cdd:PRK08203 395 AGAHDPVAALVLCGPPR-ADRVMVGGRWVVRDGQLTTldLAALIARHRAAARRLAAG 450
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
46-392 |
1.39e-58 |
|
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: 194.64 E-value: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 46 VIPGFVNAHTHAAMTLFRGFGDDMplmpwleqkiwpneakmtrEDVYWGAKLACLEMIKSGTTTFFDMY-QRPRVTADVT 124
Cdd:pfam01979 2 VLPGLIDAHVHLEMGLLRGIPVPP-------------------EFAYEALRLGITTMLKSGTTTVLDMGaTTSTGIEALL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 125 EEM-----GLRGIIAGVCFDGFDKEEAEKCKRhnERLIQDVD----NYSKRVRFSIGPHAIYTVSGELLKWAHRFAMEHQ 195
Cdd:pfam01979 63 EAAeelplGLRFLGPGCSLDTDGELEGRKALR--EKLKAGAEfikgMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 196 IPIHLHLAETEGEVKDSLDRFG-----LTPVRYLYKLGVLSP-RLIIAHGIYIDDDELRMLADH--EVKVVHNPASNMKL 267
Cdd:pfam01979 141 LPVAIHALETKGEVEDAIAAFGggiehGTHLEVAESGGLLDIiKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 268 ASGIhFKFKEMRQLGITVGLGTDGCSSSNNLDMIEAMKLASLLGKAWRkdpEALTANEMLQAATAEGAAMFGL--KAGQI 345
Cdd:pfam01979 221 RSGR-IALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPE---GGLSPLEALRMATINPAKALGLddKVGSI 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 496047653 346 KEGYLADLCLIDLntpaftpnfNFVSNLVYAANGSCVDTVICDGKIL 392
Cdd:pfam01979 297 EVGKDADLVVVDL---------DPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
16-418 |
1.55e-50 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 176.80 E-value: 1.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 16 DIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHAAMTLFRGF--GDDMPLMPWLEQKIWPNEAKMTREDVYW 93
Cdd:PRK12393 27 DIRIRDGRIAAIGALTPLPGERVIDATDCVVYPGWVNTHHHLFQSLLKGVpaGINQSLTAWLAAVPYRFRARFDEDLFRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 94 GAKLACLEMIKSGTTTFFD---MYQR--PRVTADV----TEEMGLRGIIA---GVCFDGFDKEEAEKCKRHN-ERLIQDV 160
Cdd:PRK12393 107 AARIGLVELLRSGCTTVADhhyLYHPgmPFDTGDIlfdeAEALGMRFVLCrggATQTRGDHPGLPTALRPETlDQMLADV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 161 DNYSKRV---------RFSIGPH-AIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVRYLYKLGVL 230
Cdd:PRK12393 187 ERLVSRYhdaspdslrRVVVAPTtPTFSLPPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYGMTPVQFVAEHDWL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 231 SPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIHfKFKEMRQLGITVGLGTDGCSSSNNLDMIEAMKLASLL 310
Cdd:PRK12393 267 GPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIA-PALAMEAAGVPVSLGVDGAASNESADMLSEAHAAWLL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 311 GKAwRKDPEALTANEMLQAATAEGAAMFGLKA-GQIKEGYLADLCLIDLNTPAFtpnFNFVSNL---VYAANGSCVDTVI 386
Cdd:PRK12393 346 HRA-EGGADATTVEDVVHWGTAGGARVLGLDAiGTLAVGQAADLAIYDLDDPRF---FGLHDPAiapVACGGPAPVKALL 421
|
410 420 430
....*....|....*....|....*....|....
gi 496047653 387 CDGKILMENKKVPGED--EIMEKATEIAYNLMKR 418
Cdd:PRK12393 422 VNGRPVVENGAIPGLDlaELRHDARAAVRRLLQR 455
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
17-403 |
3.60e-48 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 170.99 E-value: 3.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 17 IYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHAAM-TLFRGFgDDMPlmPWLEQKIWPNE-------AKMTR 88
Cdd:PRK06151 26 VVFEGDRILFVGHRFDGEVDRVIDAGNALVGPGFIDLDALSDLdTTILGL-DNGP--GWAKGRVWSRDyveagrrEMYTP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 89 EDVYWGAKLACLEMIKSGTTTFF-----------DMYQRPRVTADVTEEMGLRGIIaGVCF---------DG-----FDK 143
Cdd:PRK06151 103 EELAFQKRYAFAQLLRNGITTAMpiaslfyrqwaETYAEFAAAAEAAGRLGLRVYL-GPAYrsggsvleaDGslevvFDE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 144 EEAEKCKRHNERLIQDVDN-YSKRVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLDRFGLTPVR 222
Cdd:PRK06151 182 ARGLAGLEEAIAFIKRVDGaHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHGTTPLE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 223 YLYKLGVLSPRLIIAHGIYIDD---------DELRMLADHEVKVVHNPasnmkLASGIHFK----FKEMRQLGITVGLGT 289
Cdd:PRK06151 262 WLADVGLLGPRLLIPHATYISGsprlnysggDDLALLAEHGVSIVHCP-----LVSARHGSalnsFDRYREAGINLALGT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 290 DgcssSNNLDMIEAMKLASLLGKAWRKDPEALTANEMLQAATAEGAAMFGLK-AGQIKEGYLADLCLIDLNTPAFTPNFN 368
Cdd:PRK06151 337 D----TFPPDMVMNMRVGLILGRVVEGDLDAASAADLFDAATLGGARALGRDdLGRLAPGAKADIVVFDLDGLHMGPVFD 412
|
410 420 430
....*....|....*....|....*....|....*
gi 496047653 369 FVSNLVYAANGSCVDTVICDGKILMENKKVPGEDE 403
Cdd:PRK06151 413 PIRTLVTGGSGRDVRAVFVDGRVVMEDGRLPGVDL 447
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
33-359 |
2.94e-46 |
|
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: 164.76 E-value: 2.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 33 FPADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLMPWLEQKIWPNEAKMTRED----VYwgaKLACLEMIKSGTT 108
Cdd:cd01303 50 KPGARVIDSPNQFILPGFIDTHIHAPQYANIGSGLGEPLLDWLETYTFPEEAKFADPAyareVY---GRFLDELLRNGTT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 109 T--------------FFDMYQRprvtadvteeMGLRGIIAGVCFD----GFDKEEAEKCKRHNERLIQDVDNYSKRVRFS 170
