|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
1-435 |
0e+00 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 866.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 1 MKTTYVNATIVTMNEQNEVIENGYIIVENNQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDM 80
Cdd:PRK15493 1 MKTTYVNATIVTMNEQNEVIENGYIIVENDQIIDVNSGEFASDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 81 LLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKDD 160
Cdd:PRK15493 81 LLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 161 EKKAIEEAEKYVKRYYKESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAA 240
Cdd:PRK15493 161 EKKAIEEAEKYVKRYYNESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 241 SCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEELRI 320
Cdd:PRK15493 241 SCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 321 ATLLQKGIHHDATALPVETALSLATKGAAEVIGMKQTGSLEVGKCADFITIDPSNKPHLQPADEVLSHLVYAASGKDISD 400
Cdd:PRK15493 321 ATLLQKGIHQDATALPVETALTLATKGAAEVIGMKQTGSLEVGKCADFITIDPSNKPHLQPADEVLSHLVYAASGKDISD 400
|
410 420 430
....*....|....*....|....*....|....*
gi 558579131 401 VIINGKRVVWNGECKTLDEERIIFEASRYKRGLQR 435
Cdd:PRK15493 401 VIINGKRVVWNGECKTLDEERIIFEASRYKRGLQR 435
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
7-415 |
0e+00 |
|
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: 557.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 7 NATIVTMNEqNEVIENGYIIVENNQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWL 86
Cdd:cd01298 5 NGTIVTTDP-RRVLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDLPLMEWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 87 ETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGvdqDAIMETVSRSGMRAAVSRTLFSFGTKDDEK--KA 164
Cdd:cd01298 84 KDLIWPLERLLTEEDVYLGALLALAEMIRSGTTTFADMYFFYP---DAVAEAAEELGIRAVLGRGIMDLGTEDVEEteEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 165 IEEAEKYVKRYY-KESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCG 243
Cdd:cd01298 161 LAEAERLIREWHgAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEKYGKRPVEYLEELG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 244 LFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEELRIATL 323
Cdd:cd01298 241 LLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGAASNNNLDMFEEMRLAAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 324 LQKGIHHDATALPVETALSLATKGAAEVIGMKQTGSLEVGKCADFITIDPsNKPHLQPADEVLSHLVYAASGKDISDVII 403
Cdd:cd01298 321 LQKLAHGDPTALPAEEALEMATIGGAKALGLDEIGSLEVGKKADLILIDL-DGPHLLPVHDPISHLVYSANGGDVDTVIV 399
|
410
....*....|..
gi 558579131 404 NGKRVVWNGECK 415
Cdd:cd01298 400 NGRVVMEDGELL 411
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-411 |
1.34e-178 |
|
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: 504.75 E-value: 1.34e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 2 KTTYVNATIVTMNEQNEVIENGYIIVENNQIIDV-KSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDM 80
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGVLEDGAVLVEDGRIAAVgPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 81 LLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGT--- 157
Cdd:COG0402 81 PLLDWLEEYIWPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGLMDRGFpdg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 158 -KDDEKKAIEEAEKYVKRYY-KESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRP 235
Cdd:COG0402 161 lREDADEGLADSERLIERWHgAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYGKRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 236 VEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMF 315
Cdd:COG0402 241 VEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 316 EELRIATLLQKGIHHDATALPVETALSLATKGAAEVIGM-KQTGSLEVGKCADFITIDPsNKPHLQPADEVLSHLVYAAS 394
Cdd:COG0402 321 EEMRLAALLQRLRGGDPTALSAREALEMATLGGARALGLdDEIGSLEPGKRADLVVLDL-DAPHLAPLHDPLSALVYAAD 399
|
410
....*....|....*..
gi 558579131 395 GKDISDVIINGKRVVWN 411
Cdd:COG0402 400 GRDVRTVWVAGRVVVRD 416
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
1-418 |
3.49e-143 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 415.17 E-value: 3.49e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 1 MKTtYVNATIVTMNEQNEVIENGYIIVENNQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDM 80
Cdd:PRK06687 1 MKV-FQHVNIVTCDQDFHVYLDGILAVKDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 81 LLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKDD 160
Cdd:PRK06687 80 NLHEWLNDYIWPAESEFTPDMTTNAVKEALTEMLQSGTTTFNDMYNPNGVDIQQIYQVVKTSKMRCYFSPTLFSSETETT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 161 E------KKAIEEAEKYVKRYYKesgmltTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKR 234
Cdd:PRK06687 160 AetisrtRSIIDEILKYKNPNFK------VMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYGKR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 235 PVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDM 314
Cdd:PRK06687 234 PLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVASNNNLDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 315 FEELRIATLLQKGIHHDATALPVETALSLATKGAAEVIGMK-QTGSLEVGKCADFITIDPSNKPHLQPADEVLSHLVYAA 393
Cdd:PRK06687 314 FEEGRTAALLQKMKSGDASQFPIETALKVLTIEGAKALGMEnQIGSLEVGKQADFLVIQPQGKIHLQPQENMLSHLVYAV 393
|
410 420
....*....|....*....|....*
gi 558579131 394 SGKDISDVIINGKRVVWNGECKTLD 418
Cdd:PRK06687 394 KSSDVDDVYIAGEQVVKQGQVLTVE 418
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
7-433 |
8.19e-139 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 404.52 E-value: 8.19e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 7 NATIVTMNEQNevIENGYIIVENNQIIDVksgefANDFE--VDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQP 84
Cdd:PRK06038 8 NAYVLTMDAGD--LKKGSVVIEDGTITEV-----SESTPgdADTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLPLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 85 WLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFnpigVDQDAIMETVSRSGMRAAVSRTLFSFGTKDDEKKA 164
Cdd:PRK06038 81 WLNDHIWPAEAKLTAEDVYAGSLLACLEMIKSGTTSFADMY----FYMDEVAKAVEESGLRAALSYGMIDLGDDEKGEAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 165 IEEAEKYVKRYYKES-GMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCG 243
Cdd:PRK06038 157 LKEGKRFVKEWHGAAdGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQYGMCSVNYLDDIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 244 LFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEELRIATL 323
Cdd:PRK06038 237 FLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDGCASNNNLDMFEEMKTAAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 324 LQKGIHHDATALPVETALSLATKGAAEVIGMKqTGSLEVGKCADFITIDpSNKPHLQPADEVLSHLVYAASGKDISDVII 403
Cdd:PRK06038 317 LHKVNTMDPTALPARQVLEMATVNGAKALGIN-TGMLKEGYLADIIIVD-MNKPHLTPVRDVPSHLVYSASGSDVDTTIV 394
|
410 420 430
....*....|....*....|....*....|
gi 558579131 404 NGKRVVWNGECKTLDEERIIFEASRYKRGL 433
Cdd:PRK06038 395 DGRILMEDYKVLCMDEQDVMEDAKKAAEEL 424
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
6-423 |
5.61e-125 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 369.63 E-value: 5.61e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 6 VNAT-IVTMNEQNEVIENGYIIVENNQIIDVKSGEFAND-FEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQ 83
Cdd:PRK09045 11 IEARwIVPVEPAGVVLEDHAVAIRDGRIVAILPRAEARArYAAAETVELPDHVLIPGLINAHTHAAMSLLRGLADDLPLM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 84 PWLETRIWPLESQFTPELAVAS-TELGLLEMVKSGTTSFSDM-FNPigvdqDAIMETVSRSGMRAAVSRTLFSFGTK--- 158
Cdd:PRK09045 91 TWLQDHIWPAEGAWVSEEFVRDgTLLAIAEMLRGGTTCFNDMyFFP-----EAAAEAAHQAGMRAQIGMPVLDFPTAwas 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 159 -DDE--KKAIEEAEKYvkryyKESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRP 235
Cdd:PRK09045 166 dADEylAKGLELHDQW-----RHHPLISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIADSLKQHGQRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 236 VEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMF 315
Cdd:PRK09045 241 LARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDGAASNNDLDLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 316 EELRIATLLQKGIHHDATALPVETALSLATKGAAEVIGM-KQTGSLEVGKCADFITIDPSNkPHLQPADEVLSHLVYAAS 394
Cdd:PRK09045 321 GEMRTAALLAKAVAGDATALPAHTALRMATLNGARALGLdDEIGSLEPGKQADLVAVDLSG-LETQPVYDPVSQLVYAAG 399
|
410 420
....*....|....*....|....*....
