|
Name |
Accession |
Description |
Interval |
E-value |
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
13-376 |
1.53e-70 |
|
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: 227.02 E-value: 1.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 13 ILRRSRTLLTRNPARPVIDNGAILEANGMICAVGKYGELSQTHH-ARLVDEGETVLLPGLINAHTHTELSHLRDRIqPGG 91
Cdd:COG0402 2 LLIRGAWVLTMDPAGGVLEDGAVLVEDGRIAAVGPGAELPARYPaAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLA-DDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 92 GFEDWVAQLLALPARDLDTKAV----SKAIDEMAAGQICAVGDISGNNPQAMASLWRQSD-----LHALLWVEQIGFAP- 161
Cdd:COG0402 81 PLLDWLEEYIWPLEARLDPEDVyagaLLALAEMLRSGTTTVADFYYVHPESADALAEAAAeagirAVLGRGLMDRGFPDg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 162 LPQGQPRGLPDAGA---------TPKLRVAPAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIEFlttgrgpfg 232
Cdd:COG0402 161 LREDADEGLADSERlierwhgaaDGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEW--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 233 amlTKRLVPKSfsppglhPVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAG 312
Cdd:COG0402 232 ---VLELYGKR-------PVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAG 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257798586 313 VPLCLGTDSLASNWDLDLWQE---AWYIAQHWSG---TLTLDKLVSFMTTTPARILGLP-RLGRLAPGKRA 376
Cdd:COG0402 302 VRVGLGTDGAASNNSLDMFEEmrlAALLQRLRGGdptALSAREALEMATLGGARALGLDdEIGSLEPGKRA 372
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
19-391 |
1.53e-43 |
|
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: 156.21 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 19 TLLTRNPARpVIDNGAILEANGMICAVGKYGELSQTHHARLVDEGETVLLPGLINAHTHTELSHLRDrIQPGGGFEDWVA 98
Cdd:cd01298 7 TIVTTDPRR-VLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRG-LADDLPLMEWLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 99 QLLALPARDLDTKAV---SK-AIDEMAAGQICAVGDISGNNPQAMASLWRQSDLHALLWVEQIGFA-PLPQGQPRGLPDA 173
Cdd:cd01298 85 DLIWPLERLLTEEDVylgALlALAEMIRSGTTTFADMYFFYPDAVAEAAEELGIRAVLGRGIMDLGtEDVEETEEALAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 174 ---------GATPKLRVAPAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIEFlttgrgpfgamltkrlVPKSF 244
Cdd:cd01298 165 erlirewhgAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEE----------------SLEKY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 245 sppGLHPVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTDSLAS 324
Cdd:cd01298 229 ---GKRPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGAAS 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257798586 325 NWDLDLWQE---AWYI--AQHWSGT-LTLDKLVSFMTTTPARILGLPRLGRLAPGKRAVYARLSLEKANRLPL 391
Cdd:cd01298 306 NNNLDMFEEmrlAALLqkLAHGDPTaLPAEEALEMATIGGAKALGLDEIGSLEVGKKADLILIDLDGPHLLPV 378
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
40-384 |
1.49e-42 |
|
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: 152.99 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 40 GMICAVGKYGEL-SQTHHARLVDEGETVLLPGLINAHTHTELSHLRDRIQPGGgFEDWVAQLLALPARDLDT---KAVSK 115
Cdd:cd01312 1 DKILEVGDYEKLeKRYPGAKHEFFPNGVLLPGLINAHTHLEFSANVAQFTYGR-FRAWLLSVINSRDELLKQpweEAIRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 116 AIDEMAAGQICAVGDIS--GNNPQAMASlwrqSDLHALLWVEQIGFAP---------LPQGQPRGLPDAGATPKLRVAPa 184
Cdd:cd01312 80 GIRQMLESGTTSIGAISsdGSLLPALAS----SGLRGVFFNEVIGSNPsaidfkgetFLERFKRSKSFESQLFIPAISP- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 185 gHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIEFLTTGRGPFG---AMLTKRLVPKSFSPPglhpVAYADSLGLL 261
Cdd:cd01312 155 -HAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKhfwESFLKLPKPKKLATA----IDFLDMLGGL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 262 DSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTDSLASNWDLDLWQEAWYIAQHW 341
Cdd:cd01312 230 GTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLH 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 257798586 342 SGTLTLD---KLVSFMTTTPARILGLpRLGRLAPGKRAVYARLSLE 384
Cdd:cd01312 310 PEEDLLElasELLLMATLGGARALGL-NNGEIEAGKRADFAVFELP 354
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
20-391 |
5.43e-30 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 119.30 E-value: 5.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 20 LLTRNPARPVIDNGAILeANGMICAVGKYGELSQTH-HARLVDEGETVLLPGLINAHTHTELS----HLRdriqpGGGFE 94
Cdd:PRK08418 9 IFTCDENFEILEDGAVV-FDDKILEIGDYENLKKKYpNAKIQFFKNSVLLPAFINPHTHLEFSanktTLD-----YGDFI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 95 DWVAQLLAlpARDL-----DTKAVSKAIDEMAAGQICAVGDIS--GNNPQAMASlwrqSDLHALLWVEQIGFAP------ 161
Cdd:PRK08418 83 PWLGSVIN--HREDllekcKGALIQQAINEMLKSGVGTIGAISsfGIDLEICAK----SPLRVVFFNEILGSNAsavdel 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 162 -------LPQGQprglpdAGATPKLRVAPAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIEFLTTGRGPFGAM 234
Cdd:PRK08418 157 yqdflarFEESK------KFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 235 LTKRL-VPKSFSPPglhpvayADSLGLL-DSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAG 312
Cdd:PRK08418 231 FEKFLkEPKPLYTP-------KEFLELFkGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 313 VPLCLGTDSLASNWDLDLWQE--AWYIAQHWSGTLTLDK-LVSFMTTTPARILGLPrLGRLAPGKRAVYARLSLE----K 385
Cdd:PRK08418 304 INYSIATDGLSSNISLSLLDElrAALLTHANMPLLELAKiLLLSATRYGAKALGLN-NGEIKEGKDADLSVFELPeectK 382
|
....*.
