|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
1-444 |
1.17e-175 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 499.38 E-value: 1.17e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 1 MSTWFFPSALVEGRIAHNVRVQ-SQNGVITAVTIGA-EPHRHTFDGVAVPGFANTHSHIFHRGLRGAGE-----GEDFWS 73
Cdd:PRK09229 2 MTTLFAERALLPDGWARNVRLTvDADGRIAAVEPGAaPAGAERLAGPVLPGMPNLHSHAFQRAMAGLTEvrgppQDSFWS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 74 WRTEMYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFHYVHHQPDGTPYRD-HAMELALVNAAIEAGIRITVLDTCYL 152
Cdd:PRK09229 82 WRELMYRFALRLTPDQLEAIARQLYVEMLEAGYTSVGEFHYLHHDPDGTPYADpAEMALRIVAAARAAGIGLTLLPVLYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 153 HAGPG-ASLGVDQKRFGDgSVEGWLERWRALRDALPDSPLVTVGAALHSVRAVSPDEMATAVSGLPERVPIHIHVSEQPR 231
Cdd:PRK09229 162 HSGFGgQPPNPGQRRFIN-DPDGFLRLLEALRRALAALPGARLGLAPHSLRAVTPDQLAAVLALAAPDGPVHIHIAEQTK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 232 ENTECLAAHGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIG 311
Cdd:PRK09229 241 EVDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 312 TDEDVITDPFTELRMLESTARLVTGTRGVIGCEA-------LWKIGTQNGVESLrpaaeplprqtstpGPGSAGLAAGDP 384
Cdd:PRK09229 321 SDSHVSIDLVEELRLLEYGQRLRDRRRNVLAAAAqpsvgrrLFDAALAGGAQAL--------------GRAIGGLAVGAR 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 385 ADIVVVEPSSARLAGVDP----TRWPLVATANDVAATIVAGEW------NRLDAAVAEDLRHVLDELRGR 444
Cdd:PRK09229 387 ADLVVLDLDHPALAGREGdallDRWVFAGGDAAVRDVWVAGRWvvrdgrHRLREAIAAAFRAALAALLAA 456
|
|
| hutF |
TIGR02022 |
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to ... |
1-444 |
3.90e-123 |
|
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to glutamate in four step, the last being removal of formamide. This model describes an alternate fourth step, formiminoglutamate hydrolase, which leads to N-formyl-L-glutamate. This product may be acted on by formylglutamate amidohydrolase (TIGR02017) and bypass glutamate as a product during its degradation. Alternatively, removal of formate (by EC 3.5.1.68) would yield glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273931 [Multi-domain] Cd Length: 454 Bit Score: 365.62 E-value: 3.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 1 MSTWFFPSALVEGRIAHNVRVQSQNGVITAVTIG--AEPHRHTFDGVAVPGFANTHSHIFHRGLRG----AGEGED-FWS 73
Cdd:TIGR02022 1 MHVYWAERALLPDGWAEGVRIAVADGRILAIETGvpAAPGDERLSGPLLPGLANLHSHAFQRAMAGlaevAGSGGDsFWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 74 WRTEMYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFHYVHHQPDGTPYRDHA-MELALVNAAIEAGIRITVLDTCYL 152
Cdd:TIGR02022 81 WRELMYRFADRLTPEQLQAIARQLYVEMLEAGFTRVGEFHYLHHAPDGTPYADPAeMAERIAAAAADAGIGLTLLPVFYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 153 HAGPGASLGVD-QKRFGDgSVEGWLERWRALRDALPDSPLVTVGAALHSVRAVSPDEMATAVSGLPERVPIHIHVSEQPR 231
Cdd:TIGR02022 161 HSGFGGAAPNPgQRRFIH-DPERFARLVEVLRRTLAAQPGAVLGLAPHSLRAVTPEQLAAVLQASDRQAPVHIHVAEQQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 232 ENTECLAAHGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIG 311
Cdd:TIGR02022 240 EVDDCLAWSGRRPVEWLLDHGPVDARWCLVHATHLTDEETKLLAKSGAVAGLCPTTEANLGDGIFPAVDFAAAGGRFGIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 312 TDEDVITDPFTELRMLESTARLVTGTRGVIGCEALWKIGTQNGVESLRPAAEPLPRQTStpgpgsaGLAAGDPADIVVVE 391
Cdd:TIGR02022 320 SDSHVLIDVAEELRQLEYGQRLRDRARNVLAAGPGPSVGRALYDAALLGGAQALGRATG-------GLRAGARADFLTLD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 488476045 392 PSSARLAGVDPT----RWPLVATANDVAATIVAGEWnrldaaVAEDLRHVLDELRGR 444
Cdd:TIGR02022 393 GDHPRLAGALGDslldRWLFAGGKAAVRDVWVGGRW------VVRDGRHALREEIGR 443
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
9-422 |
3.24e-115 |
|
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: 344.05 E-value: 3.24e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 9 ALVEGRIAHNVRVQ-SQNGVITAVTIGAEPHR-HTFDGVAVPGFANTHSHIFHRGLRGAGEG-----EDFWSWRTEMYRL 81
Cdd:cd01313 1 ALLPEGWERNVRIEvDADGRIAAVNPDTATEAvALLGGALLPGMPNLHSHAFQRAMAGLTEYrgsaaDSFWTWRELMYRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 82 ANRLDPDSYYRLARAAFAEMVAAGYTSVGEFHYVHHQPDGTPYRDHA-MELALVNAAIEAGIRITVLDTCYLHAG-PGAS 159
Cdd:cd01313 81 AARLTPEQIEAIARQLYIEMLLAGITAVGEFHYVHHDPDGTPYADPAeLAQRVIAAASDAGIGITLLPVLYARAGfGGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 160 LGVDQKRFGDGSVEGWLERWRALRdALPDSPLVTVGAALHSVRAVSPDEMATAVSGLPERVPIHIHVSEQPRENTECLAA 239
Cdd:cd01313 161 PNPGQRRFINGYEDFLGLLEKALR-AVKEHAAARIGVAPHSLRAVPAEQLAALAALASEKAPVHIHLAEQPKEVDDCLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 240 HGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTDEDVITD 319
Cdd:cd01313 240 HGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSDSNARID 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 320 PFTELRMLESTARLVTGTRGVIGC------EALWKIGTQNGVESLrpaaeplprqtstpGPGSAGLAAGDPADIVVVEPS 393
Cdd:cd01313 320 LLEELRQLEYSQRLRDRARNVLATaggssaRALLDAALAGGAQAL--------------GLATGALEAGARADLLSLDLD 385
|
410 420 430
....*....|....*....|....*....|...
