|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
1-402 |
0e+00 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 570.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 1 MQIIVPHFILMSD---SIVTERAIAFEKTILKIAPLEELLQEFPHAKITTlAKNSLLMPGLINAHVHLEFSANKTHLSYG 77
Cdd:PRK08418 1 MKIIGASYIFTCDenfEILEDGAVVFDDKILEIGDYENLKKKYPNAKIQF-FKNSVLLPAFINPHTHLEFSANKTTLDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 78 DFISWLYSVIENREELIGGCDTACMAQAIDSMLACGITTFGAVSSHGMDLQACADAPQNVIFFNELIGSQATMADALFND 157
Cdd:PRK08418 80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 158 FSARLDASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDFKEFFESLLKQNT 237
Cdd:PRK08418 160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 238 CVSDSAEFLEHFNAIPTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKL 317
Cdd:PRK08418 240 PLYTPKEFLELFKGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 318 DLFEEMKISLFMHSDAPLLEFAKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDATPTP--ELAIHLLLHRYNVSK 395
Cdd:PRK08418 320 SLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECTKkeQLPLQFILHAKEVKK 399
|
....*..
gi 1277938128 396 VYINGKL 402
Cdd:PRK08418 400 LFIGGKE 406
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
27-401 |
1.52e-114 |
|
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: 339.43 E-value: 1.52e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 27 ILKIAPLEELLQEFPHAKITTLaKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENREELIG-GCDTAcMAQA 105
Cdd:cd01312 3 ILEVGDYEKLEKRYPGAKHEFF-PNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLKqPWEEA-IRQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 106 IDSMLACGITTFGAVSSHGMDLQACADAPQNVIFFNELIGSQATMADALFNDFSARLDASKSVTREGFHTGVAIHSPYSV 185
Cdd:cd01312 81 IRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 186 HPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDFKEFFESLLK--QNTCVSDSAEFLEHFNAI--PTLFTHVVQ 261
Cdd:cd01312 161 HPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFWESFLKlpKPKKLATAIDFLDMLGGLgtRVSFVHCVY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 262 ANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSDAPLLEFAKA 341
Cdd:cd01312 241 ANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLLELASE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277938128 342 LLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDATPTPELAIHL-LLHRYNVSKVYINGK 401
Cdd:cd01312 321 LLLMATLGGARALGLNNGEIEAGKRADFAVFELPGPGIKEQAPLQfILHAKEVRHLFISGK 381
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
20-402 |
5.03e-75 |
|
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: 239.34 E-value: 5.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 20 AIAFEK-TILKIAPLEELLQEFPHAKITTlAKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENREE-LIGGC 97
Cdd:COG0402 23 AVLVEDgRIAAVGPGAELPARYPAAEVID-AGGKLVLPGLVNTHTHLPQTLLRGLADDLPLLDWLEEYIWPLEArLDPED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 98 DTACMAQAIDSMLACGITTFGAVSSHGMD-----LQACADAPQNVIFFNELIG-----SQATMADALFNDFSARLDASKS 167
Cdd:COG0402 102 VYAGALLALAEMLRSGTTTVADFYYVHPEsadalAEAAAEAGIRAVLGRGLMDrgfpdGLREDADEGLADSERLIERWHG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 168 VTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDfkeffesllkqntcvsDSAEFLE 247
Cdd:COG0402 182 AADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYGK----------------RPVEYLD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 248 HFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKI 325
Cdd:COG0402 246 ELGLLgpRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 326 SLFMH----SDAPLLEfAKALLKGATLDAAKALGLN--TGEIAVGKNADMIVLDLDA---TPTPELAIHLLL--HRYNVS 394
Cdd:COG0402 326 AALLQrlrgGDPTALS-AREALEMATLGGARALGLDdeIGSLEPGKRADLVVLDLDAphlAPLHDPLSALVYaaDGRDVR 404
|
....*...
gi 1277938128 395 KVYINGKL 402
Cdd:COG0402 405 TVWVAGRV 412
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
8-402 |
7.40e-49 |
|
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: 170.85 E-value: 7.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 8 FILMSDSIVTERAIAFEK-TILKIAPLEELLQEfpHAKITTLAKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSV 86
Cdd:cd01298 9 VTTDPRRVLEDGDVLVEDgRIVAVGPALPLPAY--PADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDLPLMEWLKDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 87 IENREELIGGCDTACMAQ-AIDSMLACGITTFgaVSSHGMDLQACADAPQNV--------IFFNELIGSQATMADALFNd 157
Cdd:cd01298 87 IWPLERLLTEEDVYLGALlALAEMIRSGTTTF--ADMYFFYPDAVAEAAEELgiravlgrGIMDLGTEDVEETEEALAE- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 158 fSARL-DASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGdfkeffesllkqn 236
Cdd:cd01298 164 -AERLiREWHGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEKYG------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 237 tcvSDSAEFLEHFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSN 314
Cdd:cd01298 230 ---KRPVEYLEELGLLgpDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGAASN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 315 YKLDLFEEMKISLFMH----SDAPLLEFAKAlLKGATLDAAKALGLN-TGEIAVGKNADMIVLDLDA---TPTPELAIHL 386
Cdd:cd01298 307 NNLDMFEEMRLAALLQklahGDPTALPAEEA-LEMATIGGAKALGLDeIGSLEVGKKADLILIDLDGphlLPVHDPISHL 385
|
410
....*....|....*...
