|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
13-444 |
0e+00 |
|
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: 642.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 13 FRGTFVHSTWTCPMEvLRDHLLGVSDSGKIVFLEEASQQEKLAKEW--CFKPCEIRELSHHEFFMPGLVDTHIHASQYSF 90
Cdd:cd01303 1 FRGTFIHTKSLPELE-LVEDALRVVEDGLIVVVDGNIIAAGAAETLkrAAKPGARVIDSPNQFILPGFIDTHIHAPQYAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 91 AGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVC 170
Cdd:cd01303 80 IGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 171 MDLNDtfPEYK-ETTEESIKETERFVSEMLQKnYSRVKPIVTPRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEV 248
Cdd:cd01303 160 MDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 249 EAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLG 328
Cdd:cd01303 237 AWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 329 TDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSP 408
Cdd:cd01303 317 TDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLL 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 4758426 409 IDLfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGG 444
Cdd:cd01303 397 ADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
26-444 |
0e+00 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 575.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 26 MEVLRDHLLGVSDsGKIVFLEEASQQeklaKEWCFKPCEIRELSHHeFFMPGLVDTHIHASQYSFAGSsIDLPLLEWLTK 105
Cdd:TIGR02967 1 LEYFEDGLLVVEN-GRIVAVGDYAEL----KETLPAGVEIDDYRGH-LIMPGFIDTHIHYPQTEMIAS-YGEQLLEWLEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 106 YTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNdtFPEY-KETT 184
Cdd:TIGR02967 74 YTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDRN--APDYlRDTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 185 EESIKETERFVSEMLQKNysRVKPIVTPRFSLSCSETLMGELGNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTS 263
Cdd:TIGR02967 152 ESSYDESKALIERWHGKG--RLLYAVTPRFAPTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 264 VYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAI 343
Cdd:TIGR02967 230 VYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 344 RRAVMVSNILlinkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGdffGDISEA 423
Cdd:TIGR02967 310 REAYKVSQLQ------GARLSPFEAFYLATLGGARALDLDDRIGNFEPGKEADFVVLDPAATPLLALRFEG---ADTLED 380
|
410 420
....*....|....*....|.
gi 4758426 424 VIQKFLYLGDDRNIEEVYVGG 444
Cdd:TIGR02967 381 KLFKLMYLGDDRNVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-448 |
7.78e-119 |
|
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: 353.36 E-value: 7.78e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 16 TFVHSTWTCPM----EVLRDHLLGVSDsGKIVFLEEASQQEKLakewcFKPCEIRELSHHeFFMPGLVDTHIHASQYSFA 91
Cdd:COG0402 2 LLIRGAWVLTMdpagGVLEDGAVLVED-GRIAAVGPGAELPAR-----YPAAEVIDAGGK-LVLPGLVNTHTHLPQTLLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 92 GSSIDLPLLEWLTKYTFPAEHRFqNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCM 171
Cdd:COG0402 75 GLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 172 DLNdtFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEA 250
Cdd:COG0402 154 DRG--FPDgLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 251 VKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD 330
Cdd:COG0402 232 VLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 331 VAGG-YSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASD-SP 408
Cdd:COG0402 310 GAASnNSLDMFEEMRLAALLQRLR---GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHlAP 386
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 4758426 409 IDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:COG0402 387 LH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
11-447 |
3.50e-105 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 319.06 E-value: 3.50e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 11 HIFRGTFVHST---WTCP----MEVLRDHLLGVSDsGKIVFLEEASQ-QEKLAKEwcfkpCEIRELSHHeFFMPGLVDTH 82