gi 257798586 386 ANRLPL 391
Cdd:PRK08418 383 KEQLPL 388
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
28-376 |
3.94e-29 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 117.32 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 28 PVIDNGAILE------ANGMICAVGKYGELSQTHHAR-LVDEGETVLLPGLINAHTHTELSHLRdriqpggGFED----- 95
Cdd:PRK09045 18 PVEPAGVVLEdhavaiRDGRIVAILPRAEARARYAAAeTVELPDHVLIPGLINAHTHAAMSLLR-------GLADdlplm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 96 -WVAQLLaLPArdlDTKAVSK---------AIDEMAAGQICAVGDISgNNPQAMASLWRQSDLHALLWVEQIGFaPLPQG 165
Cdd:PRK09045 91 tWLQDHI-WPA---EGAWVSEefvrdgtllAIAEMLRGGTTCFNDMY-FFPEAAAEAAHQAGMRAQIGMPVLDF-PTAWA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 166 QP------RGLP---DAGATPKLRVAPAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIEflttgrgpfgamlt 236
Cdd:PRK09045 165 SDadeylaKGLElhdQWRHHPLISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIA-------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 237 krlvpKSFSPPGLHPVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLC 316
Cdd:PRK09045 231 -----DSLKQHGQRPLARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVA 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257798586 317 LGTDSLASNWDLDLWQE---AWYIAQHWSGTLT-LD--KLVSFMTTTPARILGL-PRLGRLAPGKRA 376
Cdd:PRK09045 306 LGTDGAASNNDLDLFGEmrtAALLAKAVAGDATaLPahTALRMATLNGARALGLdDEIGSLEPGKQA 372
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
66-376 |
4.61e-27 |
|
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: 109.90 E-value: 4.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 66 VLLPGLINAHTHTELSHLRDRIQPGG----GFEDWVAQLL------ALPARDLDTKAVS---KAIDEMAAGQICAVGDIS 132
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEfayeALRLGITTMLksgtttVLDMGATTSTGIEallEAAEELPLGLRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 133 GNnpqamaslWRQSDLHALLWVEQIgfAPLPqgqprGLPDAGATPKLRVAPAGHALYSTSPETLRQTKAWCRSHELPFSL 212
Cdd:pfam01979 81 LD--------TDGELEGRKALREKL--KAGA-----EFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 213 HLAEHSGEIEfLTTGRGPFGAMLTkrlvpksfsppglHPVAYADSLGLLDSSTLV-VHAVHLDPGHPHLIAHR--GSTVC 289
Cdd:pfam01979 146 HALETKGEVE-DAIAAFGGGIEHG-------------THLEVAESGGLLDIIKLIlAHGVHLSPTEANLLAEHlkGAGVA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 290 LCPRSNDFIGVGR-ALWEALDaAGVPLCLGTDSLASNWDLDLWQE---AWYIAQHWSGTLTLDKLVSFMTTTPARILGLP 365
Cdd:pfam01979 212 HCPFSNSKLRSGRiALRKALE-DGVKVGLGTDGAGSGNSLNMLEElrlALELQFDPEGGLSPLEALRMATINPAKALGLD 290
|
330
....*....|..
gi 257798586 366 -RLGRLAPGKRA 376
Cdd:pfam01979 291 dKVGSIEVGKDA 302
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
20-376 |
1.55e-21 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 95.46 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 20 LLTRNPARPVIDNGAILEANGMICAVGKYGELSQTHHARLVDEGETVLLPGLINAHTHTELSHLRDrIQPGGGFEDWVAQ 99
Cdd:PRK06687 9 IVTCDQDFHVYLDGILAVKDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRG-IRDDSNLHEWLND 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 100 LLaLPAR-----DLDTKAVSKAIDEMAAGQICAVGDI---SGNNPQAMASLWRQSDLHAL----LWVEQIGFAPLPQGQP 167
Cdd:PRK06687 88 YI-WPAEseftpDMTTNAVKEALTEMLQSGTTTFNDMynpNGVDIQQIYQVVKTSKMRCYfsptLFSSETETTAETISRT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 168 RGLPD---AGATPKLRVAPAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEieflttgrgpfGAMLTKRLvpksf 244
Cdd:PRK06687 167 RSIIDeilKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEE-----------SGIILKRY----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 245 sppGLHPVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTDSLAS 324
Cdd:PRK06687 231 ---GKRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVAS 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 257798586 325 NWDLDLWQE---AWYIAQHWSG---TLTLDKLVSFMTTTPARILGLP-RLGRLAPGKRA 376
Cdd:PRK06687 308 NNNLDMFEEgrtAALLQKMKSGdasQFPIETALKVLTIEGAKALGMEnQIGSLEVGKQA 366
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
171-376 |
3.11e-18 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 85.89 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 171 PDAGATPKLRVAPAGhALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIEFLttgRGPFGamltkrlvpksfsppgLH 250