gi 488476045 394 SARLAGVDP----TRWPLVATANDVAATIVAGE 422
Cdd:cd01313 386 HPSLAGALPdtllDAWVFAAGDREVRDVVVGGR 418
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
12-423 |
4.33e-100 |
|
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: 305.21 E-value: 4.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 12 EGRIAHNVRVQSQNGVITAVTIGAEPHRH-----TFDG---VAVPGFANTHSHIFHRGLRGAGEGEDFWSWRTE-MYRLA 82
Cdd:COG0402 15 AGGVLEDGAVLVEDGRIAAVGPGAELPARypaaeVIDAggkLVLPGLVNTHTHLPQTLLRGLADDLPLLDWLEEyIWPLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 83 NRLDPDSYYRLARAAFAEMVAAGYTSVGEFHYVHHqpdgtpyrdhAMELALVNAAIEAGIRITVLDTCYLHAGPGASLGv 162
Cdd:COG0402 95 ARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHP----------ESADALAEAAAEAGIRAVLGRGLMDRGFPDGLRE- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 163 dqkrfgdgSVEGWLERWRALRDAL--PDSPLVTVGAALHSVRAVSPDEMATAVSGLPER-VPIHIHVSEQPRENTECLAA 239
Cdd:COG0402 164 --------DADEGLADSERLIERWhgAADGRIRVALAPHAPYTVSPELLRAAAALARELgLPLHTHLAETRDEVEWVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 240 HGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTDE---DV 316
Cdd:COG0402 236 YGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGaasNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 317 ITDPFTELRMLESTARLVTGTRGVIGCEALWKIGTQNGVESLRpaaepLPRQTstpgpGSagLAAGDPADIVVVEPSSAR 396
Cdd:COG0402 316 SLDMFEEMRLAALLQRLRGGDPTALSAREALEMATLGGARALG-----LDDEI-----GS--LEPGKRADLVVLDLDAPH 383
|
410 420
....*....|....*....|....*....
gi 488476045 397 LAGVDPTRWPLV--ATANDVAATIVAGEW 423
Cdd:COG0402 384 LAPLHDPLSALVyaADGRDVRTVWVAGRV 412
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
12-423 |
2.86e-53 |
|
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: 183.56 E-value: 2.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 12 EGRIAHNVRVQSQNGVITAV----TIGAEPHRHTFDG---VAVPGFANTHSHIFHRGLRGAGEGEDFWSWRTEMY-RLAN 83
Cdd:cd01298 13 PRRVLEDGDVLVEDGRIVAVgpalPLPAYPADEVIDAkgkVVMPGLVNTHTHLAMTLLRGLADDLPLMEWLKDLIwPLER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 84 RLDPDSYYRLARAAFAEMVAAGYTSVGEFHYVHHQpdgtpyrdhamelALVNAAIEAGIRitvldtcyLHAGPG-ASLGV 162
Cdd:cd01298 93 LLTEEDVYLGALLALAEMIRSGTTTFADMYFFYPD-------------AVAEAAEELGIR--------AVLGRGiMDLGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 163 DQKRFGDGSVEGWLERWRALRDalPDSPLVTVGAALHSVRAVSPDEMAtAVSGLPER--VPIHIHVSEQPRENTECLAAH 240
Cdd:cd01298 152 EDVEETEEALAEAERLIREWHG--AADGRIRVALAPHAPYTCSDELLR-EVAELAREygVPLHIHLAETEDEVEESLEKY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 241 GLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTD-----ED 315
Cdd:cd01298 229 GKRPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgaasnNN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 316 VitDPFTELRMLESTARLVTGTRGVIGCEALWKIGTQNGVESLRpaaeplprqtsTPGPGSagLAAGDPADIVVVEPSSA 395
Cdd:cd01298 309 L--DMFEEMRLAALLQKLAHGDPTALPAEEALEMATIGGAKALG-----------LDEIGS--LEVGKKADLILIDLDGP 373
|
410 420 430
....*....|....*....|....*....|
gi 488476045 396 RLAGVDPTRWPLV--ATANDVAATIVAGEW 423
Cdd:cd01298 374 HLLPVHDPISHLVysANGGDVDTVIVNGRV 403
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
24-444 |
1.15e-33 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 131.51 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 24 QNGVITAVTIGAEPHR---HTFDG---VAVPGFANTHSHIFH---RGLRGAGEGEDFwSWRTEMYRLANRLDPDSYYRLA 94
Cdd:PRK08203 29 EGGRIVEVGPGGALPQpadEVFDArghVVTPGLVNTHHHFYQtltRALPAAQDAELF-PWLTTLYPVWARLTPEMVRVAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 95 RAAFAEMVAAGYTSVGEFHYVHhqPDGtpyRDHAMElALVNAAIEAGIRitvldtcyLHAGPGA-SLGVDQkrfG----D 169
Cdd:PRK08203 108 QTALAELLLSGCTTSSDHHYLF--PNG---LRDALD-DQIEAAREIGMR--------FHATRGSmSLGESD---GglppD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 170 GSVEG----------WLERWRalrDALPDSpLVTVGAALHSVRAVSPDEM-ATAVSGLPERVPIHIHVSEQPRENTECLA 238
Cdd:PRK08203 171 SVVEDedailadsqrLIDRYH---DPGPGA-MLRIALAPCSPFSVSRELMrESAALARRLGVRLHTHLAETLDEEAFCLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 239 AHGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTDEDVIT 318
Cdd:PRK08203 247 RFGMRPVDYLEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 319 DP---FTELRMLESTARLVTGTRGVIGCEALWkIGTQNGveslrpaAEPLPRqtstPGPGSagLAAGDPADIVVVEPSSA 395