Cdd:PRK09228 4 KAYRGRLLHFTadpAEVDdedaLRYIEDGLLLVED-GRIVAAGPYAElRAQLPAD-----AEVTDYRGK-LILPGFIDTH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 83 IHASQYSFAGSsidlP---LLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSsllladiTDK 159
Cdd:PRK09228 77 IHYPQTDMIAS----YgeqLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFGTVHPQS-------VDA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 160 F-------GQRAFVGKVCMDLNdtFPEY-KETTEESIKETERfvseMLQK--NYSRVKPIVTPRFSLSCSETLMGELGNI 229
Cdd:PRK09228 146 LfeaaearNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKA----LIERwhGKGRLLYAITPRFAPTSTPEQLEAAGAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 230 AKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSL 308
Cdd:PRK09228 220 AREHpDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 309 SSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSnillinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGN 388
Cdd:PRK09228 300 GSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAFYLATLGGARALGLDDRIGN 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758426 389 FEVGKEFDAILINPKA----------SDSPIDLFYGdffgdiseaviqkFLYLGDDRNIEEVYVGGKQV 447
Cdd:PRK09228 374 LAPGKEADFVVLDPAAtpllalrtarAESLEELLFA-------------LMTLGDDRAVAETYVAGRPV 429
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
23-448 |
1.14e-70 |
|
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: 229.40 E-value: 1.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 23 TCPMEVLRDHLLGVSDsGKIVFLEEASQQEKLAKEwcfkpcEIRELSHHeFFMPGLVDTHIHASQYSFAGSSIDLPLLEW 102
Cdd:cd01298 11 TDPRRVLEDGDVLVED-GRIVAVGPALPLPAYPAD------EVIDAKGK-VVMPGLVNTHTHLAMTLLRGLADDLPLMEW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 103 LTKYTFPAEHRFQnidfAEEVY--TRV-VRRTLKNGTTTAC--YFatIHTDSsllLADITDKFGQRAFVGKVCMDLNDtf 177
Cdd:cd01298 83 LKDLIWPLERLLT----EEDVYlgALLaLAEMIRSGTTTFAdmYF--FYPDA---VAEAAEELGIRAVLGRGIMDLGT-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 178 pEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYps 257
Cdd:cd01298 152 -EDVEETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEKY-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 258 ykNYTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGG 334
Cdd:cd01298 229 --GKRPVeYlEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgAASN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 335 YSYSMLDAIRRAvmvsniLLINKV---NEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPkasDSPidl 411
Cdd:cd01298 307 NNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATIGGAKALGLD-EIGSLEVGKKADLILIDL---DGP--- 373
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 4758426 412 fygDFFG---DISEAViqkflYLGDDRNIEEVYVGGKQVV 448
Cdd:cd01298 374 ---HLLPvhdPISHLV-----YSANGGDVDTVIVNGRVVM 405
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
75-401 |
6.60e-61 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 204.85 E-value: 6.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 75 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAE--HRfqnidfAEEVYTRV---VRRTLKNGTTTACYFATI-HTD 148
Cdd:PRK07228 55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEaaHD------AESMYYSAllgIGELIESGTTTIVDMESVhHTD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 149 SSL-LLADItdkfGQRAFVGKVCMDLNDTFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGEL 226
Cdd:PRK07228 129 SAFeAAGES----GIRAVLGKVMMDYGDDVPEgLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 227 GNIAKTRDLHIQSHISENRDEVEAVKNlYPSYKNYTsVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNL 306
Cdd:PRK07228 205 RDLADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 307 SLSSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDA---IRRAVmvsnilLINKVNE---KSLTLKEVFRLATLGGSQAL 380
Cdd:PRK07228 283 KLASGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA------LIQKVDRlgpTAMPARTVFEMATLGGAKAA 354
|
330 340
....*....|....*....|.