gi 1277938128 387 LL--HRYNVSKVYINGKL 402
Cdd:cd01298 386 VYsaNGGDVDTVIVNGRV 403
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
53-402 |
1.10e-39 |
|
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: 144.57 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 53 LLMPGLINAHVHLEFSANKTHLSYGDFISWlysvienreeligGCDTACMAqaidsMLACGITTFGAVS-SHGMDLQACA 131
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYE-------------ALRLGITT-----MLKSGTTTVLDMGaTTSTGIEALL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 132 DAPQNVIFFNELIGSQATMA--------DALFNDFSARLDASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLK 203
Cdd:pfam01979 63 EAAEELPLGLRFLGPGCSLDtdgelegrKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 204 LTAHFMESKAEREWLDKSEGDFKEFFESLlkqntcvsDSAEFLEHFNAIPTLFTHVVQANKSELSTLAK--NGHTVIHCP 281
Cdd:pfam01979 143 VAIHALETKGEVEDAIAAFGGGIEHGTHL--------EVAESGGLLDIIKLILAHGVHLSPTEANLLAEhlKGAGVAHCP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 282 ISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSDAPLLEFAKALLKGATLDAAKALGL--NTG 359
Cdd:pfam01979 215 FSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLddKVG 294
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1277938128 360 EIAVGKNADMIVLDLDATPtpelAIHLLLHRYNVSKVYINGKL 402
Cdd:pfam01979 295 SIEVGKDADLVVVDLDPLA----AFFGLKPDGNVKKVIVKGKI 333
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
54-401 |
1.44e-32 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 127.04 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 54 LMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENRE-ELIGGCDTACMAQAIDSMLACGITTFGAV-SSHGMDL---- 127
Cdd:PRK06687 56 IMPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAEsEFTPDMTTNAVKEALTEMLQSGTTTFNDMyNPNGVDIqqiy 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 128 QACADAPQNVIFFNELIGSQATMADALFNDFSARLDASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAH 207
Cdd:PRK06687 136 QVVKTSKMRCYFSPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 208 FMESKAEREWLDKSEGDFK-EFFESLlkqntcvsdsaEFLEHfnaiPTLFTHVVQANKSELSTLAKNGHTVIHCPISNRL 286
Cdd:PRK06687 216 VAETKEESGIILKRYGKRPlAFLEEL-----------GYLDH----PSVFAHGVELNEREIERLASSQVAIAHNPISNLK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 287 LGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHS----DAPLLEFAKAlLKGATLDAAKALGLNT--GE 360
Cdd:PRK06687 281 LASGIAPIIQLQKAGVAVGIATDSVASNNNLDMFEEGRTAALLQKmksgDASQFPIETA-LKVLTIEGAKALGMENqiGS 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1277938128 361 IAVGKNADMIVLD----LDATPTPELAIHLL--LHRYNVSKVYINGK 401
Cdd:PRK06687 360 LEVGKQADFLVIQpqgkIHLQPQENMLSHLVyaVKSSDVDDVYIAGE 406
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
41-406 |
3.54e-27 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 111.90 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 41 PHAKITTLAKNSLLMPGLINAHVHLEFSANK-----THLSygDFI--SWLYSVIENREELIGGCDTAcmaqaIDSMLACG 113
Cdd:PRK06380 39 EEADYIIDATGKVVMPGLINTHAHVGMTASKglfddVDLE--EFLmkTFKYDSKRTREGIYNSAKLG-----MYEMINSG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 114 ITTFgavsshgMDLQACADAPQNVIffnELIGSQATMADALFN-DFSAR----LDASKSVTREGFHT-----GVAIHSPY 183
Cdd:PRK06380 112 ITAF-------VDLYYSEDIIAKAA---EELGIRAFLSWAVLDeEITTQkgdpLNNAENFIREHRNEelvtpSIGVQGIY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 184 SVHPVLIKKALAIVKSEKLKLTAHFMESKaerewldksegdfKEFFESLLKQntcvsdSAEFLEHFNAIPTLFT-----H 258
Cdd:PRK06380 182 VANDETYLKAKEIAEKYDTIMHMHLSETR-------------KEVYDHVKRT------GERPVEHLEKIGFLNSkliaaH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 259 VVQANKSELSTLAKNGHTVIHCPISNRLLGNE-TLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHS----DA 333
Cdd:PRK06380 243 CVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGgSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALSVKnerwDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 334 PLLEfAKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDAT---PTPELA----IHLLLHRYNVSKVYINGKLEKGN 406
Cdd:PRK06380 323 SIIK-AQEILDFATINAAKALELNAGSIEVGKLADLVILDARAPnmiPTRKNNivsnIVYSLNPLNVDHVIVNGKILKEN 401
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
49-402 |
