|
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: 760.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 2 LILKNVTAVQLHPAK-VQEGVDIAIENDVIVAIDDA--LTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIA 78
Cdd:TIGR03314 1 LLIGNGTAVQLDPTRpIQEGGDIAIDGDVIKAVGPTeeLKQKYPEATFIDAKGKLIMPGFINTHNHFYSTFARGMMADIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 79 PCPDFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAYIDGSLSTLRNAFLKVGLRAMTCFETTD 158
Cdd:TIGR03314 81 PPPDFISILKNLWWRLDRALTLEDVYYSGLICSLDAIKSGCTTVIDHHASPNAITGSLSTIRKAADEAGLRTMLCYETSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 159 RNNGiKELQEGVEENIRFARqideaKKAATEPYLVEAHIGAHAPFTVPDAGLEMLREAVKSTGRGLHIHAAEDLYDVSYS 238
Cdd:TIGR03314 161 RDGG-KEMQEGVEENIAFIK-----KSSGKEPYLVEAHIGAHAPFTVSDAGLEMCREAVQATGRGFHIHVAEDIYDVEDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 239 HHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYNHHLSDIRN---LALGTDGIG 315
Cdd:TIGR03314 235 HHKYGKDIVERLADFGLLGSKTLAAHCIYLSDREIELLNETDTFVVHNPESNMGNAVGYNPVLRMFKNgilLGLGTDGYT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 316 SDMFEEMKFAFFKHRDAGGPL---WPDSFAKALANGNELMSRNFGAKFGLLEAGYKADLTICDYNSPTPLLADNIAGHIA 392
Cdd:TIGR03314 315 SDMFESLKFANFKHKDAGGDLnaaWPESPAMLFENNNEIAERNFGAKFGRLEPGAKADLIIVDYNAPTPLTADNINGHIL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 535277512 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: 714.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 1 MLILKNVTAVQLHPAK-VQEGVDIAIENDVIVAID--DALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANI 77
Cdd:PRK07203 1 MLLIGNGTAITRDPAKpVIEDGAIAIEGNVIVEIGttDELKAKYPDAEFIDAKGKLIMPGLINSHNHIYSGLARGMMANI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 78 APCPDFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAYIDGSLSTLRNAFLKVGLRAMTCFETT 157
Cdd:PRK07203 81 PPPPDFISILKNLWWRLDRALTLEDVYYSALICSLEAIKNGVTTVFDHHASPNYIGGSLFTIADAAKKVGLRAMLCYETS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 158 DRnNGIKELQEGVEENIRFARQIDEAKKAatepyLVEAHIGAHAPFTVPDAGLEMLREAVKSTGRGLHIHAAEDLYDVSY 237
Cdd:PRK07203 161 DR-DGEKELQEGVEENIRFIKHIDEAKDD-----MVEAMFGLHASFTLSDATLEKCREAVKETGRGYHIHVAEGIYDVSD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 238 SHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYNHHLSDIRN---LALGTDGI 314
Cdd:PRK07203 235 SHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNgilLGLGTDGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 315 GSDMFEEMKFAFFKHRDAGGPL---WPDSFAKALANGNELMSRNFGAKFGLLEAGYKADLTICDYNSPTPLLADNIAGHI 391
Cdd:PRK07203 315 TSDMFESYKVANFKHKHAGGDPnvgWPESPAMLFENNNKIAERYFGAKFGILEEGAKADLIIVDYNPPTPLNEDNINGHI 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 535277512 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 |
1.81e-135 |
|
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: 395.42 E-value: 1.81e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 2 LILKNVTAVQLHPAKVQEGVDIAIENDVIVAIDDALTQR-YPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIapc 80
Cdd:cd01298 1 ILIRNGTIVTTDPRRVLEDGDVLVEDGRIVAVGPALPLPaYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 81 pDFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAyidgslSTLRNAFLKVGLRAMTCFETTDRN 160
Cdd:cd01298 78 -PLMEWLKDLIWPLERLLTEEDVYLGALLALAEMIRSGTTTFADMYFFYP------DAVAEAAEELGIRAVLGRGIMDLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 161 NGI-KELQEGVEENIRFARQIDEAKkaatePYLVEAHIGAHAPFTVPDAGLEMLREAVKSTGRGLHIHAAEDLYDVSYSH 239
Cdd:cd01298 151 TEDvEETEEALAEAERLIREWHGAA-----DGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 240 HWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVG---YNHHLSDIRNLALGTDGIGS 316
Cdd:cd01298 226 EKYGKRPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGiapVPEMLEAGVNVGLGTDGAAS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 317 ----DMFEEMKFAFFKHRDAGGPLWPDSFAKALANGNELMSRNFG-AKFGLLEAGYKADLTICDYNSPTPLLADNIAGHI 391
Cdd:cd01298 306 nnnlDMFEEMRLAALLQKLAHGDPTALPAEEALEMATIGGAKALGlDEIGSLEVGKKADLILIDLDGPHLLPVHDPISHL 385
|
410 420
....*....|....*....|....*.