Cdd:PRK08203 327 DGsnlIGEARQALLLQRLRYGPDAMTAREALE-WATLGG-------ARVLGR----DDIGS--LAPGKLADLALFDLDEL 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 488476045 396 RLAGV-DPTRWPLVATANDVAATIVAGEWNRLD--------AAVAEDLRHVLDELRGR 444
Cdd:PRK08203 393 RFAGAhDPVAALVLCGPPRADRVMVGGRWVVRDgqlttldlAALIARHRAAARRLAAG 450
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
24-421 |
2.94e-26 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 110.54 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 24 QNGVITAV-TIGAEPHRHTFD---GVAVPGFANTHSHIFHRGLRG--AGEGEDFWSW-RTEMYRLANRLDPDSYYRLARA 96
Cdd:PRK12393 31 RDGRIAAIgALTPLPGERVIDatdCVVYPGWVNTHHHLFQSLLKGvpAGINQSLTAWlAAVPYRFRARFDEDLFRLAARI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 97 AFAEMVAAGYTSVGEFHYVHHqPDGTPyrdhAMELALVNAAIEAGIRITV-----LDTCYLHAGPGASLGVDqkrfgdgS 171
Cdd:PRK12393 111 GLVELLRSGCTTVADHHYLYH-PGMPF----DTGDILFDEAEALGMRFVLcrggaTQTRGDHPGLPTALRPE-------T 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 172 VEGWLERWRALR----DALPDSPLVTVGA---ALHSVRAVSPDEMATAVSGLPERvpIHIHVSEQPRENTECLAAHGLTP 244
Cdd:PRK12393 179 LDQMLADVERLVsryhDASPDSLRRVVVApttPTFSLPPELLREVARAARGMGLR--LHSHLSETVDYVDFCREKYGMTP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 245 TAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTD---EDVITDPF 321
Cdd:PRK12393 257 VQFVAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDgaaSNESADML 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 322 TELRMLESTARLVTGTRGViGCEALWKIGTQNGVESLrpaaeplprqtstpG-PGSAGLAAGDPADIVVVEPSSARLAGV 400
Cdd:PRK12393 337 SEAHAAWLLHRAEGGADAT-TVEDVVHWGTAGGARVL--------------GlDAIGTLAVGQAADLAIYDLDDPRFFGL 401
|
410 420
....*....|....*....|...
gi 488476045 401 -DPTRWPLVATAN-DVAATIVAG 421
Cdd:PRK12393 402 hDPAIAPVACGGPaPVKALLVNG 424
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
45-423 |
4.74e-26 |
|
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: 107.97 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 45 VAVPGFANTHSHIFHRGLRGAGEGEDFWSWRtemyrlanrldpdsyyrlARAAFAEMVAAGYTSVGEFHYVHHQPDgtpy 124
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYEA------------------LRLGITTMLKSGTTTVLDMGATTSTGI---- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 125 rdhameLALVNAAIEA--GIRITvldtcylhaGPGASLGvdqkrfGDGSVEGWLERWRALRDA-----LPDSPLVTVGAA 197
Cdd:pfam01979 59 ------EALLEAAEELplGLRFL---------GPGCSLD------TDGELEGRKALREKLKAGaefikGMADGVVFVGLA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 198 LHSVRAVSPDEMATAVSGLPER-VPIHIHVSEQPRENTECLAAHG-----LTPTAVLDRAGVLSDRTTII-HATHLTGGD 270
Cdd:pfam01979 118 PHGAPTFSDDELKAALEEAKKYgLPVAIHALETKGEVEDAIAAFGggiehGTHLEVAESGGLLDIIKLILaHGVHLSPTE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 271 IAMIA--ASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTDEDVITDPFTelrMLESTARLV-TGTRGVIGCEAL- 346
Cdd:pfam01979 198 ANLLAehLKGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLN---MLEELRLALeLQFDPEGGLSPLe 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488476045 347 -WKIGTQNGVESLRpaaepLPRQTSTpgpgsagLAAGDPADIVVVEP-SSARLAGVDPTRWplvatandVAATIVAGEW 423
Cdd:pfam01979 275 aLRMATINPAKALG-----LDDKVGS-------IEVGKDADLVVVDLdPLAAFFGLKPDGN--------VKKVIVKGKI 333
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
97-358 |
9.73e-26 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 108.85 E-value: 9.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 97 AFAEMVAAGYTSVGEfHYVHHQpdgtpyrdhamelALVNAAIEAGIR----ITVLDtcylHAGPGASlgvdqkrfgdgSV 172
Cdd:PRK09045 117 AIAEMLRGGTTCFND-MYFFPE-------------AAAEAAHQAGMRaqigMPVLD----FPTAWAS-----------DA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 173 EGWLERWRALRDALPDSPLVTVGAALHSVRAVSpDEMATAVSGLPER--VPIHIHVSEQPRENTECLAAHGLTPTAVLDR 250
Cdd:PRK09045 168 DEYLAKGLELHDQWRHHPLISTAFAPHAPYTVS-DENLERIRTLAEQldLPIHIHLHETAQEIADSLKQHGQRPLARLAR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 251 AGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTD-----EDVitDPFTELR 325
Cdd:PRK09045 247 LGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDgaasnNDL--DLFGEMR 324
|
250 260 270
....*....|....*....|....*....|...