Cdd:PRK12393 196 ASPDSLRRVVVAPTT-PTFSLPPELLREVARAARGMGLRLHSHLSETVDYVDFC---REKYG----------------MT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 251 PVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTDSLASNWDLDL 330
Cdd:PRK12393 256 PVQFVAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADM 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 257798586 331 WQE---AWYI--AQHWSGTLTLDKLVSFMTTTPARILGLPRLGRLAPGKRA 376
Cdd:PRK12393 336 LSEahaAWLLhrAEGGADATTVEDVVHWGTAGGARVLGLDAIGTLAVGQAA 386
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
172-376 |
9.02e-18 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 84.52 E-value: 9.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 172 DAGATPKLRVAPAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIEFLttgRGPFgamltkrlvpksfsppGLHP 251
Cdd:PRK08203 192 DPGPGAMLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFC---LERF----------------GMRP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 252 VAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTDSLASNWDLDLW 331
Cdd:PRK08203 253 VDYLEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNLI 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 257798586 332 QE---AWYIAQHWSG--TLTLDKLVSFMTTTPARILGLPRLGRLAPGKRA 376
Cdd:PRK08203 333 GEarqALLLQRLRYGpdAMTAREALEWATLGGARVLGRDDIGSLAPGKLA 382
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
17-388 |
1.23e-17 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 83.95 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 17 SRTLLTRNPARPVIDNGAILEANGMICAVgKYGELSQTHHA-RLVDEGETVLLPGLINAHTHTELSHLRD-----RIQPG 90
Cdd:PRK15493 7 NATIVTMNEQNEVIENGYIIVENDQIIDV-NSGEFASDFEVdEVIDMKGKWVLPGLVNTHTHVVMSLLRGigddmLLQPW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 91 GGFEDWVAQLLALParDLDTKAVSKAIDEMAAGQICAVGDI---SGNNPQAMASLWRQSDLHALLWVEQIGFAPlPQGQP 167
Cdd:PRK15493 86 LETRIWPLESQFTP--ELAVASTELGLLEMVKSGTTSFSDMfnpIGVDQDAIMETVSRSGMRAAVSRTLFSFGT-KEDEK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 168 RGLPDAGATPK--------LRVAPAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIeflttgrgpfgamltkRL 239
Cdd:PRK15493 163 KAIEEAEKYVKryynesgmLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREV----------------RD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 240 VPKSFsppGLHPVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGT 319
Cdd:PRK15493 227 IEAQY---GKRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIAT 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257798586 320 DSLASNWDLDLWQEAwYIAQ------HWSGT-LTLDKLVSFMTTTPARILGLPRLGRLAPGKRAVYarLSLEKANR 388
Cdd:PRK15493 304 DSVASNNNLDMFEEM-RIATllqkgiHQDATaLPVETALTLATKGAAEVIGMKQTGSLEVGKCADF--ITIDPSNK 376
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
23-390 |
1.36e-16 |
|
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: 80.96 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 23 RNPARPVIDNGAILEANGMICAVGkygelsqthharlVDEGETVLLPGLINAHTHTELSHLRDRIQPGGG----FEDWVA 98
Cdd:cd01313 9 RNVRIEVDADGRIAAVNPDTATEA-------------VALLGGALLPGMPNLHSHAFQRAMAGLTEYRGSaadsFWTWRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 99 QLLALPAR----DLDTKAVSKAIdEMAAGQICAVG-------DISGN---NPQAMASLWRQSDLHA-----LLWV--EQI 157
Cdd:cd01313 76 LMYRFAARltpeQIEAIARQLYI-EMLLAGITAVGefhyvhhDPDGTpyaDPAELAQRVIAAASDAgigitLLPVlyARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 158 GF--APLPQGQPR----------GLPDAGATPK----LRVAPAGHALYSTSPETLRQTKAWCrSHELPFSLHLAEHSGEI 221
Cdd:cd01313 155 GFggPAPNPGQRRfingyedflgLLEKALRAVKehaaARIGVAPHSLRAVPAEQLAALAALA-SEKAPVHIHLAEQPKEV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 222 EFLTTGRGPfgamltkrlvpksfsppglHPVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVG 301
Cdd:cd01313 234 DDCLAAHGR-------------------RPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 302 RALWEALDAAGVPLCLGTDSLASnwdLDLWQEA----------------WYIAQHWSGtltlDKLVSFMTTTPARILGLP 365
Cdd:cd01313 295 IFPAAALLAAGGRIGIGSDSNAR---IDLLEELrqleysqrlrdrarnvLATAGGSSA----RALLDAALAGGAQALGLA 367
|
410 420
....*....|....*....|....*...
