|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
13-470 |
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: 597.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 13 FRGTFVHSTWTCPMEvLRDHLLGVSDSGKIVFLEEASQQEKLAKEW--CFKPCEIRELSHHEFFMPGLVDTHIHASQYSF 90
Cdd:cd01303 1 FRGTFIHTKSLPELE-LVEDALRVVEDGLIVVVDGNIIAAGAAETLkrAAKPGARVIDSPNQFILPGFIDTHIHAPQYAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 91 AGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVtlellmsvlvkktlffhkggnmeckqpsqghvannrqnRRTL 170
Cdd:cd01303 80 IGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFL--------------------------------------DELL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 171 KNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDtfPEYK-ETTEESIKETERFVSEMLQKnYSRVKPIVT 249
Cdd:cd01303 122 RNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAIT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 250 PRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 328
Cdd:cd01303 199 PRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 329 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFR 408
Cdd:cd01303 279 LKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFY 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462627304 409 LATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLfygDFFGDISEAVIQKFLYLG 470
Cdd:cd01303 359 LATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLG 417
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
26-470 |
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: 532.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 26 MEVLRDHLLGVSDsGKIVFLEEASQQeklaKEWCFKPCEIRELSHHeFFMPGLVDTHIHASQYSFAGSsIDLPLLEWLTK 105
Cdd:TIGR02967 1 LEYFEDGLLVVEN-GRIVAVGDYAEL----KETLPAGVEIDDYRGH-LIMPGFIDTHIHYPQTEMIAS-YGEQLLEWLEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 106 YTFPAEHRFQNIDFAEEVYTRVVtlellmsvlvkktlffhkggnmeckqpsqghvannrqnRRTLKNGTTTACYFATIHT 185
Cdd:TIGR02967 74 YTFPTEARFADPDHAEEVAEFFL--------------------------------------DELLRNGTTTALVFATVHP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 186 DSSLLLADITDKFGQRAFVGKVCMDLNdtFPEY-KETTEESIKETERFVSEMLQKNysRVKPIVTPRFSLSCSETLMGEL 264
Cdd:TIGR02967 116 ESVDALFEAALKRGMRMIAGKVLMDRN--APDYlRDTAESSYDESKALIERWHGKG--RLLYAVTPRFAPTSSPEQLAAA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 265 GNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSN 343
Cdd:TIGR02967 192 GELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 344 LSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvnEKSLTLKEVFRLATLGGSQALGLDGE 423
Cdd:TIGR02967 272 LFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQ------GARLSPFEAFYLATLGGARALDLDDR 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2462627304 424 IGNFEVGKEFDAILINPKASDSPIDLFYGdffGDISEAVIQKFLYLG 470
Cdd:TIGR02967 346 IGNFEPGKEADFVVLDPAATPLLALRFEG---ADTLEDKLFKLMYLG 389
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-442 |
1.05e-105 |
|
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: 321.39 E-value: 1.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 16 TFVHSTWTCPM----EVLRDHLLGVSDsGKIVFLEEASQQEKLakewcFKPCEIRELSHHeFFMPGLVDTHIHASQYSFA 91
Cdd:COG0402 2 LLIRGAWVLTMdpagGVLEDGAVLVED-GRIAAVGPGAELPAR-----YPAAEVIDAGGK-LVLPGLVNTHTHLPQTLLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 92 GSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkggnmeckqpsqghvannrqnrrt 169
Cdd:COG0402 75 GLADDLPLLDWLEEYIWPLEARLD----PEDVYagALLALAEML------------------------------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 170 lKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNdtFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIV 248
Cdd:COG0402 115 -RSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGLMDRG--FPDgLREDADEGLADSERLIERWHGAADGRIRVAL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 249 TPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 328
Cdd:COG0402 192 APHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIAL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 329 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGG-YSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVF 407