Cdd:cd01303 127 TacyfatihpesteaLFEEAAK----------RGQRAIAGKVCMDrnapEYYRDTAESSYRDTKRLIERWHGKSGRVKPA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 171 IGPHAIYTVSGELLKWAHRFAMEHQ-IPIHLHLAETEGEVK-------------DSLDRFGLtpvrylyklgvLSPRLII 236
Cdd:cd01303 197 ITPRFAPSCSEELLAALGKLAKEHPdLHIQTHISENLDEIAwvkelfpgardylDVYDKYGL-----------LTEKTVL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 237 AHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIhFKFKEMRQLGITVGLGTD--GCSSSNNLDMI-EAMKLASLLGKA 313
Cdd:cd01303 266 AHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGL-FDVRKLLDAGIKVGLGTDvgGGTSFSMLDTLrQAYKVSRLLGYE 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 496047653 314 wRKDPEALTANEMLQAATAEGAAMFGL--KAGQIKEGYLADLCLIDLN 359
Cdd:cd01303 345 -LGGHAKLSPAEAFYLATLGGAEALGLddKIGNFEVGKEFDAVVIDPS 391
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
16-402 |
2.50e-41 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 151.69 E-value: 2.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 16 DIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMPLMPWLeQKIWPNEAKMTR-EDVYWG 94
Cdd:PRK08204 25 DILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGADWTLQTYF-REIHGNLGPMFRpEDVYIA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 95 AKLACLEMIKSGTTTFFD--MYQRprvTADVTEEMgLRGI----IAGVCFDGFDKEEAEKCKRHNERLIQDVDNYSKRvR 168
Cdd:PRK08204 104 NLLGALEALDAGVTTLLDwsHINN---SPEHADAA-IRGLaeagIRAVFAHGSPGPSPYWPFDSVPHPREDIRRVKKR-Y 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 169 FS------------IGPHAIytvSGELLKWAHRFAMEHQIPIHLHLAETEGEVKDSLdrfgltpVRYLYKLGVLSPRLII 236
Cdd:PRK08204 179 FSsddglltlglaiRGPEFS---SWEVARADFRLARELGLPISMHQGFGPWGATPRG-------VEQLHDAGLLGPDLNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 237 AHGIYIDDDELRMLADHEVKVVHNPasNMKLASGIHF-KFKEMRQLGITVGLGTDgCSSSNNLDMIEAMKLASLLGKAW- 314
Cdd:PRK08204 249 VHGNDLSDDELKLLADSGGSFSVTP--EIEMMMGHGYpVTGRLLAHGVRPSLGVD-VVTSTGGDMFTQMRFALQAERARd 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 315 ----------RKDPEALTANEMLQAATAEGAAMFGL--KAGQIKEGYLADLCLIDLNTPAFTPNFNFVSNLVYAANGSCV 382
Cdd:PRK08204 326 navhlreggmPPPRLTLTARQVLEWATIEGARALGLedRIGSLTPGKQADLVLIDATDLNLAPVHDPVGAVVQSAHPGNV 405
|
410 420
....*....|....*....|
gi 496047653 383 DTVICDGKILMENKKVPGED 402
Cdd:PRK08204 406 DSVMVAGRAVKRNGKLLGVD 425
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
46-361 |
2.19e-40 |
|
Metallo-dependent hydrolases, subgroup D 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: 238637 [Multi-domain] Cd Length: 381 Bit Score: 147.60 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 46 VIPGFVNAHTHAAMT------LFRGFGDdmplmpWLEQKIwPNEAKMTREdvywGAKLACLE----MIKSGTTTFFDMYQ 115
Cdd:cd01312 29 LLPGLINAHTHLEFSanvaqfTYGRFRA------WLLSVI-NSRDELLKQ----PWEEAIRQgirqMLESGTTSIGAISS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 116 RpRVTADVTEEMGLRGIIAGVCFDGFDKEEAEKCKRHNERLIQDVDNYSKRVRFSIGPHAIYTVSGELLKWAHRFAMEHQ 195
Cdd:cd01312 98 D-GSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYSVHPELAQDLIDLAKKLN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 196 IPIHLHLAETEGEV----------KDSLDRF--------GLTPVRYLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKV 257
Cdd:cd01312 177 LPLSTHFLESKEERewleeskgwfKHFWESFlklpkpkkLATAIDFLDMLGGLGTRVSFVHCVYANLEEAEILASRGASI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 258 VHNPASNMKLASGIhFKFKEMRQLGITVGLGTDGCSSSNNLDMIEAMKlASLLgkAWRKDPEALTANEMLQAATAEGAAM 337
Cdd:cd01312 257 ALCPRSNRLLNGGK-LDVSELKKAGIPVSLGTDGLSSNISLSLLDELR-ALLD--LHPEEDLLELASELLLMATLGGARA 332
|
330 340
....*....|....*....|....
gi 496047653 338 FGLKAGQIKEGYLADLCLIDLNTP 361
Cdd:cd01312 333 LGLNNGEIEAGKRADFAVFELPGP 356
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
12-390 |
4.28e-30 |
|
Metallo-dependent hydrolases, subgroup D 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: 238638 [Multi-domain] Cd Length: 418 Bit Score: 120.25 E-value: 4.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 12 DRTIDIYIEGKeIKQIGEGLSFPADKILDGsrkAVIPGFVNAHTHA---AM---TLFRGFGDDmPLMPWLEQkIWPNEAK 85
Cdd:cd01313 10 NVRIEVDADGR-IAAVNPDTATEAVALLGG---ALLPGMPNLHSHAfqrAMaglTEYRGSAAD-SFWTWREL-MYRFAAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 86 MTREDVYWGAKLACLEMIKSGTTT---FFDMYQRP--RVTADVTE----------EMGLRGIIAGVCFD--GFDKEEAEK 148
Cdd:cd01313 84 LTPEQIEAIARQLYIEMLLAGITAvgeFHYVHHDPdgTPYADPAElaqrviaaasDAGIGITLLPVLYAraGFGGPAPNP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 149 ckrHNERLIQDVDNY-------------SKRVRFSIGPHAIYTVSGE----LLKWAHRfamehQIPIHLHLAETEGEVKD 211
Cdd:cd01313 164 ---GQRRFINGYEDFlgllekalravkeHAAARIGVAPHSLRAVPAEqlaaLAALASE-----KAPVHIHLAEQPKEVDD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 212 SLDRFGLTPVRYLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIhFKFKEMRQLGITVGLGTDg 291
Cdd:cd01313 236 CLAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGI-FPAAALLAAGGRIGIGSD- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 292 csSSNNLDMIEAMKLASL------LGKAWRKDPEALTANEMLQAATAEGAAMFGLKAGQIKEGYLADLCLIDLNTPAF-- 363
Cdd:cd01313 314 --SNARIDLLEELRQLEYsqrlrdRARNVLATAGGSSARALLDAALAGGAQALGLATGALEAGARADLLSLDLDHPSLag 391
|
410 420
....*....|....*....|....*...
