|
Name |
Accession |
Description |
Interval |
E-value |
| Se_ssnA |
TIGR03314 |
putative selenium metabolism protein SsnA; Members of this protein family are found ... |
2-438 |
0e+00 |
|
putative selenium metabolism protein SsnA; Members of this protein family are found exclusively in genomes that contain putative set of labile selenium-dependent enzyme accessory proteins as well as homologs of a labile selenium-dependent purine hydroxylase. A mutant in this gene in Escherichia coli had improved stationary phase viability. The function is unknown.
Pssm-ID: 132357 [Multi-domain] Cd Length: 441 Bit Score: 765.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 2 LILKNVTAVQLHPAK-VQEGVDIAIENDVIVAIGDA--LTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIA 78
Cdd:TIGR03314 1 LLIGNGTAVQLDPTRpIQEGGDIAIDGDVIKAVGPTeeLKQKYPEATFIDAKGKLIMPGFINTHNHFYSTFARGMMADIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 79 PSPDFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAYIGGSLSTLRDAFLKVGLRAMTCFETTD 158
Cdd:TIGR03314 81 PPPDFISILKNLWWRLDRALTLEDVYYSGLICSLDAIKSGCTTVIDHHASPNAITGSLSTIRKAADEAGLRTMLCYETSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 159 RNNGiKELQEGVEENIRFARqideaKKAATEPYLVEAHIGAHAPFTVPDAGLEMLREAVNATGRGLHIHAAEDLYDVSYS 238
Cdd:TIGR03314 161 RDGG-KEMQEGVEENIAFIK-----KSSGKEPYLVEAHIGAHAPFTVSDAGLEMCREAVQATGRGFHIHVAEDIYDVEDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 239 HHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYNHHLSDIRN---LALGTDGIG 315
Cdd:TIGR03314 235 HHKYGKDIVERLADFGLLGSKTLAAHCIYLSDREIELLNETDTFVVHNPESNMGNAVGYNPVLRMFKNgilLGLGTDGYT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 316 SDMFEEMKFAFFKHRDAGGPL---WPDSFAKALTNGNELMSRNFGAKFGLLEAGYKADLTICDYNSPTPLLADNIAGHIA 392
Cdd:TIGR03314 315 SDMFESLKFANFKHKDAGGDLnaaWPESPAMLFENNNEIAERNFGAKFGRLEPGAKADLIIVDYNAPTPLTADNINGHIL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15833006 393 FGMGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARKAAASMWRRM 438
Cdd:TIGR03314 395 FGMNGGSVDSTMVNGKVVMEDREFlHFDEAPIYARARKLAQSVWKRM 441
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
1-438 |
0e+00 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 718.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 1 MLILKNVTAVQLHPAK-VQEGVDIAIENDVIVAIG--DALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANI 77
Cdd:PRK07203 1 MLLIGNGTAITRDPAKpVIEDGAIAIEGNVIVEIGttDELKAKYPDAEFIDAKGKLIMPGLINSHNHIYSGLARGMMANI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 78 APSPDFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAYIGGSLSTLRDAFLKVGLRAMTCFETT 157
Cdd:PRK07203 81 PPPPDFISILKNLWWRLDRALTLEDVYYSALICSLEAIKNGVTTVFDHHASPNYIGGSLFTIADAAKKVGLRAMLCYETS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 158 DRnNGIKELQEGVEENIRFARQIDEAKKAatepyLVEAHIGAHAPFTVPDAGLEMLREAVNATGRGLHIHAAEDLYDVSY 237
Cdd:PRK07203 161 DR-DGEKELQEGVEENIRFIKHIDEAKDD-----MVEAMFGLHASFTLSDATLEKCREAVKETGRGYHIHVAEGIYDVSD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 238 SHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYNHHLSDIRN---LALGTDGI 314
Cdd:PRK07203 235 SHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNgilLGLGTDGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 315 GSDMFEEMKFAFFKHRDAGGPL---WPDSFAKALTNGNELMSRNFGAKFGLLEAGYKADLTICDYNSPTPLLADNIAGHI 391
Cdd:PRK07203 315 TSDMFESYKVANFKHKHAGGDPnvgWPESPAMLFENNNKIAERYFGAKFGILEEGAKADLIIVDYNPPTPLNEDNINGHI 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15833006 392 AFGMGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARKAAASMWRRM 438
Cdd:PRK07203 395 LFGMNGGSVDTTIVNGKVVMEDRKFlNFDEESIYARARKAAAKLWKRM 442
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
2-417 |
7.19e-136 |
|
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: 396.19 E-value: 7.19e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 2 LILKNVTAVQLHPAKVQEGVDIAIENDVIVAIGDALTQR-YPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIaps 80
Cdd:cd01298 1 ILIRNGTIVTTDPRRVLEDGDVLVEDGRIVAVGPALPLPaYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 81 pDFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAyiggslSTLRDAFLKVGLRAMTCFETTDRN 160
Cdd:cd01298 78 -PLMEWLKDLIWPLERLLTEEDVYLGALLALAEMIRSGTTTFADMYFFYP------DAVAEAAEELGIRAVLGRGIMDLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 161 NGI-KELQEGVEENIRFARQIDEAKkaatePYLVEAHIGAHAPFTVPDAGLEMLREAVNATGRGLHIHAAEDLYDVSYSH 239
Cdd:cd01298 151 TEDvEETEEALAEAERLIREWHGAA-----DGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 240 HWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVG---YNHHLSDIRNLALGTDGIGS 316
Cdd:cd01298 226 EKYGKRPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGiapVPEMLEAGVNVGLGTDGAAS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 317 ----DMFEEMKFAFFKHRDAGGPLWPDSFAKALTNGNELMSRNFG-AKFGLLEAGYKADLTICDYNSPTPLLADNIAGHI 391
Cdd:cd01298 306 nnnlDMFEEMRLAALLQKLAHGDPTALPAEEALEMATIGGAKALGlDEIGSLEVGKKADLILIDLDGPHLLPVHDPISHL 385
|
410 420
....*....|....*....|....*.