gi 558579131 395 GKDISDVIINGKRVVWNGECKTLDEERII 423
Cdd:PRK09045 400 REQVSHVWVAGKQLLDDRELTTLDEAELL 428
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-428 |
8.89e-117 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 348.53 E-value: 8.89e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 1 MKTTYVNATIVTMNEQNEvIENGYIIVENNQIIDVKSGEFANDfeVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDM 80
Cdd:PRK07228 1 MTILIKNAGIVTMNAKRE-IVDGDVLIEDDRIAAVGDRLDLED--YDDHIDATGKVVIPGLIQGHIHLCQTLFRGIADDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 81 LLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNpigVDQ-DAIMETVSRSGMRAAVSRTLFSFGT-- 157
Cdd:PRK07228 78 ELLDWLKDRIWPLEAAHDAESMYYSALLGIGELIESGTTTIVDMES---VHHtDSAFEAAGESGIRAVLGKVMMDYGDdv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 158 ----KDDEKKAIEEAEKYVKRYY-KESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYG 232
Cdd:PRK07228 155 peglQEDTEASLAESVRLLEKWHgADNGRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEEETG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 233 KRPVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNL 312
Cdd:PRK07228 235 MRNIHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGAPCNNTL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 313 DMFEELRIATLLQKGIHHDATALPVETALSLATKGAAEVIGM-KQTGSLEVGKCADFITIDpSNKPHLQPADE--VLSHL 389
Cdd:PRK07228 315 DPFTEMRQAALIQKVDRLGPTAMPARTVFEMATLGGAKAAGFeDEIGSLEEGKKADLAILD-LDGLHATPSHGvdVLSHL 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 558579131 390 VYAASGKDISDVIINGKRVVWNGECKTLDEERIIFEASR 428
Cdd:PRK07228 394 VYAAHGSDVETTMVDGKIVMEDGELTTIDADAVRREANR 432
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
19-428 |
9.28e-115 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 342.94 E-value: 9.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 19 VIENGYII-------------VENNQIIDVKSGEFAndfEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPW 85
Cdd:PRK08393 4 LIKNGYVIygenlkviradvlIEGNKIVEVKRNINK---PADTVIDASGSVVSPGFINAHTHSPMVLLRGLADDVPLMEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 86 LETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIgvdqDAIMETVSRSGMRAAVSRTLFSFGTKDDEKKAI 165
Cdd:PRK08393 81 LQNYIWPRERKLKRKDIYWGAYLGLLEMIKSGTTTFVDMYFHM----EEVAKATLEVGLRGYLSYGMVDLGDEEKREKEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 166 EEAEKYVKRYYK-ESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGL 244
Cdd:PRK08393 157 KETEKLMEFIEKlNSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYGKSPVVLLDEIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 245 FKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEELRIATLL 324
Cdd:PRK08393 237 LNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDMLREMKLAALL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 325 QKGIHHDATALPVETALSLATKGAAEVIGMKqTGSLEVGKCADFITIDpSNKPHLQPADEVLSHLVYAASGKDISDVIIN 404
Cdd:PRK08393 317 HKVHNLDPTIADAETVFRMATQNGAKALGLK-AGVIKEGYLADIAVID-FNRPHLRPINNPISHLVYSANGNDVETTIVD 394
|
410 420
....*....|....*....|....
gi 558579131 405 GKRVVWNGECKTLDEERIIFEASR 428
Cdd:PRK08393 395 GKIVMLDGEVLTLDEEKILDKFLK 418
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
7-435 |
6.23e-98 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 300.62 E-value: 6.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 7 NATIVTMNEQNEVIENGYIIVENNQIIDVKSGEfANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGD--DMLLQP 84
Cdd:PRK08203 8 PLAIVTMDAARREIADGGLVVEGGRIVEVGPGG-ALPQPADEVFDARGHVVTPGLVNTHHHFYQTLTRALPAaqDAELFP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 85 WLETrIWPLESQFTPELAVASTELGLLEMVKSGTTSFSD---MFnPIGVDQ--DAIMETVSRSGMRAAVSRTLFSFGTKD 159
Cdd:PRK08203 87 WLTT-LYPVWARLTPEMVRVATQTALAELLLSGCTTSSDhhyLF-PNGLRDalDDQIEAAREIGMRFHATRGSMSLGESD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 160 ----------DEKKAIEEAEKYVKRYYKES--GMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDI 227
Cdd:PRK08203 165 gglppdsvveDEDAILADSQRLIDRYHDPGpgAMLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 228 EAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVA 307
Cdd:PRK08203 245 LERFGMRPVDYLEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 308 SNNNLDMFEELRIATLLQKgIHHDATALPVETALSLATKGAAEVIGMKQTGSLEVGKCADFITIDPSNKPHLQPADEVlS 387
Cdd:PRK08203 325 SNDGSNLIGEARQALLLQR-LRYGPDAMTAREALEWATLGGARVLGRDDIGSLAPGKLADLALFDLDELRFAGAHDPV-A 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 558579131 388 HLVYAASGKdISDVIINGKRVVWNGECKTLDEERIIFEASRYKRGLQR 435
Cdd:PRK08203 403 ALVLCGPPR-ADRVMVGGRWVVRDGQLTTLDLAALIARHRAAARRLAA 449
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-423 |
2.46e-83 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 261.74 E-value: 2.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 1 MKTTYVNATIVTMNEQNEVIEnGYIIVENNQIIDVKSGEFandfEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDM 80
Cdd:PRK06380 1 MSILIKNAWIVTQNEKREILQ-GNVYIEGNKIVYVGDVNE----EADYIIDATGKVVMPGLINTHAHVGMTASKGLFDDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 81 LLQPWLEtRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNpigvDQDAIMETVSRSGMRAAVSRTLFSFGTKDD 160
Cdd:PRK06380 76 DLEEFLM-KTFKYDSKRTREGIYNSAKLGMYEMINSGITAFVDLYY----SEDIIAKAAEELGIRAFLSWAVLDEEITTQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 161 EKKAIEEAEKYVKRYYKESgMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAA 240
Cdd:PRK06380 151 KGDPLNNAENFIREHRNEE-LVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEVYDHVKRTGERPVEHLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 241 SCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGS-GIANVKAMLEAGIKVGIATDSVASNNNLDMFEELR 319
Cdd:PRK06380 230 KIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 320 IATLLQKGIHHDATALPVETALSLATKGAAEVIGMkQTGSLEVGKCADFITIDPSnKPHLQPADE--VLSHLVYAASGKD 397
Cdd:PRK06380 310 FSALSVKNERWDASIIKAQEILDFATINAAKALEL-NAGSIEVGKLADLVILDAR-APNMIPTRKnnIVSNIVYSLNPLN 387
|
410 420
....*....|....*....|....*.
gi 558579131 398 ISDVIINGKRVVWNGECKTLDEERII 423
Cdd:PRK06380 388 VDHVIVNGKILKENGRLNGFNPDEFI 413
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
47-435 |
1.53e-70 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 229.95 E-value: 1.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 47 DEVIDMKGKWVLPGLVNTHTHVVMSLLRGI--GDDMLLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSD- 123
Cdd:PRK12393 47 ERVIDATDCVVYPGWVNTHHHLFQSLLKGVpaGINQSLTAWLAAVPYRFRARFDEDLFRLAARIGLVELLRSGCTTVADh 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 124 --MFNPIGVDQ--DAIMETVSRSGMRAAVSR--TLFSFGTKDDEKKAI---------EEAEKYVKRYYKES--GMLTTMV 186
Cdd:PRK12393 127 hyLYHPGMPFDtgDILFDEAEALGMRFVLCRggATQTRGDHPGLPTALrpetldqmlADVERLVSRYHDASpdSLRRVVV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 187 APHSP-YTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDDERAFL 265
Cdd:PRK12393 207 APTTPtFSLPPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYGMTPVQFVAEHDWLGPDVWFAHLVKLDAEEIALL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 266 AEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEELRIATLLQKGiHHDATALPVETALSLAT 345
Cdd:PRK12393 287 AQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADMLSEAHAAWLLHRA-EGGADATTVEDVVHWGT 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 346 KGAAEVIGMKQTGSLEVGKCADFITIDPSNKPHLQPADeVLSHLVYAASGKDISDVIINGKRVVWNGECKTLDEERIIFE 425
Cdd:PRK12393 366 AGGARVLGLDAIGTLAVGQAADLAIYDLDDPRFFGLHD-PAIAPVACGGPAPVKALLVNGRPVVENGAIPGLDLAELRHD 444
|
410
....*....|
gi 558579131 426 ASRYKRGLQR 435
Cdd:PRK12393 445 ARAAVRRLLQ 454
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
56-408 |
2.85e-65 |
|
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: 212.36 E-value: 2.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 56 WVLPGLVNTHTHVVMSLLRGIGDDmllqpwletriwplesqftPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAI 135
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVP-------------------PEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEAL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 136 METVSRS--GMRAAVSRTlfSFGTKDDEKKAIEEAEKYVKRYYKE----SGMLTTMVAPHSPYTCSTELLEECARIAVEN 209
Cdd:pfam01979 62 LEAAEELplGLRFLGPGC--SLDTDGELEGRKALREKLKAGAEFIkgmaDGVVFVGLAPHGAPTFSDDELKAALEEAKKY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 210 QTMVHIHLSETEREVRDIEAQYGKR-----PVEYAASCGLFKRP-TVIAHGVVLNDDERAFLAEH--DVRVAHNPNSNLK 281
Cdd:pfam01979 140 GLPVAIHALETKGEVEDAIAAFGGGiehgtHLEVAESGGLLDIIkLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 282 LGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEELRIATLLQKGIHHdatALPVETALSLATKGAAEVIGM-KQTGSL 360
Cdd:pfam01979 220 LRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEG---GLSPLEALRMATINPAKALGLdDKVGSI 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 558579131 361 EVGKCADFITIDPsnkphlqpadEVLSHLVYAASGKDISDVIINGKRV 408
Cdd:pfam01979 297 EVGKDADLVVVDL----------DPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
18-405 |
4.20e-65 |
|
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: 214.83 E-value: 4.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 18 EVIENGYIIVENNQIIDVKSGE--FANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLES 95
Cdd:cd01303 22 RVVEDGLIVVVDGNIIAAGAAEtlKRAAKPGARVIDSPNQFILPGFIDTHIHAPQYANIGSGLGEPLLDWLETYTFPEEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 96 QFTpELAVASTELGLL--EMVKSGTTSFSdMFNPIGVDQ-DAIMETVSRSGMRAAVSRTLFSF----GTKDDEKKAIEEA 168
Cdd:cd01303 102 KFA-DPAYAREVYGRFldELLRNGTTTAC-YFATIHPEStEALFEEAAKRGQRAIAGKVCMDRnapeYYRDTAESSYRDT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 169 EKYVKRYYKESGMLTTMVAPHSPYTCSTELLEECARIAVENQTM-VHIHLSETEREVRDIEAQYGKRPvEYAA---SCGL 244
Cdd:cd01303 180 KRLIERWHGKSGRVKPAITPRFAPSCSEELLAALGKLAKEHPDLhIQTHISENLDEIAWVKELFPGAR-DYLDvydKYGL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 245 FKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDsVASNNNLDMFEELRIATLL 324
Cdd:cd01303 259 LTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTD-VGGGTSFSMLDTLRQAYKV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 325 QKgiHH-----DATALPVETALSLATKGAAEVIGMK-QTGSLEVGKCADFITIDPSNKPHLQP-------ADEVLSHLVY 391
Cdd:cd01303 338 SR--LLgyelgGHAKLSPAEAFYLATLGGAEALGLDdKIGNFEVGKEFDAVVIDPSATPLLADrmfrvesLEEALFKFLY 415
|
410
....*....|....