gi 257798586 366 rLGRLAPGKRAVYARLSLEK---ANRLP 390
Cdd:cd01313 368 -TGALEAGARADLLSLDLDHpslAGALP 394
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
19-376 |
3.11e-16 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 79.62 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 19 TLLTrNPARPVIDNGAILEANGMICAVGKYGELSQTHHARLVDEGETVLLPGLINAHTHTELSHLR-DRIQPGGGFEDWV 97
Cdd:COG1228 16 TLVD-GTGGGVIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRaVEFEAGGGITPTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 98 AqlLALPArdldtkavSKAIDEMAAGQICAVGDISGNNPQAMASLwrQSDLHALLWVEQIGFAPLPQGQPRGLPDAG--- 174
Cdd:COG1228 95 D--LVNPA--------DKRLRRALAAGVTTVRDLPGGPLGLRDAI--IAGESKLLPGPRVLAAGPALSLTGGAHARGpee 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 175 ATPKLRVA----------PAGHALYSTSPETLRQTKAWCRSHELPFSLHLaehsgeieflttgrgpfgamltkrlvpksf 244
Cdd:COG1228 163 ARAALRELlaegadyikvFAEGGAPDFSLEELRAILEAAHALGLPVAAHA------------------------------ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 245 spPGLHPVAYADSLGLlDSstlVVHAVHLDPGHPHLIAHRGsTVCLCP------------------RSNDFIGVGRALWE 306
Cdd:COG1228 213 --HQADDIRLAVEAGV-DS---IEHGTYLDDEVADLLAEAG-TVVLVPtlslflallegaaapvaaKARKVREAALANAR 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257798586 307 ALDAAGVPLCLGTDSLA-SNWDLDLWQEAWYIAQHwsGtLTLDKLVSFMTTTPARILGLP-RLGRLAPGKRA 376
Cdd:COG1228 286 RLHDAGVPVALGTDAGVgVPPGRSLHRELALAVEA--G-LTPEEALRAATINAAKALGLDdDVGSLEPGKLA 354
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
30-391 |
6.30e-16 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 79.02 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 30 IDNGAILEANGMICAVGkygELSQTHHARLVDEGETVLLPGLINAHTHTELSHLR---DRIQPGGGFEDWVaqllaLPAR 106
Cdd:PRK06038 19 LKKGSVVIEDGTITEVS---ESTPGDADTVIDAKGSVVMPGLVNTHTHAAMTLFRgyaDDLPLAEWLNDHI-----WPAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 107 DLDTKAVSKAIDEMAAGQICAVGDISGNN----PQAMASLWRQSDLHALL-------WVEQIGFAPLPQGQpRGLPD--A 173
Cdd:PRK06038 91 AKLTAEDVYAGSLLACLEMIKSGTTSFADmyfyMDEVAKAVEESGLRAALsygmidlGDDEKGEAELKEGK-RFVKEwhG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 174 GATPKLRVAPAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIEflttgrgpfgAMLTKRlvpksfsppGLHPVA 253
Cdd:PRK06038 170 AADGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELN----------QMKEQY---------GMCSVN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 254 YADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTDSLASNWDLDLWQE 333
Cdd:PRK06038 231 YLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDGCASNNNLDMFEE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257798586 334 AWYIA------QHWSGTLTLDKLVSFMTTTPARILGLpRLGRLAPGKRAVYARLSLEKANRLPL 391
Cdd:PRK06038 311 MKTAAllhkvnTMDPTALPARQVLEMATVNGAKALGI-NTGMLKEGYLADIIIVDMNKPHLTPV 373
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
176-391 |
5.18e-15 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 75.99 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 176 TPKLRVAPAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHSGEIEflttgrgpfgaMLTKRLvpksfsppGLHPVAYA 255
Cdd:PRK08393 171 SPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIK-----------QIREKY--------GKSPVVLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 256 DSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTDSLASNWDLDLWQEAW 335
Cdd:PRK08393 232 DEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDMLREMK 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257798586 336 YIA-----QHWSGTLTLDKLVSFMTT-TPARILGLpRLGRLAPGKRAVYARLSLEKANRLPL 391
Cdd:PRK08393 312 LAAllhkvHNLDPTIADAETVFRMATqNGAKALGL-KAGVIKEGYLADIAVIDFNRPHLRPI 372
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
11-391 |
1.70e-14 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 74.65 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 11 TPILRRSRTLLTRNPARPVIDnGAILEANGMICAVGKYGELsqTHHARLVDEGETVLLPGLINAHTH------------T 78
Cdd:PRK07228 1 MTILIKNAGIVTMNAKREIVD-GDVLIEDDRIAAVGDRLDL--EDYDDHIDATGKVVIPGLIQGHIHlcqtlfrgiaddL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 79 EL-SHLRDRIQPGGGFED----WVAQLLAL---------PARDLDTKAVSKAIDEmAAGQIC--AVG-----DISGNNPQ 137
Cdd:PRK07228 78 ELlDWLKDRIWPLEAAHDaesmYYSALLGIgeliesgttTIVDMESVHHTDSAFE-AAGESGirAVLgkvmmDYGDDVPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 138 AM-----ASLwRQSDlhALL--WveqigfaplpQGQPRGLPDAGATPKLRVapaghalySTSPETLRQTKAWCRSHELPF 210
Cdd:PRK07228 157 GLqedteASL-AESV--RLLekW----------HGADNGRIRYAFTPRFAV--------SCTEELLRGVRDLADEYGVRI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 211 SLHLAEHSGEIEFLTTGRGpfgamltkrlvpksfsppgLHPVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCL 290
Cdd:PRK07228 216 HTHASENRGEIETVEEETG-------------------MRNIHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 291 CPRSNDFIGVGRA-LWEALDaAGVPLCLGTDSLASNWDLDLWQE---AWYIA---QHWSGTLTLDKLVSFMTTTPARILG 363
Cdd:PRK07228 277 CPSSNLKLASGIApVPDLLE-RGINVALGADGAPCNNTLDPFTEmrqAALIQkvdRLGPTAMPARTVFEMATLGGAKAAG 355
|
410 420
....*....|....*....|....*....