gi 15833006 392 AFGMGSGSVHSVMVNGVMVYEDRQFN 417
Cdd:cd01298 386 VYSANGGDVDTVIVNGRVVMEDGELL 411
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-413 |
6.04e-99 |
|
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: 302.13 E-value: 6.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 2 LILKNVTAVQLHPAK-VQEGVDIAIENDVIVAIGD--ALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGImaniA 78
Cdd:COG0402 2 LLIRGAWVLTMDPAGgVLEDGAVLVEDGRIAAVGPgaELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGL----A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 79 PSPDFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAyigGSLSTLRDAFLKVGLRAMTCFETTD 158
Cdd:COG0402 78 DDLPLLDWLEEYIWPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHP---ESADALAEAAAEAGIRAVLGRGLMD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 159 RN---NGIKELQEGVEENIRFARQIDEAKKAatepyLVEAHIGAHAPFTVPDAGLEMLREAVNATGRGLHIHAAEDLYDV 235
Cdd:COG0402 155 RGfpdGLREDADEGLADSERLIERWHGAADG-----RIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 236 SYSHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDIR-------NLA 308
Cdd:COG0402 230 EWVLELYGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSG----IAPVPrllaagvRVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 309 LGTDGIGS----DMFEEMKFAFFKHRDAGG----PLWPDSFAKALTNGNELMsrNFGAKFGLLEAGYKADLTICDYNSPT 380
Cdd:COG0402 306 LGTDGAASnnslDMFEEMRLAALLQRLRGGdptaLSAREALEMATLGGARAL--GLDDEIGSLEPGKRADLVVLDLDAPH 383
|
410 420 430
....*....|....*....|....*....|...
gi 15833006 381 PLLADNIAGHIAFGMGSGSVHSVMVNGVMVYED 413
Cdd:COG0402 384 LAPLHDPLSALVYAADGRDVRTVWVAGRVVVRD 416
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
53-410 |
2.41e-50 |
|
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: 173.46 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 53 IVMPGIVCSHNHFYSGLSRGImaniapspdfistlknlwwrldrALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAYi 132
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGI-----------------------PVPPEFAYEALRLGITTMLKSGTTTVLDMGATTST- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 133 ggSLSTLRDAFLK--VGLRAMTCFETTDrnnGIKELQEGVEENIRFARQIDEAKKAATEpyLVEAHIGAHAPFTVPDAGL 210
Cdd:pfam01979 57 --GIEALLEAAEElpLGLRFLGPGCSLD---TDGELEGRKALREKLKAGAEFIKGMADG--VVFVGLAPHGAPTFSDDEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 211 EMLREAVNATGRGLHIHAAEDLYDVSYSHHWYGKD-----LLARLAQFDLIDS-KTLVAHGLYLSKDDIALLNQR--DAF 282
Cdd:pfam01979 130 KAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGGiehgtHLEVAESGGLLDIiKLILAHGVHLSPTEANLLAEHlkGAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 283 LVHNARSNMNNHVGYNHHLSDIR---NLALGTDGIGS----DMFEEMKFAFFKHRDAGGPLWPDSFAKALTNGNElMSRN 355
Cdd:pfam01979 210 VAHCPFSNSKLRSGRIALRKALEdgvKVGLGTDGAGSgnslNMLEELRLALELQFDPEGGLSPLEALRMATINPA-KALG 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15833006 356 FGAKFGLLEAGYKADLTICDYnsptplladNIAGHIAFGMGSGSVHSVMVNGVMV 410
Cdd:pfam01979 289 LDDKVGSIEVGKDADLVVVDL---------DPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
2-440 |
2.56e-44 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 159.92 E-value: 2.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 2 LILKNVTAVQLHPAKVQEGVdIAIENDVIVAIGDALTQrypDAS-YKEMHGRIVMPGIVCSHNHFYSGLSRGiMANIAPS 80
Cdd:PRK06038 4 IIIKNAYVLTMDAGDLKKGS-VVIEDGTITEVSESTPG---DADtVIDAKGSVVMPGLVNTHTHAAMTLFRG-YADDLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 81 PDFistLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHAspaYIGGSLSTLRDAflkvGLRAMTCFETTDRN 160
Cdd:PRK06038 79 AEW---LNDHIWPAEAKLTAEDVYAGSLLACLEMIKSGTTSFADMYF---YMDEVAKAVEES----GLRAALSYGMIDLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 161 NGIKELQEgVEENIRFARQIDEAKKAAtepylVEAHIGAHAPFTVPDAGLEMLREAVNATGRGLHIHAAEDLYDVSYSHH 240
Cdd:PRK06038 149 DDEKGEAE-LKEGKRFVKEWHGAADGR-----IKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 241 WYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYN---HHLSDIRNLALGTDGIGS- 316
Cdd:PRK06038 223 QYGMCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIApvpKLLERGVNVSLGTDGCASn 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 317 ---DMFEEMKFAFFKHR----DAGGPLWPDSFAKALTNGnelmSRNFGAKFGLLEAGYKADLTICDYNSP--TPLLadNI 387
Cdd:PRK06038 303 nnlDMFEEMKTAALLHKvntmDPTALPARQVLEMATVNG----AKALGINTGMLKEGYLADIIIVDMNKPhlTPVR--DV 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15833006 388 AGHIAFGMGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARKAAASMWRRMDA 440
Cdd:PRK06038 377 PSHLVYSASGSDVDTTIVDGRILMEDYKVlCMDEQDVMEDAKKAAEELVSRVNA 430
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
22-416 |
9.57e-42 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 153.03 E-value: 9.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 22 DIAIENDVIVAIGDALTQryPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGiMANIAPSPDFistLKNLWWRLDRALDEE 101
Cdd:PRK08393 22 DVLIEGNKIVEVKRNINK--PADTVIDASGSVVSPGFINAHTHSPMVLLRG-LADDVPLMEW---LQNYIWPRERKLKRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 102 SLYYSGLICSLEAIKSGCTSVIDHHASpayiggsLSTLRDAFLKVGLRAMTCFETTDRNNgikelQEGVEENIRFARQID 181
Cdd:PRK08393 96 DIYWGAYLGLLEMIKSGTTTFVDMYFH-------MEEVAKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEKLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 182 EAKKAATEPyLVEAHIGAHAPFTVPDAGLEMLREAVNATGRGLHIHAAEDLYDVSYSHHWYGKDLLARLAQFDLIDSKTL 261
Cdd:PRK08393 164 EFIEKLNSP-RVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYGKSPVVLLDEIGFLNEDVI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 262 VAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVG---YNHHLSDIRNLALGTDGIGS----DMFEEMKFAFFKHRDAG- 333
Cdd:PRK08393 243 AAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGvmpLRKLLNAGVNVALGTDGAASnnnlDMLREMKLAALLHKVHNl 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 334 GPLWPDS---FAKALTNGnelmSRNFGAKFGLLEAGYKADLTICDYNSPTPLLADNIAGHIAFGMGSGSVHSVMVNGVMV 410
Cdd:PRK08393 323 DPTIADAetvFRMATQNG----AKALGLKAGVIKEGYLADIAVIDFNRPHLRPINNPISHLVYSANGNDVETTIVDGKIV 398
|
....*.