gi 496047653 364 -TPNfNFVSNLVYAANGSCVDTVICDGK 390
Cdd:cd01313 392 aLPD-TLLDAWVFAAGDREVRDVVVGGR 418
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
19-365 |
7.66e-30 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 119.91 E-value: 7.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 19 IEGKEIKQIG---EGLS-FPADKILDGSRKAVI-PGFVNAHTHAAMTlfrgfgdDM------PLMPWLEQKIWPNEAKMt 87
Cdd:PRK09228 36 VEDGRIVAAGpyaELRAqLPADAEVTDYRGKLIlPGFIDTHIHYPQT-------DMiasygeQLLDWLNTYTFPEERRF- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 88 rEDVYWGAKLA---CLEMIKSGTTT--------------FFDMYQRprvtadvteeMGLRgIIAG-VCFDGFDKEE---- 145
Cdd:PRK09228 108 -ADPAYAREVAeffLDELLRNGTTTalvfgtvhpqsvdaLFEAAEA----------RNMR-MIAGkVLMDRNAPDGlrdt 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 146 AEKCKRHNERLIQDVDN-----YSKRVRFSIgphaiyTVSGELLKWAHRFAMEHqiP---IHLHLAETEGEVK------- 210
Cdd:PRK09228 176 AESGYDDSKALIERWHGkgrllYAITPRFAP------TSTPEQLEAAGALAREH--PdvwIQTHLSENLDEIAwvkelfp 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 211 ------DSLDRFGLtpvrylyklgvLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIhFKFKEMRQLGIT 284
Cdd:PRK09228 248 eardylDVYERYGL-----------LGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGL-FDLKRADAAGVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 285 VGLGTD-GCSSSNNL--DMIEAMKLASLLGkawrkdpEALTANEMLQAATAEGAAMFGL--KAGQIKEGYLADLCLIDln 359
Cdd:PRK09228 316 VGLGTDvGGGTSFSMlqTMNEAYKVQQLQG-------YRLSPFQAFYLATLGGARALGLddRIGNLAPGKEADFVVLD-- 386
|
....*.
gi 496047653 360 tPAFTP 365
Cdd:PRK09228 387 -PAATP 391
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
11-404 |
8.78e-30 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 119.95 E-value: 8.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 11 NDRTIDIYIEGKeIKQIGEGLSFPADKILDGsrkAVIPGFVNAHTHA---AM---TLFRGFGDD--------MPLMPwle 76
Cdd:PRK09229 18 RNVRLTVDADGR-IAAVEPGAAPAGAERLAG---PVLPGMPNLHSHAfqrAMaglTEVRGPPQDsfwswrelMYRFA--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 77 qkiwpneAKMTREDVYWGAKLACLEMIKSGTTT---FFDMYQRP--RVTADVTeEMGLRgIIAG------------VC-- 137
Cdd:PRK09229 91 -------LRLTPDQLEAIARQLYVEMLEAGYTSvgeFHYLHHDPdgTPYADPA-EMALR-IVAAaraagigltllpVLya 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 138 FDGFDKEEAEKCKRhneRLIQDVDNYSKRV-------------RFSIGPHAIYTVSGE----LLKWAHRfamehQIPIHL 200
Cdd:PRK09229 162 HSGFGGQPPNPGQR---RFINDPDGFLRLLealrralaalpgaRLGLAPHSLRAVTPDqlaaVLALAAP-----DGPVHI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 201 HLAETEGEVKDSLDRFGLTPVRYLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIhFKFKEMRQ 280
Cdd:PRK09229 234 HIAEQTKEVDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDGI-FPAVDYLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 281 LGITVGLGTDgcssSN-NLDMIE-------AMKLASLLGKAWRKDPEALTANEMLQAATAEGAAMFGLKAGQIKEGYLAD 352
Cdd:PRK09229 313 AGGRFGIGSD----SHvSIDLVEelrlleyGQRLRDRRRNVLAAAAQPSVGRRLFDAALAGGAQALGRAIGGLAVGARAD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 496047653 353 LCLIDLNTPAF--TPNFNFVSNLVYAANGSCVDTVICDGKILMENKKVPGEDEI 404
Cdd:PRK09229 389 LVVLDLDHPALagREGDALLDRWVFAGGDAAVRDVWVAGRWVVRDGRHRLREAI 442
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
50-335 |
2.15e-29 |
|
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: 115.51 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 50 FVNAHTHAAMTLFRGFGDDMPLMpwleqkiwpNEAKMTREDVYWGAKLACLEMIKSGTTTFFDMY---------QRPRVT 120
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELK---------EAEELSPEDLYEDTLRALEALLAGGVTTVVDMGstppptttkAAIEAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 121 ADVTEEmgLRGIIAGVCFDGFDKEEAEKCKR--HNERLIQDVDNYSKRVRFSIGPHAIYTVSGELLKWAHRFAMEHQIPI 198
Cdd:cd01292 72 AEAARA--SAGIRVVLGLGIPGVPAAVDEDAeaLLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLEEARKLGLPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 199 HLHLAETEGEVKDSLDrfgltpvryLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKVVHNPASNMKLAS-GIHFK-FK 276
Cdd:cd01292 150 VIHAGELPDPTRALED---------LVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRdGEGAEaLR 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 496047653 277 EMRQLGITVGLGTDGCSSSNNLDMIEAMKLASLLGKAWrkdpeaLTANEMLQAATAEGA 335
Cdd:cd01292 221 RLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG------LSLEEALRLATINPA 273
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
4-359 |
1.41e-28 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 115.84 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 4 LIKN--VLFNDRTIDIYIEGKEIKQigeglsFPADKILDGSRKAVIPGFVNAHTH----AAMTLFRgFGDdmpLMPWLEQ 77
Cdd:PRK08418 18 ILEDgaVVFDDKILEIGDYENLKKK------YPNAKIQFFKNSVLLPAFINPHTHlefsANKTTLD-YGD---FIPWLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 78 KIwpneakMTREDVYWGAKLACL-----EMIKSGTTTF-------FDMyqrprvtaDVTEEMGLRGII-----------A 134
Cdd:PRK08418 88 VI------NHREDLLEKCKGALIqqainEMLKSGVGTIgaissfgIDL--------EICAKSPLRVVFfneilgsnasaV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 135 GVCFDGFDK--EEAEKCKrhNERLIQDVdnyskrvrfSIgpHAIYTVSGELLKWAHRFAMEHQIPIHLH----------L 202
Cdd:PRK08418 154 DELYQDFLArfEESKKFK--SKKFIPAI---------AI--HSPYSVHPILAKKALQLAKKENLLVSTHfleskaerewL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 203 AETEGEVKDSLDRFGLTPvRYLYK----LGVLSP-RLIIAHGIYIDDDELRMLADHEVKVVHNPASNmKLASGIHFKFKE 277
Cdd:PRK08418 221 EESKGWFKKFFEKFLKEP-KPLYTpkefLELFKGlRTLFTHCVYASEEELEKIKSKNASITHCPFSN-RLLSNKALDLEK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 278 MRQLGITVGLGTDGCSSSNNLDMIEAMKlASLLGKAwRKDPEALtANEMLQAATAEGAAMFGLKAGQIKEGYLADLCLID 357
Cdd:PRK08418 299 AKKAGINYSIATDGLSSNISLSLLDELR-AALLTHA-NMPLLEL-AKILLLSATRYGAKALGLNNGEIKEGKDADLSVFE 375
|
..