gi 558579131 392 AASGKDISDVIING 405
Cdd:cd01303 416 LGDDRNIREVYVAG 429
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
7-428 |
2.17e-64 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 213.26 E-value: 2.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 7 NATIVTMNEQNEVIENGYIIVENNQIIDV-KSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGD------- 78
Cdd:PRK07203 6 NGTAITRDPAKPVIEDGAIAIEGNVIVEIgTTDELKAKYPDAEFIDAKGKLIMPGLINSHNHIYSGLARGMMAnippppd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 79 --DMLLQPWletriWPLESQFTPELAVASTELGLLEMVKSGTTSFSD---MFNPIGVDQDAIMETVSRSGMRAAvsrTLF 153
Cdd:PRK07203 86 fiSILKNLW-----WRLDRALTLEDVYYSALICSLEAIKNGVTTVFDhhaSPNYIGGSLFTIADAAKKVGLRAM---LCY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 154 SFGTKDDEKK---AIEEAEKYVKRYYKE-SGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEA 229
Cdd:PRK07203 158 ETSDRDGEKElqeGVEENIRFIKHIDEAkDDMVEAMFGLHASFTLSDATLEKCREAVKETGRGYHIHVAEGIYDVSDSHK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 230 QYGKRPVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASn 309
Cdd:PRK07203 238 KYGKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTDGYTS- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 310 nnlDMFEELRIATLLQKGIHHDATALPVETALSLATKG---AAEVIGmKQTGSLEVGKCADFITIDpSNKPHLQPADEVL 386
Cdd:PRK07203 317 ---DMFESYKVANFKHKHAGGDPNVGWPESPAMLFENNnkiAERYFG-AKFGILEEGAKADLIIVD-YNPPTPLNEDNIN 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 558579131 387 SHLVYAASGKDISDVIINGKRVVWNGECKTLDEERIIFEASR 428
Cdd:PRK07203 392 GHILFGMNGGSVDTTIVNGKVVMEDRKFLNFDEESIYARARK 433
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-412 |
1.35e-53 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 185.21 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 1 MKTTYVNATIVTMNEQNEVIENGYIIVENNQIIDVKSGEFANDfevDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDM 80
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIGDLPRGDILIEGDRIAAVAPSIEAPD---AEVVDARGMIVMPGLVDTHRHTWQSVLRGIGADW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 81 LLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSD--MFNPIGVDQDAIMETVSRSGMRAAvsrtlFSFGT- 157
Cdd:PRK08204 79 TLQTYFREIHGNLGPMFRPEDVYIANLLGALEALDAGVTTLLDwsHINNSPEHADAAIRGLAEAGIRAV-----FAHGSp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 158 -------KDDEKKAIEEAEKYVKRYYKESGMLTTM-VAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDiea 229
Cdd:PRK08204 154 gpspywpFDSVPHPREDIRRVKKRYFSSDDGLLTLgLAIRGPEFSSWEVARADFRLARELGLPISMHQGFGPWGATP--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 230 qygkRPVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASN 309
Cdd:PRK08204 231 ----RGVEQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 310 NNlDMFEELRIATLLQKGIHH-----------DATALPVETALSLATKGAAEVIGMK-QTGSLEVGKCADFITIDPSNkP 377
Cdd:PRK08204 307 GG-DMFTQMRFALQAERARDNavhlreggmppPRLTLTARQVLEWATIEGARALGLEdRIGSLTPGKQADLVLIDATD-L 384
|
410 420 430
....*....|....*....|....*....|....*
gi 558579131 378 HLQPADEVLSHLVYAASGKDISDVIINGKRVVWNG 412
Cdd:PRK08204 385 NLAPVHDPVGAVVQSAHPGNVDSVMVAGRAVKRNG 419
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
18-408 |
5.52e-42 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 153.81 E-value: 5.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 18 EVIENGYIIVENNQIIDVksGEFAndfEV-------DEVIDMKGKWVLPGLVNTHTH-----VVMSLlrgiGDDMLlqPW 85
Cdd:PRK09228 27 RYIEDGLLLVEDGRIVAA--GPYA---ELraqlpadAEVTDYRGKLILPGFIDTHIHypqtdMIASY----GEQLL--DW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 86 LETRIWPLESQFT-PELAVASTELGLLEMVKSGTTS---FSDMFnPIGVDqdAIMETVSRSGMRAAVSRTLFSF----GT 157
Cdd:PRK09228 96 LNTYTFPEERRFAdPAYAREVAEFFLDELLRNGTTTalvFGTVH-PQSVD--ALFEAAEARNMRMIAGKVLMDRnapdGL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 158 KDDEKKAIEEAEKYVKRYYKEsGMLTTMVAPHSPYTCSTELLEECARIAVEN-QTMVHIHLSETEREVR----------- 225
Cdd:PRK09228 173 RDTAESGYDDSKALIERWHGK-GRLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAwvkelfpeard 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 226 --DIEAQYGkrpveyaascgLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIAT 303
Cdd:PRK09228 252 ylDVYERYG-----------LLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 304 DsVASNNNLDMFEelriaTLLQ--KGIHHDATALPVETALSLATKGAAEVIGMKQT-GSLEVGKCADFITIDPSNKPHLQ 380
Cdd:PRK09228 321 D-VGGGTSFSMLQ-----TMNEayKVQQLQGYRLSPFQAFYLATLGGARALGLDDRiGNLAPGKEADFVVLDPAATPLLA 394
|
410 420 430
....*....|....*....|....*....|....*
gi 558579131 381 P-------ADEVLSHLVYAASGKDISDVIINGKRV 408
Cdd:PRK09228 395 LrtaraesLEELLFALMTLGDDRAVAETYVAGRPV 429
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
14-435 |
7.96e-42 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 154.43 E-value: 7.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 14 NEQNEVIENGYIIVENNQIIDVKSGeFanDFEVDEVIDMKGKWVLPGLVNTHT-----HVVMSLLRGIG---DDMLLQPW 85
Cdd:PRK06151 15 DGDHRLLRDGEVVFEGDRILFVGHR-F--DGEVDRVIDAGNALVGPGFIDLDAlsdldTTILGLDNGPGwakGRVWSRDY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 86 LETRIWPLesqFTPELAVASTELGLLEMVKSGTTSFSdmfnPIG----------VDQDAIMETVS-------------RS 142
Cdd:PRK06151 92 VEAGRREM---YTPEELAFQKRYAFAQLLRNGITTAM----PIAslfyrqwaetYAEFAAAAEAAgrlglrvylgpayRS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 143 GM---RAAVSRTLFSfgtkDDEK--KAIEEAEKYVKRYY-KESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIH 216
Cdd:PRK06151 165 GGsvlEADGSLEVVF----DEARglAGLEEAIAFIKRVDgAHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 217 LSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDDERAF---------LAEHDVRVAHNPNSNLKLGSGIA 287
Cdd:PRK06151 241 CAQGVLEVETVRRLHGTTPLEWLADVGLLGPRLLIPHATYISGSPRLNysggddlalLAEHGVSIVHCPLVSARHGSALN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 288 NVKAMLEAGIKVGIATDSVASnnnlDMFEELRIATLLQKGIHHDATALPVETALSLATKGAAEVIGMKQTGSLEVGKCAD 367
Cdd:PRK06151 321 SFDRYREAGINLALGTDTFPP----DMVMNMRVGLILGRVVEGDLDAASAADLFDAATLGGARALGRDDLGRLAPGAKAD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558579131 368 FITIDPSNkPHLQPADEVLSHLVYAASGKDISDVIINGKRVVWNGECKTLDEERIIFEASRYKRGLQR 435
Cdd:PRK06151 397 IVVFDLDG-LHMGPVFDPIRTLVTGGSGRDVRAVFVDGRVVMEDGRLPGVDLAALRAQAQQQFDKLVA 463
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
57-406 |
1.01e-38 |
|
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: 143.74 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 57 VLPGLVNTHTHV-----VMSLLRGIGDDMLLQpWLETRiwpleSQFTPELAVASTELGLLEMVKSGTTSFSDmfnpIGVD 131
Cdd:cd01312 29 LLPGLINAHTHLefsanVAQFTYGRFRAWLLS-VINSR-----DELLKQPWEEAIRQGIRQMLESGTTSIGA----ISSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 132 QDAiMETVSRSGMRAAVSRTLFSFGTKDDEKKAIEEAEKYVKRYYKESGMLTTMVAPHSPYTCSTELLEECARIAVENQT 211
Cdd:cd01312 99 GSL-LPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYSVHPELAQDLIDLAKKLNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 212 MVHIHLSET------------------EREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVA 273
Cdd:cd01312 178 PLSTHFLESkeerewleeskgwfkhfwESFLKLPKPKKLATAIDFLDMLGGLGTRVSFVHCVYANLEEAEILASRGASIA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 274 HNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEELRIATLLQKGIHHDATAlpvETALSLATKGAAEVIG 353
Cdd:cd01312 258 LCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLLELA---SELLLMATLGGARALG 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 558579131 354 MkQTGSLEVGKCADFITIDPSnkphlQPADEVLSHLVYAASGKDISDVIINGK 406
Cdd:cd01312 335 L-NNGEIEAGKRADFAVFELP-----GPGIKEQAPLQFILHAKEVRHLFISGK 381
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-409 |
1.83e-35 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 134.70 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 3 TTYVNATIVTMNEQnEVIENGYIIVENNQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMsllrgiGDDMLL 82
Cdd:COG1228 10 LLITNATLVDGTGG-GVIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGL------GGGRAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 83 QPWLETRIWPLESQFTPELAVastelgLLEMVKSGTTSFSDMF-NPIGVdQDAIMETVSRS--GMRAAVSRTLFSFgTKD 159
Cdd:COG1228 83 EFEAGGGITPTVDLVNPADKR------LRRALAAGVTTVRDLPgGPLGL-RDAIIAGESKLlpGPRVLAAGPALSL-TGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 160 DEKKAIEEAEKYVKRYYKE-SGMLTTMVAPHSP-YTcstelLEECARI---AVENQTMVHIHLseterevrdieaqYGKR 234
Cdd:COG1228 155 AHARGPEEARAALRELLAEgADYIKVFAEGGAPdFS-----LEELRAIleaAHALGLPVAAHA-------------HQAD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 235 PVEYAASCGLfkrpTVIAHGVVLNDDERAFLAEHDV-----------------RVAHNPNSNLKLGSGIANVKAMLEAGI 297
Cdd:COG1228 217 DIRLAVEAGV----DSIEHGTYLDDEVADLLAEAGTvvlvptlslflallegaAAPVAAKARKVREAALANARRLHDAGV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 298 KVGIATDSVASNN-NLDMFEELRIATLLQkgihhdataLPVETALSLATKGAAEVIGM-KQTGSLEVGKCADFI--TIDP 373
Cdd:COG1228 293 PVALGTDAGVGVPpGRSLHRELALAVEAG---------LTPEEALRAATINAAKALGLdDDVGSLEPGKLADLVllDGDP 363
|
410 420 430
....*....|....*....|....*....|....*.