gi 15833006 411 YEDRQF 416
Cdd:PRK08393 399 MLDGEV 404
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
2-438 |
2.75e-37 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 141.29 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 2 LILKNVTAVQLHPAKVQEGVDIAIENDVIVAIGDAL-TQRYPDasYKEMHGRIVMPGIVCSHNHFYSGLSRGImaniAPS 80
Cdd:PRK07228 3 ILIKNAGIVTMNAKREIVDGDVLIEDDRIAAVGDRLdLEDYDD--HIDATGKVVIPGLIQGHIHLCQTLFRGI----ADD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 81 PDFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVID----HHASPAYiggslstlrDAFLKVGLRAMTCFET 156
Cdd:PRK07228 77 LELLDWLKDRIWPLEAAHDAESMYYSALLGIGELIESGTTTIVDmesvHHTDSAF---------EAAGESGIRAVLGKVM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 157 TDRNNGIKE-LQEGVEENIrfarqideakkAATEPYLVEAHiGAH--------APFTVPDAGLEMLREA---VNATGRGL 224
Cdd:PRK07228 148 MDYGDDVPEgLQEDTEASL-----------AESVRLLEKWH-GADngriryafTPRFAVSCTEELLRGVrdlADEYGVRI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 225 HIHAAEDLYDVSYSHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDI 304
Cdd:PRK07228 216 HTHASENRGEIETVEEETGMRNIHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASG----IAPV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 305 R-------NLALGTDGIGS----DMFEEMKFAFFKHR-DAGGPLWPDS---FAKALTNGNELMSrnFGAKFGLLEAGYKA 369
Cdd:PRK07228 292 PdllergiNVALGADGAPCnntlDPFTEMRQAALIQKvDRLGPTAMPArtvFEMATLGGAKAAG--FEDEIGSLEEGKKA 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833006 370 DLTICDYNS--PTPLLADNIAGHIAFGMGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARKAAASMWRRM 438
Cdd:PRK07228 370 DLAILDLDGlhATPSHGVDVLSHLVYAAHGSDVETTMVDGKIVMEDGELtTIDADAVRREANRSIKRLLKRA 441
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
22-421 |
7.71e-28 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 114.60 E-value: 7.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 22 DIAIENDVIVAIGDAltqrYPDASYK-EMHGRIVMPGIVCSHNHFYSGLSRGIMANIAPSpDFISTLknlwWRLDRALDE 100
Cdd:PRK06380 23 NVYIEGNKIVYVGDV----NEEADYIiDATGKVVMPGLINTHAHVGMTASKGLFDDVDLE-EFLMKT----FKYDSKRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 101 ESLYYSGLICSLEAIKSGCTSVIDHHASPAYIGgslstlrDAFLKVGLRAMTCFETTDRNngiKELQEG--VEENIRFAR 178
Cdd:PRK06380 94 EGIYNSAKLGMYEMINSGITAFVDLYYSEDIIA-------KAAEELGIRAFLSWAVLDEE---ITTQKGdpLNNAENFIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 179 QIDEakkaatePYLVEAHIGAHAPFTVPDAGLEMLREAVNATGRGLHIHAAEDLYDVSYSHHWYGKDLLARLAQFDLIDS 258
Cdd:PRK06380 164 EHRN-------EELVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEVYDHVKRTGERPVEHLEKIGFLNS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 259 KTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYNHHLSDIR----NLALGTDGIGS----DMFEEMKFAFFKHR 330
Cdd:PRK06380 237 KLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGGSPPIPEMLdngiNVTIGTDSNGSnnslDMFEAMKFSALSVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 331 DAggpLWPDSFAK-------ALTNGNELMSRNFGAkfglLEAGYKADLTICDYNSPT--PLLADNIAGHIAFGMGSGSVH 401
Cdd:PRK06380 317 NE---RWDASIIKaqeildfATINAAKALELNAGS----IEVGKLADLVILDARAPNmiPTRKNNIVSNIVYSLNPLNVD 389
|
410 420
....*....|....*....|.
