|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
5-415 |
1.47e-171 |
|
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: 487.17 E-value: 1.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 5 LKGNIIFTKTSETFTVFENSYIILEKGK--VKGIFKEIPKEYKNLK--------VVDYTDKLIIPGMNDLHAHASQFKNL 74
Cdd:cd01303 1 FRGTFIHTKSLPELELVEDALRVVEDGLivVVDGNIIAAGAAETLKraakpgarVIDSPNQFILPGFIDTHIHAPQYANI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 75 GMAMDKELLPWLETYTFPEESNYKDIEYATKMYKKFVKELWKSGTTRIAVFATVHKEASMKLMDIFKEVGLGAYVGKVNM 154
Cdd:cd01303 81 GSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 155 NMNCPDTLLENTQDSIADTEEIINKYSDTDSIVKPIITPRFIPSCTSELLKGLGDLCLKYN-IPIQSHLSENYDEIEWVR 233
Cdd:cd01303 161 DRNAPEYYRDTAESSYRDTKRLIERWHGKSGRVKPAITPRFAPSCSEELLAALGKLAKEHPdLHIQTHISENLDEIAWVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 234 NLEPESKFYGDAYNRYNLFGqTPTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSDI 313
Cdd:cd01303 241 ELFPGARDYLDVYDKYGLLT-EKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 314 SGGHTLSIFKAMVSAIQLSKLYWVNSGKKyNFLSLSEAFYIATKSGGSFFG---KVGSFEEGYDFDALIIDDSNLNH--- 387
Cdd:cd01303 320 GGGTSFSMLDTLRQAYKVSRLLGYELGGH-AKLSPAEAFYLATLGGAEALGlddKIGNFEVGKEFDAVVIDPSATPLlad 398
|
410 420 430
....*....|....*....|....*....|.
gi 489525352 388 ---DNYSILERLERFIYVGDDRNIIHRYVCG 415
Cdd:cd01303 399 rmfRVESLEEALFKFLYLGDDRNIREVYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
20-415 |
9.89e-129 |
|
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: 376.98 E-value: 9.89e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 20 VFENSYIILEKGKVKGI--FKEI-PKEYKNLKVVDYTDKLIIPGMNDLHAHASQFKNLGmAMDKELLPWLETYTFPEESN 96
Cdd:TIGR02967 3 YFEDGLLVVENGRIVAVgdYAELkETLPAGVEIDDYRGHLIMPGFIDTHIHYPQTEMIA-SYGEQLLEWLEKYTFPTEAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 97 YKDIEYATKMYKKFVKELWKSGTTRIAVFATVHKEASMKLMDIFKEVGLGAYVGKVNMNMNCPDTLLENTQDSIADTEEI 176
Cdd:TIGR02967 82 FADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDRNAPDYLRDTAESSYDESKAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 177 INKYSDTDSiVKPIITPRFIPSCTSELLKGLGDLCLKY-NIPIQSHLSENYDEIEWVRNLEPESKFYGDAYNRYNLFGQT 255
Cdd:TIGR02967 162 IERWHGKGR-LLYAVTPRFAPTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 256 pTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSDISGGHTLSIFKAMVSAIQLSKLy 335
Cdd:TIGR02967 241 -SVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQL- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 336 wvnSGKKynfLSLSEAFYIATKSGG---SFFGKVGSFEEGYDFDALIID--DSNLNHDNY----SILERLERFIYVGDDR 406
Cdd:TIGR02967 319 ---QGAR---LSPFEAFYLATLGGAralDLDDRIGNFEPGKEADFVVLDpaATPLLALRFegadTLEDKLFKLMYLGDDR 392
|
....*....
gi 489525352 407 NIIHRYVCG 415
Cdd:TIGR02967 393 NVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-418 |
2.06e-121 |
|
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: 358.76 E-value: 2.06e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 4 VLKGNIIFTkTSETFTVFENSYIILEKGKVKGI--FKEIPKEYKNLKVVDYTDKLIIPGMNDLHAHASQFKNLGMAMDKE 81
Cdd:COG0402 3 LIRGAWVLT-MDPAGGVLEDGAVLVEDGRIAAVgpGAELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLADDLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 82 LLPWLETYTFPEESNYkDIEYATKMYKKFVKELWKSGTTRIAVFATVHKEASMKLMDIFKEVGLGAYVGKVNMNMNCPDT 161
Cdd:COG0402 82 LLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGLMDRGFPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 162 LLENTQDSIADTEEIINKYSDT-DSIVKPIITPRFIPSCTSELLKGLGDLCLKYNIPIQSHLSENYDEIEWVRNLEPESk 240
Cdd:COG0402 161 LREDADEGLADSERLIERWHGAaDGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYGKR- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 241 fYGDAYNRYNLFGQtPTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSDISGGHT-L 319
Cdd:COG0402 240 -PVEYLDELGLLGP-RTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASNNsL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 320 SIFKAMVSAIQLSKLywvnSGKKYNFLSLSEAFYIATKSGGSFFG---KVGSFEEGYDFDALIIDDSNLNHdnYSILERL 396
Cdd:COG0402 318 DMFEEMRLAALLQRL----RGGDPTALSAREALEMATLGGARALGlddEIGSLEPGKRADLVVLDLDAPHL--APLHDPL 391
|
410 420
....*....|....*....|..