gi 4758426 381 GLDGEIGNFEVGKEFDAILIN 401
Cdd:PRK07228 355 GFEDEIGSLEEGKKADLAILD 375
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
75-447 |
6.45e-56 |
|
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: 188.48 E-value: 6.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 75 MPGLVDTHIHASQYSFAGSSIDLpllewltkytfpaehrfqniDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLA 154
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 155 DITDK--FGQRAFVGKVCMDLNDTFPEYKETTEESIKETErfvsEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKT 232
Cdd:pfam01979 63 EAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE----FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 233 RDLHIQSHISENRDEVEAVKNLYPS---YKNYTSVYDKNNLL-TNKTVMAHGCYLSAEELNVFHER--GASIAHCPNSNL 306
Cdd:pfam01979 139 YGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 307 SLSSGFLNVLEVLKHEVKIGLGTDVAG-GYSYSMLDAIRRAVmvsnilLINKVNEKSLTLKEVFRLATLGGSQALGLDGE 385
Cdd:pfam01979 219 KLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGLDDK 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758426 386 IGNFEVGKEFDAILINPKasdspidlfygdffgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 447
Cdd:pfam01979 293 VGSIEVGKDADLVVVDLD--------------------PLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
16-448 |
1.34e-50 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 177.41 E-value: 1.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 16 TFVHSTWTCPME----VLRDHLLGVSDsGKIVFLeeASQQEKLAKewcFKPCEIRELSHHeFFMPGLVDTHIHASQYSFA 91
Cdd:PRK09045 9 LLIEARWIVPVEpagvVLEDHAVAIRD-GRIVAI--LPRAEARAR---YAAAETVELPDH-VLIPGLINAHTHAAMSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 92 GSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTA--CYFatiHTDSsllLADITDKFGQRAFVGKV 169
Cdd:PRK09045 82 GLADDLPLMTWLQDHIWPAEGAWVSEEFVRDGTLLAIAEMLRGGTTCFndMYF---FPEA---AAEAAHQAGMRAQIGMP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 170 CMDlndtFP-EYKETTEESI----KETERFvsemlqKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISEN 244
Cdd:PRK09045 156 VLD----FPtAWASDADEYLakglELHDQW------RHHPLISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHET 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 245 RDEVEAvknlypSYKNY----TSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLK 320
Cdd:PRK09045 226 AQEIAD------SLKQHgqrpLARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 321 HEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSnillinKV---NEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFD 396
Cdd:PRK09045 300 AGVNVALGTDgAASNNDLDLFGEMRTAALLA------KAvagDATALPAHTALRMATLNGARALGLDDEIGSLEPGKQAD 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 4758426 397 AILINPKASDS-PIdlfygdfFGDISEAViqkflYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK09045 374 LVAVDLSGLETqPV-------YDPVSQLV-----YAAGREQVSHVWVAGKQLL 414
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
71-448 |
1.33e-46 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 166.51 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 71 HEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRrTLKNGTTTAC--YFatiHTD 148
Cdd:PRK08393 49 GSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYLGLLE-MIKSGTTTFVdmYF---HME 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 149 SsllLADITDKFGQRAFVGKVCMDLNDtfpeyKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGN 228
Cdd:PRK08393 125 E---VAKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVRE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 229 IAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSL 308
Cdd:PRK08393 197 KAREWNKLITIHLSETMDEIKQIREKYG--KSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 309 SSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDAIRRAVMVSnilLINKVNEKSLTL---KEVFRLATLGGSQALGLDGe 385
Cdd:PRK08393 275 GSGVMPLRKLLNAGVNVALGTD--GAASNNNLDMLREMKLAA---LLHKVHNLDPTIadaETVFRMATQNGAKALGLKA- 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758426 386 iGNFEVGKEFDAILIN-PKASDSPIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK08393 349 -GVIKEGYLADIAVIDfNRPHLRPIN------------NPISHLVYSANGNDVETTIVDGKIVM 399
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
70-403 |
9.57e-44 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 158.76 E-value: 9.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 70 HHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVYTRVVRRTL---KNGTTTacyFAT-- 144
Cdd:PRK06038 49 KGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYAGSLLACLemiKSGTTS---FADmy 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 145 IHTDSSlllADITDKFGQRAFVGKVCMDLNDTfpeykETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMG 224
Cdd:PRK06038 122 FYMDEV---AKAVEESGLRAALSYGMIDLGDD-----EKGEAELKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 225 ELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSVY--DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCP 302
Cdd:PRK06038 194 KVKKLANKDGVGIHIHVLETEAELNQMKEQY----GMCSVNylDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 303 NSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALG 381
Cdd:PRK06038 270 VSNMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAALLHK---VNTMDPTALPARQVLEMATVNGAKALG 346
|
330 340
....*....|....*....|..
gi 4758426 382 LdgEIGNFEVGKEFDAILINPK 403
Cdd:PRK06038 347 I--NTGMLKEGYLADIIIVDMN 366
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
23-448 |
9.30e-43 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 155.93 E-value: 9.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 23 TC--PMEVLRDHLLGVSDSgKIV--------FLEEASQQEKLAKEWcfkpceirelshhefFMPGLVDTHIHASQYSFAG 92
Cdd:PRK06687 11 TCdqDFHVYLDGILAVKDS-QIVyvgqdkpaFLEQAEQIIDYQGAW---------------IMPGLVNCHTHSAMTGLRG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 93 SSIDLPLLEWLTKYTFPAEHRFqNIDFAEEVYTRVVRRTLKNGTTTacyFATIHTDSSLLLADITDKFGQRafvGKVCMD 172
Cdd:PRK06687 75 IRDDSNLHEWLNDYIWPAESEF-TPDMTTNAVKEALTEMLQSGTTT---FNDMYNPNGVDIQQIYQVVKTS---KMRCYF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 173 LNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVK 252
Cdd:PRK06687 148 SPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 253 NLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-V 331
Cdd:PRK06687 228 KRYG--KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDsV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 332 AGGYSYSMLDAIRRAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASdspIDL 411
Cdd:PRK06687 306 ASNNNLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLTIEGAKALGMENQIGSLEVGKQADFLVIQPQGK---IHL 379
|
410 420 430
....*....|....*....|....*....|....*..