gi 15833006 402 SVMVNGVMVYED-RQFNFDCD 421
Cdd:PRK06380 390 HVIVNGKILKENgRLNGFNPD 410
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
23-437 |
2.81e-25 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 107.30 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 23 IAIENDVIVAIG--DALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGiMANIAPSPDFIStlKNLWWRLDRALDE 100
Cdd:PRK09045 31 VAIRDGRIVAILprAEARARYAAAETVELPDHVLIPGLINAHTHAAMSLLRG-LADDLPLMTWLQ--DHIWPAEGAWVSE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 101 ESLYYSGLICSLEAIKSGCTSVIDHHASPAYIGgslstlrDAFLKVGLRAMTC-----FETTDRNNGIKELQEGVEENir 175
Cdd:PRK09045 108 EFVRDGTLLAIAEMLRGGTTCFNDMYFFPEAAA-------EAAHQAGMRAQIGmpvldFPTAWASDADEYLAKGLELH-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 176 farqiDEAKkaaTEPyLVEAHIGAHAPFTVPDAGLEMLREAVNATGRGLHIHAAEDLYDVSYSHHWYGKDLLARLAQFDL 255
Cdd:PRK09045 179 -----DQWR---HHP-LISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIADSLKQHGQRPLARLARLGL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 256 IDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYN--HHLSDIR-NLALGTDGIGS----DMFEEMKFAFFk 328
Cdd:PRK09045 250 LGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCpvAKLLQAGvNVALGTDGAASnndlDLFGEMRTAAL- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 329 hrdaggplwpdsFAKALT-----------------NGNELMsrNFGAKFGLLEAGYKADLTICDYNSPTPLLADNIAGHI 391
Cdd:PRK09045 329 ------------LAKAVAgdatalpahtalrmatlNGARAL--GLDDEIGSLEPGKQADLVAVDLSGLETQPVYDPVSQL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15833006 392 AFGMGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARkaaasMWRR 437
Cdd:PRK09045 395 VYAAGREQVSHVWVAGKQLLDDRELtTLDEAELLARAR-----QWRE 436
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
6-437 |
2.30e-24 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 104.75 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 6 NVTAVQLHPA-KVQEGVDIAIENDVIVAI--GDALTQRYPDASYkEMHGRIVMPGIVCSHNHFYSGLSRGIMANIAPSPd 82
Cdd:PRK15493 7 NATIVTMNEQnEVIENGYIIVENDQIIDVnsGEFASDFEVDEVI-DMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 83 fisTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHaSPayIGGSLSTLRDAFLKVGLRAM---TCFETTDR 159
Cdd:PRK15493 85 ---WLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMF-NP--IGVDQDAIMETVSRSGMRAAvsrTLFSFGTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 160 NNGIKELQEGVEENIRFARQIDeakkaatepyLVEAHIGAHAPFTVPDAGLEMLREAVNATGRGLHIHAAEDLYDVSYSH 239
Cdd:PRK15493 159 EDEKKAIEEAEKYVKRYYNESG----------MLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 240 HWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYNH---HLSDIRNLALGTDGIGS 316
Cdd:PRK15493 229 AQYGKRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANvkaMLEAGIKVGIATDSVAS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 317 ----DMFEEMKFAFFK----HRDAGGPLWPDSFAKALTNGNELMSRNfgaKFGLLEAGYKAD-LTICDYNSPTPLLADNI 387
Cdd:PRK15493 309 nnnlDMFEEMRIATLLqkgiHQDATALPVETALTLATKGAAEVIGMK---QTGSLEVGKCADfITIDPSNKPHLQPADEV 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15833006 388 AGHIAFGMGSGSVHSVMVNGVMVYedrqFNFDCDSIYAQARKAAASMWRR 437
Cdd:PRK15493 386 LSHLVYAASGKDISDVIINGKRVV----WNGECKTLDEERIIFEASRYKR 431
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
20-439 |
3.72e-21 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 95.52 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 20 GVDIAIENDVIVAIGdALTQRyPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANI-APSPDFISTLKNLWWRLdraL 98
Cdd:PRK12393 25 GPDIRIRDGRIAAIG-ALTPL-PGERVIDATDCVVYPGWVNTHHHLFQSLLKGVPAGInQSLTAWLAAVPYRFRAR---F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 99 DEESLYYSGLICSLEAIKSGCTSVIDHHA--SPAYIGGSLSTLRDAFLKVGLRAMTCfettdRNNGIKelqegveenirf 176
Cdd:PRK12393 100 DEDLFRLAARIGLVELLRSGCTTVADHHYlyHPGMPFDTGDILFDEAEALGMRFVLC-----RGGATQ------------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 177 ARQIDEAKKAATEPYLVEAHIG--------------------AHAPFTVP-DAGLEMLRE-AVNATGRG--LHIHAAEDL 232
Cdd:PRK12393 163 TRGDHPGLPTALRPETLDQMLAdverlvsryhdaspdslrrvVVAPTTPTfSLPPELLREvARAARGMGlrLHSHLSETV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 233 YDVSYSHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDIRNLA---- 308
Cdd:PRK12393 243 DYVDFCREKYGMTPVQFVAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSG----IAPALAMEaagv 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 309 ---LGTDGIGS----DMFEEMKFAFFKHRDAGGplwpdsfAKALT----------NGNELMSRNfgaKFGLLEAGYKADL 371
Cdd:PRK12393 319 pvsLGVDGAASnesaDMLSEAHAAWLLHRAEGG-------ADATTvedvvhwgtaGGARVLGLD---AIGTLAVGQAADL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 372 TICDYNSPTPL-LADNIAGHIAFGmGSGSVHSVMVNG-VMVYEDRQFNFDCDSIYAQARKAAASMWRRMD 439
Cdd:PRK12393 389 AIYDLDDPRFFgLHDPAIAPVACG-GPAPVKALLVNGrPVVENGAIPGLDLAELRHDARAAVRRLLQRAA 457
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
3-437 |
7.63e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 88.52 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 3 ILKNVTAVQLHPA--KVQEGvDIAIENDVIVAIGDALtqRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIAPS 80
Cdd:PRK08204 5 LIRGGTVLTMDPAigDLPRG-DILIEGDRIAAVAPSI--EAPDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGADWTLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 81 PDFISTLKNlwwrLDRALDEESLYYSGLICSLEAIKSGCTSVID--H-HASPAYIGGSLSTLRDAflkvGLRAMTCFETT 157