gi 558579131 374 snkphlqpadevLSHLVYAasgKDISDVIINGKRVV 409
Cdd:COG1228 364 ------------LEDIAYL---EDVRAVMKDGRVVD 384
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
10-409 |
6.75e-35 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 133.94 E-value: 6.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 10 IVTMNEQNEVIENGYIIVENnQIIDV--------KSGEFANDFEVDEVIdmkgkwvLPGLVNTHTHVVMSLLRG---IGD 78
Cdd:PRK08418 9 IFTCDENFEILEDGAVVFDD-KILEIgdyenlkkKYPNAKIQFFKNSVL-------LPAFINPHTHLEFSANKTtldYGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 79 DMllqPWLETRIWPLEsqftpELAVASTELGLL----EMVKSGTTSFSDMFNpIGVDqdaiMETVSRSGMRAAV-SRTLF 153
Cdd:PRK08418 81 FI---PWLGSVINHRE-----DLLEKCKGALIQqainEMLKSGVGTIGAISS-FGID----LEICAKSPLRVVFfNEILG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 154 SFGTKDDEKKA-----IEEAEKYvkryykESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHL--SETERE-VR 225
Cdd:PRK08418 148 SNASAVDELYQdflarFEESKKF------KSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFleSKAEREwLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 226 DIEAQYGK-------------RPVEYAAscgLFKR-PTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKA 291
Cdd:PRK08418 222 ESKGWFKKffekflkepkplyTPKEFLE---LFKGlRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 292 MLEAGIKVGIATDSVASNNNLDMFEELRIATLlqkgIHHDATALPV-ETALSLATKGAAEVIGMkQTGSLEVGKCADFIT 370
Cdd:PRK08418 299 AKKAGINYSIATDGLSSNISLSLLDELRAALL----THANMPLLELaKILLLSATRYGAKALGL-NNGEIKEGKDADLSV 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 558579131 371 IDPSNKPHlQPADEVLSHLVYAasgKDISDVIINGKRVV 409
Cdd:PRK08418 374 FELPEECT-KKEQLPLQFILHA---KEVKKLFIGGKEVK 408
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
26-406 |
1.16e-33 |
|
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: 130.65 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 26 IVENNQIIDVKSGEFandfevDEVIDMKGKWVLPGLVNTHTHVVMSLLRGI------GDDMLLQpWLETrIWPLESQFTP 99
Cdd:cd01313 15 VDADGRIAAVNPDTA------TEAVALLGGALLPGMPNLHSHAFQRAMAGLteyrgsAADSFWT-WREL-MYRFAARLTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 100 E-LAVASTELgLLEMVKSGTTSFSDMF------------NPIGVDQdAIMETVSRSGMRAAVSRTLFS---FGTK---DD 160
Cdd:cd01313 87 EqIEAIARQL-YIEMLLAGITAVGEFHyvhhdpdgtpyaDPAELAQ-RVIAAASDAGIGITLLPVLYAragFGGPapnPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 161 EKKAIEEAEKYV------KRYYKESGMLTTMVAPHSPYTCSTELLEECARIAVENQTmVHIHLSETEREVRDIEAQYGKR 234
Cdd:cd01313 165 QRRFINGYEDFLgllekaLRAVKEHAAARIGVAPHSLRAVPAEQLAALAALASEKAP-VHIHLAEQPKEVDDCLAAHGRR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 235 PVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDsvaSNNNLDM 314
Cdd:cd01313 244 PVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSD---SNARIDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 315 FEELRIATL------LQKGIHHDATALPVETALSLATKGAAEVIGMkQTGSLEVGKCADFITID---PSNKPHLqpADEV 385
Cdd:cd01313 321 LEELRQLEYsqrlrdRARNVLATAGGSSARALLDAALAGGAQALGL-ATGALEAGARADLLSLDldhPSLAGAL--PDTL 397
|
410 420
....*....|....*....|.
gi 558579131 386 LSHLVYAASGKDISDVIINGK 406
Cdd:cd01313 398 LDAWVFAAGDREVRDVVVGGR 418
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
57-435 |
1.42e-32 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 128.04 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 57 VLPGLVNTHTHVVMSLLRGIGddmllqpwlETRIWPLES-------------QFTPELAVASTELGLLEMVKSGTTSFSD 123
Cdd:PRK09229 49 VLPGMPNLHSHAFQRAMAGLT---------EVRGPPQDSfwswrelmyrfalRLTPDQLEAIARQLYVEMLEAGYTSVGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 124 mFNPIGVDQD------------AIMETVSRSGMRAAVSRTLFS---FGTK---DDEKKAIEEAEKY------VKRYYKES 179
Cdd:PRK09229 120 -FHYLHHDPDgtpyadpaemalRIVAAARAAGIGLTLLPVLYAhsgFGGQppnPGQRRFINDPDGFlrlleaLRRALAAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 180 GMLTTMVAPHSPYTCSTELLEECARiAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLND 259
Cdd:PRK09229 199 PGARLGLAPHSLRAVTPDQLAAVLA-LAAPDGPVHIHIAEQTKEVDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 260 DERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASnnnLDMFEELRI----ATLLQKGIHHDATAL 335
Cdd:PRK09229 278 AETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGSDSHVS---IDLVEELRLleygQRLRDRRRNVLAAAA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 336 PVETALSL---ATKGAAEVIGMKqTGSLEVGKCADFITIDPSNkPHLQ--PADEVLSHLVYAASGKDISDVIINGKRVVW 410
Cdd:PRK09229 355 QPSVGRRLfdaALAGGAQALGRA-IGGLAVGARADLVVLDLDH-PALAgrEGDALLDRWVFAGGDAAVRDVWVAGRWVVR 432
|
410 420
....*....|....*....|....*
gi 558579131 411 NGecKTLDEERIifeASRYKRGLQR 435
Cdd:PRK09229 433 DG--RHRLREAI---AAAFRAALAA 452
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
61-350 |
1.29e-27 |
|
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: 110.89 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 61 LVNTHTHVVMSLLRGigddmllqpWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIG------VDQDA 134
Cdd:cd01292 1 FIDTHVHLDGSALRG---------TRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPptttkaAIEAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 135 IMETVSRSGMRAAVSRTlFSFGTKDDEKKAIEEAEKYVKRYYKEsgmLTTMVAPHSPYTC---STELLEECARIAVENQT 211
Cdd:cd01292 72 AEAARASAGIRVVLGLG-IPGVPAAVDEDAEALLLELLRRGLEL---GAVGLKLAGPYTAtglSDESLRRVLEEARKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 212 MVHIHLSETEREVRDIEAQYgkrpveyaASCGLFKRpTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGS---GIAN 288
Cdd:cd01292 148 PVVIHAGELPDPTRALEDLV--------ALLRLGGR-VVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRdgeGAEA 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 558579131 289 VKAMLEAGIKVGIATDSVASNNNLDMFEELRIATLLQKGihhdatALPVETALSLATKGAAE 350
Cdd:cd01292 219 LRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRL------GLSLEEALRLATINPAR 274
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
3-406 |
2.47e-26 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 109.36 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 3 TTYVNATIV-----TMNEQNEVIENGYIIvennqiidvksgEFANDFEVDEVIDMKGKwVLPGLVNTHTHVVMSLLRGIG 77
Cdd:PRK07213 2 LVYLNGNFLygedfEPKKGNLVIEDGIIK------------GFTNEVHEGNVIDAKGL-VIPPLINAHTHIGDSSIKDIG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 78 D----DMLLQP--WLETRIwpLESQFTPELaVASTELGLLEMVKSGTTSFSDmFNPIGVDqdaimetvsrsGMRaavsrt 151
Cdd:PRK07213 69 IgkslDELVKPpnGLKHKF--LNSCSDKEL-VEGMKEGLYDMYNNGIKAFCD-FREGGIK-----------GIN------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 152 LFSFGTKDDEKKAI------EEAEKYVKRYYKESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVR 225
Cdd:PRK07213 128 LLKKASSDLPIKPIilgrptEADENELKKEIREILKNSDGIGLSGANEYSDEELKFICKECKREKKIFSIHAAEHKGSVE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 226 DIEAQYGKRPVEYAASCGLfkRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDS 305
Cdd:PRK07213 208 YSLEKYGMTEIERLINLGF--KPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTDN 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 306 VASNNNlDMFEELRiatLLQKGIHHDatalPVETaLSLATKGAAEVIGMKQTGSLEVGKCADFITIDPSNKphLQPADEV 385
Cdd:PRK07213 286 FMANSP-SIFREME---FIYKLYHIE----PKEI-LKMATINGAKILGLINVGLIEEGFKADFTFIKPTNI--KFSKNPY 354
|
410 420
....*....|....*....|.