gi 535277512 392 AFGMGSGSVHSVMVNGVMVYEDRQFN 417
Cdd:cd01298 386 VYSANGGDVDTVIVNGRVVMEDGELL 411
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-413 |
2.20e-97 |
|
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: 298.28 E-value: 2.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 2 LILKNVTAVQLHPAK-VQEGVDIAIENDVIVAI--DDALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGImaniA 78
Cdd:COG0402 2 LLIRGAWVLTMDPAGgVLEDGAVLVEDGRIAAVgpGAELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGL----A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 79 PCPDFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAyidGSLSTLRNAFLKVGLRAMTCFETTD 158
Cdd:COG0402 78 DDLPLLDWLEEYIWPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHP---ESADALAEAAAEAGIRAVLGRGLMD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 159 RN---NGIKELQEGVEENIRFARQIDEAKKAatepyLVEAHIGAHAPFTVPDAGLEMLREAVKSTGRGLHIHAAEDLYDV 235
Cdd:COG0402 155 RGfpdGLREDADEGLADSERLIERWHGAADG-----RIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 236 SYSHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDIR-------NLA 308
Cdd:COG0402 230 EWVLELYGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSG----IAPVPrllaagvRVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 309 LGTDGIGS----DMFEEMKFAFFKHRDAGG----PLWPDSFAKALANGNELMsrNFGAKFGLLEAGYKADLTICDYNSPT 380
Cdd:COG0402 306 LGTDGAASnnslDMFEEMRLAALLQRLRGGdptaLSAREALEMATLGGARAL--GLDDEIGSLEPGKRADLVVLDLDAPH 383
|
410 420 430
....*....|....*....|....*....|...