Cdd:PRK08204 82 TYFREIHGN----LGPMFRPEDVYIANLLGALEALDAGVTTLLDwsHiNNSPEHADAAIRGLAEA----GIRAVFAHGSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 158 DRnngikELQEGVEENIRFARQIDEAKKA--ATEPYLVEAHIGAHAP-FTVPD---AGLEMLREavnatgRGLHI--HAA 229
Cdd:PRK08204 154 GP-----SPYWPFDSVPHPREDIRRVKKRyfSSDDGLLTLGLAIRGPeFSSWEvarADFRLARE------LGLPIsmHQG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 230 EDLYDVSYshhwygkDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYNHHLSDIRN--- 306
Cdd:PRK08204 223 FGPWGATP-------RGVEQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHgvr 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 307 LALGTD---GIGSDMFEEMKFAFFKHR--------DAGGPLWP-------DSFAKALTNG-NELMsrnFGAKFGLLEAGY 367
Cdd:PRK08204 296 PSLGVDvvtSTGGDMFTQMRFALQAERardnavhlREGGMPPPrltltarQVLEWATIEGaRALG---LEDRIGSLTPGK 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833006 368 KADLTICDYNSPTPLLADNIAGHIAFGMGSGSVHSVMVNGVMVYED-RQFNFDCDSIYAQARKAAASMWRR 437
Cdd:PRK08204 373 QADLVLIDATDLNLAPVHDPVGAVVQSAHPGNVDSVMVAGRAVKRNgKLLGVDLERLRRLAAASRDRLLSR 443
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
22-437 |
1.88e-18 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 87.21 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 22 DIAIENDVIVAIGDALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANI-APSPDFISTLKNLWWRldraLDE 100
Cdd:PRK08203 25 GLVVEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHHFYQTLTRALPAAQdAELFPWLTTLYPVWAR----LTP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 101 ESLYYSGLICSLEAIKSGCTSVIDHH-ASPAYIGGSLSTLRDAFLKVGLRAMTCFETTDRNngikELQEG------VEEn 173
Cdd:PRK08203 101 EMVRVATQTALAELLLSGCTTSSDHHyLFPNGLRDALDDQIEAAREIGMRFHATRGSMSLG----ESDGGlppdsvVED- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 174 irfarqiDEAKKAATEPyLVEAH--IGAHA----------PFTVPDaglEMLRE-AVNATGRG--LHIHAAEDLYDVSYS 238
Cdd:PRK08203 176 -------EDAILADSQR-LIDRYhdPGPGAmlrialapcsPFSVSR---ELMREsAALARRLGvrLHTHLAETLDEEAFC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 239 HHWYGkdllARLAQF--DL--IDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDIRNL------- 307
Cdd:PRK08203 245 LERFG----MRPVDYleDLgwLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASG----IAPVRELraagvpv 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 308 ALGTDGI----GSDMFEEMKFAFFKHRDAGGPlwpdsfaKALT----------NGNELMSRnfgAKFGLLEAGYKADLTI 373
Cdd:PRK08203 317 GLGVDGSasndGSNLIGEARQALLLQRLRYGP-------DAMTarealewatlGGARVLGR---DDIGSLAPGKLADLAL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833006 374 CDYNSPT------PLLAdniaghIAFGmGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARKAAASMWRR 437
Cdd:PRK08203 387 FDLDELRfagahdPVAA------LVLC-GPPRADRVMVGGRWVVRDGQLtTLDLAALIARHRAAARRLAAG 450
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
28-379 |
8.05e-18 |
|
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: 84.81 E-value: 8.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 28 DVIVAIGDA--LTQRYPDASYKEMHGRIVMPGIVCSHNHF----------YSGLSRGIMANIAPSPDFISTLKNLWWRld 95
Cdd:cd01312 1 DKILEVGDYekLEKRYPGAKHEFFPNGVLLPGLINAHTHLefsanvaqftYGRFRAWLLSVINSRDELLKQPWEEAIR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 96 RALDEEslyysglicsleaIKSGCTSVidhhaspayigGSLSTLRD---AFLKVGLRAMTCFETTDRNNgIKELQEGVEE 172
Cdd:cd01312 79 QGIRQM-------------LESGTTSI-----------GAISSDGSllpALASSGLRGVFFNEVIGSNP-SAIDFKGETF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 173 NIRFARqideaKKAATEPYLVEAhIGAHAPFTV-PDAGLEMLREAVNATGRgLHIHAAE-----DLYDVS--YSHHWY-- 242
Cdd:cd01312 134 LERFKR-----SKSFESQLFIPA-ISPHAPYSVhPELAQDLIDLAKKLNLP-LSTHFLEskeerEWLEESkgWFKHFWes 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 243 ---------GKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDIR-------N 306
Cdd:cd01312 207 flklpkpkkLATAIDFLDMLGGLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGG----KLDVSelkkagiP 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833006 307 LALGTDGIGS----DMFEEMKFAFFKHRDAGGPLWPDSFAKALTNGNelmSRNFGAKFGLLEAGYKADLTICDYNSP 379
Cdd:cd01312 283 VSLGTDGLSSnislSLLDELRALLDLHPEEDLLELASELLLMATLGG---ARALGLNNGEIEAGKRADFAVFELPGP 356
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-413 |
2.03e-17 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 83.47 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 1 MLILKNVTAVQLHPAKVQEGVDIAIENDVIVAIGDALTQRYP-DASYKEMHGRIVMPGIVCSHNHF-YSGLSRGIMANIA 78
Cdd:COG1228 9 TLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPaGAEVIDATGKTVLPGLIDAHTHLgLGGGRAVEFEAGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 79 PSPDFISTLKNLWWRLDRALdeeslyysglicsleaiKSGCTSVIDHHASP-----AYIGGSLSTLrdaflkVGLRAMTC 153
Cdd:COG1228 89 GITPTVDLVNPADKRLRRAL-----------------AAGVTTVRDLPGGPlglrdAIIAGESKLL------PGPRVLAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 154 FETTDRNNGIKelQEGVEENIRFARQIdeAKKAATepylveaHIGAHAPFTVPDAGLEMLREAVN-ATGRGLHIHAaedl 232
Cdd:COG1228 146 GPALSLTGGAH--ARGPEEARAALREL--LAEGAD-------YIKVFAEGGAPDFSLEELRAILEaAHALGLPVAA---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 233 ydvsyshHWYGKDLLARLAQFDlIDSktlVAHGLYLSKDDIALLNQRD-AFLV------------HNARSNMNNHVGYNH 299