gi 558579131 386 LShLVYAASGKDISDVIINGK 406
Cdd:PRK07213 355 AS-IITRCESGDIVNKILKGK 374
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
57-351 |
2.45e-22 |
|
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: 95.93 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 57 VLPGLVNTHTHVVMSLLRGIGDDMLLqpwLETRIWP------LESQFTPELAVASTELGLLEMVKSGTTSFSDmFNPIGV 130
Cdd:cd01305 2 LIPALVNAHTHLGDSAIKEVGDGLPL---DDLVAPPdglkhrLLAQADDRELAEAMRKVLRDMRETGIGAFAD-FREGGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 131 dqdAIMETVSRS-GMRAAVSRTLFSFGTKDDEKKAIEEaekyvkryykesgmLTTMVAPHSPY-TCSTELLEECARiave 208
Cdd:cd01305 78 ---EGIELLRRAlGKLPVPFEVILGRPTEPDDPEILLE--------------VADGLGLSSANdVDLEDILELLRR---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 209 NQTMVHIHLSETEREVRDIEaqygkrpVEYAASCGlfkrPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIAN 288
Cdd:cd01305 137 RGKLFAIHASETRESVGMTD-------IERALDLE----PDLLVHGTHLTDEDLELVRENGVPVVLCPRSNLYFGVGIPP 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 558579131 289 VKAMLEAGIKVGIATDSVASnNNLDMFEELRIATLLQKGihhdATALPVETALSLATKGAAEV 351
Cdd:cd01305 206 VAELLKLGIKVLLGTDNVMV-NEPDMWAEMEFLAKYSRL----QGYLSPLEILRMATVNAAEF 263
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
47-372 |
4.14e-15 |
|
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: 76.18 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 47 DEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWP-----LESQFTPELAVASTELGLL-EMVKSGTTS 120
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEYRTIRATRqaraaLRAGFTTVRDAGGADYGLLrDAIDAGLIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 121 FSDMF-----------------NPIGVDQDAIMETV-SRSGMRAAVSR--------------------------TLFSfg 156
Cdd:cd01299 81 GPRVFasgralsqtgghgdprgLSGLFPAGGLAAVVdGVEEVRAAVREqlrrgadqikimatggvlspgdpppdTQFS-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 157 tkDDEKKAI-EEAEKYvkryykesGmltTMVAPHSpYTcstellEECARIAVENQtmVHI--HLSETEREVrdieaqygk 233
Cdd:cd01299 159 --EEELRAIvDEAHKA--------G---LYVAAHA-YG------AEAIRRAIRAG--VDTieHGFLIDDET--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 234 rpVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRvahnpNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLD 313
Cdd:cd01299 208 --IELMKEKGIFLVPTLATYEALAAEGAAPGLPADSAE-----KVALVLEAGRDALRRAHKAGVKIAFGTDAGFPVPPHG 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558579131 314 -MFEELRIATllqkgihhDATALPVEtALSLATKGAAEVIGM-KQTGSLEVGKCADFITID 372
Cdd:cd01299 281 wNARELELLV--------KAGGTPAE-ALRAATANAAELLGLsDELGVIEAGKLADLLVVD 332
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
47-369 |
2.13e-14 |
|
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: 74.59 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 47 DEVIDMKGKWVLPGLVNTHTHVVMSLLrgigddmlLQPWLETRIWPL----------ESQFTPELAVASTELGLLEMVKS 116
Cdd:cd01293 37 AEEVDAKGRLVLPAFVDPHIHLDKTFT--------GGRWPNNSGGTLleaiiaweerKLLLTAEDVKERAERALELAIAH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 117 GTT---SFSDMFNPIGVDQ-DAIMETvsRSGMRAAVSRTLFSF------GTKDDEKKAIEEAEKYVkryykesgmltTMV 186
Cdd:cd01293 109 GTTairTHVDVDPAAGLKAlEALLEL--REEWADLIDLQIVAFpqhgllSTPGGEELMREALKMGA-----------DVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 187 --APHSPYTCSTE-LLEECARIAVENQTMVHIHLSET-EREVRDIEaqygkRPVEYAASCGLFKRpTVIAHGVVLND-DE 261
Cdd:cd01293 176 ggIPPAEIDEDGEeSLDTLFELAQEHGLDIDLHLDETdDPGSRTLE-----ELAEEAERRGMQGR-VTCSHATALGSlPE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 262 RAF------LAEHDVRVAHNPNSNLKLGS---------GIANVKAMLEAGIKVGIATDSV----ASNNNLDMFEELRIAT 322
Cdd:cd01293 250 AEVsrladlLAEAGISVVSLPPINLYLQGredttpkrrGVTPVKELRAAGVNVALGSDNVrdpwYPFGSGDMLEVANLAA 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 558579131 323 LlqkgIHHDATALPVETALSLATKGAAEVIGMKQTGsLEVGKCADFI 369
Cdd:cd01293 330 H----IAQLGTPEDLALALDLITGNAARALGLEDYG-IKVGCPADLV 371
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
25-405 |
1.74e-12 |
|
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: 68.44 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 25 IIVENNQIIDVKSGE--FANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSllrgiGD-----DMLLQ--PWLE-------- 87
Cdd:cd01296 1 IAIRDGRIAAVGPAAslPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFA-----GDrvdefAARLAgaSYEEilaagggi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 88 ------TR---IWPLESQFTPELAvastelgllEMVKSGTTSFsDMFNPIGVDQDA------IMETVSRSGMrAAVSRTL 152
Cdd:cd01296 76 lstvraTRaasEDELFASALRRLA---------RMLRHGTTTV-EVKSGYGLDLETelkmlrVIRRLKEEGP-VDLVSTF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 153 FSFGTKDDEKKAIEEAEKYVKRYykesgMLTTMVAPHSPYTCS--TEL----LEECARI---AVENQTMVHIHLSEtere 223
Cdd:cd01296 145 LGAHAVPPEYKGREEYIDLVIEE-----VLPAVAEENLADFCDvfCEKgafsLEQSRRIleaAKEAGLPVKIHADE---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 224 vrdIEAQYGkrpVEYAASCGLfkrpTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIAT 303
Cdd:cd01296 216 ---LSNIGG---AELAAELGA----LSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 304 D-----SVASNNNLDMfeelRIATLLQKgihhdataLPVETALSLATKGAAEVIGMKQT-GSLEVGKCADFITID-PSNK 376
Cdd:cd01296 286 DfnpgsSPTSSMPLVM----HLACRLMR--------MTPEEALTAATINAAAALGLGETvGSLEVGKQADLVILDaPSYE 353
|
410 420
....*....|....*....|....*....
gi 558579131 377 phlqpadevlsHLVYAASGKDISDVIING 405
Cdd:cd01296 354 -----------HLAYRFGVNLVEYVIKNG 371
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
5-408 |
3.05e-12 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 68.29 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 5 YVNATIVTMNEQNEVIEngYIIVENNQIIDVKSGEFANDF--EVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIG----- 77
Cdd:COG1574 12 LTNGRIYTMDPAQPVAE--AVAVRDGRIVAVGSDAEVRALagPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGvdlsg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 78 ----DDML--LQ---------PWLETRIW-----------------------P-----------------LE-------- 94
Cdd:COG1574 90 arslDELLarLRaaaaelppgEWILGRGWdeslwpegrfptradldavspdrPvvltrvdghaawvnsaaLElagitadt 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 95 --------------------------------SQFTPELAVASTELGLLEMVKSGTTSFSDMFnpIGVDQDAIMETVSRS 142
Cdd:COG1574 170 pdpeggeierdadgeptgvlreaamdlvraaiPPPTPEELRAALRAALRELASLGITSVHDAG--LGPDDLAAYRELAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 143 GMRAAvsRTLFSFGTKDDEkkaIEEAEKYVKRYYKESGMLTtmVAP----------------HSPYTC----------ST 196
Cdd:COG1574 248 GELPL--RVVLYLGADDED---LEELLALGLRTGYGDDRLR--VGGvklfadgslgsrtaalLEPYADdpgnrgllllDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 197 ELLEECARIAVEN--QTMVH------IHLSeterevrdIEAqygkrpVEYA-ASCGLFKRPTVIAHGVVLNDDERAFLAE 267
Cdd:COG1574 321 EELRELVRAADAAglQVAVHaigdaaVDEV--------LDA------YEAArAANGRRDRRHRIEHAQLVDPDDLARFAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 268 HDVRVAHNPN----------SNL--KLGSGIANVKAMLEAGIKVGIATDS-VASnnnLDMFEELRIA----TLLQKGIHH 330
Cdd:COG1574 387 LGVIASMQPThatsdgdwaeDRLgpERAARAYPFRSLLDAGAPLAFGSDApVEP---LDPLLGIYAAvtrrTPSGRGLGP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 331 DAtALPVETALSLATKGAAEVIGM-KQTGSLEVGKCADFItidpsnkphlqpadeVLSHLVYAASGKDISDV-----IIN 404
Cdd:COG1574 464 EE-RLTVEEALRAYTIGAAYAAFEeDEKGSLEPGKLADFV---------------VLDRDPLTVPPEEIKDIkvlltVVG 527
|
....