gi 535277512 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 |
2.14e-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: 173.84 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 53 IVMPGIVCSHNHFYSGLSRGImaniapcpdfistlknlwwrldrALDEESLYYSGLICSLEAIKSGCTSVIDHHASPAYi 132
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGI-----------------------PVPPEFAYEALRLGITTMLKSGTTTVLDMGATTST- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 133 dgSLSTLRNAFLK--VGLRAMTCFETTDrnnGIKELQEGVEENIRFARQIDEAKKAATEpyLVEAHIGAHAPFTVPDAGL 210
Cdd:pfam01979 57 --GIEALLEAAEElpLGLRFLGPGCSLD---TDGELEGRKALREKLKAGAEFIKGMADG--VVFVGLAPHGAPTFSDDEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 211 EMLREAVKSTGRGLHIHAAEDLYDVSYSHHWYGKD-----LLARLAQFDLIDS-KTLVAHGLYLSKDDIALLNQR--DAF 282
Cdd:pfam01979 130 KAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGGiehgtHLEVAESGGLLDIiKLILAHGVHLSPTEANLLAEHlkGAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 283 LVHNARSNMNNHVGYNHHLSDIR---NLALGTDGIGS----DMFEEMKFAFFKHRDAGGPLWP-DSFAKALANGNELMsr 354
Cdd:pfam01979 210 VAHCPFSNSKLRSGRIALRKALEdgvKVGLGTDGAGSgnslNMLEELRLALELQFDPEGGLSPlEALRMATINPAKAL-- 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 535277512 355 NFGAKFGLLEAGYKADLTICDYnsptplladNIAGHIAFGMGSGSVHSVMVNGVMV 410
Cdd:pfam01979 288 GLDDKVGSIEVGKDADLVVVDL---------DPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
2-440 |
1.00e-42 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 155.68 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 2 LILKNVTAVQLHPAKVQEGVdIAIENDVIVAIDDALTQrypDAS-YKEMHGRIVMPGIVCSHNHFYSGLSRGiMANIAPC 80
Cdd:PRK06038 4 IIIKNAYVLTMDAGDLKKGS-VVIEDGTITEVSESTPG---DADtVIDAKGSVVMPGLVNTHTHAAMTLFRG-YADDLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 81 PDFistLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHAspaYIDGSLSTLRNAflkvGLRAMTCFETTDRN 160
Cdd:PRK06038 79 AEW---LNDHIWPAEAKLTAEDVYAGSLLACLEMIKSGTTSFADMYF---YMDEVAKAVEES----GLRAALSYGMIDLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 161 NGIKELQEgVEENIRFARQIDEAKKAAtepylVEAHIGAHAPFTVPDAGLEMLREAVKSTGRGLHIHAAEDLYDVSYSHH 240
Cdd:PRK06038 149 DDEKGEAE-LKEGKRFVKEWHGAADGR-----IKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 241 WYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYN---HHLSDIRNLALGTDGIGS- 316
Cdd:PRK06038 223 QYGMCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIApvpKLLERGVNVSLGTDGCASn 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 317 ---DMFEEMKFAFFKHR----DAGGPLWPDSFAKALANGnelmSRNFGAKFGLLEAGYKADLTICDYNSP--TPLLadNI 387
Cdd:PRK06038 303 nnlDMFEEMKTAALLHKvntmDPTALPARQVLEMATVNG----AKALGINTGMLKEGYLADIIIVDMNKPhlTPVR--DV 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 535277512 388 AGHIAFGMGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARKAAASMWRRMDA 440
Cdd:PRK06038 377 PSHLVYSASGSDVDTTIVDGRILMEDYKVlCMDEQDVMEDAKKAAEELVSRVNA 430
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
22-416 |
6.95e-41 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 150.72 E-value: 6.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 22 DIAIENDVIVAIDDALTQryPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGiMANIAPCPDFistLKNLWWRLDRALDEE 101
Cdd:PRK08393 22 DVLIEGNKIVEVKRNINK--PADTVIDASGSVVSPGFINAHTHSPMVLLRG-LADDVPLMEW---LQNYIWPRERKLKRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 102 SLYYSGLICSLEAIKSGCTSVIDHHAspaYIDgslsTLRNAFLKVGLRAMTCFETTDRNNgikelQEGVEENIRFARQID 181
Cdd:PRK08393 96 DIYWGAYLGLLEMIKSGTTTFVDMYF---HME----EVAKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEKLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 182 EAKKAATEPyLVEAHIGAHAPFTVPDAGLEMLREAVKSTGRGLHIHAAEDLYDVSYSHHWYGKDLLARLAQFDLIDSKTL 261
Cdd:PRK08393 164 EFIEKLNSP-RVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYGKSPVVLLDEIGFLNEDVI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 262 VAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVG---YNHHLSDIRNLALGTDGIGS----DMFEEMKFAFFKHRDAG- 333
Cdd:PRK08393 243 AAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGvmpLRKLLNAGVNVALGTDGAASnnnlDMLREMKLAALLHKVHNl 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 334 GPLWPDS---FAKALANGnelmSRNFGAKFGLLEAGYKADLTICDYNSPTPLLADNIAGHIAFGMGSGSVHSVMVNGVMV 410
Cdd:PRK08393 323 DPTIADAetvFRMATQNG----AKALGLKAGVIKEGYLADIAVIDFNRPHLRPINNPISHLVYSANGNDVETTIVDGKIV 398
|
....*.