gi 496047653 358 LN 359
Cdd:PRK08418 376 LP 377
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-391 |
3.10e-26 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 108.89 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 2 SILIKNV-LF---NDRTI---DIYIEGKEIKQIGEGLSF---PADKILDGSRKAVIPGFVNAHTHAamtlfrGFGDDMPL 71
Cdd:COG1228 9 TLLITNAtLVdgtGGGVIengTVLVEDGKIAAVGPAADLavpAGAEVIDATGKTVLPGLIDAHTHL------GLGGGRAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 72 MPWLEQKIWPneakmtREDVYWGAKLACLEMIKSGTTTFFDMYQRPRVTADVTEEmGLRGIIAG----------VCFDGF 141
Cdd:COG1228 83 EFEAGGGITP------TVDLVNPADKRLRRALAAGVTTVRDLPGGPLGLRDAIIA-GESKLLPGprvlaagpalSLTGGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 142 DKEEAEKCKRHNERLIQD----VDNYSKRVRFSIGPHAIYTVsgelLKWAHRfameHQIPIHLHlAETEGEVKDSLdrfg 217
Cdd:COG1228 156 HARGPEEARAALRELLAEgadyIKVFAEGGAPDFSLEELRAI----LEAAHA----LGLPVAAH-AHQADDIRLAV---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 218 ltpvrylyKLGVLSprliIAHGIYIDDDELRMLADHEV---------------KVVHNPASNMKLASGIHFK-FKEMRQL 281
Cdd:COG1228 223 --------EAGVDS----IEHGTYLDDEVADLLAEAGTvvlvptlslflalleGAAAPVAAKARKVREAALAnARRLHDA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 282 GITVGLGTD-GCSSSNNLDMIEAMKLASLLGkawrkdpeaLTANEMLQAATAEGAAMFGL--KAGQIKEGYLADLCLIDL 358
Cdd:COG1228 291 GVPVALGTDaGVGVPPGRSLHRELALAVEAG---------LTPEEALRAATINAAKALGLddDVGSLEPGKLADLVLLDG 361
|
410 420 430
....*....|....*....|....*....|...
gi 496047653 359 NTPAftpnfnfvsNLVYAANgscVDTVICDGKI 391
Cdd:COG1228 362 DPLE---------DIAYLED---VRAVMKDGRV 382
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
4-362 |
3.93e-22 |
|
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: 97.32 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 4 LIKNVLFND---RTIDIYIEGKEIKQIGEGLSFPADK-ILDGSRKAVIPGFVNAHTHAAMTLFrgfgddmpLMPWLEQKI 79
Cdd:cd01293 1 LLRNARLADggtALVDIAIEDGRIAAIGPALAVPPDAeEVDAKGRLVLPAFVDPHIHLDKTFT--------GGRWPNNSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 80 WPN----------EAKMTREDVYWGAKLACLEMIKSGTTTFfdmyqrpRVTADVTEEMGLRGI---------------IA 134
Cdd:cd01293 73 GTLleaiiaweerKLLLTAEDVKERAERALELAIAHGTTAI-------RTHVDVDPAAGLKALeallelreewadlidLQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 135 GVCF--DGFDKEEaekckrHNERLIQDV-DNYSKRV----RFSIGPHAIytvsgELLKWAHRFAMEHQIPIHLHLAETeg 207
Cdd:cd01293 146 IVAFpqHGLLSTP------GGEELMREAlKMGADVVggipPAEIDEDGE-----ESLDTLFELAQEHGLDIDLHLDET-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 208 evkDSLDRFGLTPV-RYLYKLGVLsPRLIIAH----GIYiDDDELR----MLADHEVKVVHNPASNMKLASGIHFK---- 274
Cdd:cd01293 213 ---DDPGSRTLEELaEEAERRGMQ-GRVTCSHatalGSL-PEAEVSrladLLAEAGISVVSLPPINLYLQGREDTTpkrr 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 275 ----FKEMRQLGITVGLGTDGCSSS----NNLDMIEAMKLAslLGKAWRKDPEALTAneMLQAATAEGAAMFGLKAGQIK 346
Cdd:cd01293 288 gvtpVKELRAAGVNVALGSDNVRDPwypfGSGDMLEVANLA--AHIAQLGTPEDLAL--ALDLITGNAARALGLEDYGIK 363
|
410
....*....|....*.