gi 488476045 326 MLESTARLVTGTRGVIGCEALWKIGTQNGVESL 358
Cdd:PRK09045 325 TAALLAKAVAGDATALPAHTALRMATLNGARAL 357
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
45-430 |
1.28e-21 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 96.41 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 45 VAVPGFANTHSHIFHRGLRGAGEGEDFWSWRTE-MYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFhYVHhqpdgtp 123
Cdd:PRK08393 51 VVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNyIWPRERKLKRKDIYWGAYLGLLEMIKSGTTTFVDM-YFH------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 124 yrdhaMElALVNAAIEAGIRitvldtCYLHAGPgASLGVDQKRfgDGSVEGWLERWRALRDAlpDSPLVTVGAALHSVRA 203
Cdd:PRK08393 123 -----ME-EVAKATLEVGLR------GYLSYGM-VDLGDEEKR--EKEIKETEKLMEFIEKL--NSPRVHFVFGPHAPYT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 204 VSPDeMATAVSGLPER--VPIHIHVSEQPRENTECLAAHGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVV 281
Cdd:PRK08393 186 CSLA-LLKWVREKAREwnKLITIHLSETMDEIKQIREKYGKSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 282 SLCPTTEADLGDGIARVKDLQDAGVRMAIGTD---EDVITDPFTELRMLESTARLVTGTRGVIGCEALWKIGTQNGVESL 358
Cdd:PRK08393 265 AHNPASNMKLGSGVMPLRKLLNAGVNVALGTDgaaSNNNLDMLREMKLAALLHKVHNLDPTIADAETVFRMATQNGAKAL 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488476045 359 RPAAeplprqtstpgpgsAGLAAGDPADIVVVEPSSARLAGVDPTRWPLV--ATANDVAATIVAGEWNRLDAAV 430
Cdd:PRK08393 345 GLKA--------------GVIKEGYLADIAVIDFNRPHLRPINNPISHLVysANGNDVETTIVDGKIVMLDGEV 404
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
44-421 |
5.36e-20 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 91.74 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 44 GVAVPGFANTHSHIFHRGLRGAGEGEDFWSWRTE-MYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFHYvhhqpdgt 122
Cdd:PRK06038 51 SVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLNDhIWPAEAKLTAEDVYAGSLLACLEMIKSGTTSFADMYF-------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 123 pYRDHAMElalvnAAIEAGIRitvldtCYLHAGPgASLGVDQKrfGDGSVEGWLERWRALRDALPDSPLVTVGAalHSVR 202
Cdd:PRK06038 123 -YMDEVAK-----AVEESGLR------AALSYGM-IDLGDDEK--GEAELKEGKRFVKEWHGAADGRIKVMYGP--HAPY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 203 AVSpDEMATAVSGLP--ERVPIHIHVSEQPRENTECLAAHGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTV 280
Cdd:PRK06038 186 TCS-EEFLSKVKKLAnkDGVGIHIHVLETEAELNQMKEQYGMCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 281 VSLCPTTEADLGDGIARVKDLQDAGVRMAIGTD---EDVITDPFTELRMLESTARLVTGTRGVIGCEALWKIGTQNGVES 357
Cdd:PRK06038 265 VSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDgcaSNNNLDMFEEMKTAALLHKVNTMDPTALPARQVLEMATVNGAKA 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488476045 358 LrpaaeplprqtstpGPGSAGLAAGDPADIVVVEPSSARLAGVDPTRWPLV--ATANDVAATIVAG 421
Cdd:PRK06038 345 L--------------GINTGMLKEGYLADIIIVDMNKPHLTPVRDVPSHLVysASGSDVDTTIVDG 396
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
45-444 |
2.28e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 90.06 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 45 VAVPGFANTHSHIFHRGLRGAGEGEDFWSWRTEMY-RLANRLDPDSYYRLARAAFAEMVAAGYTSVgeFHYVHHQPdgTP 123
Cdd:PRK08204 54 IVMPGLVDTHRHTWQSVLRGIGADWTLQTYFREIHgNLGPMFRPEDVYIANLLGALEALDAGVTTL--LDWSHINN--SP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 124 yrDHAMelALVNAAIEAGIRitvldTCYLHAGPGASLgvdqkRFGDGSVEGWLERWRALRDAL--PDSPLVTVGAALHSv 201
Cdd:PRK08204 130 --EHAD--AAIRGLAEAGIR-----AVFAHGSPGPSP-----YWPFDSVPHPREDIRRVKKRYfsSDDGLLTLGLAIRG- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 202 RAVSPDEMATAVSGLPER--VPIHIHVSEQPRENTeclaAHGLTptaVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDT 279
Cdd:PRK08204 195 PEFSSWEVARADFRLARElgLPISMHQGFGPWGAT----PRGVE---QLHDAGLLGPDLNLVHGNDLSDDELKLLADSGG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 280 VVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTDEDVIT--DPFTELRMlestarLVTGTRGVIGcEALWKIGTQNGVES 357
Cdd:PRK08204 268 SFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTggDMFTQMRF------ALQAERARDN-AVHLREGGMPPPRL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 358 LRPAAEPLPRQTsTPGPGSAG-------LAAGDPADIVVVEPSSARLAGV-DPTRwPLVATAN--DVAATIVAGEW---- 423
Cdd:PRK08204 341 TLTARQVLEWAT-IEGARALGledrigsLTPGKQADLVLIDATDLNLAPVhDPVG-AVVQSAHpgNVDSVMVAGRAvkrn 418
|
410 420
....*....|....*....|.