gi 535277512 411 YEDRQF 416
Cdd:PRK08393 399 MLDGEV 404
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
2-438 |
3.39e-35 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 135.51 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 2 LILKNVTAVQLHPAKVQEGVDIAIENDVIVAIDDAL-TQRYPDasYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIApc 80
Cdd:PRK07228 3 ILIKNAGIVTMNAKREIVDGDVLIEDDRIAAVGDRLdLEDYDD--HIDATGKVVIPGLIQGHIHLCQTLFRGIADDLE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 81 pdFISTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVID----HHASPAYidgslstlrNAFLKVGLRAMTCFET 156
Cdd:PRK07228 79 --LLDWLKDRIWPLEAAHDAESMYYSALLGIGELIESGTTTIVDmesvHHTDSAF---------EAAGESGIRAVLGKVM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 157 TDRNNGIKE-LQEGVEENIrfarqideakkAATEPYLVEAHiGAH--------APFTVPDAGLEMLREA---VKSTGRGL 224
Cdd:PRK07228 148 MDYGDDVPEgLQEDTEASL-----------AESVRLLEKWH-GADngriryafTPRFAVSCTEELLRGVrdlADEYGVRI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 225 HIHAAEDLYDVSYSHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDI 304
Cdd:PRK07228 216 HTHASENRGEIETVEEETGMRNIHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASG----IAPV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 305 R-------NLALGTDGIGS----DMFEEMKFAFFKHR-DAGGPLWPDS---FAKALANGNELMSrnFGAKFGLLEAGYKA 369
Cdd:PRK07228 292 PdllergiNVALGADGAPCnntlDPFTEMRQAALIQKvDRLGPTAMPArtvFEMATLGGAKAAG--FEDEIGSLEEGKKA 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535277512 370 DLTICDYNS--PTPLLADNIAGHIAFGMGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARKAAASMWRRM 438
Cdd:PRK07228 370 DLAILDLDGlhATPSHGVDVLSHLVYAAHGSDVETTMVDGKIVMEDGELtTIDADAVRREANRSIKRLLKRA 441
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
22-421 |
5.48e-28 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 114.98 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 22 DIAIENDVIVAIDDAltqrYPDASYK-EMHGRIVMPGIVCSHNHFYSGLSRGIMANIapcpDFISTLKNLWwRLDRALDE 100
Cdd:PRK06380 23 NVYIEGNKIVYVGDV----NEEADYIiDATGKVVMPGLINTHAHVGMTASKGLFDDV----DLEEFLMKTF-KYDSKRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 101 ESLYYSGLICSLEAIKSGCTSVIDHHASPAYIdgslstlRNAFLKVGLRAMTCFETTDRNngiKELQEG--VEENIRFAR 178
Cdd:PRK06380 94 EGIYNSAKLGMYEMINSGITAFVDLYYSEDII-------AKAAEELGIRAFLSWAVLDEE---ITTQKGdpLNNAENFIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 179 QIDEakkaatePYLVEAHIGAHAPFTVPDAGLEMLREAVKSTGRGLHIHAAEDLYDVSYSHHWYGKDLLARLAQFDLIDS 258
Cdd:PRK06380 164 EHRN-------EELVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEVYDHVKRTGERPVEHLEKIGFLNS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 259 KTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYNHHLSDIR----NLALGTDGIGS----DMFEEMKFAFFKHR 330
Cdd:PRK06380 237 KLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGGSPPIPEMLdngiNVTIGTDSNGSnnslDMFEAMKFSALSVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 331 DAggpLWPDSFAKA-----LANGNELMSRNFGAkfGLLEAGYKADLTICDYNSPT--PLLADNIAGHIAFGMGSGSVHSV 403
Cdd:PRK06380 317 NE---RWDASIIKAqeildFATINAAKALELNA--GSIEVGKLADLVILDARAPNmiPTRKNNIVSNIVYSLNPLNVDHV 391
|
410
....*....|....*....