gi 496047653 347 EGYLADLCLIDLNTPA 362
Cdd:cd01293 364 VGCPADLVLLDAEDVA 379
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
46-336 |
4.85e-21 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are 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. They 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. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 92.08 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 46 VIPGFVNAHTHAAMTLFRGFGDDMPLmpwLEQKIWPNE------AKMTREDVYWGAKLACLEMIKSGTTTFFDMyqrprv 119
Cdd:cd01305 2 LIPALVNAHTHLGDSAIKEVGDGLPL---DDLVAPPDGlkhrllAQADDRELAEAMRKVLRDMRETGIGAFADF------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 120 tadvtEEMGLRGIIAGvcfdgfdKEEAEKCKRHNE----RLIQ-DVDNYSKRVRFSIGPHAIYTVSGEL-LKWAHRFAMe 193
Cdd:cd01305 73 -----REGGVEGIELL-------RRALGKLPVPFEvilgRPTEpDDPEILLEVADGLGLSSANDVDLEDiLELLRRRGK- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 194 hqiPIHLHLAETEGEVkdsldrfGLTPVRYLYKLGvlsPRLIIaHGIYIDDDELRMLADHEVKVVHNPASNMKLASGIHf 273
Cdd:cd01305 140 ---LFAIHASETRESV-------GMTDIERALDLE---PDLLV-HGTHLTDEDLELVRENGVPVVLCPRSNLYFGVGIP- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496047653 274 KFKEMRQLGITVGLGTDGcSSSNNLDMIEAMKLASLLGKAWRKDPEaltaNEMLQAATAEGAA 336
Cdd:cd01305 205 PVAELLKLGIKVLLGTDN-VMVNEPDMWAEMEFLAKYSRLQGYLSP----LEILRMATVNAAE 262
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
17-366 |
8.18e-21 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 93.18 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 17 IYIEGKEIKQIGEglSFPADKILDGSrKAVIPGFVNAHTHAAMTLFRGFGDDMPLMPWLEQkiwPNEAK------MTRED 90
Cdd:PRK07213 22 LVIEDGIIKGFTN--EVHEGNVIDAK-GLVIPPLINAHTHIGDSSIKDIGIGKSLDELVKP---PNGLKhkflnsCSDKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 91 VYWGAKLACLEMIKSGTTTFFDMyqrprvtadvtEEMGLRGI-----------IAGVCFDGFDKEEAEKCKRHNERLIQD 159
Cdd:PRK07213 96 LVEGMKEGLYDMYNNGIKAFCDF-----------REGGIKGInllkkassdlpIKPIILGRPTEADENELKKEIREILKN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 160 VDnyskrvrfSIGPHAIYTVSGELLKW-AHRFAMEHQIpIHLHLAETEGEVKDSLDRFGLTPVRYLYKLGVlSPRLIIaH 238
Cdd:PRK07213 165 SD--------GIGLSGANEYSDEELKFiCKECKREKKI-FSIHAAEHKGSVEYSLEKYGMTEIERLINLGF-KPDFIV-H 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 239 GIYIDDDELRMLADHEVKVVHNPASNMKLASGIHfKFKEMRQLGITVGLGTDGCsSSNNLDMIEAMKLASllgKAWRKDP 318
Cdd:PRK07213 234 ATHPSNDDLELLKENNIPVVVCPRANASFNVGLP-PLNEMLEKGILLGIGTDNF-MANSPSIFREMEFIY---KLYHIEP 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496047653 319 EaltanEMLQAATAEGAAMFGLK-AGQIKEGYLADLCLIDLNTPAFTPN 366
Cdd:PRK07213 309 K-----EILKMATINGAKILGLInVGLIEEGFKADFTFIKPTNIKFSKN 352
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
17-391 |
9.53e-16 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 78.22 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 17 IYIEGKEIKQIGEGLSFP---ADKILDGSRKAVIPGFVNAHTHAAmtlfrgFGDD------MPL--MPWLEQKIWPNEAK 85
Cdd:TIGR01224 6 ILIHGGKIVWIGQLAALPgeeATEIIDCGGGLVTPGLVDPHTHLV------FAGDrvnefeMKLqgASYLEILAQGGGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 86 MTREDVYWGAKLACLE--------MIKSGTTT----------FFDMYQRPRVTADVTEEMGLR----GIIAGVCFDGFDK 143
Cdd:TIGR01224 80 STVRATRAASEEELLKlalfrlksMLRSGTTTaevksgygldLETELKMLRAAKALHEEQPVDvvttFLGAHAVPPEFQG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 144 EEAE---------KCKRHNERLIQDVDNYSKRVRFSigPHAIYTVsgeLLKwahrfAMEHQIPIHLHlaetegevKDSLD 214
Cdd:TIGR01224 160 RPDDyvdgiceelIPQVAEEGLASFADVFCEAGVFS--VEQSRRI---LQA-----AQEAGLPVKLH--------AEELS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 215 RFGltPVRYLYKLGVLSprliIAHGIYIDDDELRMLADHEVKVVHNPASNMKLASGiHFKFKEMRQLGITVGLGTD-GCS 293
Cdd:TIGR01224 222 NLG--GAELAAKLGAVS----ADHLEHASDAGIKALAEAGTVAVLLPGTTFYLRET-YPPARQLIDYGVPVALATDlNPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 294 SSNNLDMIEAMKLASLLGKawrkdpeaLTANEMLQAATAEGAAMFGL--KAGQIKEGYLADLCLIDLNTPAFTPnfnfvs 371
Cdd:TIGR01224 295 SSPTLSMQLIMSLACRLMK--------MTPEEALHAATVNAAYALGLgeERGTLEAGRDADLVILSAPSYAEIP------ 360
|
410 420
....*....|....*....|
gi 496047653 372 nlvYAANGSCVDTVICDGKI 391
Cdd:TIGR01224 361 ---YHYGVNHVHAVIKNGNI 377
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
17-389 |
3.60e-13 |
|
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: 70.36 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 17 IYIEGKEIKQIG-----EGLSFPADKILDGSRKAVIPGFVNAHTHAamtLFRGF-GDDMplmpwlEQKI--WPNEAKM-- 86
Cdd:cd01296 1 IAIRDGRIAAVGpaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL---VFAGDrVDEF------AARLagASYEEILaa 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 87 ----------TR----EDVYWGAKLACLEMIKSGTTTF-----FDMYQRP-----RVTADVTEE---------MGLRGII 133
Cdd:cd01296 72 gggilstvraTRaaseDELFASALRRLARMLRHGTTTVevksgYGLDLETelkmlRVIRRLKEEgpvdlvstfLGAHAVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 134 AGvcFDGFDK-------EEAEKCKRHNerLIQDVDNYSKRVRFSigPHAIYTVsgelLKwahrFAMEHQIPIHLHlaete 206
Cdd:cd01296 152 PE--YKGREEyidlvieEVLPAVAEEN--LADFCDVFCEKGAFS--LEQSRRI----LE----AAKEAGLPVKIH----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 207 gevKDSLDRFGltPVRYLYKLGVLSprliIAHGIYIDDDELRMLADHEVKVVhnpasnmkLASGIHFKFKE-------MR 279
Cdd:cd01296 213 ---ADELSNIG--GAELAAELGALS----ADHLEHTSDEGIAALAEAGTVAV--------LLPGTAFSLREtypparkLI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 280 QLGITVGLGTD---GCSSSNNldMIEAMKLASLLGKawrkdpeaLTANEMLQAATAEGAAMFGL--KAGQIKEGYLADLC 354
Cdd:cd01296 276 DAGVPVALGTDfnpGSSPTSS--MPLVMHLACRLMR--------MTPEEALTAATINAAAALGLgeTVGSLEVGKQADLV 345
|
410 420 430
....*....|....*....|....*....|....*
gi 496047653 355 LIDLNTPAFtpnfnfvsnLVYAANGSCVDTVICDG 389