Cdd:COG1228 211 -------HAHQADDIRLAVEAG-VDS---IEHGTYLDDEVADLLAEAGtVVLVptlslflallegAAAPVAAKARKVREA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 300 HLSDIRNL-------ALGTDG-----IGSDMFEEMKFAffkhRDAGgpLwpdSFAKAL----TNGNELMsrNFGAKFGLL 363
Cdd:COG1228 280 ALANARRLhdagvpvALGTDAgvgvpPGRSLHRELALA----VEAG--L---TPEEALraatINAAKAL--GLDDDVGSL 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15833006 364 EAGYKADLTICDYNsptPLlaDNIAgHIAfgmgsgSVHSVMVNGVMVYED 413
Cdd:COG1228 349 EPGKLADLVLLDGD---PL--EDIA-YLE------DVRAVMKDGRVVDRS 386
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
167-437 |
1.35e-14 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 75.46 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 167 QEGVEENIRFARQIDEAKKAatepyLVEahiGAHAPFTVPDAGLEMLRE---AVNATGRGLHIHAAEDLYDVSYSHHWYG 243
Cdd:PRK06151 185 LAGLEEAIAFIKRVDGAHNG-----LVR---GMLAPDRIETCTVDLLRRtaaAARELGCPVRLHCAQGVLEVETVRRLHG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 244 KDLLARLAQFDLIDSKTLVAHGLYLS---------KDDIALLNQRDAFLVHnARSNMNNHVGYNHHLSDIR----NLALG 310
Cdd:PRK06151 257 TTPLEWLADVGLLGPRLLIPHATYISgsprlnysgGDDLALLAEHGVSIVH-CPLVSARHGSALNSFDRYReagiNLALG 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 311 TDGIGSDMFEEMKFAFFKHRDAGGPLWPDSFA---KALTNGnelmsrnfGAKF------GLLEAGYKADLTICDYNSP-- 379
Cdd:PRK06151 336 TDTFPPDMVMNMRVGLILGRVVEGDLDAASAAdlfDAATLG--------GARAlgrddlGRLAPGAKADIVVFDLDGLhm 407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15833006 380 TPLLaDNIAGHIAFGMGSgSVHSVMVNGVMVYEDRQFN-FDCDSIYAQARKAAASMWRR 437
Cdd:PRK06151 408 GPVF-DPIRTLVTGGSGR-DVRAVFVDGRVVMEDGRLPgVDLAALRAQAQQQFDKLVAD 464
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
23-415 |
8.14e-14 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 72.73 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 23 IAIENDVIVAIGDALTQRYPDASYK-EMHGRIVMPGIVCSHNHFYSGLSRGIMANiapspdfiSTLKNlwWRLDRALDEE 101
Cdd:PRK06687 24 LAVKDSQIVYVGQDKPAFLEQAEQIiDYQGAWIMPGLVNCHTHSAMTGLRGIRDD--------SNLHE--WLNDYIWPAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 102 SLYYSGLICS------LEAIKSGCTSVIDHHaSPAyiGGSLSTLRDAFLKVGLR---AMTCFETTdrnngikelQEGVEE 172
Cdd:PRK06687 94 SEFTPDMTTNavkealTEMLQSGTTTFNDMY-NPN--GVDIQQIYQVVKTSKMRcyfSPTLFSSE---------TETTAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 173 NIRFARQI-DEAKKAATEPYLVeaHIGAHAPFTVP----DAGLEMLREavnaTGRGLHIHAAEDLYDVSYSHHWYGKDLL 247
Cdd:PRK06687 162 TISRTRSIiDEILKYKNPNFKV--MVAPHSPYSCSrdllEASLEMAKE----LNIPLHVHVAETKEESGIILKRYGKRPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 248 ARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDIRNL-------ALGTDGIGS---- 316
Cdd:PRK06687 236 AFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASG----IAPIIQLqkagvavGIATDSVASnnnl 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 317 DMFEEMKFAFF--KHRDAGGPLWP-DSFAKALT-NGNELMSRNfgAKFGLLEAGYKADLTICDYNSPTPLLA-DNIAGHI 391
Cdd:PRK06687 312 DMFEEGRTAALlqKMKSGDASQFPiETALKVLTiEGAKALGME--NQIGSLEVGKQADFLVIQPQGKIHLQPqENMLSHL 389
|
410 420
....*....|....*....|....
gi 15833006 392 AFGMGSGSVHSVMVNGVMVYEDRQ 415
Cdd:PRK06687 390 VYAVKSSDVDDVYIAGEQVVKQGQ 413
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
207-409 |
2.14e-12 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 68.14 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 207 DAGLEMLREAVNATGRGLHIHAAEDLYDVSYSHHWYGKDLLARLaqFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHN 286
Cdd:PRK07213 178 DEELKFICKECKREKKIFSIHAAEHKGSVEYSLEKYGMTEIERL--INLGFKPDFIVHATHPSNDDLELLKENNIPVVVC 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 287 ARSNMNNHVG----YNHHLSDIrNLALGTDGI---GSDMFEEMKFAF-FKHRDAggplwPDSFAKALTNGNELMSRNfga 358
Cdd:PRK07213 256 PRANASFNVGlpplNEMLEKGI-LLGIGTDNFmanSPSIFREMEFIYkLYHIEP-----KEILKMATINGAKILGLI--- 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15833006 359 KFGLLEAGYKADLTICDYNSptPLLADNIAGHIAFGMGSGSVHSVMVNGVM 409
Cdd:PRK07213 327 NVGLIEEGFKADFTFIKPTN--IKFSKNPYASIITRCESGDIVNKILKGKL 375
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
14-408 |
4.46e-11 |
|
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: 64.40 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 14 PAKVQEGVDIAI-ENDVIVAIGdaltqryPDASYKEMH--GRIVMPGIVCSHNHFYSGLSRGIMANIAPSPDFISTLKNL 90
Cdd:cd01313 4 PEGWERNVRIEVdADGRIAAVN-------PDTATEAVAllGGALLPGMPNLHSHAFQRAMAGLTEYRGSAADSFWTWREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 91 WWRLDRALDEESLYYSGLICSLEAIKSGCTSVID----HH-------ASPAYIGGSLStlrDAFLKVGLRaMTCFETTDR 159
Cdd:cd01313 77 MYRFAARLTPEQIEAIARQLYIEMLLAGITAVGEfhyvHHdpdgtpyADPAELAQRVI---AAASDAGIG-ITLLPVLYA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 160 NNGIKE--LQEGVEENI----RFARQIDEAKKAATEPYLVEAHIGAHAPFTVPDAGLEMLREAVNATGRgLHIHAAEDLY 233
Cdd:cd01313 153 RAGFGGpaPNPGQRRFIngyeDFLGLLEKALRAVKEHAAARIGVAPHSLRAVPAEQLAALAALASEKAP-VHIHLAEQPK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 234 DVSYSHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAF--LVHNARSNMNNHVG-YNHHLSDIRNLALG 310
Cdd:cd01313 232 EVDDCLAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVvgLCPTTEANLGDGIFpAAALLAAGGRIGIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 311 TDG-IGSDMFEEMKFAFFKHR---------DAGGPLWPDS-FAKALTNGNELMSRNFGAkfglLEAGYKADLTICDYNSP 379
Cdd:cd01313 312 SDSnARIDLLEELRQLEYSQRlrdrarnvlATAGGSSARAlLDAALAGGAQALGLATGA----LEAGARADLLSLDLDHP 387
|
410 420 430
....*....|....*....|....*....|.