4.16e-27 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 111.77 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 49 AKNSLLMPGLINAHVHLEFSANKthlSYGDFI---SWLYSVIENREELIGGCDTAcmaqaIDSMLAC------GITTFGA 119
Cdd:PRK06038 48 AKGSVVMPGLVNTHTHAAMTLFR---GYADDLplaEWLNDHIWPAEAKLTAEDVY-----AGSLLAClemiksGTTSFAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 120 VSSHgMDlqacaDAPQNViffnELIGSQAT----MADaLFNDFSAR--LDASKSVTREgFH--------TGVAIHSPYSV 185
Cdd:PRK06038 120 MYFY-MD-----EVAKAV----EESGLRAAlsygMID-LGDDEKGEaeLKEGKRFVKE-WHgaadgrikVMYGPHAPYTC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 186 HPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGdfKEFFESLlkqntcvsDSAEFLEHfnaiPTLFTHVVQANKS 265
Cdd:PRK06038 188 SEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQYG--MCSVNYL--------DDIGFLGP----DVLAAHCVWLSDG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 266 ELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMH---SDAPLLEFAKAL 342
Cdd:PRK06038 254 DIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDGCASNNNLDMFEEMKTAALLHkvnTMDPTALPARQV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277938128 343 LKGATLDAAKALGLNTGEIAVGKNADMIVLDLDA---TPTPELAIHLLLHRY--NVSKVYINGKL 402
Cdd:PRK06038 334 LEMATVNGAKALGINTGMLKEGYLADIIIVDMNKphlTPVRDVPSHLVYSASgsDVDTTIVDGRI 398
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
27-402 |
2.68e-25 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 106.92 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 27 ILKIAPLEELLQEFPHAKITTLAkNSLLMPGLINAHVHLEFS-----ANKTHLsygdfISWLYSVI---ENR---EELIG 95
Cdd:PRK09045 38 IVAILPRAEARARYAAAETVELP-DHVLIPGLINAHTHAAMSllrglADDLPL-----MTWLQDHIwpaEGAwvsEEFVR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 96 -GCDTAcMAQaidsMLACGITTF-----------GAVSSHGMDLQACA---DAPqnviffnelIGSQATMADALFNDFSA 160
Cdd:PRK09045 112 dGTLLA-IAE----MLRGGTTCFndmyffpeaaaEAAHQAGMRAQIGMpvlDFP---------TAWASDADEYLAKGLEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 161 RlDASKSVTRegFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAErewLDKSEgdfKEFFE---------S 231
Cdd:PRK09045 178 H-DQWRHHPL--ISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQE---IADSL---KQHGQrplarlarlG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 232 LLKQNT-CVsdsaeflehfnaiptlftHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDG 310
Cdd:PRK09045 249 LLGPRLiAV------------------HMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 311 LSSNYKLDLFEEMKISLF----MHSDAPLLEfAKALLKGATLDAAKALGLN--TGEIAVGKNADMIVLDLDA---TPTPE 381
Cdd:PRK09045 311 AASNNDLDLFGEMRTAALlakaVAGDATALP-AHTALRMATLNGARALGLDdeIGSLEPGKQADLVAVDLSGletQPVYD 389
|
410 420
....*....|....*....|...
gi 1277938128 382 LAIHLL--LHRYNVSKVYINGKL 402
Cdd:PRK09045 390 PVSQLVyaAGREQVSHVWVAGKQ 412
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
50-401 |
2.44e-24 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 103.98 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 50 KNSLLMPGLINAHVHLEFSANKthlSYGD---FISWLYSVIENRE-ELIGGCDTACMAQAIDSMLACGITTFGAV-SSHG 124
Cdd:PRK15493 53 KGKWVLPGLVNTHTHVVMSLLR---GIGDdmlLQPWLETRIWPLEsQFTPELAVASTELGLLEMVKSGTTSFSDMfNPIG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 125 MDLQACADAPQNViffneliGSQATMADALFNdFSARLDASKSVT----------REG--FHTGVAIHSPYSVHPVLIKK 192
Cdd:PRK15493 130 VDQDAIMETVSRS-------GMRAAVSRTLFS-FGTKEDEKKAIEeaekyvkryyNESgmLTTMVAPHSPYTCSTELLEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 193 ALAIVKSEKLKLTAHFMESKAEREWLDKSEGDFK-EFFES--LLKQntcvsdsaeflehfnaiPTLFTHVVQANKSELST 269
Cdd:PRK15493 202 CARIAVENQTMVHIHLSETEREVRDIEAQYGKRPvEYAAScgLFKR-----------------PTVIAHGVVLNDNERAF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 270 LAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFM----HSDAPLLEFAKAlLKG 345
Cdd:PRK15493 265 LAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLqkgiHQDATALPVETA-LTL 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277938128 346 ATLDAAKALGL-NTGEIAVGKNADMIVLDLDATPTPELAIHLLLHRY------NVSKVYINGK 401
Cdd:PRK15493 344 ATKGAAEVIGMkQTGSLEVGKCADFITIDPSNKPHLQPADEVLSHLVyaasgkDISDVIINGK 406
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
49-374 |