gi 4758426 412 FygdffgdISEAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK06687 380 Q-------PQENMLSHLVYAVKSSDVDDVYIAGEQVV 409
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
72-448 |
2.37e-33 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 130.56 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 72 EFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNiDFAEEVYTRVVRRTLKNGTTT-ACYFATIHTDSS 150
Cdd:PRK15493 55 KWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFTP-ELAVASTELGLLEMVKSGTTSfSDMFNPIGVDQD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 151 LLLADITDKfGQRAFVGKVCMDLNDtfpeyKETTEESIKETERFVSEMLQKNySRVKPIVTPRFSLSCSETLMGELGNIA 230
Cdd:PRK15493 134 AIMETVSRS-GMRAAVSRTLFSFGT-----KEDEKKAIEEAEKYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 231 KTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSS 310
Cdd:PRK15493 207 VENQTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 311 GFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVFRLATLGGSQALGLDgEIGNF 389
Cdd:PRK15493 285 GIANVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQKGI---HQDATALPVETALTLATKGAAEVIGMK-QTGSL 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758426 390 EVGKEFDAILINP--KASDSPidlfygdffgdiSEAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK15493 361 EVGKCADFITIDPsnKPHLQP------------ADEVLSHLVYAASGKDISDVIINGKRVV 409
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
75-445 |
6.73e-26 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 109.20 E-value: 6.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 75 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKyTFPAEHRFQNidfaEEVYTRV---VRRTLKNGTTTacyFATIHTDSSL 151
Cdd:PRK06380 53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TFKYDSKRTR----EGIYNSAklgMYEMINSGITA---FVDLYYSEDI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 152 LlADITDKFGQRAFVGKVCMDlndtfPEYKETTEESIKETERFVSEMLQKNYsrVKPIVTPRFSLSCSETLMGELGNIAK 231
Cdd:PRK06380 125 I-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIREHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 232 TRDLHIQSHISENRDEVeavknlYPSYKNY----TSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLS 307
Cdd:PRK06380 197 KYDTIMHMHLSETRKEV------YDHVKRTgerpVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 308 LSS-GFLNVLEVLKHEVKIGLGTDVAGgySYSMLDAIrRAVMVSNILLINKVNEKSLT-LKEVFRLATLGGSQALGLDGe 385
Cdd:PRK06380 271 LGTgGSPPIPEMLDNGINVTIGTDSNG--SNNSLDMF-EAMKFSALSVKNERWDASIIkAQEILDFATINAAKALELNA- 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 386 iGNFEVGKEFDAILINPKASdSPIDLFYGDFFGDIseaviqkfLYLGDDRNIEEVYVGGK 445
Cdd:PRK06380 347 -GSIEVGKLADLVILDARAP-NMIPTRKNNIVSNI--------VYSLNPLNVDHVIVNGK 396
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
76-448 |
2.95e-23 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 101.68 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 76 PGLVDTHIHASQYSFAG--SSIDLPLLEWL--TKYTFPA---EHRFQ---NIDFAEevytrvvrrTLKNGTTTAC----- 140
Cdd:PRK12393 59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLaaVPYRFRArfdEDLFRlaaRIGLVE---------LLRSGCTTVAdhhyl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 141 YFATIHTDSSLLLADITDKFGQRaFV---GKVCMDLNDTfPEYK-----ETTEESIKETERFVSEMLQKNYSRVKPIV-- 210
Cdd:PRK12393 130 YHPGMPFDTGDILFDEAEALGMR-FVlcrGGATQTRGDH-PGLPtalrpETLDQMLADVERLVSRYHDASPDSLRRVVva 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 211 --TPRFSLScsETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSVY--DKNNLLTNKTVMAHGCYLSAE 286
Cdd:PRK12393 208 ptTPTFSLP--PELLREVARAARGMGLRLHSHLSETVDYVDFCREKY----GMTPVQfvAEHDWLGPDVWFAHLVKLDAE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 287 ELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNILlinkVNEKSLTL 365
Cdd:PRK12393 282 EIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDgAASNESADMLSEAHAAWLLHRAE----GGADATTV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 366 KEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINpkaSDSPidLFYGdfFGDISEAVIQKflylGDDRNIEEVYVGGK 445
Cdd:PRK12393 358 EDVVHWGTAGGARVLGLD-AIGTLAVGQAADLAIYD---LDDP--RFFG--LHDPAIAPVAC----GGPAPVKALLVNGR 425
|
...