gi 488476045 424 NRLDAAVAEDLRHVLDELRGR 444
Cdd:PRK08204 419 GKLLGVDLERLRRLAAASRDR 439
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
47-392 |
9.66e-19 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 87.75 E-value: 9.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 47 VPGFANTHSHIFHRGLRGAGEGEDFWSWRTE-MYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFhyvhhqpdgtpYR 125
Cdd:PRK06687 57 MPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDyIWPAESEFTPDMTTNAVKEALTEMLQSGTTTFNDM-----------YN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 126 DHAMELALVNAAI-EAGIRitvldtCYLhagpGASLGVDQKRfgdgSVEGWLERWRALRDALP--DSPLVTVGAALHSVR 202
Cdd:PRK06687 126 PNGVDIQQIYQVVkTSKMR------CYF----SPTLFSSETE----TTAETISRTRSIIDEILkyKNPNFKVMVAPHSPY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 203 AVSPDEMATAVSGLPE-RVPIHIHVSEQPRENTECLAAHGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVV 281
Cdd:PRK06687 192 SCSRDLLEASLEMAKElNIPLHVHVAETKEESGIILKRYGKRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 282 SLCPTTEADLGDGIARVKDLQDAGVRMAIGTDEDVIT---DPFTELRMLESTARLVTGTRGVIGCEALWKIGTQNGVESL 358
Cdd:PRK06687 272 AHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVASNnnlDMFEEGRTAALLQKMKSGDASQFPIETALKVLTIEGAKAL 351
|
330 340 350
....*....|....*....|....*....|....
gi 488476045 359 rpaaePLPRQTSTpgpgsagLAAGDPADIVVVEP 392
Cdd:PRK06687 352 -----GMENQIGS-------LEVGKQADFLVIQP 373
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
47-424 |
2.05e-18 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 87.04 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 47 VPGFANTHSHIFHRGLRGAGEGEDFWSW-RTEMYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFHyvhhQPDGTPyR 125
Cdd:PRK15493 58 LPGLVNTHTHVVMSLLRGIGDDMLLQPWlETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMF----NPIGVD-Q 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 126 DHAMElalvnAAIEAGIRITVLDTCYlhagpgaSLGV--DQKRfGDGSVEGWLERWralrdaLPDSPLVTVGAALHSVRA 203
Cdd:PRK15493 133 DAIME-----TVSRSGMRAAVSRTLF-------SFGTkeDEKK-AIEEAEKYVKRY------YNESGMLTTMVAPHSPYT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 204 VSPDEMAT-AVSGLPERVPIHIHVSEQPRENTECLAAHGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVS 282
Cdd:PRK15493 194 CSTELLEEcARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 283 LCPTTEADLGDGIARVKDLQDAGVRMAIGTDEDVIT---DPFTELRMLESTARLVTGTRGVIGCEALWKIGTQNGVESLR 359
Cdd:PRK15493 274 HNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNnnlDMFEEMRIATLLQKGIHQDATALPVETALTLATKGAAEVIG 353
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488476045 360 paaeplPRQTSTpgpgsagLAAGDPADIVVVEPSSA-RLAGVDPTRWPLV--ATANDVAATIVAGE---WN 424
Cdd:PRK15493 354 ------MKQTGS-------LEVGKCADFITIDPSNKpHLQPADEVLSHLVyaASGKDISDVIINGKrvvWN 411
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
24-422 |
4.28e-18 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 86.21 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 24 QNGVITAV-----TIGAEPHRHTFDGVAVPGFANTHSHIFHRGLRGAGEGEDFWSW-RTEMYRLANRLDPDSYYRLARAA 97
Cdd:PRK07228 27 EDDRIAAVgdrldLEDYDDHIDATGKVVIPGLIQGHIHLCQTLFRGIADDLELLDWlKDRIWPLEAAHDAESMYYSALLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 98 FAEMVAAGYTSVGEFHYVHHQpdgtpyrDHAMElalvnAAIEAGIRiTVLDTCYLHAGPGASLGVDQKRfgDGSV---EG 174
Cdd:PRK07228 107 IGELIESGTTTIVDMESVHHT-------DSAFE-----AAGESGIR-AVLGKVMMDYGDDVPEGLQEDT--EASLaesVR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 175 WLERWRalrdalpdsplvtvGAALHSVR-AVSP-------DEMATAVSGLPER--VPIHIHVSEQPRENTECLAAHGLTP 244
Cdd:PRK07228 172 LLEKWH--------------GADNGRIRyAFTPrfavsctEELLRGVRDLADEygVRIHTHASENRGEIETVEEETGMRN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 245 TAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTDE---DVITDPF 321
Cdd:PRK07228 238 IHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGapcNNTLDPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 322 TELRM--LESTARLVTGTrgVIGCEALWKIGTQNGVESLRPAAEplprqtstpgPGSagLAAGDPADIVVVEPSSAR--- 396
Cdd:PRK07228 318 TEMRQaaLIQKVDRLGPT--AMPARTVFEMATLGGAKAAGFEDE----------IGS--LEEGKKADLAILDLDGLHatp 383
|
410 420
....*....|....*....|....*..
gi 488476045 397 LAGVDP-TRWPLVATANDVAATIVAGE 422
Cdd:PRK07228 384 SHGVDVlSHLVYAAHGSDVETTMVDGK 410
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
35-421 |
1.98e-17 |
|
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: 83.87 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 35 AEPHRHTFDGVAVPGFANTHSHIFHRGLRGAGEGEDFWSWrTEMYRL---ANRLDPDSYYRLARAAFAEMVAAGYTSVGE 111
Cdd:cd01303 52 GARVIDSPNQFILPGFIDTHIHAPQYANIGSGLGEPLLDW-LETYTFpeeAKFADPAYAREVYGRFLDELLRNGTTTACY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 112 FHYVHhqPDGTpyrdhameLALVNAAIEAGIRITVLDTC-------YLHAGPGASLGvDQKRFgdgsvegwLERWRALRD 184
Cdd:cd01303 131 FATIH--PEST--------EALFEEAAKRGQRAIAGKVCmdrnapeYYRDTAESSYR-DTKRL--------IERWHGKSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 185 ALpdSPLVTVGAALHSvravSPDEMAtAVSGLPER---VPIHIHVSEQPREnteCLAAHGLTPTA-----VLDRAGVLSD 256
Cdd:cd01303 192 RV--KPAITPRFAPSC----SEELLA-ALGKLAKEhpdLHIQTHISENLDE---IAWVKELFPGArdyldVYDKYGLLTE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 257 RTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTDE---------DVITDPFTELRML 327
Cdd:cd01303 262 KTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVgggtsfsmlDTLRQAYKVSRLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 328 EstaRLVTGTRGVIGCEALWkIGTQNGVESLRpaaepLPRQTSTpgpgsagLAAGDPADIVVVEPSSARLAGVDPTRW-- 405
Cdd:cd01303 342 G---YELGGHAKLSPAEAFY-LATLGGAEALG-----LDDKIGN-------FEVGKEFDAVVIDPSATPLLADRMFRVes 405
|
410 420
....*....|....*....|....