gi 489525352 397 ERFIYVGDDRNIIHRYVCGKLI 418
Cdd:COG0402 392 SALVYAADGRDVRTVWVAGRVV 413
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
21-417 |
5.73e-96 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 294.41 E-value: 5.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 21 FENSYIILEKGKVK--GIFKEIPKEY-KNLKVVDYTDKLIIPGMNDLHAHASQFKNLGmAMDKELLPWLETYTFPEESNY 97
Cdd:PRK09228 29 IEDGLLLVEDGRIVaaGPYAELRAQLpADAEVTDYRGKLILPGFIDTHIHYPQTDMIA-SYGEQLLDWLNTYTFPEERRF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 98 KDIEYATKMYKKFVKELWKSGTTRIAVFATVHKEAsmklMDIF----KEVGLGAYVGKVNMNMNCPDTLLENTQDSIADT 173
Cdd:PRK09228 108 ADPAYAREVAEFFLDELLRNGTTTALVFGTVHPQS----VDALfeaaEARNMRMIAGKVLMDRNAPDGLRDTAESGYDDS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 174 EEIINKYSDTD--SIVkpiITPRFIPSCTSELLKGLGDLCLKYniP---IQSHLSENYDEIEWVRNLEPESKFYGDAYNR 248
Cdd:PRK09228 184 KALIERWHGKGrlLYA---ITPRFAPTSTPEQLEAAGALAREH--PdvwIQTHLSENLDEIAWVKELFPEARDYLDVYER 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 249 YNLFGQTpTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSDISGGHTLSIFKAMVSA 328
Cdd:PRK09228 259 YGLLGPR-AVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 329 IQLSKLywvnSGKKynfLSLSEAFYIATKSGG---SFFGKVGSFEEGYDFDALIID-------DSNLNHDNySILERLER 398
Cdd:PRK09228 338 YKVQQL----QGYR---LSPFQAFYLATLGGAralGLDDRIGNLAPGKEADFVVLDpaatpllALRTARAE-SLEELLFA 409
|
410
....*....|....*....
gi 489525352 399 FIYVGDDRNIIHRYVCGKL 417
Cdd:PRK09228 410 LMTLGDDRAVAETYVAGRP 428
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
19-391 |
1.63e-62 |
|
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: 207.05 E-value: 1.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 19 TVFENSYIILEKGKVKGIFKEIP-KEYKNLKVVDYTDKLIIPGMNDLHAHASQ--FKNLgmAMDKELLPWLETYTFPEES 95
Cdd:cd01298 15 RVLEDGDVLVEDGRIVAVGPALPlPAYPADEVIDAKGKVVMPGLVNTHTHLAMtlLRGL--ADDLPLMEWLKDLIWPLER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 96 NY--KDIEYATKMYkkfVKELWKSGTTRIAVFATVHKEAsmkLMDIFKEVGLGAYVGKVNMNmnCPDTLLENTQDSIADT 173
Cdd:cd01298 93 LLteEDVYLGALLA---LAEMIRSGTTTFADMYFFYPDA---VAEAAEELGIRAVLGRGIMD--LGTEDVEETEEALAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 174 EEIINKYSDT-DSIVKPIITPRFIPSCTSELLKGLGDLCLKYNIPIQSHLSENYDEIEWVRnlepesKFYG----DAYNR 248
Cdd:cd01298 165 ERLIREWHGAaDGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESL------EKYGkrpvEYLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 249 YNLFGqTPTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSD-ISGGHTLSIFKAMVS 327
Cdd:cd01298 239 LGLLG-PDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRL 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 328 AIQLSKLYwvnsGKKYNFLSLSEAFYIATKSGGSFFG--KVGSFEEGYDFDALIIDDSNLN----HDNYS 391
Cdd:cd01298 318 AALLQKLA----HGDPTALPAEEALEMATIGGAKALGldEIGSLEVGKKADLILIDLDGPHllpvHDPIS 383
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
48-381 |
1.20e-52 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 182.12 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 48 KVVDYTDKLIIPGMNDLHAHASQFKNLGMAMDKELLPWLETYTFP------EESNYkdieYATKMYkkfVKELWKSGTTR 121
Cdd:PRK07228 45 DHIDATGKVVIPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPleaahdAESMY----YSALLG---IGELIESGTTT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 122 IAVFATV-HKEASMKLMdifKEVGLGAYVGKVNMNM--NCPDTLLENTQDSIADTEEIINKYSDT-DSIVKPIITPRFIP 197
Cdd:PRK07228 118 IVDMESVhHTDSAFEAA---GESGIRAVLGKVMMDYgdDVPEGLQEDTEASLAESVRLLEKWHGAdNGRIRYAFTPRFAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 198 SCTSELLKGLGDLCLKYNIPIQSHLSENYDEIEWV------RNLEpeskfYGDaynRYNLFGQTPTLmAHCVHCSQDEID 271
Cdd:PRK07228 195 SCTEELLRGVRDLADEYGVRIHTHASENRGEIETVeeetgmRNIH-----YLD---EVGLTGEDLIL-AHCVWLDEEERE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 272 LMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSDisG---GHTLSIFKAMVSAIQLSKLYWVNSgkkyNFLSL 348
Cdd:PRK07228 266 ILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGAD--GapcNNTLDPFTEMRQAALIQKVDRLGP----TAMPA 339
|
330 340 350
....*....|....*....|....*....|....*.