1.71e-21 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 95.64 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 49 AKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENREELIGGCDTACMAQ-AIDSMLACGITTFGAVSSHgmdL 127
Cdd:PRK08393 47 ASGSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYlGLLEMIKSGTTTFVDMYFH---M 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 128 QACADAPQNV----------IFFNELIGSQATMADAL-FNDFSARLDASKsvtregFHTGVAIHSPYSVHPVLIKKALAI 196
Cdd:PRK08393 124 EEVAKATLEVglrgylsygmVDLGDEEKREKEIKETEkLMEFIEKLNSPR------VHFVFGPHAPYTCSLALLKWVREK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 197 VKSEKLKLTAHFMESKAEREWLDKSEGdfkeffesllKQNTCVSDSAEFLEHfnaiPTLFTHVVQANKSELSTLAKNGHT 276
Cdd:PRK08393 198 AREWNKLITIHLSETMDEIKQIREKYG----------KSPVVLLDEIGFLNE----DVIAAHGVWLSSRDIRILASAGVT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 277 VIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSDA---PLLEFAKALLKGATLDAAKA 353
Cdd:PRK08393 264 VAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDMLREMKLAALLHKVHnldPTIADAETVFRMATQNGAKA 343
|
330 340
....*....|....*....|.
gi 1277938128 354 LGLNTGEIAVGKNADMIVLDL 374
Cdd:PRK08393 344 LGLKAGVIKEGYLADIAVIDF 364
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
6-400 |
5.34e-20 |
|
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: 91.19 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 6 PHFILMSDSIVTER--AIAFEKTILKIAPLEELL--QEFPHAKITTLaKNSLLMPGLINAHVHLEFSANkTHLSYGD-FI 80
Cdd:cd01303 12 PELELVEDALRVVEdgLIVVVDGNIIAAGAAETLkrAAKPGARVIDS-PNQFILPGFIDTHIHAPQYAN-IGSGLGEpLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 81 SWL----------YSVIENREELIGGcdtacmaqAIDSMLACGITT---FGAVSSHGMDL--QACADAPQNVIffnelIG 145
Cdd:cd01303 90 DWLetytfpeeakFADPAYAREVYGR--------FLDELLRNGTTTacyFATIHPESTEAlfEEAAKRGQRAI-----AG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 146 SqaTMADALFNDFsaRLDASKSVTREG--FHTGVAIHSPySVHPVlIKKALAIVKSEKL-----KLTA---------HFM 209
Cdd:cd01303 157 K--VCMDRNAPEY--YRDTAESSYRDTkrLIERWHGKSG-RVKPA-ITPRFAPSCSEELlaalgKLAKehpdlhiqtHIS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 210 ESKAEREWLdksegdfKEFFESllkqntcVSDSAEFLEHFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLL 287
Cdd:cd01303 231 ENLDEIAWV-------KELFPG-------ARDYLDVYDKYGLLteKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 288 GNETLNIKELAENNIPWIVATDgLSSNYKLDLFEEM----KIS--LFMHSDAPLLEFAKALLKGATLDAAKALGLN--TG 359
Cdd:cd01303 297 GSGLFDVRKLLDAGIKVGLGTD-VGGGTSFSMLDTLrqayKVSrlLGYELGGHAKLSPAEAFYLATLGGAEALGLDdkIG 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1277938128 360 EIAVGKNADMIVLDLDATPTP--------ELAIHLLLHRY-----NVSKVYING 400
Cdd:cd01303 376 NFEVGKEFDAVVIDPSATPLLadrmfrveSLEEALFKFLYlgddrNIREVYVAG 429
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
51-401 |
1.81e-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: 238638 [Multi-domain] Cd Length: 418 Bit Score: 83.66 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 51 NSLLMPGLINAHVHlEFS---ANKTHL---SYGDFISW---LYSVIE--NREELiggcdTACMAQAIDSMLACGITTFGA 119
Cdd:cd01313 37 GGALLPGMPNLHSH-AFQramAGLTEYrgsAADSFWTWrelMYRFAArlTPEQI-----EAIARQLYIEMLLAGITAVGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 120 V-----SSHGMDLQACADAPQNVIFFNELIGSQATMADALF---------------------NDFSARLDASKSVTREGF 173
Cdd:cd01313 111 FhyvhhDPDGTPYADPAELAQRVIAAASDAGIGITLLPVLYaragfggpapnpgqrrfingyEDFLGLLEKALRAVKEHA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 174 HT--GVAIHSPYSVHPVLIKKALAIVkSEKLKLTAHFMESKAEREWLDKSEGDFKEffeSLLKQNTCVSdsaeflEHFNA 251
Cdd:cd01313 191 AAriGVAPHSLRAVPAEQLAALAALA-SEKAPVHIHLAEQPKEVDDCLAAHGRRPV---ELLLDHGHLD------ARWCL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 252 IptlftHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDglsSNYKLDLFEEMKISLF--- 328
Cdd:cd01313 261 V-----HATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSD---SNARIDLLEELRQLEYsqr 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 329 --------MHSDAPLLefAKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLD----ATPTPELAIHLLL---HRYNV 393
Cdd:cd01313 333 lrdrarnvLATAGGSS--ARALLDAALAGGAQALGLATGALEAGARADLLSLDLDhpslAGALPDTLLDAWVfaaGDREV 410
|
....*...