Cdd:COG0402 270 LAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASnNSLDMFEEMRLAALLQRLR---GGDPTALSAREAL 346
|
410 420 430
....*....|....*....|....*....|....*
gi 2462627304 408 RLATLGGSQALGLDGEIGNFEVGKEFDAILINPKA 442
Cdd:COG0402 347 EMATLGGARALGLDDEIGSLEPGKRADLVVLDLDA 381
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
11-442 |
1.16e-91 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 285.93 E-value: 1.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 11 HIFRGTFVHST---WTCP----MEVLRDHLLGVSDsGKIVFLEEASQ-QEKLAKEwcfkpCEIRELSHHeFFMPGLVDTH 82
Cdd:PRK09228 4 KAYRGRLLHFTadpAEVDdedaLRYIEDGLLLVED-GRIVAAGPYAElRAQLPAD-----AEVTDYRGK-LILPGFIDTH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 83 IHASQYSFAGSsidlP---LLEWLTKYTFPAEHRFQNIDFAEEVYTRVVTlELLmsvlvkktlffhkggnmeckqpsqgh 159
Cdd:PRK09228 77 IHYPQTDMIAS----YgeqLLDWLNTYTFPEERRFADPAYAREVAEFFLD-ELL-------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 160 vannrqnrrtlKNGTTTACYFATIHTDSsllladiTDKF-------GQRAFVGKVCMDLNdtFPEY-KETTEESIKETER 231
Cdd:PRK09228 126 -----------RNGTTTALVFGTVHPQS-------VDALfeaaearNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 232 fvseMLQK--NYSRVKPIVTPRFSLSCSETLMGELGNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNL 308
Cdd:PRK09228 186 ----LIERwhGKGRLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 309 LTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVS 388
Cdd:PRK09228 262 LGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462627304 389 nillinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKA 442
Cdd:PRK09228 342 ------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDPAA 389
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
23-442 |
7.58e-66 |
|
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: 218.23 E-value: 7.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 23 TCPMEVLRDHLLGVSDsGKIVFLEEASQQEKLAKEwcfkpcEIRELSHHeFFMPGLVDTHIHASQYSFAGSSIDLPLLEW 102
Cdd:cd01298 11 TDPRRVLEDGDVLVED-GRIVAVGPALPLPAYPAD------EVIDAKGK-VVMPGLVNTHTHLAMTLLRGLADDLPLMEW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 103 LTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkggnmeckqpsqghvannrqnrrtlKNGTTTAC-- 178
Cdd:cd01298 83 LKDLIWPLERLLT----EEDVYlgALLALAEMI-------------------------------------RSGTTTFAdm 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 179 YFatIHTDSsllLADITDKFGQRAFVGKVCMDLNDtfpEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSE 258
Cdd:cd01298 122 YF--FYPDA---VAEAAEELGIRAVLGRGIMDLGT---EDVEETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 259 TLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASI 336
Cdd:cd01298 194 ELLREVAELAREYGVPLHIHLAETEDEVEESLEKY----GKRPVeYlEELGLLGPDVVLAHCVWLTDEEIELLAETGTGV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 337 AHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAvmvsniLLINKV---NEKSLTLKEVFRLATL 412
Cdd:cd01298 270 AHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATI 343
|
410 420 430
....*....|....*....|....*....|
gi 2462627304 413 GGSQALGLDgEIGNFEVGKEFDAILINPKA 442
Cdd:cd01298 344 GGAKALGLD-EIGSLEVGKKADLILIDLDG 372
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
75-439 |
1.43e-57 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 197.14 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 75 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAE--HRfqnidfAEEVYTrvvtlellmSVLVkktlffhkgGNMEC 152
Cdd:PRK07228 55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEaaHD------AESMYY---------SALL---------GIGEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 153 kqpsqghvannrqnrrtLKNGTTTACYFATI-HTDSSL-LLADItdkfGQRAFVGKVCMDLNDTFPE-YKETTEESIKET 229
Cdd:PRK07228 111 -----------------IESGTTTIVDMESVhHTDSAFeAAGES----GIRAVLGKVMMDYGDDVPEgLQEDTEASLAES 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 230 ERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNlYPSYKNYTsVYDKNNLL 309
Cdd:PRK07228 170 VRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 310 TNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDA---IRRAVm 386