Cdd:cd01296 346 ILDAPSYEH---------LAYRFGVNLVEYVIKNG 371
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
36-359 |
8.31e-11 |
|
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 63.08 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 36 DKILDGSRKAVIPGFVNAHTHAAMTLFRGFGDDMplmpwleqkiwpneakMTREDVYWGAKLACLEMIKSGTTTFFDMyq 115
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLA----------------LPVEYRTIRATRQARAALRAGFTTVRDA-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 116 rPRVTADVTEEMGLRGIIAG----VC----------FDGFDKEEaEKCKRHNERLIQDVDNYSKRVRFSI--GPHAI-YT 178
Cdd:cd01299 63 -GGADYGLLRDAIDAGLIPGprvfASgralsqtgghGDPRGLSG-LFPAGGLAAVVDGVEEVRAAVREQLrrGADQIkIM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 179 VSGellkwahRFAMEHQIPIHLHLaeTEGEVKDSLD---RFGLT---------PVRYLYKLGVLSprliIAHGIYIDDDE 246
Cdd:cd01299 141 ATG-------GVLSPGDPPPDTQF--SEEELRAIVDeahKAGLYvaahaygaeAIRRAIRAGVDT----IEHGFLIDDET 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 247 LRMLADHEVKVV---HNPASNMKLASGIH------FKFKEMRQL-----------GITVGLGTD-GCSSSNNLDMIEAMK 305
Cdd:cd01299 208 IELMKEKGIFLVptlATYEALAAEGAAPGlpadsaEKVALVLEAgrdalrrahkaGVKIAFGTDaGFPVPPHGWNARELE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 496047653 306 LASLLGkawrkdpeaLTANEMLQAATAEGAAMFGL--KAGQIKEGYLADLCLIDLN 359
Cdd:cd01299 288 LLVKAG---------GTPAEALRAATANAAELLGLsdELGVIEAGKLADLLVVDGD 334
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-401 |
1.60e-10 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 62.42 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 4 LIKNV-LFNDRTI---DIYIEGKEIKQIGEGLS-FPADKILDGSRKAVIPGFVNAHTHaamtlFRgfgddmplMPWLEQK 78
Cdd:COG0044 1 LIKNGrVVDPGGLeraDVLIEDGRIAAIGPDLAaPEAAEVIDATGLLVLPGLIDLHVH-----LR--------EPGLEHK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 79 iwpneakmtrEDVYWGAKLAclemIKSGTTTFFDM-YQRP-RVTADVTEEM------------GLRGII----------- 133
Cdd:COG0044 68 ----------EDIETGTRAA----AAGGVTTVVDMpNTNPvTDTPEALEFKlaraeekalvdvGPHGALtkglgenlael 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 134 -----AGVC-FDGFDKEEAEKCkRHNERLIQDVDNYSKRVRFSIGPHA-IYTVSGELLKWAHRFAMEHQIPIHLHLAETE 206
Cdd:COG0044 134 galaeAGAVaFKVFMGSDDGNP-VLDDGLLRRALEYAAEFGALVAVHAeDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 207 gevkdSLDRFgltpVRYLYKLGVlspRLIIAH----------------GIYI-----------DDDELRMLaDHEVKVvh 259
Cdd:COG0044 213 -----AVARD----IALAEETGA---RLHIVHvstaeavelireakarGLPVtaevcphhltlTDEDLERY-GTNFKV-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 260 NP----ASNMK-----LASGIhfkfkemrqlgITVgLGTDGCSSSN---NLDMIEAM--------KLASLLGKAWRKdpE 319
Cdd:COG0044 278 NPplrtEEDREalwegLADGT-----------IDV-IATDHAPHTLeekELPFAEAPngipgletALPLLLTELVHK--G 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 320 ALTANEMLQAATAEGAAMFGL-KAGQIKEGYLADLCLIDLNTP-AFTPnfnfvSNLVYAANGSC---------VDTVICD 388
Cdd:COG0044 344 RLSLERLVELLSTNPARIFGLpRKGRIAVGADADLVLFDPDAEwTVTA-----EDLHSKSKNTPfegreltgrVVATIVR 418
|
490
....*....|...
gi 496047653 389 GKILMENKKVPGE 401
Cdd:COG0044 419 GRVVYEDGEVVGE 431
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
182-392 |
1.93e-09 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 59.08 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 182 ELLKWAHrfamEHQIPIHLHlAETEGEVKDSLDRFGLTPVRYlYKLGVlsPRLIIAHGIYIDDDEL-----RMLADHEVK 256
Cdd:pfam07969 254 ELVAAAR----ERGLDVAIH-AIGDATIDTALDAFEAVAEKL-GNQGR--VRIEHAQGVVPYTYSQiervaALGGAAGVQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 257 VVHNPASNMKLASGI-------HFKFKEMRQLGITVGLGTDG-CSSSNNLDMIEAM-KLASLLGKAWRKDPEALTANEML 327
Cdd:pfam07969 326 PVFDPLWGDWLQDRLgaerargLTPVKELLNAGVKVALGSDApVGPFDPWPRIGAAvMRQTAGGGEVLGPDEELSLEEAL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496047653 328 QAATAEGAAMFGL--KAGQIKEGYLADLCLIDLNTPAFTPNFNFVSNLVYaangscvdtVICDGKIL 392
Cdd:pfam07969 406 ALYTSGPAKALGLedRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRL---------TVVDGRVV 463
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-138 |
3.28e-09 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 58.28 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 1 MSILIKNV-LFN----DRTIDIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHaamtlFRgfgddmplMPWL 75
Cdd:PRK09357 1 MMILIKNGrVIDpkglDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVH-----LR--------EPGQ 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496047653 76 EQKiwpneakmtrEDVYWGAKLAclemIKSGTTTFFDMYQ-RPRV-TADVTEEMGLRGIIAGVCF 138
Cdd:PRK09357 68 EDK----------ETIETGSRAA----AAGGFTTVVAMPNtKPVIdTPEVVEYVLDRAKEAGLVD 118
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
3-401 |
4.63e-09 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 58.08 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 3 ILIKNVLFND------RTIDIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHAAMTLFRgfgddmplMPWLE 76
Cdd:cd01297 2 LVIRNGTVVDgtgappFTADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTHYDGQVFW--------DPDLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 77 QKIWpneakmtredvywgaklaclemikSGTTTFFDM-------YQRPRVTADvtEEMGLRGIIAGVCFDGFDKEEAEKC 149
Cdd:cd01297 74 PSSR------------------------QGVTTVVLGncgvspaPANPDDLAR--LIMLMEGLVALGEGLPWGWATFAEY 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 150 KRHNERLIQDVdNYSKRVrfsigPHAiyTVSGELLKWAHRFAMEHQIPIHLHLAEtegevkDSLDRFGltpvrylykLGv 229
Cdd:cd01297 128 LDALEARPPAV-NVAALV-----GHA--ALRRAVMGLDAREATEEELAKMRELLR------EALEAGA---------LG- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 230 LSPRLIIAHGIYIDDDELRMLAD--HEVKVVHNPASNMKLASgIHFKFKEMRQLGITVGLGTD----GCSSSNN------ 297