gi 558579131 405 GKRV 408
Cdd:COG1574 528 GRVV 531
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
86-409 |
9.51e-12 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 66.40 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 86 LETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMetvsrsgMRAAVSRtlfsfGTKDDEKKAI 165
Cdd:pfam07969 133 LREGAYALPPLLAREAEAAAVAAALAALPGFGITSVDGGGGNVHSLDDYEP-------LRELTAA-----EKLKELLDAP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 166 EEAEKYVKRYYKESGML--------------TTMVAPHSPYT----CSTELLEECARIAVENQTMVHIHlSETEREVRDI 227
Cdd:pfam07969 201 ERLGLPHSIYELRIGAMklfadgvlgsrtaaLTEPYFDAPGTgwpdFEDEALAELVAAARERGLDVAIH-AIGDATIDTA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 228 EAQYGKRPVEYaascGLFKRPTvIAHG---VVLNDDERAFLAE----------HDVRVAHNPNSNLKL--GSGIANVKAM 292
Cdd:pfam07969 280 LDAFEAVAEKL----GNQGRVR-IEHAqgvVPYTYSQIERVAAlggaagvqpvFDPLWGDWLQDRLGAerARGLTPVKEL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 293 LEAGIKVGIATDSvasnnNLDMFEEL-RIATLL---QKGIHHDATA---LPVETALSLATKGAAEVIGM-KQTGSLEVGK 364
Cdd:pfam07969 355 LNAGVKVALGSDA-----PVGPFDPWpRIGAAVmrqTAGGGEVLGPdeeLSLEEALALYTSGPAKALGLeDRKGTLGVGK 429
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 558579131 365 CADFITIDPsNKPHLQPADEVLSHLVYaasgkdisdVIINGKRVV 409
Cdd:pfam07969 430 DADLVVLDD-DPLTVDPPAIADIRVRL---------TVVDGRVVY 464
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
48-408 |
2.07e-10 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 61.94 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 48 EVIDMKGKWVLPGLVNTHTHVVMSLLRGI---------GDDMLLQPWLETRIWPLESQFtpELAVASTELGLLEMVKSGt 118
Cdd:cd01309 18 EVIDAKGKHVTPGLIDAHSHLGLDEEGGVretsdaneeTDPVTPHVRAIDGINPDDEAF--KRARAGGVTTVQVLPGSA- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 119 tsfsdmfNPIGvDQDAIMETVSR----------SGMRAAVSRTLFSF------------GTKDDEKKAIEEAEKYVKRYY 176
Cdd:cd01309 95 -------NLIG-GQGVVIKTDGGtiedmfikapAGLKMALGENPKRVyggkgkepatrmGVAALLRDAFIKAQEYGRKYD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 177 KESGMLTTMVAPhspytcstELLEECARIAVENQTMVHIHLSEtereVRDIEAQygkrpVEYAAScglFKRPTVIAHGVv 256
Cdd:cd01309 167 LGKNAKKDPPER--------DLKLEALLPVLKGEIPVRIHAHR----ADDILTA-----IRIAKE---FGIKITIEHGA- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 257 lnDDERAF--LAEHDVRVAHNP-----NSNLKLGSGIANVKAMLEAG-IKVGIATDsvasnnnldmFEELRIATLLQKGI 328
Cdd:cd01309 226 --EGYKLAdeLAKHGIPVIYGPtltlpKKVEEVNDAIDTNAYLLKKGgVAFAISSD----------HPVLNIRNLNLEAA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 329 HHDATALPVETALSLATKGAAEVIGM-KQTGSLEVGKCADFITIDpsnkphlqpaDEVLSHLVYAAsgkdisDVIINGKR 407
Cdd:cd01309 294 KAVKYGLSYEEALKAITINPAKILGIeDRVGSLEPGKDADLVVWN----------GDPLEPTSKPE------QVYIDGRL 357
|
.
gi 558579131 408 V 408
Cdd:cd01309 358 V 358
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
7-413 |
1.77e-09 |
|
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: 59.33 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 7 NATIVTMNEqnevIENGYIIVENNQIIDVksGEFANDFEVDEVIDMKGKWVLPGLVNTHTHvvmslLRgigddmllQPWL 86
Cdd:COG0044 4 NGRVVDPGG----LERADVLIEDGRIAAI--GPDLAAPEAAEVIDATGLLVLPGLIDLHVH-----LR--------EPGL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 87 ETRiwplESqFTPELAVAstelgllemVKSGTTSFSDMFNPI-GVDQDAIMETVSRSGMRAAVSRTLFSFG-TKDDEK-- 162
Cdd:COG0044 65 EHK----ED-IETGTRAA---------AAGGVTTVVDMPNTNpVTDTPEALEFKLARAEEKALVDVGPHGAlTKGLGEnl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 163 ---------------------------------KAIEEAEKY-------------VKRYYKESGMLTTMVAPHS-PYTCS 195
Cdd:COG0044 131 aelgalaeagavafkvfmgsddgnpvlddgllrRALEYAAEFgalvavhaedpdlIRGGVMNEGKTSPRLGLKGrPAEAE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 196 TELLEECARIAVENQTMVHI-HLSeTEREVRDIEA--QYGKRpveyaASCGlfkrptVIAHGVVLNDDErafLAEHDvrv 272
Cdd:COG0044 211 EEAVARDIALAEETGARLHIvHVS-TAEAVELIREakARGLP-----VTAE------VCPHHLTLTDED---LERYG--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 273 ahnpnSNLK----LGSGiANVKAMLEaGIKVG----IATDSV---ASNNNLDMFE--------ELRIATLLQKGIHhdAT 333
Cdd:COG0044 273 -----TNFKvnppLRTE-EDREALWE-GLADGtidvIATDHAphtLEEKELPFAEapngipglETALPLLLTELVH--KG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 334 ALPVETALSLATKGAAEVIGMKQTGSLEVGKCADFITIDPsNKPHLQPADEVLSHLVYAA------SGKdISDVIINGKR 407
Cdd:COG0044 344 RLSLERLVELLSTNPARIFGLPRKGRIAVGADADLVLFDP-DAEWTVTAEDLHSKSKNTPfegrelTGR-VVATIVRGRV 421
|
....*.
gi 558579131 408 VVWNGE 413
Cdd:COG0044 422 VYEDGE 427
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
25-369 |
8.35e-09 |
|
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: 57.32 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 25 IIVENNQIIDVKSGEFANDFEVD--EVIDMKGKWVLPGLVNTHTHVVMSL-------LRG-----IGDDMLLQ------- 83
Cdd:cd01300 2 VAVRDGRIVAVGSDAEAKALKGPatEVIDLKGKTVLPGFIDSHSHLLLGGlsllwldLSGvtskeEALARIREdaaaapp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 84 -PWLETRIWPlESQF----------------------------------------------------------------- 97
Cdd:cd01300 82 gEWILGFGWD-ESLLgegryptraeldavspdrpvlllrrdghsawvnsaalrlagitrdtpdppggeivrdadgeptgv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 98 ----------------TPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFsfgtKDDE 161
Cdd:cd01300 161 lveaaaalvleavpppTPEERRAALRAAARELASLGVTTVHDAGGGAADDIEAYRRLAAAGELTLRVRVALY----VSPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 162 KKAIEEAEKYVKRYYkESGMLT---------------TMvAPHSPYTCST----------ELLEECARIAVENQTMVHIH 216
Cdd:cd01300 237 AEDLLEELGARKNGA-GDDRLRlggvklfadgslgsrTA-ALSEPYLDSPgtgglllispEELEELVRAADEAGLQVAIH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 217 L--SETEREVRDIeaqygkrpVEYAAS-CGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPN---------SNLKLGS 284
Cdd:cd01300 315 AigDRAVDTVLDA--------LEAALKdNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNhlysdgdaaEDRRLGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 285 GIAN----VKAMLEAGIKVGIATDS-VASNNNLDMFEEL--RIaTLLQKGIHHDATALPVETALSLATKGAAEVIGM-KQ 356
Cdd:cd01300 387 ERAKrsypFRSLLDAGVPVALGSDApVAPPDPLLGIWAAvtRK-TPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEeDE 465
|
490
....*....|...
gi 558579131 357 TGSLEVGKCADFI 369
Cdd:cd01300 466 KGSLEPGKLADFV 478
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-67 |
1.34e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 56.26 E-value: 1.34e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558579131 4 TYVNATIVTmneQNEVIENGYIIVENNQIIDVKSGEFANDfevdEVIDMKGKWVLPGLVNTHTH 67
Cdd:COG1820 1 AITNARIFT---GDGVLEDGALLIEDGRIAAIGPGAEPDA----EVIDLGGGYLAPGFIDLHVH 57
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
20-405 |
4.57e-08 |
|
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: 54.72 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 20 IENGYIIVENNQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQ--PWLETRIWPLESQF 97
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQLAALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQgaSYLEILAQGGGILS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 98 TPELAVASTELGLLE--------MVKSGTTSfSDMFNPIGVDQDA---IMETVSRSGMRAAVSRTLFSFGTKDDEKKAIE 166
Cdd:TIGR01224 81 TVRATRAASEEELLKlalfrlksMLRSGTTT-AEVKSGYGLDLETelkMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 167 EAEKYVKryykesGMLTTM---VAPHSPYT-----CSTELL--EECARIAVENQTM---VHIHLSETERevrdieaqygK 233
Cdd:TIGR01224 160 RPDDYVD------GICEELipqVAEEGLASfadvfCEAGVFsvEQSRRILQAAQEAglpVKLHAEELSN----------L 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 234 RPVEYAASCGLfkrpTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATD-SVASNNNL 312
Cdd:TIGR01224 224 GGAELAAKLGA----VSADHLEHASDAGIKALAEAGTVAVLLPGTTFYLRETYPPARQLIDYGVPVALATDlNPGSSPTL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 313 DMFEELRIATLLQKgihhdataLPVETALSLATKGAAEVIGM-KQTGSLEVGKCADFITIDPSNKphlqpadevlSHLVY 391
Cdd:TIGR01224 300 SMQLIMSLACRLMK--------MTPEEALHAATVNAAYALGLgEERGTLEAGRDADLVILSAPSY----------AEIPY 361
|
410
....*....|....