Cdd:PRK07228 248 GEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA- 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462627304 387 vsnilLINKVNE---KSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILIN 439
Cdd:PRK07228 325 -----LIQKVDRlgpTAMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILD 375
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
75-441 |
2.54e-47 |
|
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: 166.91 E-value: 2.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 75 MPGLVDTHIHASQYSFAGSSIDLpllewltkytfpaehrfqniDFAEEVYTRVVTlellmsvlvkktlffhkggnmeckq 154
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGIT------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 155 psqghvannrqnrRTLKNGTTTACYFATIHTDSSLLLADITDK--FGQRAFVGKVCMDLNDTFPEYKETTEESIKETErf 232
Cdd:pfam01979 38 -------------TMLKSGTTTVLDMGATTSTGIEALLEAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE-- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 233 vsEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPS---YKNYTSVYDKNNLL 309
Cdd:pfam01979 103 --FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 310 -TNKTVMAHGCYLSAEELNVFHER--GASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAG-GYSYSMLDAIRRAV 385
Cdd:pfam01979 181 dIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462627304 386 mvsnilLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPK 441
Cdd:pfam01979 261 ------ELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD 310
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
16-439 |
1.93e-45 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 164.70 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 16 TFVHSTWTCPME----VLRDHLLGVSDsGKIVFLeeASQQEKLAKewcFKPCEIRELSHHeFFMPGLVDTHIHASQYSFA 91
Cdd:PRK09045 9 LLIEARWIVPVEpagvVLEDHAVAIRD-GRIVAI--LPRAEARAR---YAAAETVELPDH-VLIPGLINAHTHAAMSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 92 GSSIDLPLLEWLTKYTFPAEHRFQNIDFaeeVY--TRVVTLELLmsvlvkktlffhkggnmeckqpsqghvannrqnrrt 169
Cdd:PRK09045 82 GLADDLPLMTWLQDHIWPAEGAWVSEEF---VRdgTLLAIAEML------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 170 lKNGTTTA--CYFatiHTDSsllLADITDKFGQRAFVGKVCMDlndtFP-EYKETTEESI----KETERFvsemlqKNYS 242
Cdd:PRK09045 123 -RGGTTCFndMYF---FPEA---AAEAAHQAGMRAQIGMPVLD----FPtAWASDADEYLakglELHDQW------RHHP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 243 RVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAvknlypSYKNY----TSVYDKNNLLTNKTVMAHG 318
Cdd:PRK09045 186 LISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIAD------SLKQHgqrpLARLARLGLLGPRLIAVHM 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 319 CYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSnillinKV- 396
Cdd:PRK09045 260 TQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLA------KAv 333
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2462627304 397 --NEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILIN 439
Cdd:PRK09045 334 agDATALPAHTALRMATLNGARALGLDDEIGSLEPGKQADLVAVD 378
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
71-439 |
1.11e-42 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 156.88 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 71 HEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNidfaEEVY--TRVVTLELLmsvlvkktlffhkgg 148
Cdd:PRK08393 49 GSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKR----KDIYwgAYLGLLEMI--------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 149 nmeckqpsqghvannrqnrrtlKNGTTT--ACYFatiHTDSsllLADITDKFGQRAFVGKVCMDLNDtfpeyKETTEESI 226
Cdd:PRK08393 110 ----------------------KSGTTTfvDMYF---HMEE---VAKATLEVGLRGYLSYGMVDLGD-----EEKREKEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 227 KETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKN 306
Cdd:PRK08393 157 KETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYG--KSPVVLLDEI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 307 NLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDAIRRAVM 386