Cdd:cd01297 184 ISTGLAYAPRLYAGTAELVALARvaARYGGVYQTHVRYEGDS-ILEALDELLRLGRETGRPVHishlKSAGAPNwgkidr 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 298 -LDMIEAMKLASL-------------------------------------------------LGKaWRKDPEALTANEML 327
Cdd:cd01297 263 lLALIEAARAEGLqvtadvypygagseddvrrimahpvvmggsdggalgkphprsygdftrvLGH-YVRERKLLSLEEAV 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496047653 328 QAATAEGAAMFGLKA-GQIKEGYLADLCLIDLNTPAFTPNFNfvsNLVYAANGscVDTVICDGKILMENKKVPGE 401
Cdd:cd01297 342 RKMTGLPARVFGLADrGRIAPGYRADIVVFDPDTLADRATFT---RPNQPAEG--IEAVLVNGVPVVRDGAFTGA 411
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-59 |
7.30e-09 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 57.49 E-value: 7.30e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496047653 1 MSILIKN--VLFNDRTI--DIYIEGKEIKQIGEGlsfPADKILDGSRKAVIPGFVNAHTHAAM 59
Cdd:PRK08323 1 MSTLIKNgtVVTADDTYkaDVLIEDGKIAAIGAN---LGDEVIDATGKYVMPGGIDPHTHMEM 60
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-113 |
3.37e-08 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 55.30 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 3 ILIKN--VLFNDRTI--DIYIEGKEIKQIGEGLSFPAD-KILDGSRKAVIPGFVNAHTHAamtlfrgfgdDMPLMpwleq 77
Cdd:cd01314 1 LIIKNgtIVTADGSFkaDILIEDGKIVAIGPNLEAPGGvEVIDATGKYVLPGGIDPHTHL----------ELPFM----- 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 496047653 78 kiwpneAKMTREDVYWGAKLAclemIKSGTTTFFDM 113
Cdd:cd01314 66 ------GTVTADDFESGTRAA----AAGGTTTIIDF 91
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
1-362 |
3.37e-08 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 54.94 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 1 MSILIKNV-LFNDRTIDIYIEGKEIKQIGEGLSFPAD-KILDGSRKAVIPGFVNAHTHAAMTLFrgfGddmplMPWLEQK 78
Cdd:PRK05985 2 TDLLFRNVrPAGGAAVDILIRDGRIAAIGPALAAPPGaEVEDGGGALALPGLVDGHIHLDKTFW---G-----DPWYPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 79 IWPNEAKMTREDVYWGAKLA----------CLEMIKSGTTTFfdmyqrpRVTADVTEEMGLRGIiAGVcfdgfdKEEAEK 148
Cdd:PRK05985 74 PGPSLRERIANERRRRAASGhpaaeralalARAAAAAGTTAM-------RSHVDVDPDAGLRHL-EAV------LAARET 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 149 CkrhneRLIQDVdnysKRVRFsigP-HAIYTVSG--ELLKWAHR-------------------------FAM--EHQIPI 198
Cdd:PRK05985 140 L-----RGLIDI----QIVAF---PqSGVLSRPGtaELLDAALRagadvvggldpagidgdpegqldivFGLaeRHGVGI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 199 HLHLAETeGE-----VKDSLDRF------GLTPVRYLYKLGVLSPRLIiahgiyidDDELRMLADHEVKVVHNPASNMKL 267
Cdd:PRK05985 208 DIHLHEP-GElgafqLERIAARTralgmqGRVAVSHAFCLGDLPEREV--------DRLAERLAEAGVAIMTNAPGSVPV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 268 ASgihfkFKEMRQLGITVGLGTDGCSSS----NNLDMIE-AMKLASLLGkaWRKDPEALTANEMlqaATAEGAAMFGLKA 342
Cdd:PRK05985 279 PP-----VAALRAAGVTVFGGNDGIRDTwwpyGNGDMLErAMLIGYRSG--FRTDDELAAALDC---VTHGGARALGLED 348
|
410 420
....*....|....*....|
gi 496047653 343 GQIKEGYLADLCLIDLNTPA 362
Cdd:PRK05985 349 YGLAVGARADFVLVDAETVA 368
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
178-355 |
1.68e-06 |
|
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: 50.00 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 178 TVSGELLKWAHRFAMEHQIPIHLHlAETEGEVKDSLDRFGLTPVRYlyklGVLSPRLIIAHGIYIDDDELRMLADHEVKV 257
Cdd:cd01300 291 LISPEELEELVRAADEAGLQVAIH-AIGDRAVDTVLDALEAALKDN----PRADHRHRIEHAQLVSPDDIPRFAKLGVIA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 258 VHNP--------ASNMKL----ASGIHFKFKEMRQLGITVGLGTD-GCSSSNNLDMIE-AMKLASLLGKAWRKDPEALTA 323
Cdd:cd01300 366 SVQPnhlysdgdAAEDRRlgeeRAKRSYPFRSLLDAGVPVALGSDaPVAPPDPLLGIWaAVTRKTPGGGVLGNPEERLSL 445
|
170 180 190
....*....|....*....|....*....|....
gi 496047653 324 NEMLQAATAEGA-AMFGL-KAGQIKEGYLADLCL 355
Cdd:cd01300 446 EEALRAYTIGAAyAIGEEdEKGSLEPGKLADFVV 479
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
16-113 |
4.42e-06 |
|
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: 48.59 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 16 DIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHaamtlFRGFGddmplmpwLEQKiwpneakmtrEDVYWGA 95
Cdd:TIGR00857 7 DILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVH-----LRDPG--------EEYK----------EDIESGS 63
|
90
....*....|....*...
gi 496047653 96 KLAclemIKSGTTTFFDM 113
Cdd:TIGR00857 64 KAA----AHGGFTTVADM 77
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-357 |
1.18e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 47.19 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 3 ILIKNVLFNDRTI---DIYIEGKEIKQIGEGLS-FPADKILDGSRKAVIPGFVNAHTHAamtlfrGFGDDMPlmpwleqk 78
Cdd:cd00854 2 IIKNARILTPGGLedgAVLVEDGKIVAIGPEDElEEADEIIDLKGQYLVPGFIDIHIHG------GGGADFM-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 79 iwpneakmtrEDVYWGAKLACLEMIKSGTTTFF---------DMYQRPRVTADVTEEmGLRGIIAGVCFDG--FdkeEAE 147
Cdd:cd00854 68 ----------DGTAEALKTIAEALAKHGTTSFLpttvtappeEIAKALAAIAEAIAE-GQGAEILGIHLEGpfI---SPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 148 KCKRHNERLIQ--DVDNYSKRVRFSIGPHAIYTVSGELLKwAH---RFAMEHQIPIHL-HLAETEGEVKDSLDrFGLTPV 221
Cdd:cd00854 134 KKGAHPPEYLRapDPEELKKWLEAAGGLIKLVTLAPELDG-ALeliRYLVERGIIVSIgHSDATYEQAVAAFE-AGATHV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 222 RYLY---------KLGV-----LSPRL---IIAHGIYIDDDELRMLADhevkvvHNPASNMKL------ASGI---HFKF 275
Cdd:cd00854 212 THLFnamsplhhrEPGVvgaalSDDDVyaeLIADGIHVHPAAVRLAYR------AKGADKIVLvtdamaAAGLpdgEYEL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 276 KEMRqlgITVGLGT----DGCSSSNNLDMIEAMK-LASLLGkawrkdpeaLTANEMLQAATAEGAAMFGL--KAGQIKEG 348
Cdd:cd00854 286 GGQT---VTVKDGVarlaDGTLAGSTLTMDQAVRnMVKWGG---------CPLEEAVRMASLNPAKLLGLddRKGSLKPG 353
|
....*....