gi 489525352 349 SEAFYIATKSGGSFFG---KVGSFEEGYDFDALIID 381
Cdd:PRK07228 340 RTVFEMATLGGAKAAGfedEIGSLEEGKKADLAILD 375
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
56-418 |
8.05e-43 |
|
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: 153.04 E-value: 8.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 56 LIIPGMNDLHAHASQFKNLGMAMDKELLPWletytfpeesnykdieyatkMYKKFVKELWKSGTTRIAVFATVHKEASMK 135
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYE--------------------ALRLGITTMLKSGTTTVLDMGATTSTGIEA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 136 LMDIFKE--VGLGAYVGKVNMNMNCPDTLLENTQDSIADTEEIINKYSDtdSIVKPIITPRFIPSCTSELLKGLGDLCLK 213
Cdd:pfam01979 61 LLEAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMAD--GVVFVGLAPHGAPTFSDDELKAALEEAKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 214 YNIPIQSHLSENYDEIEWVRNLEP---ESKFYGDAYNRYNLFGQTPTLMAHCVHCSQDEIDLMRE--NNVMAVHCPASNF 288
Cdd:pfam01979 139 YGLPVAIHALETKGEVEDAIAAFGggiEHGTHLEVAESGGLLDIIKLILAHGVHLSPTEANLLAEhlKGAGVAHCPFSNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 289 NVGSGAMPIRKLIDNNIRLALGSD-ISGGHTLSIFKAMVSAIQLSklywvnSGKKYNFlSLSEAFYIATKSGGSFFG--- 364
Cdd:pfam01979 219 KLRSGRIALRKALEDGVKVGLGTDgAGSGNSLNMLEELRLALELQ------FDPEGGL-SPLEALRMATINPAKALGldd 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489525352 365 KVGSFEEGYDFDALIIDdsnlnhdnysiLERLERFIYVGDDRNIIHRYVCGKLI 418
Cdd:pfam01979 292 KVGSIEVGKDADLVVVD-----------LDPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
26-381 |
1.18e-34 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 133.39 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 26 IILEKGKVKGIFKEIPKEYKnlKVVDYTDKLIIPGMNDLHAHASQFKNLGMAMDKELLPWLETYTFPEESNYK--DIEYA 103
Cdd:PRK08393 23 VLIEGNKIVEVKRNINKPAD--TVIDASGSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKrkDIYWG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 104 TKMYkkfVKELWKSGTTRIaVFATVHKEASMKLMDifkEVGLGAYVGKVNMNMNCPdtllENTQDSIADTEEIINKYSDT 183
Cdd:PRK08393 101 AYLG---LLEMIKSGTTTF-VDMYFHMEEVAKATL---EVGLRGYLSYGMVDLGDE----EKREKEIKETEKLMEFIEKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 184 DS-IVKPIITPRFIPSCTSELLKGLGDLCLKYNIPIQSHLSENYDEIEWVRnlEPESKFYGDAYNRYNLFGQTpTLMAHC 262
Cdd:PRK08393 170 NSpRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIR--EKYGKSPVVLLDEIGFLNED-VIAAHG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 263 VHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSDISGG-HTLSIFKAMVSAIQLSKLYWVNSgk 341
Cdd:PRK08393 247 VWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASnNNLDMLREMKLAALLHKVHNLDP-- 324
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489525352 342 kyNFLSLSEAFYIATKSGGSFFG-KVGSFEEGYDFDALIID 381
Cdd:PRK08393 325 --TIADAETVFRMATQNGAKALGlKAGVIKEGYLADIAVID 363
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
15-418 |
5.52e-32 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 125.94 E-value: 5.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 15 SETFTVFENSYIILEKGKVKGI-FKEIPKEYKNLKVVDYTDKLIIPGMNDLHAHASQFKNLGMAMDKELLPWLETYTFPE 93
Cdd:PRK15493 14 NEQNEVIENGYIIVENDQIIDVnSGEFASDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 94 ESNYKDiEYATKMYKKFVKELWKSGTTRIA-VFATVHKEASmKLMDIFKEVGLGAYVGKVNMNMNCPdtllENTQDSIAD 172
Cdd:PRK15493 94 ESQFTP-ELAVASTELGLLEMVKSGTTSFSdMFNPIGVDQD-AIMETVSRSGMRAAVSRTLFSFGTK----EDEKKAIEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 173 TEEIINKYSDTDSIVKPIITPRFIPSCTSELLKGLGDLCLKYNIPIQSHLSENYDEiewVRNLEPEskfYGDAYNRY--- 249
Cdd:PRK15493 168 AEKYVKRYYNESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETERE---VRDIEAQ---YGKRPVEYaas 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 250 -NLFgQTPTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSD-ISGGHTLSIFKAMVS 327
Cdd:PRK15493 242 cGLF-KRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDsVASNNNLDMFEEMRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 328 AIQLSKlywvNSGKKYNFLSLSEAFYIATKSGGSFFG--KVGSFEEGYDFDALIIDDSNLNHDNYSIlERLERFIYVGDD 405
Cdd:PRK15493 321 ATLLQK----GIHQDATALPVETALTLATKGAAEVIGmkQTGSLEVGKCADFITIDPSNKPHLQPAD-EVLSHLVYAASG 395
|
410
....*....|...