gi 257798586 364 LP-RLGRLAPGKRAVYARLSLEKANRLPL 391
Cdd:PRK07228 356 FEdEIGSLEEGKKADLAILDLDGLHATPS 384
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
71-361 |
3.00e-14 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 72.37 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 71 LINAHTHTELSHLRDRIQPGGGFEDWVAQLLALPARDLdtkavsKAIDEMAAGQICAVGDISGNNP--------QAMASL 142
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELSPEDLYEDTL------RALEALLAGGVTTVVDMGSTPPptttkaaiEAVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 143 WRQSDLHALLWVEQIGFAPLPQGQPRGLPDAGATPKLRVAPA-GHALYS------TSPETLRQTKAWCRSHELPFSLHLA 215
Cdd:cd01292 75 ARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAvGLKLAGpytatgLSDESLRRVLEEARKLGLPVVIHAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 216 EhsgeieflttgrGPFGAMLTKRLVpksfsppglhpvayadSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSN 295
Cdd:cd01292 155 E------------LPDPTRALEDLV----------------ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSN 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257798586 296 DFIGVGRALWEALDAA---GVPLCLGTDSLASNWDLDLWQEAWYIAQHWSGTLTLDKLVSFMTTTPARI 361
Cdd:cd01292 207 YLLGRDGEGAEALRRLlelGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLGLSLEEALRLATINPARA 275
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
19-320 |
9.38e-13 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 69.19 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 19 TLLTRNPARPVIDNGAILEANGMICAVGKYGELSQTH-HARLVDEGETVLLPGLINAHTHTELSHLRDRIQPGGGFEDWV 97
Cdd:PRK07203 8 TAITRDPAKPVIEDGAIAIEGNVIVEIGTTDELKAKYpDAEFIDAKGKLIMPGLINSHNHIYSGLARGMMANIPPPPDFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 98 AQLLALPARdLDtkavsKAIDE---MAAGQICAVGDI-SG--------NNPQAMA-SLWRQSD------LHALLWV---- 154
Cdd:PRK07203 88 SILKNLWWR-LD-----RALTLedvYYSALICSLEAIkNGvttvfdhhASPNYIGgSLFTIADaakkvgLRAMLCYetsd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 155 ------------EQIGFAPLPQGQPRGLPDA--GAtpklrvapagHALYSTSPETLRQTKAWCRSHELPFSLHLAEhsgE 220
Cdd:PRK07203 162 rdgekelqegveENIRFIKHIDEAKDDMVEAmfGL----------HASFTLSDATLEKCREAVKETGRGYHIHVAE---G 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 221 IEFLTTGRGPFGAMLTKRLvpksfsppglhpvayaDSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGV 300
Cdd:PRK07203 229 IYDVSDSHKKYGKDIVERL----------------ADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAV 292
|
330 340
....*....|....*....|
gi 257798586 301 GRALWEALDAAGVPLCLGTD 320
Cdd:PRK07203 293 GYNPVLEMIKNGILLGLGTD 312
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
13-376 |
1.09e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 68.88 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 13 ILRRSRTLLTRNPARPVIDNGAILEANGMICAVGkygELSQTHHARLVDEGETVLLPGLINAHTHTELSHLRDrIQPG-- 90
Cdd:PRK08204 4 TLIRGGTVLTMDPAIGDLPRGDILIEGDRIAAVA---PSIEAPDAEVVDARGMIVMPGLVDTHRHTWQSVLRG-IGADwt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 91 ---------GGF-------EDWVAQLL-ALPARDLDTKAV-------------SKAIDEMAAGQICAVgdISGNNPQAMA 140
Cdd:PRK08204 80 lqtyfreihGNLgpmfrpeDVYIANLLgALEALDAGVTTLldwshinnspehaDAAIRGLAEAGIRAV--FAHGSPGPSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 141 SLWRQSDLHALLWVEQIgfaplpqgQPRGLPDAGATPKLRVAPAGHAlySTSPETLRQTKAWCRSHELPFSLHLaehsge 220
Cdd:PRK08204 158 YWPFDSVPHPREDIRRV--------KKRYFSSDDGLLTLGLAIRGPE--FSSWEVARADFRLARELGLPISMHQ------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 221 ieflttGRGPFGAmltkrlvpksfsPPGLhpVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGV 300
Cdd:PRK08204 222 ------GFGPWGA------------TPRG--VEQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGH 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 301 GRALWEALDAAGVPLCLGTDSLAS-NWDL------DLW-QEAWYIAQHWSG--------TLTLDKLVSFMTTTPARILGL 364
Cdd:PRK08204 282 GYPVTGRLLAHGVRPSLGVDVVTStGGDMftqmrfALQaERARDNAVHLREggmppprlTLTARQVLEWATIEGARALGL 361
|
410
....*....|...