gi 1277938128 394 SKVYINGK 401
Cdd:cd01313 411 RDVVVGGR 418
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
258-401 |
4.78e-17 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 82.35 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 258 HVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMH---SDAP 334
Cdd:PRK07228 255 HCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGAPCNNTLDPFTEMRQAALIQkvdRLGP 334
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277938128 335 LLEFAKALLKGATLDAAKALGL--NTGEIAVGKNADMIVLDLD---ATPTPELAI--HLLL--HRYNVSKVYINGK 401
Cdd:PRK07228 335 TAMPARTVFEMATLGGAKAAGFedEIGSLEEGKKADLAILDLDglhATPSHGVDVlsHLVYaaHGSDVETTMVDGK 410
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
58-353 |
3.75e-15 |
|
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: 75.06 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 58 LINAHVHLEFSANKTHLSYGDFISWLYSVIENREELIggcdtacmAQAIDSMLACGITTFGAVSSHGMDLQACADAPQNV 137
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELSPEDLYEDT--------LRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 138 IFFNELIGSQATMADALFNDFSARLDASKSVTRE--------GFHtGVAIHSPYSVHPV---LIKKALAIVKSEKLKLTA 206
Cdd:cd01292 73 EAARASAGIRVVLGLGIPGVPAAVDEDAEALLLEllrrglelGAV-GLKLAGPYTATGLsdeSLRRVLEEARKLGLPVVI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 207 HFMESKAEREwldksegDFKEFFESLLKQNTCVsdsaeflehfnaiptlFTHVVQANKSELSTLAKNGHTVIHCPISNRL 286
Cdd:cd01292 152 HAGELPDPTR-------ALEDLVALLRLGGRVV----------------IGHVSHLDPELLELLKEAGVSLEVCPLSNYL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 287 LGNE---TLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSdapLLEFAKALLKGATLDAAKA 353
Cdd:cd01292 209 LGRDgegAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLR---LGLSLEEALRLATINPARA 275
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
12-402 |
2.54e-14 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 73.84 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 12 SDSIVTERAIAFEK-TILKIAPLEELlqEFPHAKITTLAKNSLLMPGLINAHVHLEFSANKTH-LSYGDFISWLYSVIEN 89
Cdd:COG1228 22 GGGVIENGTVLVEDgKIAAVGPAADL--AVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVeFEAGGGITPTVDLVNP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 90 reeliggcdtacMAQAIDSMLACGITTfgavsshgmdlqaCADAPqnviffneliGSQATMADALfndfsarlDASKSVT 169
Cdd:COG1228 100 ------------ADKRLRRALAAGVTT-------------VRDLP----------GGPLGLRDAI--------IAGESKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 170 REG---FHTGVAIHSPYSVHPVLIKKALAIVKsEKLKLTAHFMESKAEREWLDKSEGDFKEFFESllkqntcvsdsaefl 246
Cdd:COG1228 137 LPGprvLAAGPALSLTGGAHARGPEEARAALR-ELLAEGADYIKVFAEGGAPDFSLEELRAILEA--------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 247 EHFNAIPtLFTHVVQAnkSELSTLAKNGHTVI-HCPisnrLLGNETlnIKELAENNIPWIVATDGLSSNYKLDLFEEMKI 325
Cdd:COG1228 201 AHALGLP-VAAHAHQA--DDIRLAVEAGVDSIeHGT----YLDDEV--ADLLAEAGTVVLVPTLSLFLALLEGAAAPVAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 326 SLF---------------------MHSDAP---------LLEFAKAL---------LKGATLDAAKALGL--NTGEIAVG 364
Cdd:COG1228 272 KARkvreaalanarrlhdagvpvaLGTDAGvgvppgrslHRELALAVeagltpeeaLRAATINAAKALGLddDVGSLEPG 351
|
410 420 430
....*....|....*....|....*....|....*...