gi 535277512 404 MVNGVMVYED-RQFNFDCD 421
Cdd:PRK06380 392 IVNGKILKENgRLNGFNPD 410
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
23-437 |
4.89e-25 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 106.53 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 23 IAIENDVIVAI---DDALtQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGiMANIAPCPDFIStlKNLWWRLDRALD 99
Cdd:PRK09045 31 VAIRDGRIVAIlprAEAR-ARYAAAETVELPDHVLIPGLINAHTHAAMSLLRG-LADDLPLMTWLQ--DHIWPAEGAWVS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 100 EESLYYSGLICSLEAIKSGCTSVIDHHASPAyidgslsTLRNAFLKVGLRAMTC-----FETTDRNNGIKELQEGVEENi 174
Cdd:PRK09045 107 EEFVRDGTLLAIAEMLRGGTTCFNDMYFFPE-------AAAEAAHQAGMRAQIGmpvldFPTAWASDADEYLAKGLELH- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 175 rfarqiDEAKkaaTEPyLVEAHIGAHAPFTVPDAGLEMLREAVKSTGRGLHIHAAEDLYDVSYSHHWYGKDLLARLAQFD 254
Cdd:PRK09045 179 ------DQWR---HHP-LISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIADSLKQHGQRPLARLARLG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 255 LIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYN--HHLSDIR-NLALGTDGIGS----DMFEEMKFAFF 327
Cdd:PRK09045 249 LLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCpvAKLLQAGvNVALGTDGAASnndlDLFGEMRTAAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 328 khrdaggplwpdsFAKALA-----------------NGNELMsrNFGAKFGLLEAGYKADLTICDYNSPTPLLADNIAGH 390
Cdd:PRK09045 329 -------------LAKAVAgdatalpahtalrmatlNGARAL--GLDDEIGSLEPGKQADLVAVDLSGLETQPVYDPVSQ 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 535277512 391 IAFGMGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARkaaasMWRR 437
Cdd:PRK09045 394 LVYAAGREQVSHVWVAGKQLLDDRELtTLDEAELLARAR-----QWRE 436
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
6-437 |
1.16e-24 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 105.52 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 6 NVTAVQLHPA-KVQEGVDIAIENDVIVAIDDA-LTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIAPCPdf 83
Cdd:PRK15493 7 NATIVTMNEQnEVIENGYIIVENDQIIDVNSGeFASDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQP-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 84 isTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVIDHHaSPAYIDGS--LSTLRNAFLKVGL-RAMTCFETT-DR 159
Cdd:PRK15493 85 --WLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMF-NPIGVDQDaiMETVSRSGMRAAVsRTLFSFGTKeDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 160 NNGIKELQEGVEeniRFARQIDeakkaatepyLVEAHIGAHAPFTVPDAGLEMLREAVKSTGRGLHIHAAEDLYDVSYSH 239
Cdd:PRK15493 162 KKAIEEAEKYVK---RYYNESG----------MLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 240 HWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYNH---HLSDIRNLALGTDGIGS 316
Cdd:PRK15493 229 AQYGKRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANvkaMLEAGIKVGIATDSVAS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 317 ----DMFEEMKFAFFK----HRDAGGPLWPDSFAKALANGNELMSRNfgaKFGLLEAGYKAD-LTICDYNSPTPLLADNI 387
Cdd:PRK15493 309 nnnlDMFEEMRIATLLqkgiHQDATALPVETALTLATKGAAEVIGMK---QTGSLEVGKCADfITIDPSNKPHLQPADEV 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 535277512 388 AGHIAFGMGSGSVHSVMVNGVMVYedrqFNFDCDSIYAQARKAAASMWRR 437
Cdd:PRK15493 386 LSHLVYAASGKDISDVIINGKRVV----WNGECKTLDEERIIFEASRYKR 431