gi 489525352 406 RNIIHRYVCGKLI 418
Cdd:PRK15493 396 KDISDVIINGKRV 408
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
48-381 |
9.80e-27 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 111.00 E-value: 9.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 48 KVVDYTDKLIIPGMNDLHAHASQFKNLGMAMDKELLPWLETYTFPEESNYKDiEYATKMYKKFVKELWKSGTTRIAVFaT 127
Cdd:PRK06038 44 TVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLTA-EDVYAGSLLACLEMIKSGTTSFADM-Y 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 128 VHKEASMKLMDifkEVGLGAYVGKVNMNMNCPdtllENTQDSIADTEEIINKYSDT-DSIVKPIITPRFIPSCTSELLKG 206
Cdd:PRK06038 122 FYMDEVAKAVE---ESGLRAALSYGMIDLGDD----EKGEAELKEGKRFVKEWHGAaDGRIKVMYGPHAPYTCSEEFLSK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 207 LGDLCLKYNIPIQSHLSENYDEIEWVrnlepeSKFYG----DAYNRYNLFGQTpTLMAHCVHCSQDEIDLMRENNVMAVH 282
Cdd:PRK06038 195 VKKLANKDGVGIHIHVLETEAELNQM------KEQYGmcsvNYLDDIGFLGPD-VLAAHCVWLSDGDIEILRERGVNVSH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 283 CPASNFNVGSGAMPIRKLIDNNIRLALGSD-ISGGHTLSIFKAMVSAIQLSKlywVNSGKKyNFLSLSEAFYIATKSGGS 361
Cdd:PRK06038 268 NPVSNMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAALLHK---VNTMDP-TALPARQVLEMATVNGAK 343
|
330 340
....*....|....*....|.
gi 489525352 362 FFG-KVGSFEEGYDFDALIID 381
Cdd:PRK06038 344 ALGiNTGMLKEGYLADIIIVD 364
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
8-416 |
3.85e-26 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 109.32 E-value: 3.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 8 NIIFTKTSETFTVFENSYIILEKGKVK--GIFKEIPKEyKNLKVVDYTDKLIIPGMNDLHAHASQFKNLGMAMDKELLPW 85
Cdd:PRK06687 6 HVNIVTCDQDFHVYLDGILAVKDSQIVyvGQDKPAFLE-QAEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHEW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 86 LETYTFPEESNYKDiEYATKMYKKFVKELWKSGTTriaVFATVHKEASMKLMDIFKEVGlgayvgkvNMNMNC--PDTLL 163
Cdd:PRK06687 85 LNDYIWPAESEFTP-DMTTNAVKEALTEMLQSGTT---TFNDMYNPNGVDIQQIYQVVK--------TSKMRCyfSPTLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 164 ----ENTQDSIADTEEIINK---YSDTDsiVKPIITPRFIPSCTSELLKGLGDLCLKYNIPIQSHLSENYDeiewvrnle 236
Cdd:PRK06687 153 ssetETTAETISRTRSIIDEilkYKNPN--FKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKE--------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 237 pESKFYGDAYNRYNL-------FGQTPTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLAL 309
Cdd:PRK06687 222 -ESGIILKRYGKRPLafleelgYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 310 GSD-ISGGHTLSIFKAMVSAIQLSKLywvNSGKKYNFlSLSEAFYIATKSGGSFFG---KVGSFEEGYDFDALIIDDSNL 385
Cdd:PRK06687 301 ATDsVASNNNLDMFEEGRTAALLQKM---KSGDASQF-PIETALKVLTIEGAKALGmenQIGSLEVGKQADFLVIQPQGK 376
|
410 420 430
....*....|....*....|....*....|.