gi 558579131 392 AASGKDISDVIING 405
Cdd:TIGR01224 362 HYGVNHVHAVIKNG 375
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
19-413 |
9.80e-08 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 53.84 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 19 VIENGYII-------------VENNQIIDVKSgefANDFEVDEVIDMKGKWVLPGLVNTHTHvvmsllrgigDD--MLLQ 83
Cdd:cd01297 3 VIRNGTVVdgtgappftadvgIRDGRIAAIGP---ILSTSAREVIDAAGLVVAPGFIDVHTH----------YDgqVFWD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 84 PWLETRIW----------------PLESQFTPELAVASTELGLLEMVKS-GTTSFSDMF-----NPIGVDQDAimeTVSR 141
Cdd:cd01297 70 PDLRPSSRqgvttvvlgncgvspaPANPDDLARLIMLMEGLVALGEGLPwGWATFAEYLdaleaRPPAVNVAA---LVGH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 142 SGMRAAVSRTLFSFGTKDDEKKAIEEAEKYVkryykESGML---TTMVAPHSPYTcSTELLEECARIAVENQTMVHIHL- 217
Cdd:cd01297 147 AALRRAVMGLDAREATEEELAKMRELLREAL-----EAGALgisTGLAYAPRLYA-GTAELVALARVAARYGGVYQTHVr 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 218 SETEREVRDIEaqygkRPVEYAAscgLFKRPTVIAHGVV---LNDD---------ERAFLAEHDVRVAHNPNSNLKLgsg 285
Cdd:cd01297 221 YEGDSILEALD-----ELLRLGR---ETGRPVHISHLKSagaPNWGkidrllaliEAARAEGLQVTADVYPYGAGSE--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 286 iANVKAMLEAGIkVGIATDSVASNnnldmFEELRIATLLQKGIHH---DATALPVETALSLATKGAAEVIGMKQTGSLEV 362
Cdd:cd01297 290 -DDVRRIMAHPV-VMGGSDGGALG-----KPHPRSYGDFTRVLGHyvrERKLLSLEEAVRKMTGLPARVFGLADRGRIAP 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 558579131 363 GKCADFITIDPsNKPHLQPADEVLSHlvyAASGkdISDVIINGKRVVWNGE 413
Cdd:cd01297 363 GYRADIVVFDP-DTLADRATFTRPNQ---PAEG--IEAVLVNGVPVVRDGA 407
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
48-378 |
1.68e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 53.01 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 48 EVIDMKGKWVLPGLVNTHTHVVMSLLrgiGDdmllqPW--------LETRI-----WPLESQftPELAVASTELgLLEMV 114
Cdd:PRK05985 40 EVEDGGGALALPGLVDGHIHLDKTFW---GD-----PWypnepgpsLRERIanerrRRAASG--HPAAERALAL-ARAAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 115 KSGTTSfsdMFNPIGVDQD-------AIMETvsRSGMRAAVSRTLFSFgtkddekkaieeaekyvkryyKESGMLTtmva 187
Cdd:PRK05985 109 AAGTTA---MRSHVDVDPDaglrhleAVLAA--RETLRGLIDIQIVAF---------------------PQSGVLS---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 188 phSPYTcsTELLEECAR---------------------------IAVENQTMVHIHLSETErevrDIEAQYGKRPVEYAA 240
Cdd:PRK05985 159 --RPGT--AELLDAALRagadvvggldpagidgdpegqldivfgLAERHGVGIDIHLHEPG----ELGAFQLERIAARTR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 241 SCGLFKRpTVIAHGVVLND-DERAF------LAEHDVRVAHNPNSNLKLGSgianVKAMLEAGIKVGIATDSVASN---- 309
Cdd:PRK05985 231 ALGMQGR-VAVSHAFCLGDlPEREVdrlaerLAEAGVAIMTNAPGSVPVPP----VAALRAAGVTVFGGNDGIRDTwwpy 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558579131 310 NNLDMFEElriATLL--QKGIHHDAtALPVetALSLATKGAAEVIGMKQTGsLEVGKCADFITIDPSNKPH 378
Cdd:PRK05985 306 GNGDMLER---AMLIgyRSGFRTDD-ELAA--ALDCVTHGGARALGLEDYG-LAVGARADFVLVDAETVAE 369
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
7-67 |
3.11e-07 |
|
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: 52.20 E-value: 3.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558579131 7 NATIVTmneqNEVIENGYIIVENNQIIDVKSGEFanDFEVDEVIDMKGKWVLPGLVNTHTH 67
Cdd:cd00854 5 NARILT----PGGLEDGAVLVEDGKIVAIGPEDE--LEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
25-368 |
2.32e-06 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 49.25 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 25 IIVENNQIIDVksGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVmsllrgigddmllqpwletriwplesQFTPELAVA 104
Cdd:cd01307 2 VAIENGKIAAV--GAALAAPAATQIVDAGGCYVSPGWIDLHVHVY--------------------------QGGTRYGDR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 105 STELGllemVKSGTTSFSDMFNPIGVDQDAIMETV---SRSGMRA--AVSRT-LFSFG-----TKDDEKKAIEEAEKY-- 171
Cdd:cd01307 54 PDMIG----VKSGVTTVVDAGSAGADNIDGFRYTVierSATRVYAflNISRVgLVAQDelpdpDNIDEDAVVAAAREYpd 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 172 ----VKRYYKESGMLTTMVAPhspytcstelLEECARIAVENQ--TMVHIhlseterevrdieaqyGKRPVEYAASCGLF 245
Cdd:cd01307 130 vivgLKARASKSVVGEWGIKP----------LELAKKIAKEADlpLMVHI----------------GSPPPILDEVVPLL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 246 KRPTVIAH-------GVVLNDDE-RAFlaehdVRVAHNPNSNLKLGSGIANVK-AMLEAGIKVGIATDSVASN----NNL 312
Cdd:cd01307 184 RRGDVLTHcfngkpnGIVDEEGEvLPL-----VRRARERGVIFDVGHGTASFSfRVARAAIAAGLLPDTISSDihgrNRT 258
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 558579131 313 DmFEELRIATLLQKGIhhdATALPVETALSLATKGAAEVIGMKQTGSLEVGKCADF 368
Cdd:cd01307 259 N-GPVYALATTLSKLL---ALGMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADL 310
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-68 |
2.84e-06 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 49.42 E-value: 2.84e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558579131 1 MKTTYVNATIvtMNEQNEvIENGYIIVENNQIIDVKSGEfanDFEVDEVIDMKGKWVLPGLVNTHTHV 68
Cdd:PRK09357 1 MMILIKNGRV--IDPKGL-DEVADVLIDDGKIAAIGENI---EAEGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
47-376 |
5.57e-06 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 48.39 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 47 DEVIDMKGKWVLPGLVNTHTHvvmslLRgigddmllQPWLETRiwplesqftpelavASTELGLLEMVKSGTTSFSDMFN 126
Cdd:cd01317 2 AEVIDAEGKILAPGLVDLHVH-----LR--------EPGFEYK--------------ETLESGAKAAAAGGFTTVVCMPN 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 127 PIGV-DQDAIMETVSRSGMRAAVSRtLFSFG--TKD---------------------DEKKAIEEAE--KYVKRYYKESG 180
Cdd:cd01317 55 TNPViDNPAVVELLKNRAKDVGIVR-VLPIGalTKGlkgeelteigelleagavgfsDDGKPIQDAEllRRALEYAAMLD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 181 MLTtMVAPHSPYTC----------STEL-----LEECARIAVE------NQTMVHIHLSE--TEREVRDIEAqygkrpve 237
Cdd:cd01317 134 LPI-IVHPEDPSLAgggvmnegkvASRLglpgiPPEAETIMVArdlelaEATGARVHFQHlsTARSLELIRK-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 238 yAASCGLFKRPTVIAHGVVLNDDeraflaehDVRvahNPNSNLK----LGSgIANVKAMLEA---GIKVGIATDSVASNN 310
Cdd:cd01317 205 -AKAKGLPVTAEVTPHHLLLDDE--------ALE---SYDTNAKvnppLRS-EEDREALIEAlkdGTIDAIASDHAPHTD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 311 ---NLDMFE--------ELRIA---TLLQKGIHhdataLPVETALSLATKGAAEVIGMKQtGSLEVGKCADFITIDPSNK 376
Cdd:cd01317 272 eekDLPFAEappgiiglETALPllwTLLVKGGL-----LTLPDLIRALSTNPAKILGLPP-GRLEVGAPADLVLFDPDAE 345
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
25-410 |
1.54e-05 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 47.00 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 25 IIVENNQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHvvmsLLRGIGddmllQPWLETRiwplesqfTPELAva 104
Cdd:cd01308 20 ILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVH----IIGGGG-----EGGPSTR--------TPEVT-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 105 stelgLLEMVKSGTTSfsdMFNPIGVDqdaimeTVSRSgMRAAVSRTlfsfgtkddekKAIEE----AEKYVKRYYKESG 180
Cdd:cd01308 81 -----LSDLTTAGVTT---VVGCLGTD------GISRS-MEDLLAKA-----------RALEEegitCFVYTGSYEVPTR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 181 MLTTMV---------------APHSPYTCSTELLEECARIAVENQT---------MVHIHLSETEREVRDIEaqygkrpv 236
Cdd:cd01308 135 TITGSIrkdlllidkvigvgeIAISDHRSSQPTVEELARIAAEARVggllggkagIVHIHLGDGKRALSPIF-------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 237 EYAASCGLfkrPtvIAHGVVLNDDERAFLAEHDVRVA---------------HNPNSNLKLGSGIanvKAMLEAGIKVGI 301
Cdd:cd01308 207 ELIEETEI---P--ITQFLPTHINRTAPLFEQGVEFAkmggtidltssidpqFRKEGEVRPSEAL---KRLLEQGVPLER 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 302 ATDSVASNNNLDMFEELRIATLLQKGIHH----------DATALPVETALSLATKGAAEVIGMKQTGSLEVGKCADFITI 371
Cdd:cd01308 279 ITFSSDGNGSLPKFDENGNLVGLGVGSVDtllrevreavKCGDIPLEVALRVITSNVARILKLRKKGEIQPGFDADLVIL 358
|
410 420 430
....*....|....*....|....*....|....*....