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
20-439 |
5.76e-21 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 94.75 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 20 GVDIAIENDVIVAIddALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANI-APCPDFISTLKNLWWRLdraL 98
Cdd:PRK12393 25 GPDIRIRDGRIAAI--GALTPLPGERVIDATDCVVYPGWVNTHHHLFQSLLKGVPAGInQSLTAWLAAVPYRFRAR---F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 99 DEESLYYSGLICSLEAIKSGCTSVIDHHA--SPAYIDGSLSTLRNAFLKVGLRAMTCfettdRNNGIKelqegveenirf 176
Cdd:PRK12393 100 DEDLFRLAARIGLVELLRSGCTTVADHHYlyHPGMPFDTGDILFDEAEALGMRFVLC-----RGGATQ------------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 177 ARQIDEAKKAATEPYLVEAHIG--------------------AHAP----FTVPDAGLEMLREAVKSTGRGLHIHAAEDL 232
Cdd:PRK12393 163 TRGDHPGLPTALRPETLDQMLAdverlvsryhdaspdslrrvVVAPttptFSLPPELLREVARAARGMGLRLHSHLSETV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 233 YDVSYSHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDIRNLA---- 308
Cdd:PRK12393 243 DYVDFCREKYGMTPVQFVAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSG----IAPALAMEaagv 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 309 ---LGTDGIGS----DMFEEMKFAFFKHRDAGGP---LWPDSFAKALANGNELMSRNfgaKFGLLEAGYKADLTICDYNS 378
Cdd:PRK12393 319 pvsLGVDGAASnesaDMLSEAHAAWLLHRAEGGAdatTVEDVVHWGTAGGARVLGLD---AIGTLAVGQAADLAIYDLDD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535277512 379 PTPL-LADNIAGHIAFGmGSGSVHSVMVNG-VMVYEDRQFNFDCDSIYAQARKAAASMWRRMD 439
Cdd:PRK12393 396 PRFFgLHDPAIAPVACG-GPAPVKALLVNGrPVVENGAIPGLDLAELRHDARAAVRRLLQRAA 457
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
3-437 |
4.09e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 89.29 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 3 ILKNVTAVQLHPA--KVQEGvDIAIENDVIVAIDDALtqRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANiapc 80
Cdd:PRK08204 5 LIRGGTVLTMDPAigDLPRG-DILIEGDRIAAVAPSI--EAPDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGAD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 81 pdfistlknlwWRLDRALDE-----------ESLYYSGLICSLEAIKSGCTSVID--H-HASPAYIDGSLSTLRNAflkv 146
Cdd:PRK08204 78 -----------WTLQTYFREihgnlgpmfrpEDVYIANLLGALEALDAGVTTLLDwsHiNNSPEHADAAIRGLAEA---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 147 GLRAMTCFETTDRnngikELQEGVEENIRFARQIDEAKKA--ATEPYLVEAHIGAHAP-FTVPD---AGLEMLREavkst 220
Cdd:PRK08204 143 GIRAVFAHGSPGP-----SPYWPFDSVPHPREDIRRVKKRyfSSDDGLLTLGLAIRGPeFSSWEvarADFRLARE----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 221 gRGLHI--HAAEDLYDVSYshhwygkDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGYN 298
Cdd:PRK08204 213 -LGLPIsmHQGFGPWGATP-------RGVEQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHGYP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 299 HHLSDIRN---LALGTD---GIGSDMFEEMKFAFFKHR--------DAGGPLWP-------DSFAKALANG-NELMsrnF 356
Cdd:PRK08204 285 VTGRLLAHgvrPSLGVDvvtSTGGDMFTQMRFALQAERardnavhlREGGMPPPrltltarQVLEWATIEGaRALG---L 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 357 GAKFGLLEAGYKADLTICDYNSPTPLLADNIAGHIAFGMGSGSVHSVMVNGVMVYED-RQFNFDCDSIYAQARKAAASMW 435
Cdd:PRK08204 362 EDRIGSLTPGKQADLVLIDATDLNLAPVHDPVGAVVQSAHPGNVDSVMVAGRAVKRNgKLLGVDLERLRRLAAASRDRLL 441
|
..