gi 4758426 446 QVV 448
Cdd:PRK12393 426 PVV 428
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
75-396 |
2.43e-22 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 98.77 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 75 MPGLVDTHIHASQYSFAG--SSIDLPLLEWLTK-YTFPAehrfqNIDfAEEVY--TRV-VRRTLKNGTTTAcyfaTIH-- 146
Cdd:PRK08203 58 TPGLVNTHHHFYQTLTRAlpAAQDAELFPWLTTlYPVWA-----RLT-PEMVRvaTQTaLAELLLSGCTTS----SDHhy 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 147 ---TDSSLLLADITD---KFGQRAFVGKVCMDLN--------DTFPEyketTEESI-KETERFVSEMLQKN-YSRVKPIV 210
Cdd:PRK08203 128 lfpNGLRDALDDQIEaarEIGMRFHATRGSMSLGesdgglppDSVVE----DEDAIlADSQRLIDRYHDPGpGAMLRIAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 211 TPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSV-Y-DKNNLLTNKTVMAHGCYLSAEEL 288
Cdd:PRK08203 204 APCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERF----GMRPVdYlEDLGWLGPDVWLAHCVHLDDAEI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 289 NVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAvmvsniLLINKV--NEKSLTL 365
Cdd:PRK08203 280 ARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGSNLIGEARQA------LLLQRLryGPDAMTA 353
|
330 340 350
....*....|....*....|....*....|.
gi 4758426 366 KEVFRLATLGGSQALGLDgEIGNFEVGKEFD 396
Cdd:PRK08203 354 REALEWATLGGARVLGRD-DIGSLAPGKLAD 383
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
40-396 |
4.54e-21 |
|
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: 94.44 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 40 GKIVFLEEASQQEKLAkewcfkPCEIrelshHEFF-----MPGLVDTHIH------ASQYSFAGSSIdlplleWLTKY-T 107
Cdd:cd01312 1 DKILEVGDYEKLEKRY------PGAK-----HEFFpngvlLPGLINAHTHlefsanVAQFTYGRFRA------WLLSViN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 108 FPAEHRFQNidfAEEVYTRVVRRTLKNGTTTAcyfATIHTDSSLLLADITDKFGQRAFVGKVCMDlNDTFPEYKETTEES 187
Cdd:cd01312 64 SRDELLKQP---WEEAIRQGIRQMLESGTTSI---GAISSDGSLLPALASSGLRGVFFNEVIGSN-PSAIDFKGETFLER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 188 IKETERFVSemlqknySRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAV-------KNLYPSY-- 258
Cdd:cd01312 137 FKRSKSFES-------QLFIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLeeskgwfKHFWESFlk 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 259 -KNYTSVYDKNNL------LTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD- 330
Cdd:cd01312 210 lPKPKKLATAIDFldmlggLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDg 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758426 331 VAGGYSYSMLDAIRravmvSNILLINKVNEKSLTlKEVFRLATLGGSQALGLdgEIGNFEVGKEFD 396
Cdd:cd01312 290 LSSNISLSLLDELR-----ALLDLHPEEDLLELA-SELLLMATLGGARALGL--NNGEIEAGKRAD 347
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
228-448 |
1.61e-19 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 90.03 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 228 NIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNY--------TSVYDKNNLL----TNKTVMAHGCYLSAEELNVFHERG 295
Cdd:PRK08418 197 QLAKKENLLVSTHFLESKAEREWLEESKGWFKKFfekflkepKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 296 ASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillinkvNEKSLTL-KEVFRLAT 373
Cdd:PRK08418 277 ASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSAT 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758426 374 LGGSQALGLD-GEIgnfEVGKEFDAILINpkasdspidlfYGDFFGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 448
Cdd:PRK08418 350 RYGAKALGLNnGEI---KEGKDADLSVFE-----------LPEECTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
75-445 |
3.77e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 89.29 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 75 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRV-VRRTLKNGTTTACYFATI-----H 146