gi 1277938128 365 KNADMIVLDLDatPTPELAihlllHRYNVSKVYINGKL 402
Cdd:COG1228 352 KLADLVLLDGD--PLEDIA-----YLEDVRAVMKDGRV 382
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
256-376 |
1.06e-12 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 69.33 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 256 FTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMH----- 330
Cdd:PRK12393 272 FAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADMLSEAHAAWLLHraegg 351
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1277938128 331 SDAPLLEfakALLKGATLDAAKALGLN-TGEIAVGKNADMIVLDLDA 376
Cdd:PRK12393 352 ADATTVE---DVVHWGTAGGARVLGLDaIGTLAVGQAADLAIYDLDD 395
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
258-401 |
1.17e-11 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 66.03 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 258 HVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDglsSNYKLDLFEEMKislfmhsdapLLE 337
Cdd:PRK09229 271 HATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGSD---SHVSIDLVEELR----------LLE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 338 F--------------------AKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDATPTPELAIHLLLHRY------ 391
Cdd:PRK09229 338 YgqrlrdrrrnvlaaaaqpsvGRRLFDAALAGGAQALGRAIGGLAVGARADLVVLDLDHPALAGREGDALLDRWvfaggd 417
|
170
....*....|.
gi 1277938128 392 -NVSKVYINGK 401
Cdd:PRK09229 418 aAVRDVWVAGR 428
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
27-379 |
3.74e-10 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 61.36 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 27 ILKIAPLEELLQEFP-HAKITTLaKNSLLMPGLINAHVH---LEFSAnkthlSYGD-FISWLysviENR---EEliggCD 98
Cdd:PRK09228 41 IVAAGPYAELRAQLPaDAEVTDY-RGKLILPGFIDTHIHypqTDMIA-----SYGEqLLDWL----NTYtfpEE----RR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 99 TACMAQA-------IDSMLACGITT---FGavSSHgmdlQACADApqnviFFNE-------LIGSQATM----ADALFND 157
Cdd:PRK09228 107 FADPAYArevaeffLDELLRNGTTTalvFG--TVH----PQSVDA-----LFEAaearnmrMIAGKVLMdrnaPDGLRDT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 158 FSARLDASKSVTREgFH----TGVAI---HSPYSVHPVLikKALAIVKSEK--LKLTAHFMESKAEREWLdksegdfKEF 228
Cdd:PRK09228 176 AESGYDDSKALIER-WHgkgrLLYAItprFAPTSTPEQL--EAAGALAREHpdVWIQTHLSENLDEIAWV-------KEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 229 FesllkqntcvSDSAEFL---EHFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIP 303
Cdd:PRK09228 246 F----------PEARDYLdvyERYGLLgpRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 304 WIVATD--GLSSnykLDLFEEM----KIS-LFMHSDAPLlefakALLKGATLDAAKALGLN--TGEIAVGKNADMIVLDL 374
Cdd:PRK09228 316 VGLGTDvgGGTS---FSMLQTMneayKVQqLQGYRLSPF-----QAFYLATLGGARALGLDdrIGNLAPGKEADFVVLDP 387
|
....*
gi 1277938128 375 DATPT 379
Cdd:PRK09228 388 AATPL 392
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
20-401 |
7.77e-10 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 60.33 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 20 AIAFE-KTILKIAPLEELLQEFPHAKITTlAKNSLLMPGLINAHVHLeFSAnkthLSYG---------DFISwlysVIEN 89
Cdd:PRK07203 23 AIAIEgNVIVEIGTTDELKAKYPDAEFID-AKGKLIMPGLINSHNHI-YSG----LARGmmanippppDFIS----ILKN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 90 ---------REELIGGCDTACMAQAIDsmlaCGITTFgavsshgMDLQACadapqnvifFNELIGSQATMADALFN---- 156
Cdd:PRK07203 93 lwwrldralTLEDVYYSALICSLEAIK----NGVTTV-------FDHHAS---------PNYIGGSLFTIADAAKKvglr 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 157 ------------------------DFSARLDASKSVTREGfHTGvaIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESK 212
Cdd:PRK07203 153 amlcyetsdrdgekelqegveeniRFIKHIDEAKDDMVEA-MFG--LHASFTLSDATLEKCREAVKETGRGYHIHVAEGI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 213 AEREwldksegdfkeffESLLKQNTcvsDSAEFLEHFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNrlLGNE 290
Cdd:PRK07203 230 YDVS-------------DSHKKYGK---DIVERLADFGLLgeKTLAAHCIYLSDEEIDLLKETDTFVVHNPESN--MGNA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 291 --TLNIKELAENNIPWIVATDGlssnYKLDLFEEMKISLFMHSDA--PLLE-----FAKALLKGATLdAAKALGLNTGEI 361
Cdd:PRK07203 292 vgYNPVLEMIKNGILLGLGTDG----YTSDMFESYKVANFKHKHAggDPNVgwpesPAMLFENNNKI-AERYFGAKFGIL 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1277938128 362 AVGKNADMIVLDLDAtPTP----ELAIHLL--LHRYNVSKVYINGK 401
Cdd:PRK07203 367 EEGAKADLIIVDYNP-PTPlnedNINGHILfgMNGGSVDTTIVNGK 411
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
176-401 |
7.66e-09 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 57.17 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 176 GVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESkaerewLDksEGDFkeffesllkqntCvsdsaefLEHFNAIP-- 253
Cdd:PRK08203 202 ALAPCSPFSVSRELMRESAALARRLGVRLHTHLAET------LD--EEAF------------C-------LERFGMRPvd 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 254 -----------TLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEE 322
Cdd:PRK08203 255 yledlgwlgpdVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNLIGE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 323 MKISLFMhsdAPLLEFAKAL-----LKGATLDAAKALGLN-TGEIAVGKNADMIVLDLDatptpELA---IH-----LLL 388
Cdd:PRK08203 335 ARQALLL---QRLRYGPDAMtareaLEWATLGGARVLGRDdIGSLAPGKLADLALFDLD-----ELRfagAHdpvaaLVL 406
|
250
....*....|....*.