gi 488476045 406 ------PLVATAND--VAATIVAG 421
Cdd:cd01303 406 leealfKFLYLGDDrnIREVYVAG 429
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
43-313 |
4.46e-17 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 83.06 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 43 DGVAVPGFANTHSHI---FHRGLRGAGE-GEDFWS-----WrtemYRLANRLDPDSYYRLARAAFAEMVAAGYTSVgefh 113
Cdd:PRK07203 54 GKLIMPGLINSHNHIysgLARGMMANIPpPPDFISilknlW----WRLDRALTLEDVYYSALICSLEAIKNGVTTV---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 114 YVHHqpdGTPYRDHAMELALVNAAIEAGIRITvldTCYlhagpgaslGVDQKRFGDGSVEGWLERWRALRDA-LPDSPLV 192
Cdd:PRK07203 126 FDHH---ASPNYIGGSLFTIADAAKKVGLRAM---LCY---------ETSDRDGEKELQEGVEENIRFIKHIdEAKDDMV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 193 TVGAALHSVRAVSPDEMATAVSGLPER-VPIHIHVSEQPRENTECLAAHGLTPTAVLDRAGVLSDRTTIIHATHLTGGDI 271
Cdd:PRK07203 191 EAMFGLHASFTLSDATLEKCREAVKETgRGYHIHVAEGIYDVSDSHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEI 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488476045 272 AMIAASDTVVSLCPttEADLGD--GIARVKDLQDAGVRMAIGTD 313
Cdd:PRK07203 271 DLLKETDTFVVHNP--ESNMGNavGYNPVLEMIKNGILLGLGTD 312
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
45-419 |
2.91e-16 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 80.31 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 45 VAVPGFANTHSHIFHRGLRGAGEGEDFWSWRTEMYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFHYvhhqpdgtpy 124
Cdd:PRK06380 51 VVMPGLINTHAHVGMTASKGLFDDVDLEEFLMKTFKYDSKRTREGIYNSAKLGMYEMINSGITAFVDLYY---------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 125 rdhaMELALVNAAIEAGIRI----TVLDTCYlhagpgaslgVDQKRFGDGSVEGWLERWRALRdalpdspLVTVGAALHS 200
Cdd:PRK06380 121 ----SEDIIAKAAEELGIRAflswAVLDEEI----------TTQKGDPLNNAENFIREHRNEE-------LVTPSIGVQG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 201 VRaVSPDEMATAVSGLPER--VPIHIHVSEQPRENTECLAAHGLTPTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASD 278
Cdd:PRK06380 180 IY-VANDETYLKAKEIAEKydTIMHMHLSETRKEVYDHVKRTGERPVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 279 TVVSLCPTTEADLGD-GIARVKDLQDAGVRMAIGTDEDVITDPFTELRMLESTARLVTGTR---GVIGCEALWKIGTQNG 354
Cdd:PRK06380 259 VKVSWNSVSNFKLGTgGSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALSVKNERwdaSIIKAQEILDFATINA 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488476045 355 VESLRPAAeplprqtstpgpGSagLAAGDPADIVVVEPSSARLAgvdPTRwplvatANDVAATIV 419
Cdd:PRK06380 339 AKALELNA------------GS--IEVGKLADLVILDARAPNMI---PTR------KNNIVSNIV 380
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
206-431 |
4.67e-15 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 77.00 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 206 PDEMATAVSGLPER---------VPIHIHVSEQPRENTECLAAHGLTPTAVLDRAGVLSDRTTIIHATHLTG-------- 268
Cdd:PRK06151 212 PDRIETCTVDLLRRtaaaarelgCPVRLHCAQGVLEVETVRRLHGTTPLEWLADVGLLGPRLLIPHATYISGsprlnysg 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 269 -GDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTDedviTDP---FTELRMLESTARLVTGTRGVIGCE 344
Cdd:PRK06151 292 gDDLALLAEHGVSIVHCPLVSARHGSALNSFDRYREAGINLALGTD----TFPpdmVMNMRVGLILGRVVEGDLDAASAA 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 345 ALWKIGTQNGVESLRpaAEPLPRqtstpgpgsagLAAGDPADIVVVEPSSARLAGV-DPTRwPLV--ATANDVAATIVAG 421
Cdd:PRK06151 368 DLFDAATLGGARALG--RDDLGR-----------LAPGAKADIVVFDLDGLHMGPVfDPIR-TLVtgGSGRDVRAVFVDG 433
|
250
....*....|
gi 488476045 422 EWNRLDAAVA 431
Cdd:PRK06151 434 RVVMEDGRLP 443
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
34-313 |
6.98e-14 |
|
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: 72.87 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 34 GAEPHRHTfDGVAVPGFANTHSHIFHRGLRGAGEGEDFWSWRTEMYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFh 113
Cdd:cd01312 18 GAKHEFFP-NGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLKQPWEEAIRQGIRQMLESGTTSIGAI- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 114 yvhhqpdgtpyrdhAMELALVNAAIEAGIRITVldtcYLHAgpgasLGVDQKRFgDGSVEGWLERWRALRDAlpDSPLVT 193
Cdd:cd01312 96 --------------SSDGSLLPALASSGLRGVF----FNEV-----IGSNPSAI-DFKGETFLERFKRSKSF--ESQLFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 194 VGAALHSVRAVSPdEMATAVSGLPER--VPIHIHVSEQPRENTECLAAHGL------------------TPTAVLDRAGV 253
Cdd:cd01312 150 PAISPHAPYSVHP-ELAQDLIDLAKKlnLPLSTHFLESKEEREWLEESKGWfkhfwesflklpkpkklaTAIDFLDMLGG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 254 LSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTD 313
Cdd:cd01312 229 LGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTD 288
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
50-333 |
1.01e-10 |
|
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: 62.35 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 50 FANTHSHIFHRGLRGAGEGEDFWSwrtemyrlANRLDPDSYYRLARAAFAEMVAAGYTSVGEFHYVHhqpdgTPYRDHAM 129