Cdd:PRK08393 235 GFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTD--GAASNNNLDMLREMKL 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462627304 387 VSnilLINKVNEKSLTL---KEVFRLATLGGSQALGLDGeiGNFEVGKEFDAILIN 439
Cdd:PRK08393 313 AA---LLHKVHNLDPTIadaETVFRMATQNGAKALGLKA--GVIKEGYLADIAVID 363
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
70-441 |
1.02e-40 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 151.44 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 70 HHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkg 147
Cdd:PRK06038 49 KGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYagSLLACLEMI-------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 148 gnmeckqpsqghvannrqnrrtlKNGTTTacyFAT--IHTDSSlllADITDKFGQRAFVGKVCMDLNDTfpeykETTEES 225
Cdd:PRK06038 111 -----------------------KSGTTS---FADmyFYMDEV---AKAVEESGLRAALSYGMIDLGDD-----EKGEAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 226 IKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSVY-- 303
Cdd:PRK06038 157 LKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQY----GMCSVNyl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 304 DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIR 382
Cdd:PRK06038 233 DDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMK 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462627304 383 RAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALGLdgEIGNFEVGKEFDAILINPK 441
Cdd:PRK06038 313 TAALLHK---VNTMDPTALPARQVLEMATVNGAKALGI--NTGMLKEGYLADIIIVDMN 366
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
23-441 |
2.42e-35 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 136.67 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 23 TC--PMEVLRDHLLGVSDSgKIV--------FLEEASQQEKLAKEWcfkpceirelshhefFMPGLVDTHIHASQYSFAG 92
Cdd:PRK06687 11 TCdqDFHVYLDGILAVKDS-QIVyvgqdkpaFLEQAEQIIDYQGAW---------------IMPGLVNCHTHSAMTGLRG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 93 SSIDLPLLEWLTKYTFPAEHrfqniDFAEEVYTRVVTLELLMSVLVKKTLFfhkggnMECKQPSQGHVANNRQNRRTLKn 172
Cdd:PRK06687 75 IRDDSNLHEWLNDYIWPAES-----EFTPDMTTNAVKEALTEMLQSGTTTF------NDMYNPNGVDIQQIYQVVKTSK- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 173 gttTACYFATIhtdssllladitdkfgqrafvgkvcmdlndTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRF 252
Cdd:PRK06687 143 ---MRCYFSPT------------------------------LFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 253 SLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHER 332
Cdd:PRK06687 190 PYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYG--KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 333 GASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillINKVNEKSLTLKEVFRLAT 411
Cdd:PRK06687 268 QVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDsVASNNNLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLT 344
|
410 420 430
....*....|....*....|....*....|
gi 2462627304 412 LGGSQALGLDGEIGNFEVGKEFDAILINPK 441
Cdd:PRK06687 345 IEGAKALGMENQIGSLEVGKQADFLVIQPQ 374
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
72-463 |
7.25e-28 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 115.54 E-value: 7.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 72 EFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFqnidfAEEVYTRVVTLELLMSVlvkktlffhkggnme 151
Cdd:PRK15493 55 KWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQF-----TPELAVASTELGLLEMV--------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 152 ckqpsqghvannrqnrrtlKNGTTT-ACYFATIHTDSSLLLADITDKfGQRAFVGKVCMDLNDtfpeyKETTEESIKETE 230
Cdd:PRK15493 115 -------------------KSGTTSfSDMFNPIGVDQDAIMETVSRS-GMRAAVSRTLFSFGT-----KEDEKKAIEEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 231 RFVSEMLQKNySRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLT 310
Cdd:PRK15493 170 KYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 311 NKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSN 389
Cdd:PRK15493 247 RPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 390 ILlinKVNEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINP--KASDSPID-----LFYGDFFGDISEAV 462
Cdd:PRK15493 327 GI---HQDATALPVETALTLATKGAAEVIGMK-QTGSLEVGKCADFITIDPsnKPHLQPADevlshLVYAASGKDISDVI 402
|
.