gi 257798586 365 P-RLGRLAPGKRA 376
Cdd:PRK08204 362 EdRIGSLTPGKQA 374
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
13-391 |
3.12e-12 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 67.60 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 13 ILRRSRTLLTRNPARPVIDNGAILEANgMICAVGKYGELSQThharLVDEGETVLLPGLINAHTHTELSHLRdriqpgGG 92
Cdd:PRK06380 3 ILIKNAWIVTQNEKREILQGNVYIEGN-KIVYVGDVNEEADY----IIDATGKVVMPGLINTHAHVGMTASK------GL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 93 FEDWVAQLLALPARDLDTKAVSKAI--------DEMAAGQICAVGDISgNNPQAMASLWRQSDLHALL-WV-------EQ 156
Cdd:PRK06380 72 FDDVDLEEFLMKTFKYDSKRTREGIynsaklgmYEMINSGITAFVDLY-YSEDIIAKAAEELGIRAFLsWAvldeeitTQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 157 IGfAPLPQGQprGLPDAGATPKLRVAPAG-HALYSTSPETLRQTKAWCRSHELPFSLHLAEhsgeieflttgrgpfgaml 235
Cdd:PRK06380 151 KG-DPLNNAE--NFIREHRNEELVTPSIGvQGIYVANDETYLKAKEIAEKYDTIMHMHLSE------------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 236 TKRLVPKSFSPPGLHPVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVG--RALWEALDAaGV 313
Cdd:PRK06380 209 TRKEVYDHVKRTGERPVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGgsPPIPEMLDN-GI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 314 PLCLGTDSLASNWDLDLWQEAWYIA-----QHWSGTLT-LDKLVSFMTTTPARILGLpRLGRLAPGKRAVYARLSLEKAN 387
Cdd:PRK06380 288 NVTIGTDSNGSNNSLDMFEAMKFSAlsvknERWDASIIkAQEILDFATINAAKALEL-NAGSIEVGKLADLVILDARAPN 366
|
....
gi 257798586 388 RLPL 391
Cdd:PRK06380 367 MIPT 370
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
176-376 |
5.39e-12 |
|
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: 66.92 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 176 TPklRVAPaghalySTSPETLRQTKAWCRSH-ELPFSLHLAEHSGEIEFlttgrgpfgamlTKRLVPKSFSppglhpvaY 254
Cdd:cd01303 198 TP--RFAP------SCSEELLAALGKLAKEHpDLHIQTHISENLDEIAW------------VKELFPGARD--------Y 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 255 ADSL---GLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTD-------SLas 324
Cdd:cd01303 250 LDVYdkyGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDvgggtsfSM-- 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 257798586 325 nwdLDLWQEAWYIAQH------WSGTLTLDKLVSFMTTTPARILGLP-RLGRLAPGKRA 376
Cdd:cd01303 328 ---LDTLRQAYKVSRLlgyelgGHAKLSPAEAFYLATLGGAEALGLDdKIGNFEVGKEF 383
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
66-338 |
2.34e-11 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 63.57 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 66 VLLPGLINAHTHTELSHLRDrIQPGGGFEDWVAqllalPARDLDTKAVSKAIDEMAAGQICAVGDISGNNPQAMASLWRQ 145
Cdd:cd01305 1 ILIPALVNAHTHLGDSAIKE-VGDGLPLDDLVA-----PPDGLKHRLLAQADDRELAEAMRKVLRDMRETGIGAFADFRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 146 SDLHALLWV-EQIGFAPLPQGQPRGLPDA--GATPKLRVApAGHALYSTSPETLRQTKAWCRSHELPFSLHLAEHS---- 218
Cdd:cd01305 75 GGVEGIELLrRALGKLPVPFEVILGRPTEpdDPEILLEVA-DGLGLSSANDVDLEDILELLRRRGKLFAIHASETResvg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 219 -GEIEflttgrgpfgamltkrlvpksfsppglhpvaYADSLGlldsSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDF 297
Cdd:cd01305 154 mTDIE-------------------------------RALDLE----PDLLVHGTHLTDEDLELVRENGVPVVLCPRSNLY 198
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 257798586 298 IGVGRALWEALDAAGVPLCLGTDSLASNwDLDLWQEAWYIA 338
Cdd:cd01305 199 FGVGIPPVAELLKLGIKVLLGTDNVMVN-EPDMWAEMEFLA 238
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
176-376 |
2.43e-10 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 61.75 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 176 TPklRVAPaghalySTSPETLRQTKAWCRSH-ELPFSLHLAEHSGEIEFlttgrgpfgamlTKRLVPKSFSppglhpvaY 254
Cdd:PRK09228 201 TP--RFAP------TSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAW------------VKELFPEARD--------Y 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 255 AD---SLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTD-------SLas 324
Cdd:PRK09228 253 LDvyeRYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDvgggtsfSM-- 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 257798586 325 nwdLDLWQEAWYIAQHWSGTLTLDKLVSFMTTTPARILGLP-RLGRLAPGKRA 376
Cdd:PRK09228 331 ---LQTMNEAYKVQQLQGYRLSPFQAFYLATLGGARALGLDdRIGNLAPGKEA 380
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
30-376 |
2.85e-09 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 58.51 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 30 IDNGAILEANGMICAVGKY--GELsqthhARLVDEGETVLLPGLINAHTHTELSHLRDRIQPGGGF-------EDWV--- 97