Cdd:PRK08204 56 MPGLVDTHRHTWQSVLRGIGADWTLQTYFREIHGNLGPMFR----PEDVYiaNLLgALEALDAGVTTLLDWSHInnspeH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 147 TDSSLL-LADItdkfGQRA--FVGKVCMDLNDTFpeykETTEESIKETERFVSEMLQKNYSRVK---PIVTPRFSlsCSE 220
Cdd:PRK08204 132 ADAAIRgLAEA----GIRAvfAHGSPGPSPYWPF----DSVPHPREDIRRVKKRYFSSDDGLLTlglAIRGPEFS--SWE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 221 TLMGELGnIAKTRDLHIQSHISenrdeveavknLYPSYKNYTSV--YDKNNLLTNKTVMAHGCYLSAEELNVFHERGASI 298
Cdd:PRK08204 202 VARADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 299 AHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNILLINKV--NEKSLTLKEVFR 370
Cdd:PRK08204 270 SVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMppPRLTLTARQVLE 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758426 371 LATLGGSQALGLDGEIGNFEVGKEFDAILINPKAsdspIDLFYgdfFGDISEAVIQkflyLGDDRNIEEVYVGGK 445
Cdd:PRK08204 350 WATIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVDSVMVAGR 413
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
78-379 |
3.83e-19 |
|
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: 87.00 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 78 LVDTHIHASQYSFAGssIDLPLLEWLTKYTFPAEHRFQNIDFAEEvytrvvrrTLKNGTTTAC-----YFATIHTDSSLL 152
Cdd:cd01292 1 FIDTHVHLDGSALRG--TRLNLELKEAEELSPEDLYEDTLRALEA--------LLAGGVTTVVdmgstPPPTTTKAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 153 LAD-ITDKFGQRAFVGKVCMDLNdtfPEYKETTEESIKETERFVsemlqknYSRVKPIVTPRFSLSCSETLMGELGNI-- 229
Cdd:cd01292 71 VAEaARASAGIRVVLGLGIPGVP---AAVDEDAEALLLELLRRG-------LELGAVGLKLAGPYTATGLSDESLRRVle 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 230 -AKTRDLHIQSHISENRDEVEAVKNLYpsyknytsvydKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSL 308
Cdd:cd01292 141 eARKLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758426 309 SS---GFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLinkvneksLTLKEVFRLATLGGSQA 379
Cdd:cd01292 210 GRdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG--------LSLEEALRLATINPARA 275
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
75-353 |
1.55e-17 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 84.60 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 75 MPGLVDTHIHAsqYS-FA-GSSIDLP----LLEWLTKYTFpaehrfqNIDFA---EEVYTRVVRRTL---KNGTTT---- 138
Cdd:PRK07203 58 MPGLINSHNHI--YSgLArGMMANIPpppdFISILKNLWW-------RLDRAltlEDVYYSALICSLeaiKNGVTTvfdh 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 139 -ACYFATihTDSSLLLADITDKFGQRafvGKVCMDLNDTFPEykETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLS 217
Cdd:PRK07203 129 hASPNYI--GGSLFTIADAAKKVGLR---AMLCYETSDRDGE--KELQEGVEENIRFIKHIDEAKDDMVEAMFGLHASFT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 218 CS-ETL------MGELGniaktRDLHIqsHISENRDEVEAVKNLYpsYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 290
Cdd:PRK07203 202 LSdATLekcreaVKETG-----RGYHI--HVAEGIYDVSDSHKKY--GKDIVERLADFGLLGEKTLAAHCIYLSDEEIDL 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758426 291 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvagGYSYSMLDAIRravmVSNIL 353
Cdd:PRK07203 273 LKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTSDMFESYK----VANFK 328
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
75-377 |
2.51e-14 |
|
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: 72.82 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 75 MPGLVDTHIHASQYSFAGSSIDLPLLEwLTKYTFPAEHRF--QNIDFAEEVYTR-VVRRTLKNGTTTACYFATIHTDSSL 151
Cdd:cd01305 3 IPALVNAHTHLGDSAIKEVGDGLPLDD-LVAPPDGLKHRLlaQADDRELAEAMRkVLRDMRETGIGAFADFREGGVEGIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 152 LLADITDKFgqrAFVGKVCMDlndtFPEYKETTEESIKETERFvsemlqkNYSrvkpivtprfslSCSETLMGELGNIAK 231
Cdd:cd01305 82 LLRRALGKL---PVPFEVILG----RPTEPDDPEILLEVADGL-------GLS------------SANDVDLEDILELLR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 232 TRDLHIQSHISENRD-----EVEAVKNLYPsyknytsvydknNLLTnktvmaHGCYLSAEELNVFHERGASIAHCPNSNL 306