gi 1277938128 389 ---HRynVSKVYINGK 401
Cdd:PRK08203 407 cgpPR--ADRVMVGGR 420
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
53-353 |
9.66e-08 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 52.79 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 53 LLMPGLINAHVHLefsankthlsyGDFIswLYSVIENR--EELIGGCDTA---CMAQAIDSMLACGITTFgAVSSHGMDL 127
Cdd:cd01305 1 ILIPALVNAHTHL-----------GDSA--IKEVGDGLplDDLVAPPDGLkhrLLAQADDRELAEAMRKV-LRDMRETGI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 128 QACADAPQNVIFFNELIGSQATMADALFNDFSARLDASKSVTREGFHT-GVAIHSPYSVHpvlIKKALAIVKSEKLKLTA 206
Cdd:cd01305 67 GAFADFREGGVEGIELLRRALGKLPVPFEVILGRPTEPDDPEILLEVAdGLGLSSANDVD---LEDILELLRRRGKLFAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 207 HFMESKAEREWLDksegdfkefFESLLKqntcvsdsaefLEhfnaiPTLFTHVVQANKSELSTLAKNGHTVIHCPISNRL 286
Cdd:cd01305 144 HASETRESVGMTD---------IERALD-----------LE-----PDLLVHGTHLTDEDLELVRENGVPVVLCPRSNLY 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277938128 287 LGNETLNIKELAENNIPWIVATDGLSSNyKLDLFEEMKislFMH--SDAPLLEFAKALLKGATLDAAKA 353
Cdd:cd01305 199 FGVGIPPVAELLKLGIKVLLGTDNVMVN-EPDMWAEME---FLAkySRLQGYLSPLEILRMATVNAAEF 263
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
253-371 |
1.09e-07 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 53.50 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 253 PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNyKLDLFEEMKISL-FMHS 331
Cdd:PRK07213 228 PDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTDNFMAN-SPSIFREMEFIYkLYHI 306
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1277938128 332 DApllefaKALLKGATLDAAKALGL-NTGEIAVGKNADMIV 371
Cdd:PRK07213 307 EP------KEILKMATINGAKILGLiNVGLIEEGFKADFTF 341
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
27-400 |
5.71e-07 |
|
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: 51.10 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 27 ILKIAPLEELLQEFPHAKITTLAKNSLLMPGLINAHVHLEFSANKTH--------LSYGDfISW-----LYSVIENREEl 93
Cdd:cd01296 8 IAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDefaarlagASYEE-ILAagggiLSTVRATRAA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 94 iggCDTACMAQA---IDSMLACGITTFGAVSSHGMDLQacadapqnviffNELigsqaTMADALfndfsARLDASKSVT- 169
Cdd:cd01296 86 ---SEDELFASAlrrLARMLRHGTTTVEVKSGYGLDLE------------TEL-----KMLRVI-----RRLKEEGPVDl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 170 REGFHTGVAIHSPYSVHP----VLIKKALAIVKSEKLkltAHFMESKAErewldksEGDFKeffesllkqntcVSDSAEF 245
Cdd:cd01296 141 VSTFLGAHAVPPEYKGREeyidLVIEEVLPAVAEENL---ADFCDVFCE-------KGAFS------------LEQSRRI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 246 L--------------EHFNAIP----------TLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENN 301
Cdd:cd01296 199 LeaakeaglpvkihaDELSNIGgaelaaelgaLSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 302 IPWIVATDGLSSNYKLDlfeemKISLFMHsdaplleFAKALLK--------GATLDAAKALGL--NTGEIAVGKNADMIV 371
Cdd:cd01296 279 VPVALGTDFNPGSSPTS-----SMPLVMH-------LACRLMRmtpeealtAATINAAAALGLgeTVGSLEVGKQADLVI 346
|
410 420 430
....*....|....*....|....*....|
gi 1277938128 372 LDldaTPTP-ELAIHLLLHryNVSKVYING 400
Cdd:cd01296 347 LD---APSYeHLAYRFGVN--LVEYVIKNG 371
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
318-406 |
2.16e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 49.62 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 318 DLFEEMKISLFMH----------------SDAPLLefAKALLKGATLDAAKALGLN--TGEIAVGKNADMIVL---DLDA 376
Cdd:PRK08204 309 DMFTQMRFALQAErardnavhlreggmppPRLTLT--ARQVLEWATIEGARALGLEdrIGSLTPGKQADLVLIdatDLNL 386
|
90 100 110
....*....|....*....|....*....|..