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKE--------AEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTP-----PPTTTKAA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 130 ELALVNAAIE-AGIRITVLDTCYLHAGPGASLGVDQKRfgdgsvegwlerwRALRDALPdspLVTVGAALHS---VRAVS 205
Cdd:cd01292 68 IEAVAEAARAsAGIRVVLGLGIPGVPAAVDEDAEALLL-------------ELLRRGLE---LGAVGLKLAGpytATGLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 206 PDEMATAVSGLPER-VPIHIHVSEQPRENTeclaahglTPTAVLDRAGVLSdRTTIIHATHLTGGDIAMIAASDTVVSLC 284
Cdd:cd01292 132 DESLRRVLEEARKLgLPVVIHAGELPDPTR--------ALEDLVALLRLGG-RVVIGHVSHLDPELLELLKEAGVSLEVC 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 488476045 285 PTTEADL---GDGIARVKDLQDAGVRMAIGTDEDVI---TDPFTELRMLESTARL 333
Cdd:cd01292 203 PLSNYLLgrdGEGAEALRRLLELGIRVTLGTDGPPHplgTDLLALLRLLLKVLRL 257
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
222-313 |
2.50e-10 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 62.13 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 222 IHIHVSEQPREnteCLAAHGLTPTA-----VLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIA 296
Cdd:PRK09228 228 IQTHLSENLDE---IAWVKELFPEArdyldVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLF 304
|
90
....*....|....*..
gi 488476045 297 RVKDLQDAGVRMAIGTD 313
Cdd:PRK09228 305 DLKRADAAGVRVGLGTD 321
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
24-423 |
5.75e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 60.74 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 24 QNGVITAV----TIGAEPHRHTFDG---VAVPGFANTHSHIFHRGLRgagegedfwswRTEMYRLANRLDPDSYYRLARA 96
Cdd:COG1228 34 EDGKIAAVgpaaDLAVPAGAEVIDAtgkTVLPGLIDAHTHLGLGGGR-----------AVEFEAGGGITPTVDLVNPADK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 97 AFAEMVAAGYTSVgefhyvhhqpdgtpyRDHAMELALVNAAIEAGIRITVLDTCYLHAGPGASLgvdQKRFGDGSVEGWL 176
Cdd:COG1228 103 RLRRALAAGVTTV---------------RDLPGGPLGLRDAIIAGESKLLPGPRVLAAGPALSL---TGGAHARGPEEAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 177 ERWRALRDALPDspLVTVGAAlHSVRAVSPDEMATAVSGLPER-VPIHIHvseqprenteclaAHGLTPTAVLDRAGVLS 255
Cdd:COG1228 165 AALRELLAEGAD--YIKVFAE-GGAPDFSLEELRAILEAAHALgLPVAAH-------------AHQADDIRLAVEAGVDS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 256 drttIIHATHLTGGDIAMIAASDTVVsLCPTTEADLGDGI------------------ARVKDLQDAGVRMAIGTDEDVI 317
Cdd:COG1228 229 ----IEHGTYLDDEVADLLAEAGTVV-LVPTLSLFLALLEgaaapvaakarkvreaalANARRLHDAGVPVALGTDAGVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 318 TDPFTEL-RMLESTARL-VTGTrgvigcEALwKIGTQNGVESLRpaaepLPRQTstpgpGSagLAAGDPADIVVVEpssa 395
Cdd:COG1228 304 VPPGRSLhRELALAVEAgLTPE------EAL-RAATINAAKALG-----LDDDV-----GS--LEPGKLADLVLLD---- 360
|
410 420
....*....|....*....|....*...
gi 488476045 396 rlagVDPTRwpLVATANDVAATIVAGEW 423
Cdd:COG1228 361 ----GDPLE--DIAYLEDVRAVMKDGRV 382
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
224-324 |
6.09e-09 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 57.36 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 224 IHVSEQPRENTECLAAHGLTPTAVLDRAGVLSDRttIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQD 303
Cdd:PRK07213 197 IHAAEHKGSVEYSLEKYGMTEIERLINLGFKPDF--IVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLE 274
|
90 100
....*....|....*....|...
gi 488476045 304 AGVRMAIGTDEDVITDP--FTEL 324
Cdd:PRK07213 275 KGILLGIGTDNFMANSPsiFREM 297
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
221-356 |
1.52e-08 |
|
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: 55.48 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 221 PIHIHVSE--QPRENTECLAAHGLTPTavldragvlsdrtTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARV 298
Cdd:cd01305 140 LFAIHASEtrESVGMTDIERALDLEPD-------------LLVHGTHLTDEDLELVRENGVPVVLCPRSNLYFGVGIPPV 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 299 KDLQDAGVRMAIGTDEDVIT--DPFTELRmlesTARLVTGTRGVIGCEALWKIGTQNGVE 356
Cdd:cd01305 207 AELLKLGIKVLLGTDNVMVNepDMWAEME----FLAKYSRLQGYLSPLEILRMATVNAAE 262
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
78-313 |
2.63e-07 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 52.88 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 78 MYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEfhyvhhqPDGTPYrdhamELALVNAAIEAG---IRITV-------- 146
Cdd:COG1574 197 VRAAIPPPTPEELRAALRAALRELASLGITSVHD-------AGLGPD-----DLAAYRELAAAGelpLRVVLylgadded 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 147 LDTcYLHAGPGASLGVDQ------KRFGDGSVEGWLErwrALRDALPDSPlVTVGAALHSvravsPDEMATAVSGLPER- 219
Cdd:COG1574 265 LEE-LLALGLRTGYGDDRlrvggvKLFADGSLGSRTA---ALLEPYADDP-GNRGLLLLD-----PEELRELVRAADAAg 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 220 VPIHIHVseqpRENTECLAAHGltptAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPT--------TEADL 291
Cdd:COG1574 335 LQVAVHAig-dAAVDEVLDAYE----AARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPThatsdgdwAEDRL 409
|
250 260
....*....|....*....|....*.