gi 2462627304 463 I 463
Cdd:PRK15493 403 I 403
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
220-434 |
4.68e-21 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 95.69 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 220 ETTEESIKETERFVSEMLQKN-YSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykN 298
Cdd:PRK08203 174 EDEDAILADSQRLIDRYHDPGpGAMLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERF----G 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 299 YTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSY 375
Cdd:PRK08203 250 MRPVdYlEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGS 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462627304 376 SMLDAIRRAvmvsniLLINKV--NEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 434
Cdd:PRK08203 330 NLIGEARQA------LLLQRLryGPDAMTAREALEWATLGGARVLGRD-DIGSLAPGKLAD 383
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
75-442 |
1.05e-20 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 94.18 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 75 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKyTFPAEHRFQNidfaEEVYtrvvtlellmsvlvkktlffhKGGNMECKQ 154
Cdd:PRK06380 53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TFKYDSKRTR----EGIY---------------------NSAKLGMYE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 155 psqghvannrqnrrTLKNGTTTacyFATIHTDSSLLlADITDKFGQRAFVGKVCMDlndtfPEYKETTEESIKETERFVS 234
Cdd:PRK06380 107 --------------MINSGITA---FVDLYYSEDII-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 235 EMLQKNYsrVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVeavknlYPSYKNY----TSVYDKNNLLT 310
Cdd:PRK06380 164 EHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEV------YDHVKRTgerpVEHLEKIGFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 311 NKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSS-GFLNVLEVLKHEVKIGLGTDVAGgySYSMLDAIrRAVMVSN 389
Cdd:PRK06380 236 SKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEMLDNGINVTIGTDSNG--SNNSLDMF-EAMKFSA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2462627304 390 ILLINKVNEKSLT-LKEVFRLATLGGSQALGLDGeiGNFEVGKEFDAILINPKA 442
Cdd:PRK06380 313 LSVKNERWDASIIkAQEILDFATINAAKALELNA--GSIEVGKLADLVILDARA 364
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
76-437 |
1.48e-19 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 90.90 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 76 PGLVDTHIHASQYSFAG--SSIDLPLLEWL--TKYTFPA---EHRFQnidfaeeVYTRVVTLELLMSvlvkktlffhkgg 148
Cdd:PRK12393 59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLaaVPYRFRArfdEDLFR-------LAARIGLVELLRS------------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 149 nmeckqpsqghvannrqnrrtlknGTTTAC-----YFATIHTDSSLLLADITDKFGQRaFV---GKVCMDLNDTfPEYK- 219
Cdd:PRK12393 119 ------------------------GCTTVAdhhylYHPGMPFDTGDILFDEAEALGMR-FVlcrGGATQTRGDH-PGLPt 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 220 ----ETTEESIKETERFVSEMLQKNYSRVKPIV----TPRFSLScsETLMGELGNIAKTRDLHIQSHISENRDEVEAVKN 291
Cdd:PRK12393 173 alrpETLDQMLADVERLVSRYHDASPDSLRRVVvaptTPTFSLP--PELLREVARAARGMGLRLHSHLSETVDYVDFCRE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 292 LYpsykNYTSVY--DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD- 368
Cdd:PRK12393 251 KY----GMTPVQfvAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDg 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462627304 369 VAGGYSYSMLDAIRRAVMVSNILlinkVNEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAIL 437
Cdd:PRK12393 327 AASNESADMLSEAHAAWLLHRAE----GGADATTVEDVVHWGTAGGARVLGLD-AIGTLAVGQAADLAI 390
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
266-439 |
2.26e-17 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 83.87 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 266 NIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNY--------TSVYDKNNLL----TNKTVMAHGCYLSAEELNVFHERG 333
Cdd:PRK08418 197 QLAKKENLLVSTHFLESKAEREWLEESKGWFKKFfekflkepKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 334 ASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillinkvNEKSLTL-KEVFRLAT 411
Cdd:PRK08418 277 ASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSAT 349
|
170 180
....*....|....*....|....*....