Cdd:PRK06151 21 LRDGEVVFEGDRILFVGHRfdGEV-----DRVIDAGNALVGPGFIDLDALSDLDTTILGLDNGPGWakgrvwsRDYVeag 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 98 ------------------AQLL------ALPARDLDTKAVSKAIDEMaagqiCAVGDISGN-------NPQAMA--SLWR 144
Cdd:PRK06151 96 rremytpeelafqkryafAQLLrngittAMPIASLFYRQWAETYAEF-----AAAAEAAGRlglrvylGPAYRSggSVLE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 145 QSDLHALLWVEQIGFAplpqgqprGLPDAGATPKlRVAPAGHALY----------STSPETLRQTKAWCRSHELPFSLHL 214
Cdd:PRK06151 171 ADGSLEVVFDEARGLA--------GLEEAIAFIK-RVDGAHNGLVrgmlapdrieTCTVDLLRRTAAAARELGCPVRLHC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 215 AEHSGEIEflttgrgpfgamLTKRLVpksfsppGLHPVAYADSLGLLDSSTLVVHAVHLDPGHPH---------LIAHRG 285
Cdd:PRK06151 242 AQGVLEVE------------TVRRLH-------GTTPLEWLADVGLLGPRLLIPHATYISGSPRLnysggddlaLLAEHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 286 STVCLCPRSndFIGVGRAL--WEALDAAGVPLCLGTDS----LASNWDLDLwqeawYIAQHWSGTLTLDKLVSFM---TT 356
Cdd:PRK06151 303 VSIVHCPLV--SARHGSALnsFDRYREAGINLALGTDTfppdMVMNMRVGL-----ILGRVVEGDLDAASAADLFdaaTL 375
|
410 420
....*....|....*....|
gi 257798586 357 TPARILGLPRLGRLAPGKRA 376
Cdd:PRK06151 376 GGARALGRDDLGRLAPGAKA 395
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
171-376 |
1.40e-08 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 56.40 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 171 PDAGATPKLRVAPAGHALYSTSPETLRQTKAWCRSHeLPFSLHLAEHSGEIEflttgrgpfgAMLtkrlvpkSFSppGLH 250
Cdd:PRK09229 193 RALAALPGARLGLAPHSLRAVTPDQLAAVLALAAPD-GPVHIHIAEQTKEVD----------DCL-------AWS--GAR 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 251 PVAYADSLGLLDSSTLVVHAVHLDPGHPHLIAHRGSTVCLCP--RSNDFIGVGRAlwEALDAAGVPLCLGTDSLASnwdL 328
Cdd:PRK09229 253 PVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPttEANLGDGIFPA--VDYLAAGGRFGIGSDSHVS---I 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257798586 329 DLWQEA----------------WYIAQHWSgtlTLDKLVSFMTTTPARILGLPrLGRLAPGKRA 376
Cdd:PRK09229 328 DLVEELrlleygqrlrdrrrnvLAAAAQPS---VGRRLFDAALAGGAQALGRA-IGGLAVGARA 387
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
302-376 |
1.00e-06 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 50.48 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 302 RALWEALdAAGVPLCLGTDSLASNWD---LDLWqEAWY-----------IAQHW--SGTLTLDKLVSFMTTTPARILGLP 365
Cdd:COG0044 288 EALWEGL-ADGTIDVIATDHAPHTLEekeLPFA-EAPNgipgletalplLLTELvhKGRLSLERLVELLSTNPARIFGLP 365
|
90
....*....|.
gi 257798586 366 RLGRLAPGKRA 376
Cdd:COG0044 366 RKGRIAVGADA 376
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
192-378 |
6.52e-06 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 47.73 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 192 SPETLRQTKAWCRSHELPFSLHLAEHSGEIEFlttGRGPFGAMLTKRLVPKSFSPpglhpvayadslglldssTLVVHAV 271
Cdd:PRK07213 177 SDEELKFICKECKREKKIFSIHAAEHKGSVEY---SLEKYGMTEIERLINLGFKP------------------DFIVHAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 272 HLDPGHPHLIAHRGSTVCLCPRSNDFIGVGRALWEALDAAGVPLCLGTDSLASNwDLDLWQEAWYI--AQHwsgtLTLDK 349
Cdd:PRK07213 236 HPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTDNFMAN-SPSIFREMEFIykLYH----IEPKE 310
|
170 180
....*....|....*....|....*....
gi 257798586 350 LVSFMTTTPARILGLPRLGRLAPGKRAVY 378
Cdd:PRK07213 311 ILKMATINGAKILGLINVGLIEEGFKADF 339
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
192-376 |
1.24e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.14 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 192 SPETLRQTKAWCRSHELPFSLHLAEHSGEIEFLTTGRGpfgamltkrlVPKSFSPPGLHPVAYADSLGLLDSSTL-VVHA 270
Cdd:pfam07969 248 EDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEA----------VAEKLGNQGRVRIEHAQGVVPYTYSQIeRVAA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 271 VHLDPGhphliAHRGSTVCLCPRSNDFIGVGRA----LWEALDAAGVPLCLGTDSLASnwDLDLWQEAWYIAQHW----- 341
Cdd:pfam07969 318 LGGAAG-----VQPVFDPLWGDWLQDRLGAERArgltPVKELLNAGVKVALGSDAPVG--PFDPWPRIGAAVMRQtaggg 390
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 257798586 342 -----SGTLTLDKLVSFMTTTPARILGLP-RLGRLAPGKRA 376
Cdd:pfam07969 391 evlgpDEELSLEEALALYTSGPAKALGLEdRKGTLGVGKDA 431
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-386 |
1.09e-04 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 43.86 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 34 AILEANGMICAVGKYgeLSQTHHARLVDEGETVLLPGLINAHTH-----TELSHLRDRIQPGGGfedwvaqllalpardl 108
Cdd:cd01307 1 DVAIENGKIAAVGAA--LAAPAATQIVDAGGCYVSPGWIDLHVHvyqggTRYGDRPDMIGVKSG---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 109 dtkaVSKAIDEMAAGqicaVGDISGNNPQAMASlwRQSDLHALLWVEQIG---FAPLPqgQPRGL------------PDA 173