gi 489525352 386 NHdNYSILERLERFIYVGDDRNIIHRYVCGK 416
Cdd:PRK06687 377 IH-LQPQENMLSHLVYAVKSSDVDDVYIAGE 406
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
49-420 |
2.67e-23 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 101.11 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 49 VVDYTDKLIIPGMNDLHAHASQFKNLGMAMDKELLPWLETyTFPEESNYKDiEYATKMYKKFVKELWKSGTTriaVFATV 128
Cdd:PRK06380 44 IIDATGKVVMPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TFKYDSKRTR-EGIYNSAKLGMYEMINSGIT---AFVDL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 129 HKEASMkLMDIFKEVGLGAYVGKVNMNmncpDTLLENTQDSIADTEEIINKYsDTDSIVKPIITPRFIPSCTSELLKGLG 208
Cdd:PRK06380 119 YYSEDI-IAKAAEELGIRAFLSWAVLD----EEITTQKGDPLNNAENFIREH-RNEELVTPSIGVQGIYVANDETYLKAK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 209 DLCLKYNIPIQSHLSENYDE------------IEWVRNLEpeskfygdaynrynlFGQTPTLMAHCVHCSQDEIDLMREN 276
Cdd:PRK06380 193 EIAEKYDTIMHMHLSETRKEvydhvkrtgerpVEHLEKIG---------------FLNSKLIAAHCVWATYHEIKLLSKN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 277 NVMAVHCPASNFNVGSGA-MPIRKLIDNNIRLALGSDISGG-HTLSIFKAM-VSAIQLSKLYWVNSGKKYNflslsEAFY 353
Cdd:PRK06380 258 GVKVSWNSVSNFKLGTGGsPPIPEMLDNGINVTIGTDSNGSnNSLDMFEAMkFSALSVKNERWDASIIKAQ-----EILD 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489525352 354 IATKSGGSFFG-KVGSFEEGYDFDALIIDDSNLNHDNYSILERLERFIYVGDDRNIIHRYVCGKLIEE 420
Cdd:PRK06380 333 FATINAAKALElNAGSIEVGKLADLVILDARAPNMIPTRKNNIVSNIVYSLNPLNVDHVIVNGKILKE 400
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
49-312 |
4.65e-21 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 94.92 E-value: 4.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 49 VVDYTDKLIIPGMNDLHAHASQF--KNLGMAMDKELLPWLET-YTF-----PEesnykDIEYATKMYkkfVKELWKSGTT 120
Cdd:PRK08203 49 VFDARGHVVTPGLVNTHHHFYQTltRALPAAQDAELFPWLTTlYPVwarltPE-----MVRVATQTA---LAELLLSGCT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 121 RIAVFATVHKEASMKLMDI----FKEVGLGAYVGKVNMNMN------CPDTLLENTQDSIADTEEIINKYSDT--DSIVK 188
Cdd:PRK08203 121 TSSDHHYLFPNGLRDALDDqieaAREIGMRFHATRGSMSLGesdgglPPDSVVEDEDAILADSQRLIDRYHDPgpGAMLR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 189 PIITP--RFipSCTSELLKGLGDLCLKYNIPIQSHLSENYDEIEWVRNLepeskfygdaynrynlFGQTP---------- 256
Cdd:PRK08203 201 IALAPcsPF--SVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLER----------------FGMRPvdyledlgwl 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489525352 257 ---TLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSD 312
Cdd:PRK08203 263 gpdVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVD 321
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
2-384 |
1.82e-19 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 89.64 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 2 LKVLKGNIIFTkTSETFTVFENSYIILEKgKVKGI--FKEIPKEYKNLKVVDYTDKLIIPGMNDLHAHASQFKNLGMAMD 79
Cdd:PRK08418 1 MKIIGASYIFT-CDENFEILEDGAVVFDD-KILEIgdYENLKKKYPNAKIQFFKNSVLLPAFINPHTHLEFSANKTTLDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 80 KELLPWLET-YTFPEESNYKDieyATKMYKKFVKELWKSGTTRIAVFA------TVHKEASMKLMdIFKEVgLGAyvgkv 152
Cdd:PRK08418 79 GDFIPWLGSvINHREDLLEKC---KGALIQQAINEMLKSGVGTIGAISsfgidlEICAKSPLRVV-FFNEI-LGS----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 153 nmNMNCPDTLLENTQDSIADTEEIINKysdtdsivkpiitpRFIP--------SCTSELLKGLGDLCLKYNIPIQSHLSE 224
Cdd:PRK08418 149 --NASAVDELYQDFLARFEESKKFKSK--------------KFIPaiaihspySVHPILAKKALQLAKKENLLVSTHFLE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 225 NYDEIEWVRNLE-----------PESKFYGDAYNRYNLFGQTPTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSG 293
Cdd:PRK08418 213 SKAEREWLEESKgwfkkffekflKEPKPLYTPKEFLELFKGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 294 AMPIRKLIDNNIRLALGSD-ISGGHTLSIFKAMVSAIQLSklywvnsgKKYNFLSLS-EAFYIATKSGGSFFG-KVGSFE 370
Cdd:PRK08418 293 ALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTH--------ANMPLLELAkILLLSATRYGAKALGlNNGEIK 364
|
410
....*....|....