gi 535277512 436 RR 437
Cdd:PRK08204 442 SR 443
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
28-379 |
7.34e-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: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 28 DVIVAIDDA--LTQRYPDASYKEMHGRIVMPGIVCSHNHF-YSGLSRGImaniapCPD----FISTLKNLWWRLDRALDE 100
Cdd:cd01312 1 DKILEVGDYekLEKRYPGAKHEFFPNGVLLPGLINAHTHLeFSANVAQF------TYGrfraWLLSVINSRDELLKQPWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 101 ESLYYSGLICsleaIKSGCTSVidhhaspayidGSLSTLRN---AFLKVGLRAMTCFETTDRNNgIKELQEGVEENIRFA 177
Cdd:cd01312 75 EAIRQGIRQM----LESGTTSI-----------GAISSDGSllpALASSGLRGVFFNEVIGSNP-SAIDFKGETFLERFK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 178 RqideaKKAATEPYLVEAhIGAHAPFTV-PDAGLEMLREAVKSTGRgLHIHAAE-----DLYDVS--YSHHWY------- 242
Cdd:cd01312 139 R-----SKSFESQLFIPA-ISPHAPYSVhPELAQDLIDLAKKLNLP-LSTHFLEskeerEWLEESkgWFKHFWesflklp 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 243 ----GKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDIR-------NLALGT 311
Cdd:cd01312 212 kpkkLATAIDFLDMLGGLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGG----KLDVSelkkagiPVSLGT 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535277512 312 DGIGS----DMFEEMKFAFFKHRDAGGPLWPdsfAKALANGNELMSRNFGAKFGLLEAGYKADLTICDYNSP 379
Cdd:cd01312 288 DGLSSnislSLLDELRALLDLHPEEDLLELA---SELLLMATLGGARALGLNNGEIEAGKRADFAVFELPGP 356
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
22-437 |
1.88e-17 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 84.13 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 22 DIAIENDVIVAIDDALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANI-APCPDFISTLKNLWWRldraLDE 100
Cdd:PRK08203 25 GLVVEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHHFYQTLTRALPAAQdAELFPWLTTLYPVWAR----LTP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 101 ESLYYSGLICSLEAIKSGCTSVIDHH-----ASPAYIDGSLSTLRnaflKVGLRAMTCFETTDRNngikELQEG------ 169
Cdd:PRK08203 101 EMVRVATQTALAELLLSGCTTSSDHHylfpnGLRDALDDQIEAAR----EIGMRFHATRGSMSLG----ESDGGlppdsv 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 170 VEEnirfarqiDEAKKAATEPyLVEAH--IGAHA----------PFTVPDaglEMLREA---VKSTGRGLHIHAAEDLYD 234
Cdd:PRK08203 173 VED--------EDAILADSQR-LIDRYhdPGPGAmlrialapcsPFSVSR---ELMRESaalARRLGVRLHTHLAETLDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 235 VSYSHHWYGkdllARLAQF--DL--IDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVGynhhLSDIRNL--- 307
Cdd:PRK08203 241 EAFCLERFG----MRPVDYleDLgwLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASG----IAPVRELraa 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 308 ----ALGTDGI----GSDMFEEMKFAFFKHRDAGGplwPDSFA--KALangnELMSRNfGAK------FGLLEAGYKADL 371