Cdd:cd01305 136 RRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPRSNL 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758426 307 SLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvneKSLTLKEVFRLATLGGS 377
Cdd:cd01305 198 YFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ-------GYLSPLEILRMATVNAA 261
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
75-448 |
1.17e-13 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 72.77 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 75 MPGLVDTHIHasqysfagSSIDLPLL------EWLTKYTFPAEHRFQNidfAEEVYTRVVRRT---------LKNGTTTA 139
Cdd:PRK06151 56 GPGFIDLDAL--------SDLDTTILgldngpGWAKGRVWSRDYVEAG---RREMYTPEELAFqkryafaqlLRNGITTA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 140 CYFATI-------HTDSSLLLADITDKFGQRAFVG-------KVCMDLNDTFPEYKETT-EESIKETERFVSEMLQKNYS 204
Cdd:PRK06151 125 MPIASLfyrqwaeTYAEFAAAAEAAGRLGLRVYLGpayrsggSVLEADGSLEVVFDEARgLAGLEEAIAFIKRVDGAHNG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 205 RVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTS--VYDKNNLLTNKTVMAHGCY 282
Cdd:PRK06151 205 LVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLH----GTTPleWLADVGLLGPRLLIPHATY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 283 LS---------AEELNVFHERGASIAHCPnSNLSLSSGFLNVLEVLKHE-VKIGLGTDVAggysysmldairRAVMVSNI 352
Cdd:PRK06151 281 ISgsprlnysgGDDLALLAEHGVSIVHCP-LVSARHGSALNSFDRYREAgINLALGTDTF------------PPDMVMNM 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 353 ---LLINKVNEKSLT---LKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPKasdspiDLFYGDFFGDISEAVIQ 426
Cdd:PRK06151 348 rvgLILGRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------GLHMGPVFDPIRTLVTG 420
|
410 420
....*....|....*....|..
gi 4758426 427 kflylGDDRNIEEVYVGGKQVV 448
Cdd:PRK06151 421 -----GSGRDVRAVFVDGRVVM 437
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
240-404 |
7.61e-11 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 63.52 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 240 HISENRDEVEAVKNLYpsykNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVL 319
Cdd:PRK07213 198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 320 KHEVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnillinkvnekSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 396
Cdd:PRK07213 274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338
|
....*...
gi 4758426 397 AILINPKA 404
Cdd:PRK07213 339 FTFIKPTN 346
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
75-448 |
2.62e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 61.90 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 75 MPGLVDTHIHasqysFAGSSIDLPLLEWLTKYTfPAEHRFQNIDfaeevytRVVRRTLKNGTTTAcyFATIHTDSSLLLA 154
Cdd:COG1228 64 LPGLIDAHTH-----LGLGGGRAVEFEAGGGIT-PTVDLVNPAD-------KRLRRALAAGVTTV--RDLPGGPLGLRDA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 155 DITDKF----GQRAFVGKVCMDLNDTFPEYketteeSIKETERFVSEMLQKNYSRVKPIVT---PRFSLSCSETLMGElg 227
Cdd:COG1228 129 IIAGESkllpGPRVLAAGPALSLTGGAHAR------GPEEARAALRELLAEGADYIKVFAEggaPDFSLEELRAILEA-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 228 niAKTRDLHIQSHISENRDEVEAVKNlypsykNYTSVydknnlltnktvmAHGCYLSAEELNVFHERGASIAhCPNSNLS 307
Cdd:COG1228 201 --AHALGLPVAAHAHQADDIRLAVEA------GVDSI-------------EHGTYLDDEVADLLAEAGTVVL-VPTLSLF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 308 LSSGFL------------------NVLEVLKHEVKIGLGTDVAGGYS--YSMLDAIRRAVMVSnillinkvneksLTLKE 367
Cdd:COG1228 259 LALLEGaaapvaakarkvreaalaNARRLHDAGVPVALGTDAGVGVPpgRSLHRELALAVEAG------------LTPEE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 368 VFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspidlfyGDFFGDISeaviqkflYLgddRNIEEVYVGGKQV 447
Cdd:COG1228 327 ALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------GDPLEDIA--------YL---EDVRAVMKDGRVV 383
|
.