gi 489525352 371 EGYDFDALIIDDSN 384
Cdd:PRK08418 365 EGKDADLSVFELPE 378
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
19-417 |
1.17e-17 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 84.58 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 19 TVFENSYIILEKGKVKGIF--KEIPKEYKNLKVVDYTDKLIIPGMNDLHAHA--SQFKnlGMAMDKELLPWLETYTFPEE 94
Cdd:PRK09045 24 VVLEDHAVAIRDGRIVAILprAEARARYAAAETVELPDHVLIPGLINAHTHAamSLLR--GLADDLPLMTWLQDHIWPAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 95 SNYKDIEyatkmykkFVK--------ELWKSGTTRIA---VFATVHKEAsmklmdiFKEVGLGAYVGKVNMNMncPDTLL 163
Cdd:PRK09045 102 GAWVSEE--------FVRdgtllaiaEMLRGGTTCFNdmyFFPEAAAEA-------AHQAGMRAQIGMPVLDF--PTAWA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 164 ENTQDSIADTEEIINKYSDTdsivkPIITPRFIP----SCTSELLKGLGDLCLKYNIPIQSHLSENYDEIEwvrnlepes 239
Cdd:PRK09045 165 SDADEYLAKGLELHDQWRHH-----PLISTAFAPhapyTVSDENLERIRTLAEQLDLPIHIHLHETAQEIA--------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 240 kfygDAYNRYnlfGQTP-------------TLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIR 306
Cdd:PRK09045 231 ----DSLKQH---GQRPlarlarlgllgprLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 307 LALGSD-ISGGHTLSIFKAMVSAIQLSKlywVNSGKKyNFLSLSEAFYIATKSGGSFFG---KVGSFEEGYDFDALIIDD 382
Cdd:PRK09045 304 VALGTDgAASNNDLDLFGEMRTAALLAK---AVAGDA-TALPAHTALRMATLNGARALGlddEIGSLEPGKQADLVAVDL 379
|
410 420 430
....*....|....*....|....*....|....*....
gi 489525352 383 SNLN----HDNYSILerlerfIYVGDDRNIIHRYVCGKL 417
Cdd:PRK09045 380 SGLEtqpvYDPVSQL------VYAAGREQVSHVWVAGKQ 412
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
27-394 |
9.23e-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: 81.34 E-value: 9.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 27 ILEKGKvkgiFKEIPKEYKNLKVVDYTDKLIIPGMNDLHAHASQFKNLGMAMDKELLPWL----ETYTFPEESNYKDIey 102
Cdd:cd01312 3 ILEVGD----YEKLEKRYPGAKHEFFPNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLlsviNSRDELLKQPWEEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 103 atkmYKKFVKELWKSGTTRIAVFATvhkeaSMKLMDIFKEVGLGAYVGKVNMNMNcPDTLLENTQDSIADTEEIINKYSD 182
Cdd:cd01312 77 ----IRQGIRQMLESGTTSIGAISS-----DGSLLPALASSGLRGVFFNEVIGSN-PSAIDFKGETFLERFKRSKSFESQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 183 TdsiVKPIITPRFIPSCTSELLKGLGDLCLKYNIPIQSHLSENYDEIEWVRN-------------LEPESKFYGDAYNRY 249
Cdd:cd01312 147 L---FIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEEskgwfkhfwesflKLPKPKKLATAIDFL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 250 NLFG--QTPTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSD-ISGGHTLSIFKamv 326
Cdd:cd01312 224 DMLGglGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLLD--- 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489525352 327 saiQLSKLYWVNSGKKYNFLSlSEAFYIATKSGGSFFG-KVGSFEEGYDFDALIIDDSNLNHDNYSILE 394
Cdd:cd01312 301 ---ELRALLDLHPEEDLLELA-SELLLMATLGGARALGlNNGEIEAGKRADFAVFELPGPGIKEQAPLQ 365
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
16-390 |
3.07e-16 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 80.36 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 16 ETFTVFENSYIILEKGKVK--GIFKEIPKEYKNLKVVDYTDKLIIPGMNDLHAHA-SQF------------------KNL 74
Cdd:PRK07203 14 PAKPVIEDGAIAIEGNVIVeiGTTDELKAKYPDAEFIDAKGKLIMPGLINSHNHIySGLargmmanippppdfisilKNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 75 GMAMDKELlpwletytfPEESNYKDiEYATKMykkfvkELWKSGTTRI----AVFATVhKEASMKLMDIFKEVGLGAyvg 150
Cdd:PRK07203 94 WWRLDRAL---------TLEDVYYS-ALICSL------EAIKNGVTTVfdhhASPNYI-GGSLFTIADAAKKVGLRA--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 151 kvnmnMNCPDTL----LENTQDSIADTEEIINKYS-DTDSIVKPII---TPRFIPSCTSELLKGLGDlclKYNIPIQSHL 222