gi 2462627304 412 LGGSQALGLD-GEIgnfEVGKEFDAILIN 439
Cdd:PRK08418 350 RYGAKALGLNnGEI---KEGKDADLSVFE 375
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
167-434 |
3.43e-17 |
|
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: 83.27 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 167 RRTLKNGTTTAcyfATIHTDSSLLLADITDKFGQRAFVGKVCMDlNDTFPEYKETTEESIKETERFVSemlqknySRVKP 246
Cdd:cd01312 82 RQMLESGTTSI---GAISSDGSLLPALASSGLRGVFFNEVIGSN-PSAIDFKGETFLERFKRSKSFES-------QLFIP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 247 IVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAV-------KNLYPSY---KNYTSVYDKNNL------LT 310
Cdd:cd01312 151 AISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLeeskgwfKHFWESFlklPKPKKLATAIDFldmlggLG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 311 NKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRravmvSN 389
Cdd:cd01312 231 TRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLLDELR-----AL 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2462627304 390 ILLINKVNEKSLTlKEVFRLATLGGSQALGLdgEIGNFEVGKEFD 434
Cdd:cd01312 306 LDLHPEEDLLELA-SELLLMATLGGARALGL--NNGEIEAGKRAD 347
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
247-442 |
1.07e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 82.36 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 247 IVTPRFSlsCSETLMGELGnIAKTRDLHIQSHISenrdeveavknLYPSYKNYTSV--YDKNNLLTNKTVMAHGCYLSAE 324
Cdd:PRK08204 192 IRGPEFS--SWEVARADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDD 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 325 ELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNILLINKV-- 396
Cdd:PRK08204 258 ELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMpp 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462627304 397 NEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKA 442
Cdd:PRK08204 338 PRLTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATD 383
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
75-391 |
1.84e-16 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 81.52 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 75 MPGLVDTHIHAsqYS-FA-GSSIDLP----LLEWLTKYTFpaehrfqNIDfaeevytRVVTLE-LLMSVLVkkTLffhkg 147
Cdd:PRK07203 58 MPGLINSHNHI--YSgLArGMMANIPpppdFISILKNLWW-------RLD-------RALTLEdVYYSALI--CS----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 148 gnMECkqpsqghvannrqnrrtLKNGTTT-----ACYFATihTDSSLLLADITDKFGQRafvGKVCMDLNDTFPEykETT 222
Cdd:PRK07203 115 --LEA-----------------IKNGVTTvfdhhASPNYI--GGSLFTIADAAKKVGLR---AMLCYETSDRDGE--KEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 223 EESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCS-ETL------MGELGniaktRDLHIqsHISENRDEVEAVKNLYps 295
Cdd:PRK07203 169 QEGVEENIRFIKHIDEAKDDMVEAMFGLHASFTLSdATLekcreaVKETG-----RGYHI--HVAEGIYDVSDSHKKY-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 296 YKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvagGYSY 375
Cdd:PRK07203 240 GKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTS 316
|
330
....*....|....*.
gi 2462627304 376 SMLDAIRravmVSNIL 391
Cdd:PRK07203 317 DMFESYK----VANFK 328
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
167-417 |
1.42e-14 |
|
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: 73.91 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 167 RRTLKNGTTTAC-----YFATIHTDSSLLLAD-ITDKFGQRAFVGKVCMDLNdtfPEYKETTEESIKETERFVsemlqkn 240
Cdd:cd01292 42 EALLAGGVTTVVdmgstPPPTTTKAAIEAVAEaARASAGIRVVLGLGIPGVP---AAVDEDAEALLLELLRRG------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 241 YSRVKPIVTPRFSLSCSETLMGELGNI---AKTRDLHIQSHISENRDEVEAVKNLYpsyknytsvydKNNLLTNKTVMAH 317
Cdd:cd01292 112 LELGAVGLKLAGPYTATGLSDESLRRVleeARKLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 318 GCYLSAEELNVFHERGASIAHCPNSNLSLSS---GFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLin 394
Cdd:cd01292 181 VSHLDPELLELLKEAGVSLEVCPLSNYLLGRdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG-- 258
|
250 260
....*....|....*....|...
gi 2462627304 395 kvneksLTLKEVFRLATLGGSQA 417
Cdd:cd01292 259 ------LSLEEALRLATINPARA 275
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
226-463 |
7.10e-12 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 67.37 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 226 IKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTS--VY 303
Cdd:PRK06151 188 LEEAIAFIKRVDGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLH----GTTPleWL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 304 DKNNLLTNKTVMAHGCYLS---------AEELNVFHERGASIAHCPnSNLSLSSGFLNVLEVLKHE-VKIGLGTDVAggy 373
Cdd:PRK06151 264 ADVGLLGPRLLIPHATYISgsprlnysgGDDLALLAEHGVSIVHCP-LVSARHGSALNSFDRYREAgINLALGTDTF--- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 374 sysmldairRAVMVSNI---LLINKVNEKSLT---LKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPKasdspi 447
Cdd:PRK06151 340 ---------PPDMVMNMrvgLILGRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------ 403
|
250 260
....*....|....*....|....*..