gi 496047653 349 YLADLCLID 357
Cdd:cd00854 354 KDADLVVLD 362
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
1-80 |
2.70e-05 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 46.32 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 1 MSILIKNVLFND------RTIDIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHAAMTLFRGfgddmplmPW 74
Cdd:COG3653 2 FDLLIRGGTVVDgtgappFRADVAIKGGRIVAVGDLAAAEAARVIDATGLVVAPGFIDIHTHYDLQLLWD--------PR 73
|
....*.
gi 496047653 75 LEQKIW 80
Cdd:COG3653 74 LEPSLR 79
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
16-56 |
2.27e-04 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 43.15 E-value: 2.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 496047653 16 DIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTH 56
Cdd:PRK06189 22 DIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVH 62
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
3-56 |
1.76e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 40.22 E-value: 1.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 496047653 3 ILIKN---VLFND-RTIDIYIEGKEIKQIGEGLSFPAdKILDGSRKAVIPGFVNAHTH 56
Cdd:PRK08044 5 LIIKNgtvILENEaRVVDIAVKGGKIAAIGQDLGDAK-EVMDASGLVVSPGMVDAHTH 61
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
20-59 |
2.12e-03 |
|
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: 39.99 E-value: 2.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 496047653 20 EGKeIKQIGEGLSFPAD-KILDGSRKAVIPGFVNAHTHAAM 59
Cdd:cd01309 1 DGK-IVAVGAEITTPADaEVIDAKGKHVTPGLIDAHSHLGL 40
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
17-357 |
2.38e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 40.17 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 17 IYIEGKEIKQIG-----EGLSFPADKILDGSRKAVIPGFVNAHTHAAMT--------------------LFRGFGDDMPL 71
Cdd:COG1574 30 VAVRDGRIVAVGsdaevRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGglallgvdlsgarsldellaRLRAAAAELPP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 72 MPWL-----EQKIWPNEAKMTRED---------VY---------W----------------------------------- 93
Cdd:COG1574 110 GEWIlgrgwDESLWPEGRFPTRADldavspdrpVVltrvdghaaWvnsaalelagitadtpdpeggeierdadgeptgvl 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 94 ----------------------GAKLACLEMIKSGTTTFFDM---------YQRprvtADVTEEMGLRgIIAGVCFDGFD 142
Cdd:COG1574 190 reaamdlvraaippptpeelraALRAALRELASLGITSVHDAglgpddlaaYRE----LAAAGELPLR-VVLYLGADDED 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 143 KEEAEKCKRHNERliqdvdnYSKRVRF---------SIGPH---------------AIYTVSGELLKWAHRFAMEHQIPI 198
Cdd:COG1574 265 LEELLALGLRTGY-------GDDRLRVggvklfadgSLGSRtaallepyaddpgnrGLLLLDPEELRELVRAADAAGLQV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 199 HLH----LAetegeVKDSLDRFGltpvRYLYKLGVLSPRLIIAHGIYIDDDELRMLADHEVKVVHNP---ASNMKLASGI 271
Cdd:COG1574 338 AVHaigdAA-----VDEVLDAYE----AARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPthaTSDGDWAEDR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 272 --------HFKFKEMRQLGITVGLGTDgcSSSNNLDMIEAMKLA----SLLGKAWRKDpEALTANEMLQAATAEGAAMFG 339
Cdd:COG1574 409 lgperaarAYPFRSLLDAGAPLAFGSD--APVEPLDPLLGIYAAvtrrTPSGRGLGPE-ERLTVEEALRAYTIGAAYAAF 485
|
490 500
....*....|....*....|
gi 496047653 340 L--KAGQIKEGYLADLCLID 357
Cdd:COG1574 486 EedEKGSLEPGKLADFVVLD 505
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
3-57 |
2.44e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 39.83 E-value: 2.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496047653 3 ILIKNV------LFNDRTIDIYIEGKEIKQIGEGLSFP-ADKILDGSRKAVIPGFVNAHTHA 57
Cdd:PRK09237 1 LLLRGGrvidpaNGIDGVIDIAIEDGKIAAVAGDIDGSqAKKVIDLSGLYVSPGWIDLHVHV 62
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
16-56 |
2.60e-03 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 40.07 E-value: 2.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 496047653 16 DIYIEGKEIKQIGEGLSfPADKILDGSRKAVIPGFVNAHTH 56
Cdd:PRK13404 23 DIGIRGGRIAALGEGLG-PGAREIDATGRLVLPGGVDSHCH 62
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-61 |
3.24e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 39.62 E-value: 3.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496047653 1 MSILIKNVLFND--RTIDIYIEGKEIKQIGEGLSFPADKILDGSRKAVIPGFVNAHTHAAMTL 61
Cdd:PRK07572 2 FDLIVRNANLPDgrTGIDIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHMDATL 64
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
16-59 |
5.19e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 39.06 E-value: 5.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 496047653 16 DIYIEGKEIKQIGEGLSFPAD-KILDGSRKAVIPGFVNAHTHAAM 59
Cdd:PLN02942 24 DVYVEDGIIVAVAPNLKVPDDvRVIDATGKFVMPGGIDPHTHLAM 68
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-113 |
7.35e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 38.48 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496047653 1 MSILIKN--VLFNDR--TIDIYIEGKEIKQIGEGLS-FPADKILDGSRKAVIPGFVNAHTHaamtlFRgfgddmplMPWL 75
Cdd:PRK02382 2 RDALLKDgrVYYNNSlqPRDVRIDGGKITAVGKDLDgSSSEEVIDARGMLLLPGGIDVHVH-----FR--------EPGY 68
|
90 100 110
....*....|....*....|....*....|....*...
gi 496047653 76 EQKiwpneakmtrEDVYWGAKLAclemIKSGTTTFFDM 113
Cdd:PRK02382 69 THK----------ETWYTGSRSA----AAGGVTTVVDQ 92
|
|
| |