Cdd:PRK07203 154 -----MLCYETSdrdgEKELQEGVEENIRFIKHIDeAKDDMVEAMFglhASFTLSDATLEKCREAVK---ETGRGYHIHV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 223 SENYDEIEwvRNLEPESKFYGDAYNRYNLFGQTpTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLID 302
Cdd:PRK07203 226 AEGIYDVS--DSHKKYGKDIVERLADFGLLGEK-TLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 303 NNIRLALGSDisgGHTLSIFKAMVSAIQLSK-------LYWVNSGKKynflslseAFYIATKSGGSFFG-KVGSFEEGYD 374
Cdd:PRK07203 303 NGILLGLGTD---GYTSDMFESYKVANFKHKhaggdpnVGWPESPAM--------LFENNNKIAERYFGaKFGILEEGAK 371
|
410 420
....*....|....*....|
gi 489525352 375 FDaLIIDDSN----LNHDNY 390
Cdd:PRK07203 372 AD-LIIVDYNpptpLNEDNI 390
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
210-325 |
3.89e-13 |
|
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: 68.97 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 210 LCLKYNIPIQSHLSEN-----YDEIEWVRNLEPEskfygdaynrynlfgqtptLMAHCVHCSQDEIDLMRENNVMAVHCP 284
Cdd:cd01305 133 LLRRRGKLFAIHASETresvgMTDIERALDLEPD-------------------LLVHGTHLTDEDLELVRENGVPVVLCP 193
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489525352 285 ASNFNVGSGAMPIRKLIDNNIRLALGSDISGGHTLSIFKAM 325
Cdd:cd01305 194 RSNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEM 234
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
63-359 |
4.38e-13 |
|
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: 69.28 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 63 DLHAHasqfknLGMAMDKELLPWLETYTFPEESNykdiEYATKMYKKFVKELWKSGTTRIAVFATVH----KEASMKLMd 138
Cdd:cd01292 3 DTHVH------LDGSALRGTRLNLELKEAEELSP----EDLYEDTLRALEALLAGGVTTVVDMGSTPppttTKAAIEAV- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 139 ifKEVGLGAYVGKVNMNMNCPDTLLENTQDSIADTEEIINKYSDTDSIVKPIITPRFIPSCTSELLKGLGDLCLKYNIPI 218
Cdd:cd01292 72 --AEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLEEARKLGLPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 219 QSHLSENYDEIEwvrnlepeskFYGDAYNRYNLFGqtPTLMAHCVHCSQDEIDLMRENNVMAVHCPASNF---NVGSGAM 295
Cdd:cd01292 150 VIHAGELPDPTR----------ALEDLVALLRLGG--RVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYllgRDGEGAE 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525352 296 PIRKLIDNNIRLALGSDISgghtlsifkAMVSAIQLSKLYWVNSGKKYNFLSLSEAFYIATKSG 359
Cdd:cd01292 218 ALRRLLELGIRVTLGTDGP---------PHPLGTDLLALLRLLLKVLRLGLSLEEALRLATINP 272
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
1-397 |
1.74e-12 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 68.14 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 1 MLKVLKGNIIftkTSETFTVFENSYIILEkgkvkGIFKEIPKEYKNLKVVDYTDkLIIPGMNDLHAHA--SQFKNLGMAM 78
Cdd:PRK07213 1 MLVYLNGNFL---YGEDFEPKKGNLVIED-----GIIKGFTNEVHEGNVIDAKG-LVIPPLINAHTHIgdSSIKDIGIGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 79 D-KELL--PWLETYTFPEESNYKDIEYATKmykKFVKELWKSGTTRIAVFatvhKEASMKLMDIFKEVGL-----GAYVG 150
Cdd:PRK07213 72 SlDELVkpPNGLKHKFLNSCSDKELVEGMK---EGLYDMYNNGIKAFCDF----REGGIKGINLLKKASSdlpikPIILG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 151 KvnmnmncpDTLLENTQDSIAdTEEIInKYSDTdsivkpiITPRFIPSCTSELLKGLGDLCLKYNIPIQSHLSENYDEIE 230
Cdd:PRK07213 145 R--------PTEADENELKKE-IREIL-KNSDG-------IGLSGANEYSDEELKFICKECKREKKIFSIHAAEHKGSVE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 231 WVRN----LEPESKFYgdaynrynlFGQTPTLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIR 306
Cdd:PRK07213 208 YSLEkygmTEIERLIN---------LGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGIL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 307 LALGSDISGGHTLSIFKAMVSAIqlsKLYWVNSgkkynflslSEAFYIATKSGGSFFG--KVGSFEEGYDFDALIIDDSN 384
Cdd:PRK07213 279 LGIGTDNFMANSPSIFREMEFIY---KLYHIEP---------KEILKMATINGAKILGliNVGLIEEGFKADFTFIKPTN 346
|
410
....*....|....*.