gi 2462627304 448 DLFYGDFF-----------GDISEAVI 463
Cdd:PRK06151 404 GLHMGPVFdpirtlvtggsGRDVRAVF 430
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
267-415 |
3.85e-11 |
|
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: 63.57 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 267 IAKTRDLHIQSHISENRD-----EVEAVKNLYPsyknytsvydknNLLTnktvmaHGCYLSAEELNVFHERGASIAHCPN 341
Cdd:cd01305 133 LLRRRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPR 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462627304 342 SNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvneKSLTLKEVFRLATLGGS 415
Cdd:cd01305 195 SNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ-------GYLSPLEILRMATVNAA 261
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
278-442 |
6.97e-11 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 63.90 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 278 HISENRDEVEAVKNLYpsykNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVL 357
Cdd:PRK07213 198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 358 KHEVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnillinkvnekSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 434
Cdd:PRK07213 274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338
|
....*...
gi 2462627304 435 AILINPKA 442
Cdd:PRK07213 339 FTFIKPTN 346
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
273-446 |
7.32e-07 |
|
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: 51.30 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 273 LHIqsHISENRDEVEAVknLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLN 352
Cdd:cd01313 222 VHI--HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 353 VLEVLKHEVKIGLGTDVAGG-----------YSYSMLDAiRRAVMVSnillinkvnEKSLTLKEVFRLATLGGSQALGLD 421
Cdd:cd01313 298 AAALLAAGGRIGIGSDSNARidlleelrqleYSQRLRDR-ARNVLAT---------AGGSSARALLDAALAGGAQALGLA 367
|
170 180
....*....|....*....|....*
gi 2462627304 422 geIGNFEVGKEFDAILInpkASDSP 446
Cdd:cd01313 368 --TGALEAGARADLLSL---DLDHP 387
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
313-439 |
5.77e-06 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 48.42 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 313 TVMAHGCYLSAEELNVFHERGASIAhCPNSNLSLSSGFL------------------NVLEVLKHEVKIGLGTDVAGGYS 374
Cdd:COG1228 227 DSIEHGTYLDDEVADLLAEAGTVVL-VPTLSLFLALLEGaaapvaakarkvreaalaNARRLHDAGVPVALGTDAGVGVP 305
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462627304 375 --YSMLDAIRRAVMVSnillinkvneksLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILIN 439
Cdd:COG1228 306 pgRSLHRELALAVEAG------------LTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLD 360
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
315-465 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 315 MAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGySY---SMLDAIRRAVmvsnIL 391
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC----RL 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462627304 392 LinkvnekSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkaSDSPIDLFYgdFFG-DISEAVIQK 465
Cdd:cd01296 308 M-------RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD---APSYEHLAY--RFGvNLVEYVIKN 370
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
315-446 |
1.98e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 43.67 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 315 MAHGC---YLSAEELNVFHERGASIAHCPNSNLSLS------------SGFLNVLEVLKHEVKIGLGTDVAGGySYSMLD 379
Cdd:pfam07969 298 IEHAQgvvPYTYSQIERVAALGGAAGVQPVFDPLWGdwlqdrlgaeraRGLTPVKELLNAGVKVALGSDAPVG-PFDPWP 376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462627304 380 AIRRAVM-----VSNILLInkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSP 446
Cdd:pfam07969 377 RIGAAVMrqtagGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVD 444
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
344-439 |
2.05e-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: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462627304 344 LSLSSGFLNVLEVLKHEVKIGLGTD-----VAGGYSYSMLdairrAVMVsnillinkvnEKSLTLKEVFRLATLGGSQAL 418
Cdd:cd01299 247 LVLEAGRDALRRAHKAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELL 311
|
90 100
....*....|....*....|.
gi 2462627304 419 GLDGEIGNFEVGKEFDAILIN 439
Cdd:cd01299 312 GLSDELGVIEAGKLADLLVVD 332
|
|
| |