Cdd:cd01307 63 ----VTTVVDAGSAG----ADNIDGFRYTVIER--SATRVYAFLNISRVGlvaQDELP--DPDNIdedavvaaareyPDV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 174 GATPKLRVAPAGHALYSTSPetLRQTKAWCRSHELPFSLHLAEHSGEIEFLTTGRGPfGAMLTKRLVPKS---FSPPG-L 249
Cdd:cd01307 131 IVGLKARASKSVVGEWGIKP--LELAKKIAKEADLPLMVHIGSPPPILDEVVPLLRR-GDVLTHCFNGKPngiVDEEGeV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 250 HPVAYAdslglldsstLVVHAVHLDPGHphliahrGSTvclcprSNDFiGVGRAlweALDAAGVPLCLGTD-SLASNWDL 328
Cdd:cd01307 208 LPLVRR----------ARERGVIFDVGH-------GTA------SFSF-RVARA---AIAAGLLPDTISSDiHGRNRTNG 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 257798586 329 DLWQEAWYIAQHWSGTLTLDKLVSFMTTTPARILGLPRLGRLAPGKRAVYARLSLEKA 386
Cdd:cd01307 261 PVYALATTLSKLLALGMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFDLKDG 318
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
57-376 |
2.71e-04 |
|
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: 42.67 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 57 ARLVDEGETVLLPGLINAHTHteLSHLRDRIQPGGGFEDWVAQLLALPA------------RDL---DTKAVSKAIDEma 121
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTH--LGSDPGDLPLDLALPVEYRTIRATRQaraalragfttvRDAggaDYGLLRDAIDA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 122 agqicavGDISGnnPQAMASlwrqsdlhallwveqiGFAplpQGQPRGLPDAGATPKLRVAPAGhALYSTSPETLRqtkA 201
Cdd:cd01299 77 -------GLIPG--PRVFAS----------------GRA---LSQTGGHGDPRGLSGLFPAGGL-AAVVDGVEEVR---A 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 202 WCRSHelpfslhLAEHSGEIEFLTTGRGpfgAMLTKRLVPKSFSPPGLHP-VAYADSLGLL------------------- 261
Cdd:cd01299 125 AVREQ-------LRRGADQIKIMATGGV---LSPGDPPPDTQFSEEELRAiVDEAHKAGLYvaahaygaeairrairagv 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 262 DSstlVVHAVHLDPGHPHLIAHRGSTVCLCPRSNDFIG------------------VGRALWEAL---DAAGVPLCLGTD 320
Cdd:cd01299 195 DT---IEHGFLIDDETIELMKEKGIFLVPTLATYEALAaegaapglpadsaekvalVLEAGRDALrraHKAGVKIAFGTD 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 257798586 321 SLASNWDLD-LWQEAWYIAQHwsGTLTLDKLVSfMTTTPARILGLP-RLGRLAPGKRA 376
Cdd:cd01299 272 AGFPVPPHGwNARELELLVKA--GGTPAEALRA-ATANAAELLGLSdELGVIEAGKLA 326
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
344-376 |
6.25e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 41.62 E-value: 6.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 257798586 344 TLTLDKLVSFM---------------TTTPARILGLP-RLGRLAPGKRA 376
Cdd:COG1820 306 TLTMDDAVRNLvewtglpleeavrmaSLNPARALGLDdRKGSIAPGKDA 354
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
330-376 |
8.67e-04 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 41.07 E-value: 8.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 257798586 330 LWQEAwyiaqHWSGTLTLDKLVSFMTTTPARILGLPRlGRLAPGKRA 376
Cdd:cd01317 295 LWTLL-----VKGGLLTLPDLIRALSTNPAKILGLPP-GRLEVGAPA 335
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
19-77 |
1.85e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 40.17 E-value: 1.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257798586 19 TLLTRNPARPVIDngAILEANGMICAVGKYGELSQ--THHARLVD-EGETVLlPGLINAHTH 77
Cdd:COG1574 16 RIYTMDPAQPVAE--AVAVRDGRIVAVGSDAEVRAlaGPATEVIDlGGKTVL-PGFIDAHVH 74
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
343-376 |
2.11e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 39.79 E-value: 2.11e-03
10 20 30
....*....|....*....|....*....|....
gi 257798586 343 GTLTLDKLVSFMTTTPARILGLPRlGRLAPGKRA 376
Cdd:PRK09357 342 GLLDLEQLLEKMTINPARILGLPA-GPLAEGEPA 374
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
34-124 |
3.11e-03 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 39.60 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257798586 34 AILEANGMICAVGKYGELSQ--THHARLVDEGETVLLPGLINAHTHTElshlrdriqpGGGFEDWVAQLLALPARDLDTK 111
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKAlkGPATEVIDLKGKTVLPGFIDSHSHLL----------LGGLSLLWLDLSGVTSKEEALA 70
|
90
....*....|...
gi 257798586 112 AVSKAIDEMAAGQ 124
Cdd:cd01300 71 RIREDAAAAPPGE 83
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
16-77 |
3.14e-03 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 39.58 E-value: 3.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257798586 16 RSRTLLTRNPARPvidnGAILEANGMICAVGKygELSQTHHARLVDEGETVLLPGLINAHTH 77
Cdd:cd01315 5 KNGRVVTPDGVRE----ADIAVKGGKIAAIGP--DIANTEAEEVIDAGGLVVMPGLIDTHVH 60
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
328-384 |
7.67e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 38.20 E-value: 7.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 257798586 328 LDLWqeAWYIAQH-WSGTLTLDKLVSFMTTTPARILGLPRlGRLAPGKRAVYARLSLE 384
Cdd:PRK00369 282 LSFT--PPFIYTLvSKGILSIDRAVELISTNPARILGIPY-GEIKEGYRANFTVIQFE 336
|
|
| |