gi 489525352 385 LNHDN---YSILERLE 397
Cdd:PRK07213 347 IKFSKnpyASIITRCE 362
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
49-312 |
3.55e-11 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 64.70 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 49 VVDYTDKLIIPGMNDLHAHASQ--FKNLGMAMDKELLPWLETYTFPEESNYKDIEYATKMYKKFVkELWKSGTTRIA--- 123
Cdd:PRK12393 49 VIDATDCVVYPGWVNTHHHLFQslLKGVPAGINQSLTAWLAAVPYRFRARFDEDLFRLAARIGLV-ELLRSGCTTVAdhh 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 124 --VFATVHKEASMKLMDIFKEVGL-------GAYVGKvNMNMNCPDTLLENTQD-SIADTEEIINKYSD--TDS----IV 187
Cdd:PRK12393 128 ylYHPGMPFDTGDILFDEAEALGMrfvlcrgGATQTR-GDHPGLPTALRPETLDqMLADVERLVSRYHDasPDSlrrvVV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 188 KPiITPRFipSCTSELLKGLGDLCLKYNIPIQSHLSENYDEIEWVRnlepeskfygdaynryNLFGQTP----------- 256
Cdd:PRK12393 207 AP-TTPTF--SLPPELLREVARAARGMGLRLHSHLSETVDYVDFCR----------------EKYGMTPvqfvaehdwlg 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489525352 257 --TLMAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSD 312
Cdd:PRK12393 268 pdVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVD 325
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
259-392 |
4.42e-10 |
|
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: 60.73 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 259 MAHCVHCSQDEIDLMRENNVMAVHCPASNFNVGSGAMPIRKLIDNNIRLALGSDISGGH--TLSIFKAMVSAIQLSKlyw 336
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSspTSSMPLVMHLACRLMR--- 309
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489525352 337 vnsgkkynfLSLSEAFYIATKSGGSFFG---KVGSFEEGYDFDALIIDDSNLNHDNYSI 392
Cdd:cd01296 310 ---------MTPEEALTAATINAAAALGlgeTVGSLEVGKQADLVILDAPSYEHLAYRF 359
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-398 |
2.39e-07 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 52.66 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 4 VLKGNIIFTKTSETftVFENSYIILEKGKVKGIFKEIPKEY-KNLKVVDYTDKLIIPGMNDLHAHasqfknLGMAMDKEl 82
Cdd:COG1228 11 LITNATLVDGTGGG--VIENGTVLVEDGKIAAVGPAADLAVpAGAEVIDATGKTVLPGLIDAHTH------LGLGGGRA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 83 lpWLETYTFPEESNYKDIEYATKMYKKFVKelwkSGTT------------RIAVFATvhKEASMKLMDIFKE-VGLGAYV 149
Cdd:COG1228 82 --VEFEAGGGITPTVDLVNPADKRLRRALA----AGVTtvrdlpggplglRDAIIAG--ESKLLPGPRVLAAgPALSLTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 150 GKVNMNmncPDT---LLENTQDSIADTEEIINKYSDTDsivkpiITPrfipsctsELLKGLGDLCLKYNIPIQSHlSENY 226
Cdd:COG1228 154 GAHARG---PEEaraALRELLAEGADYIKVFAEGGAPD------FSL--------EELRAILEAAHALGLPVAAH-AHQA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 227 DEIEWVrnLEpeskfygdaynrynlFGQTptLMAHCVHCSQDEIDLMRENNVMAVhCPASNFNVGSGAM----------- 295
Cdd:COG1228 216 DDIRLA--VE---------------AGVD--SIEHGTYLDDEVADLLAEAGTVVL-VPTLSLFLALLEGaaapvaakark 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 296 -------PIRKLIDNNIRLALGSDISGG--HTLSIFKAMVSAIQLsklywvnsGkkynfLSLSEAFYIATKSGGSFFG-- 364
Cdd:COG1228 276 vreaalaNARRLHDAGVPVALGTDAGVGvpPGRSLHRELALAVEA--------G-----LTPEEALRAATINAAKALGld 342
|
410 420 430
....*....|....*....|....*....|....*
gi 489525352 365 -KVGSFEEGYDFDALIIDDSNLnhDNYSILERLER 398
Cdd:COG1228 343 dDVGSLEPGKLADLVLLDGDPL--EDIAYLEDVRA 375
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-67 |
3.13e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 42.78 E-value: 3.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489525352 4 VLKGNIIFTKTsetfTVFENSYIILEKGKVKGIFKEIPKeykNLKVVDYTDKLIIPGMNDLHAH 67
Cdd:COG1820 1 AITNARIFTGD----GVLEDGALLIEDGRIAAIGPGAEP---DAEVIDLGGGYLAPGFIDLHVH 57
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
261-333 |
5.30e-04 |
|
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.
Pssm-ID: 238645 Cd Length: 325 Bit Score: 41.81 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489525352 261 HCVHCSQDE--IDLMRENNVMAVHCPASNFNVGS----GAMPIRKLIDNNIRLALGSD---ISGGHTLSIFKAMVSAIQL 331
Cdd:cd01320 216 HGIRAIEDPelVKRLAERNIPLEVCPTSNVQTGAvkslAEHPLRELLDAGVKVTINTDdptVFGTYLTDEYELLAEAFGL 295
|
..
gi 489525352 332 SK 333
Cdd:cd01320 296 TE 297
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-67 |
3.23e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 39.48 E-value: 3.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489525352 3 KVLKGNIIFTKTSEtftvfENSYIILEKGKVKGIFKEIPKEyKNLKVVDYTDKLIIPGMNDLHAH 67
Cdd:cd00854 1 LIIKNARILTPGGL-----EDGAVLVEDGKIVAIGPEDELE-EADEIIDLKGQYLVPGFIDIHIH 59
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
26-67 |
9.44e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 38.25 E-value: 9.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489525352 26 IILEKGKVKGIFKEIPKEykNLKVVDYTDKLIIPGMNDLHAH 67
Cdd:PRK09357 22 VLIDDGKIAAIGENIEAE--GAEVIDATGLVVAPGLVDLHVH 61
|
|
| |