gi 4758426 448 V 448
Cdd:COG1228 384 D 384
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
235-445 |
4.98e-10 |
|
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: 61.32 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 235 LHIqsHISENRDEVEAVknLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLN 314
Cdd:cd01313 222 VHI--HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 315 VLEVLKHEVKIGLGTDVAGG-----------YSYSMLDAiRRAVMVSnillinkvnEKSLTLKEVFRLATLGGSQALGLD 383
Cdd:cd01313 298 AAALLAAGGRIGIGSDSNARidlleelrqleYSQRLRDR-ARNVLAT---------AGGSSARALLDAALAGGAQALGLA 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758426 384 geIGNFEVGKEFDAILInpkASDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGK 445
Cdd:cd01313 368 --TGALEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
277-448 |
1.52e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.14 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 277 MAHGC---YLSAEELNVFHERGASIAHCPNSNLSLS------------SGFLNVLEVLKHEVKIGLGTDVAGGySYSMLD 341
Cdd:pfam07969 298 IEHAQgvvPYTYSQIERVAALGGAAGVQPVFDPLWGdwlqdrlgaeraRGLTPVKELLNAGVKVALGSDAPVG-PFDPWP 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 342 AIRRAVM-----VSNILLInkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspIDLFygdf 416
Cdd:pfam07969 377 RIGAAVMrqtagGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLD-------DDPL---- 441
|
170 180 190
....*....|....*....|....*....|..
gi 4758426 417 fgDISEAVIqkflylgDDRNIEEVYVGGKQVV 448
Cdd:pfam07969 442 --TVDPPAI-------ADIRVRLTVVDGRVVY 464
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
235-448 |
6.99e-05 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 44.84 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 235 LHIqsHISENRDEVEAVKNLY---PsyknyTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSG 311
Cdd:PRK09229 231 VHI--HIAEQTKEVDDCLAWSgarP-----VEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 312 FLNVLEVLKHEVKIGLGTDvaggySYSMLDAI---------------RRAVMVSNillinkvnEKSLTLKEVFRLATLGG 376
Cdd:PRK09229 304 IFPAVDYLAAGGRFGIGSD-----SHVSIDLVeelrlleygqrlrdrRRNVLAAA--------AQPSVGRRLFDAALAGG 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758426 377 SQALGLDgeIGNFEVGKEFDAILINPkasDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK09229 371 AQALGRA--IGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
277-427 |
1.02e-04 |
|
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: 44.17 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 277 MAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGySY---SMLDAIRRAVmvsnIL 353
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC----RL 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758426 354 LinkvnekSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkaSDSPIDLFYgdFFG-DISEAVIQK 427
Cdd:cd01296 308 M-------RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD---APSYEHLAY--RFGvNLVEYVIKN 370
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
306-401 |
1.80e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 40.35 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758426 306 LSLSSGFLNVLEVLKHEVKIGLGTD-----VAGGYSYSMLdairrAVMVsnillinkvnEKSLTLKEVFRLATLGGSQAL 380
Cdd:cd01299 247 LVLEAGRDALRRAHKAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELL 311
|
90 100
....*....|....*....|.
gi 4758426 381 GLDGEIGNFEVGKEFDAILIN 401
Cdd:cd01299 312 GLSDELGVIEAGKLADLLVVD 332
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
333-393 |
9.75e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 38.03 E-value: 9.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758426 333 GGYSYSMLDAIRravmvsnilliNKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGK 393
Cdd:PRK11170 307 SGSALTMIEAVR-----------NLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGK 356
|
|
| |