gi 558579131 372 DPsnkphlqpadEVLSHLVYaASGKDIsdvIINGKRVVW 410
Cdd:cd01308 359 DK----------DLDINSVI-AKGQIM---VRNGKLLVK 383
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
17-373 |
1.97e-05 |
|
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: 46.67 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 17 NEVIENGyIIVENNQIIDVKSGEFANDfevDEVIDMKGKWVLPGLVNTHTHV--------------VMSLLRG-IGD--D 79
Cdd:TIGR00857 1 GKETEVD-ILVEGGRIKKIGKLRIPPD---AEVIDAKGLLVLPGFIDLHVHLrdpgeeykediesgSKAAAHGgFTTvaD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 80 M------LLQPwlETRIWPLES-------QFTPELAVAS-------TELGLLEMVKSGTTSFSDmfNPIGVDQDAIMETV 139
Cdd:TIGR00857 77 MpntkppIDTP--ETLEWKLQRlkkvslvDVHLYGGVTQgnqgkelTEAYELKEAGAVGRMFTD--DGSEVQDILSMRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 140 SRSGMRAAVSRTLFSfgtkdDEKKAIEEAEKYVKRYYKESGmlttmvAPHSPYTCSTELLEECARIAVENQTMVHI-HLS 218
Cdd:TIGR00857 153 LEYAAIAGVPIALHA-----EDPDLIYGGVMHEGPSAAQLG------LPARPPEAEEVAVARLLELAKHAGCPVHIcHIS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 219 --ETEREVRDIEAQYGKRPVEyaascglfkrptVIAHGVVLNDDErafLAEHDVRVAHNPNSNLKlGSGIANVKAMLEAG 296
Cdd:TIGR00857 222 tkESLELIVKAKSQGIKITAE------------VTPHHLLLSEED---VARLDGNGKVNPPLREK-EDRLALIEGLKDGI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 297 IKVgIATDSvASNNNLDMFEELRIAtllQKGIHHDATALPV------------ETALSLATKGAAEVIGMKQTGSLEVGK 364
Cdd:TIGR00857 286 IDI-IATDH-APHTLEEKTKEFAAA---PPGIPGLETALPLllqllvkglislKDLIRMLSINPARIFGLPDKGTLEEGN 360
|
....*....
gi 558579131 365 CADFITIDP 373
Cdd:TIGR00857 361 PADITVFDL 369
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
20-374 |
4.80e-05 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 45.39 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 20 IENGYI--IVENNQIIDvksgefandfEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGigddmllqPW--------LETR 89
Cdd:PRK06846 36 IQDGKIvaIRPNKQVPD----------ATLPTYDANGLLMLPAFREMHIHLDKTYYGG--------PWkacrpaktIQDR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 90 IwPLESQFTPELAVASTEL--GLLEMVKSGTTSFSDMFnpigVDQDAIMETVSRSGMRAAVSRTLFSFGT---------- 157
Cdd:PRK06846 98 I-ELEQKELPELLPTTQERaeKLIELLQSKGATHIRSH----CNIDPVIGLKNLENLQAALERYKDGFTYeivafpqhgl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 158 -KDDEKKAIEEAEKyvkryykesgMLTTMVAPHSPYTCSTEL---LEECARIAVENQTMVHIHLSET-EREVRDIeaqyg 232
Cdd:PRK06846 173 lRSNSEPLMREAMK----------MGAHLVGGVDPASVDGAIeksLDTMFQIAVDFNKGVDIHLHDTgPLGVATI----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 233 KRPVEYAASCGLFKRPTvIAHGVVLNDDERA-------FLAEHDVRVAhnpnSNLKLGSGIANVKAMLEAGIKVGIATDS 305
Cdd:PRK06846 238 KYLVETTEEAQWKGKVT-ISHAFALGDLNEEeveelaeRLAAQGISIT----STVPIGRLHMPIPLLHDKGVKVSLGTDS 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 558579131 306 V----ASNNNLDMFEELRiaTLLQKGIHHDATALpvETALSLATKGAAEVIGMKQTGSLEVGKCADFITIDPS 374
Cdd:PRK06846 313 VidhwSPFGTGDMLEKAN--LLAELYRWSDERSL--SRSLALATGGVLPLNDEGERVWPKVGDEASFVLVDAS 381
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-70 |
1.01e-04 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 44.39 E-value: 1.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 1 MKTTYVNATIVTMNEQNEvienGYIIVENNQIIDVKSGEfandfeVDEVIDMKGKWVLPGLVNTHTHVVM 70
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYK----ADVLIEDGKIAAIGANL------GDEVIDATGKYVMPGGIDPHTHMEM 60
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
25-68 |
1.05e-04 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 44.39 E-value: 1.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 558579131 25 IIVENNQIIDVksGEFANDFEVDEVIDMKGKWVLPGLVNTHTHV 68
Cdd:COG3964 22 IAIKDGKIAAV--AKDIDAAEAKKVIDASGLYVTPGLIDLHTHV 63
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-66 |
2.05e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 43.24 E-value: 2.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 558579131 1 MKTTYVNATIVTmneQNEVIEnGYIIVENNQIIDVKSGEFAndfeVDEVIDMKGKWVLPGLVNTHT 66
Cdd:PRK15446 2 MEMILSNARLVL---PDEVVD-GSLLIEDGRIAAIDPGASA----LPGAIDAEGDYLLPGLVDLHT 59
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-67 |
4.02e-04 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 42.55 E-value: 4.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558579131 1 MKTTYVNATIVtmNEQNE-----VIENGYI--IVENnqiIDVKSGefandfevDEVIDMKGKWVLPGLVNTHTH 67
Cdd:PRK09236 2 KRILIKNARIV--NEGKIfegdvLIENGRIakIASS---ISAKSA--------DTVIDAAGRYLLPGMIDDQVH 62
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
19-68 |
4.28e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 42.14 E-value: 4.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 558579131 19 VIENGYII-VENNqiIDVKSGEfandfevdEVIDMKGKWVLPGLVNTHTHV 68
Cdd:PRK09237 22 AIEDGKIAaVAGD--IDGSQAK--------KVIDLSGLYVSPGWIDLHVHV 62
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
7-68 |
4.52e-04 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 42.28 E-value: 4.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 558579131 7 NATIVTmneQNEVIENGyIIVENNQIIDVKSGEfaNDFEVDEVIDMKGKWVLPGLVNTHTHV 68
Cdd:cd01315 6 NGRVVT---PDGVREAD-IAVKGGKIAAIGPDI--ANTEAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
7-70 |
6.12e-04 |
|
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: 41.82 E-value: 6.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558579131 7 NATIVTMNEQNEV---IENGyIIVENNQIIDVKSGEfandfevdEVIDMKGKWVLPGLVNTHTHVVM 70
Cdd:cd01314 5 NGTIVTADGSFKAdilIEDG-KIVAIGPNLEAPGGV--------EVIDATGKYVLPGGIDPHTHLEL 62
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
19-74 |
7.05e-04 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 41.70 E-value: 7.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558579131 19 VIENGYII-------------VENNQIIDVksGEFANDfEVDEVIDMKGKWVLPGLVNTHTHVVMSLLR 74
Cdd:COG3653 5 LIRGGTVVdgtgappfradvaIKGGRIVAV--GDLAAA-EAARVIDATGLVVAPGFIDIHTHYDLQLLW 70
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
335-414 |
7.85e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 41.62 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 335 LPVETALSLATKGAAEVIGMKQTGSLEVGKCADFItidpsnkphlqpadeVLSHLVyaasGKDISDVIINGKRVVWNGEC 414
Cdd:COG1001 284 LDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIV---------------LLDDLE----DFKVEKVYADGKLVAEDGKL 344
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
17-67 |
8.28e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 41.29 E-value: 8.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 558579131 17 NEVIEnGYIIVENNQIIDVKsgefANDFEVDEVIDMKGKWVLPGLVNTHTH 67
Cdd:PRK04250 10 GRIVE-GGIGIENGRISKIS----LRDLKGKEVIKVKGGIILPGLIDVHVH 55
|
|
| AslB |
COG0641 |
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ... |
254-330 |
1.84e-03 |
|
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440406 [Multi-domain] Cd Length: 349 Bit Score: 40.36 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558579131 254 GVVLNDDERAFLAEHDVRV---------AHN---PNSNlklGSG-----IANVKAMLEAGIKVGIATdsVASNNNLDMFE 316
Cdd:COG0641 94 GTLLDDEWIDFLKENGFSVgisldgpkeIHDrnrVTKN---GKGsfdrvMRNIKLLKEHGVEVNIRC--TVTRENLDDPE 168
|
90
....*....|....
gi 558579131 317 ELrIATLLQKGIHH 330
Cdd:COG0641 169 EL-YDFLKELGFRS 181
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
321-375 |
3.90e-03 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 39.19 E-value: 3.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 558579131 321 ATLLQK--GIHHDATaLPVETALSLATKGAAEVIGMKQTGSLEVGKCADFITIDPSN 375
Cdd:cd01306 258 ASLLHAafRLADLGG-WSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVDDMD 313
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
19-68 |
5.52e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 39.07 E-value: 5.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 558579131 19 VIENGYIIVENN-QIID--VKSGEFA----NDFEVDEVIDMKGKWVLPGLVNTHTHV 68
Cdd:PRK08044 6 IIKNGTVILENEaRVVDiaVKGGKIAaigqDLGDAKEVMDASGLVVSPGMVDAHTHI 62
|
|
| |