gi 1277938128 377 TPT--PELAIHLLLHRYNVSKVYINGKLEKGN 406
Cdd:PRK08204 387 APVhdPVGAVVQSAHPGNVDSVMVAGRAVKRN 418
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
294-401 |
1.70e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 46.76 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 294 IKELAENNIPWIVATDGLssnykLDLFEEMK--ISLFMHSDAPLLEFAKA--------LLKGATLDAAKALGL--NTGEI 361
Cdd:pfam07969 351 VKELLNAGVKVALGSDAP-----VGPFDPWPriGAAVMRQTAGGGEVLGPdeelsleeALALYTSGPAKALGLedRKGTL 425
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1277938128 362 AVGKNADMIVLDLDATPTPELAIHLLLhrynVSKVYINGK 401
Cdd:pfam07969 426 GVGKDADLVVLDDDPLTVDPPAIADIR----VRLTVVDGR 461
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
267-376 |
2.20e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 46.57 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 267 LSTLAKNGHTVIHCPI-SNRllGNETLN-IKELAENNIPWIVATDglssNYKLDLFEEMKISLfMH-------SDAPlle 337
Cdd:PRK06151 295 LALLAEHGVSIVHCPLvSAR--HGSALNsFDRYREAGINLALGTD----TFPPDMVMNMRVGL-ILgrvvegdLDAA--- 364
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1277938128 338 FAKALLKGATLDAAKALGL-NTGEIAVGKNADMIVLDLDA 376
Cdd:PRK06151 365 SAADLFDAATLGGARALGRdDLGRLAPGAKADIVVFDLDG 404
|
|
| PLN02795 |
PLN02795 |
allantoinase |
6-65 |
2.93e-05 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 45.92 E-value: 2.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277938128 6 PHFILMSDSIVTERAI---AFE---KTILKIAPLEELLQEFPHAKITTLaKNSLLMPGLINAHVHL 65
Cdd:PLN02795 44 PHFVLYSKRVVTPAGVipgAVEvegGRIVSVTKEEEAPKSQKKPHVLDY-GNAVVMPGLIDVHVHL 108
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
295-402 |
8.08e-05 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 44.22 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 295 KELAENNIPWIVATDgLSSNYKLDLFEE-------------MKISLfmHSDAP-------LLEFAKAL---------LKG 345
Cdd:cd01309 232 DELAKHGIPVIYGPT-LTLPKKVEEVNDaidtnayllkkggVAFAI--SSDHPvlnirnlNLEAAKAVkyglsyeeaLKA 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277938128 346 ATLDAAKALGLN--TGEIAVGKNADMIVLD---LDATPTPELaihlllhrynvskVYINGKL 402
Cdd:cd01309 309 ITINPAKILGIEdrVGSLEPGKDADLVVWNgdpLEPTSKPEQ-------------VYIDGRL 357
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
346-401 |
2.23e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 43.16 E-value: 2.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1277938128 346 ATLDAAKALGL--NTGEIAVGKNADMIVLDldatptpelaihlllHRYNVSKVYINGK 401
Cdd:COG1820 331 ASLNPARALGLddRKGSIAPGKDADLVVLD---------------DDLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
343-400 |
2.24e-04 |
|
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: 42.95 E-value: 2.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 343 LKGATLDAAKALGLN--TGEIAVGKNADMIVLDLDatptpelaihlllhrYNVSKVYING 400
Cdd:cd00854 330 VRMASLNPAKLLGLDdrKGSLKPGKDADLVVLDDD---------------LNVKATWING 374
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
343-401 |
2.44e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 43.25 E-value: 2.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277938128 343 LKGATLDAAKALGL--NTGEIAVGKNADMIVLDLDATPTPELAIHLLlhryNVSKVYINGK 401
Cdd:COG1574 473 LRAYTIGAAYAAFEedEKGSLEPGKLADFVVLDRDPLTVPPEEIKDI----KVLLTVVGGR 529
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
343-375 |
2.41e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 39.58 E-value: 2.41e-03
10 20 30
....*....|....*....|....*....|....*
gi 1277938128 343 LKGATLDAAKALGL--NTGEIAVGKNADMIVLDLD 375
Cdd:cd01299 300 LRAATANAAELLGLsdELGVIEAGKLADLLVVDGD 334
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
346-402 |
3.34e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 39.70 E-value: 3.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1277938128 346 ATLDAAKALGL-NTGEIAVGKNADMIVLDlDatptpelaihllLHRYNVSKVYINGKL 402
Cdd:COG1001 293 ATLNAAEHFGLkDLGAIAPGRRADIVLLD-D------------LEDFKVEKVYADGKL 337
|
|
|