gi 15833006 380 TPL--LADNIAGHIAFGMGSGSVHSVMVNGV 408
Cdd:cd01313 388 SLAgaLPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
23-375 |
6.31e-10 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 60.75 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 23 IAIEnDVIVAIGD--ALTQRYPDASYKEMHGRIVMPGIVCSHNHF-----YSGLSRGimaniapspDFISTLKNLWWRLD 95
Cdd:PRK08418 24 VVFD-DKILEIGDyeNLKKKYPNAKIQFFKNSVLLPAFINPHTHLefsanKTTLDYG---------DFIPWLGSVINHRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 96 RALDE--ESLYYSGLICSLeaiKSGCTSvidhhaspayIGGSLSTLRD--AFLKVGLRAMTCFETTDRN-NGIKELQEgv 170
Cdd:PRK08418 94 DLLEKckGALIQQAINEML---KSGVGT----------IGAISSFGIDleICAKSPLRVVFFNEILGSNaSAVDELYQ-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 171 eeniRFARQIDEAKKAATEPYLveAHIGAHAPFTV-PDagleMLREAVN-ATGRGLHI--HAAEDLYDVSYSHHWYG--K 244
Cdd:PRK08418 159 ----DFLARFEESKKFKSKKFI--PAIAIHSPYSVhPI----LAKKALQlAKKENLLVstHFLESKAEREWLEESKGwfK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 245 DLLAR--------------LAQFDliDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSN--MNNHVgynHHLSDIR--- 305
Cdd:PRK08418 229 KFFEKflkepkplytpkefLELFK--GLRTLFTHCVYASEEELEKIKSKNASITHCPFSNrlLSNKA---LDLEKAKkag 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 306 -NLALGTDGIGS----DMFEEMKFAFFKHRDAggPLwpDSFAKALTngneLMSRNFGAKF-----GLLEAGYKADLTICD 375
Cdd:PRK08418 304 iNYSIATDGLSSnislSLLDELRAALLTHANM--PL--LELAKILL----LSATRYGAKAlglnnGEIKEGKDADLSVFE 375
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
188-346 |
4.70e-09 |
|
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: 57.03 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 188 TEPYLVEAHIGAHAPFTVPDAG---LEMLREAVNATGRGLHIHAAEDlydvsySHHWYGKDLLARLAqfdlIDSKTLVaH 264
Cdd:cd01305 102 TEPDDPEILLEVADGLGLSSANdvdLEDILELLRRRGKLFAIHASET------RESVGMTDIERALD----LEPDLLV-H 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 265 GLYLSKDDIALLNQRDAFLVHNARSNMNNHVG---YNHHLSDIRNLALGTDGIGS---DMFEEMKFAfFKHRDAGGPLWP 338
Cdd:cd01305 171 GTHLTDEDLELVRENGVPVVLCPRSNLYFGVGippVAELLKLGIKVLLGTDNVMVnepDMWAEMEFL-AKYSRLQGYLSP 249
|
....*...
gi 15833006 339 DSFAKALT 346
Cdd:cd01305 250 LEILRMAT 257
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
23-385 |
1.85e-08 |
|
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: 56.13 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 23 IAIENDVIVAIGDA---LTQRYPDASYKEMHGRIVMPGIVCSHNHFYSglsrgiMANIAPSPDfiSTLknLWWrLDR-AL 98
Cdd:cd01303 29 IVVVDGNIIAAGAAetlKRAAKPGARVIDSPNQFILPGFIDTHIHAPQ------YANIGSGLG--EPL--LDW-LETyTF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 99 DEESLY---------YSGLICSLeaIKSGCTSVidhhaspAYIG----GSLSTLRDAFLKVGLRAMTCFETTDRNNG--- 162
Cdd:cd01303 98 PEEAKFadpayarevYGRFLDEL--LRNGTTTA-------CYFAtihpESTEALFEEAAKRGQRAIAGKVCMDRNAPeyy 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 163 IKELQEGVEENIRFARQIDEaKKAATEPylveahigAHAPFTVPDAGLEMLREAVN--ATGRGLHI--HAAEDLYDVSY- 237
Cdd:cd01303 169 RDTAESSYRDTKRLIERWHG-KSGRVKP--------AITPRFAPSCSEELLAALGKlaKEHPDLHIqtHISENLDEIAWv 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 238 -SHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVG---YNHHLSDIRNLALGTD- 312
Cdd:cd01303 240 kELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGlfdVRKLLDAGIKVGLGTDv 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 313 --GIGSDMFEEMKFAFF--KHR-DAGGPLWPDSFAKAL---TNGN-ELMSRnfGAKFGLLEAGYKADLTICDYNSpTPLL 383
Cdd:cd01303 320 ggGTSFSMLDTLRQAYKvsRLLgYELGGHAKLSPAEAFylaTLGGaEALGL--DDKIGNFEVGKEFDAVVIDPSA-TPLL 396
|
..
gi 15833006 384 AD 385
Cdd:cd01303 397 AD 398
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
61-330 |
5.87e-07 |
|
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: 50.79 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 61 SHNHFYSGLSRGimaniapspdfisTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVID--HHASPAYIGGSLST 138
Cdd:cd01292 4 THVHLDGSALRG-------------TRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDmgSTPPPTTTKAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 139 LRDAFLKV-GLRAMTCFETTDRNNGIKElqEGVEENIRFARQIDEAKKAAtepylveahIGAHAPFTVPDAGLEMLREAV 217
Cdd:cd01292 71 VAEAARASaGIRVVLGLGIPGVPAAVDE--DAEALLLELLRRGLELGAVG---------LKLAGPYTATGLSDESLRRVL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 218 ---NATGRGLHIHAAEDlydvsyshHWYGKDLLaRLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNH 294
Cdd:cd01292 140 eeaRKLGLPVVIHAGEL--------PDPTRALE-DLVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLG 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15833006 295 VGYNhHLSDIRNL-------ALGTDG----IGSDMFEEMKFAFFKHR 330
Cdd:cd01292 211 RDGE-GAEALRRLlelgirvTLGTDGpphpLGTDLLALLRLLLKVLR 256
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
175-437 |
1.77e-06 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 49.85 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 175 RFARQIDEAKKAATEpyLVEAHIGAhAPFTVPDAGLEMLREAVNATGRG--LHIHAAEDLYDVSYSHHWYGK---DLLar 249
Cdd:PRK09229 183 GFLRLLEALRRALAA--LPGARLGL-APHSLRAVTPDQLAAVLALAAPDgpVHIHIAEQTKEVDDCLAWSGArpvEWL-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 250 LAQFDLIDSKTLVaHGLYLSKDDIALLNQRDA---------------------FLVHNARsnmnnhvgynhhlsdirnLA 308
Cdd:PRK09229 258 LDHAPVDARWCLV-HATHLTDAETARLARSGAvaglcptteanlgdgifpavdYLAAGGR------------------FG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 309 LGTDG-IGSDMFEEMKF----AFFKHR------DAGGPLWPDS-FAKALTNGNelmsRNFGAKFGLLEAGYKADLTICDY 376
Cdd:PRK09229 319 IGSDShVSIDLVEELRLleygQRLRDRrrnvlaAAAQPSVGRRlFDAALAGGA----QALGRAIGGLAVGARADLVVLDL 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833006 377 NSptPLLA----DNIAGHIAFGMGSGSVHSVMVNGVMVYEDRQfNFDCDSIYAQARKAAASMWRR 437