gi 488476045 292 GD----GIARVKDLQDAGVRMAIGTD 313
Cdd:COG1574 410 GPeraaRAYPFRSLLDAGAPLAFGSD 435
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
78-321 |
4.73e-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: 48.84 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 78 MYRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFHyVHHQPDGTPYRDHAMELAL---VNAAIEAGIRITVLDTCYLHA 154
Cdd:cd01300 169 VLEAVPPPTPEERRAALRAAARELASLGVTTVHDAG-GGAADDIEAYRRLAAAGELtlrVRVALYVSPLAEDLLEELGAR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 155 GPGAS------LGVdqKRFGDGSVEGWLErwrALRDALPDSPlVTVGAALHSvravsPDEMATAVSGLPER-VPIHIHVS 227
Cdd:cd01300 248 KNGAGddrlrlGGV--KLFADGSLGSRTA---ALSEPYLDSP-GTGGLLLIS-----PEELEELVRAADEAgLQVAIHAI 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 228 EQpRENTECLAAHgltpTAVLDRAGVLSDRTTIIHATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARV--------- 298
Cdd:cd01300 317 GD-RAVDTVLDAL----EAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrlgeerakr 391
|
250 260
....*....|....*....|....*...
gi 488476045 299 ----KDLQDAGVRMAIGTDEDVIT-DPF 321
Cdd:cd01300 392 sypfRSLLDAGVPVALGSDAPVAPpDPL 419
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
262-391 |
8.00e-06 |
|
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: 47.64 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 262 HATHLTGGDIAMIAASDTVVSLCPTTEADLGDGIARVKDLQDAGVRMAIGTDEDVITDPFTELRMlesTARLVTGTRGVI 341
Cdd:cd01296 235 HLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTSSMPL---VMHLACRLMRMT 311
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488476045 342 GCEALWKIgTQNGVESLRPAaeplprqtstpgpGSAG-LAAGDPADIVVVE 391
Cdd:cd01296 312 PEEALTAA-TINAAAALGLG-------------ETVGsLEVGKQADLVILD 348
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
257-391 |
1.13e-04 |
|
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: 44.16 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 257 RTTIIHAT---HLTGGD----IAMIAASDTVVSLCPTTEADLGD---------GIARVKDLQDAGVRMAIGTDEdvITDP 320
Cdd:cd01293 235 RVTCSHATalgSLPEAEvsrlADLLAEAGISVVSLPPINLYLQGredttpkrrGVTPVKELRAAGVNVALGSDN--VRDP 312
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488476045 321 FTEL---RMLESTARLV--TGTRGVIGCEALWKIGTQNGVESLrpaaePLPRQtstpgpgsaGLAAGDPADIVVVE 391
Cdd:cd01293 313 WYPFgsgDMLEVANLAAhiAQLGTPEDLALALDLITGNAARAL-----GLEDY---------GIKVGCPADLVLLD 374
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
238-313 |
1.98e-03 |
|
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: 39.97 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 238 AAHGLTPTAVLD--RAGVlsdrTTIIHATHLTGGDIAMIAASDTVVSLCPTT---------------------EADLGDG 294
Cdd:cd01299 177 AAHAYGAEAIRRaiRAGV----DTIEHGFLIDDETIELMKEKGIFLVPTLATyealaaegaapglpadsaekvALVLEAG 252
|
90
....*....|....*....
gi 488476045 295 IARVKDLQDAGVRMAIGTD 313
Cdd:cd01299 253 RDALRRAHKAGVKIAFGTD 271
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
79-422 |
3.54e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 39.44 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 79 YRLANRLDPDSYYRLARAAFAEMVAAGYTSVGEFHYVHHQPDgtpyrdhamELALVNAAIEAGIRITVLDTCYLHAGPGA 158
Cdd:pfam07969 138 YALPPLLAREAEAAAVAAALAALPGFGITSVDGGGGNVHSLD---------DYEPLRELTAAEKLKELLDAPERLGLPHS 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 159 SLGV---DQKRFGDGSvegWLERWRALRDALPDSPlvTVGAALHSvravsPDEMATAVSGLPER-VPIHIHVSEQprent 234
Cdd:pfam07969 209 IYELrigAMKLFADGV---LGSRTAALTEPYFDAP--GTGWPDFE-----DEALAELVAAARERgLDVAIHAIGD----- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 235 eclAAHGLTPTAVLDRAGVLS--DRTTIIHAT---HLTGGDIAMIAASDTVVSLCPTTEADLGD------------GIAR 297
Cdd:pfam07969 274 ---ATIDTALDAFEAVAEKLGnqGRVRIEHAQgvvPYTYSQIERVAALGGAAGVQPVFDPLWGDwlqdrlgaerarGLTP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488476045 298 VKDLQDAGVRMAIGTDEDV-ITDPFtelrmlestarlvtgtRGVIGCEALWKIGTQNgvesLRPAAEPLPRQTS----TP 372
Cdd:pfam07969 351 VKELLNAGVKVALGSDAPVgPFDPW----------------PRIGAAVMRQTAGGGE----VLGPDEELSLEEAlalyTS 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 488476045 373 GPGSA--------GLAAGDPADIVVVEPSSARlagVDPTRWPLVAtandVAATIVAGE 422
Cdd:pfam07969 411 GPAKAlgledrkgTLGVGKDADLVVLDDDPLT---VDPPAIADIR----VRLTVVDGR 461
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