Cdd:PRK09229 395 DH--PALAgregDALLDRWVFAGGDAAVRDVWVAGRWVVRDGR-HRLREAIAAAFRAALAALLAA 456
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
2-76 |
8.56e-05 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 44.52 E-value: 8.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833006 2 LILKNVTAVQlhpAKVQEGVDIAIENDVIVAIGDAL----TQRYPDASykemhGRIVMPGIVCSHNHFYSGLSRGIMAN 76
Cdd:cd01314 1 LIIKNGTIVT---ADGSFKADILIEDGKIVAIGPNLeapgGVEVIDAT-----GKYVLPGGIDPHTHLELPFMGTVTAD 71
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
22-83 |
1.54e-04 |
|
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: 43.84 E-value: 1.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833006 22 DIAIENDVIVAIGD---ALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIAPSPDF 83
Cdd:cd01300 1 AVAVRDGRIVAVGSdaeAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSK 65
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
2-69 |
4.42e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 42.39 E-value: 4.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833006 2 LILKNVTAVQLHPAKVQEGvDIAIENDVIVAIGDAltqRYPDASYKEMHGRIVMPGIVCSHNHFYSGL 69
Cdd:COG1001 7 LVIKNGRLVNVFTGEILEG-DIAIAGGRIAGVGDY---IGEATEVIDAAGRYLVPGFIDGHVHIESSM 70
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
2-75 |
5.13e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 42.14 E-value: 5.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833006 2 LILKNVTAVqlHPAKVQEGV-DIAIENDVIVAIGDALTQRyPDASYKEMHGRIVMPGIVCSHNHFYSGL-SRGIMA 75
Cdd:PRK09237 1 LLLRGGRVI--DPANGIDGViDIAIEDGKIAAVAGDIDGS-QAKKVIDLSGLYVSPGWIDLHVHVYPGStPYGDEP 73
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
21-100 |
6.35e-04 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 41.85 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 21 VDIAIENDVIVAIGDALtQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIAPSPDFISTLKNLWWRLDRALDE 100
Cdd:cd01293 15 VDIAIEDGRIAAIGPAL-AVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFTGGRWPNNSGGTLLEAIIAWEERKLLLTAED 93
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
23-68 |
7.40e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 41.71 E-value: 7.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15833006 23 IAIENDVIVAIG---DALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSG 68
Cdd:COG1574 30 VAVRDGRIVAVGsdaEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGG 78
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
361-420 |
7.46e-04 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 41.78 E-value: 7.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833006 361 GLLEAGYKADLTICDYNSPTPLLADNIAGH--------IAFgmgSGSVHSVMVNGVMVYEDRQFNFDC 420
Cdd:PRK09236 371 GFIREGYWADLVLVDLNSPWTVTKENILYKcgwspfegRTF---RSRVATTFVNGQLVYHNGQLVESC 435
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
244-384 |
1.06e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 41.33 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 244 KDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSN---------MNNHVGYNHHlsdirnLALGTD-G 313
Cdd:PRK09228 250 RDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNlflgsglfdLKRADAAGVR------VGLGTDvG 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833006 314 IGS--DMFEEMKFAFFKHRDAGGPLWP-DSF-------AKALtngnelmsrNFGAKFGLLEAGYKADLTICDYNSpTPLL 383
Cdd:PRK09228 324 GGTsfSMLQTMNEAYKVQQLQGYRLSPfQAFylatlggARAL---------GLDDRIGNLAPGKEADFVVLDPAA-TPLL 393
|
.
gi 15833006 384 A 384
Cdd:PRK09228 394 A 394
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-65 |
1.73e-03 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 40.54 E-value: 1.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833006 1 MLILKN---VTAVQLHPAkvqegvDIAIENDVIVAIGDALTQRYPDASykemhGRIVMPGIVCSHNHF 65
Cdd:PRK08323 2 STLIKNgtvVTADDTYKA------DVLIEDGKIAAIGANLGDEVIDAT-----GKYVMPGGIDPHTHM 58
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
22-85 |
2.93e-03 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 39.68 E-value: 2.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833006 22 DIAIENDVIVAIGDALTQ--RYPDASykemhGRIVMPGIVCSHNHFYSGLSRGIMAniapSPDFIS 85
Cdd:PRK13404 23 DIGIRGGRIAALGEGLGPgaREIDAT-----GRLVLPGGVDSHCHIDQPSGDGIMM----ADDFYT 79
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1-65 |
3.24e-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: 3.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833006 1 MLILKNVTAVQlhPAKVQEGvDIAIENDVIVAIGDALTQ----RYPDASykemhGRIVMPGIVCSHNHF 65
Cdd:cd01315 1 DLVIKNGRVVT--PDGVREA-DIAVKGGKIAAIGPDIANteaeEVIDAG-----GLVVMPGLIDTHVHI 61
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-65 |
3.72e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 39.41 E-value: 3.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833006 1 MLILKNVTAVQlhPAKVQEGVDIAIENDVIVAIGDALTQryPDASYKEMHGRIVMPGIVCSHNHF 65
Cdd:PRK09357 2 MILIKNGRVID--PKGLDEVADVLIDDGKIAAIGENIEA--EGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
21-65 |
4.49e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 39.15 E-value: 4.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15833006 21 VDIAIENDVIVAIGDALtQRYPDASYKEMHGRIVMPGIVCSHNHF 65
Cdd:PRK05985 17 VDILIRDGRIAAIGPAL-AAPPGAEVEDGGGALALPGLVDGHIHL 60
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
22-64 |
6.71e-03 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 38.43 E-value: 6.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15833006 22 DIAIENDVIVAIGDALT---QRYPDASykemhGRIVMPGIVCSHNH 64
Cdd:cd01297 21 DVGIRDGRIAAIGPILStsaREVIDAA-----GLVVAPGFIDVHTH 61
|
|
| |