Cdd:PRK08203 313 gvpvGLGVDGSasndGSNLIGEARQALLLQRLRYG---PDAMTarEAL----EWATLG-GARvlgrddIGSLAPGKLADL 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535277512 372 TICDYNSPT------PLLAdniaghIAFGmGSGSVHSVMVNGVMVYEDRQF-NFDCDSIYAQARKAAASMWRR 437
Cdd:PRK08203 385 ALFDLDELRfagahdPVAA------LVLC-GPPRADRVMVGGRWVVRDGQLtTLDLAALIARHRAAARRLAAG 450
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-413 |
8.31e-16 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 78.85 E-value: 8.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 1 MLILKNVTAVQLHPAKVQEGVDIAIENDVIVAIDDALTQRYP-DASYKEMHGRIVMPGIVCSHNHF-YSGLSRGIMANIA 78
Cdd:COG1228 9 TLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPaGAEVIDATGKTVLPGLIDAHTHLgLGGGRAVEFEAGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 79 PCPDFISTLKNLWWRLDRALdeeslyysglicsleaiKSGCTSVIDHHASP-----AYIDGSLSTLrnaflkVGLRAMTC 153
Cdd:COG1228 89 GITPTVDLVNPADKRLRRAL-----------------AAGVTTVRDLPGGPlglrdAIIAGESKLL------PGPRVLAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 154 FETTDRNNGIKelQEGVEENIRFARQIdeAKKAATepylveaHIGAHAPFTVPDAGLEMLREAV---KSTGRGLHIHAae 230
Cdd:COG1228 146 GPALSLTGGAH--ARGPEEARAALREL--LAEGAD-------YIKVFAEGGAPDFSLEELRAILeaaHALGLPVAAHA-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 231 dlydvsyshhwYGKDLLARLAQFDlIDSktlVAHGLYLSKDDIALLNQRD-AFLV------------HNARSNMNNHVGY 297
Cdd:COG1228 213 -----------HQADDIRLAVEAG-VDS---IEHGTYLDDEVADLLAEAGtVVLVptlslflallegAAAPVAAKARKVR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 298 NHHLSDIRNL-------ALGTDG-----IGSDMFEEMKFAffkhRDAGgpLwpdSFAKALA----NGNELMsrNFGAKFG 361
Cdd:COG1228 278 EAALANARRLhdagvpvALGTDAgvgvpPGRSLHRELALA----VEAG--L---TPEEALRaatiNAAKAL--GLDDDVG 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 535277512 362 LLEAGYKADLTICDYNsptPLlaDNIAgHIAfgmgsgSVHSVMVNGVMVYED 413
Cdd:COG1228 347 SLEPGKLADLVLLDGD---PL--EDIA-YLE------DVRAVMKDGRVVDRS 386
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
51-415 |
2.14e-14 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 74.66 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 51 GRIVMPGIVCSHNHFYSGLSRGIMANiapcpdfiSTLKNlwWRLDRALDEESLYYSGLICS------LEAIKSGCTSVID 124
Cdd:PRK06687 53 GAWIMPGLVNCHTHSAMTGLRGIRDD--------SNLHE--WLNDYIWPAESEFTPDMTTNavkealTEMLQSGTTTFND 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 125 HHaSPAYIDgslstLRNAFLKVGLRAMTCFETTDRNNGIKELQEgvEENIRFARQIDEAKKAATEPYLVeaHIGAHAPFT 204
Cdd:PRK06687 123 MY-NPNGVD-----IQQIYQVVKTSKMRCYFSPTLFSSETETTA--ETISRTRSIIDEILKYKNPNFKV--MVAPHSPYS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 205 VPDAGLEMLREAVKSTGRGLHIHAAEDLYDVSYSHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLV 284
Cdd:PRK06687 193 CSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYGKRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 285 HNARSNMNNHVGynhhLSDIRNL-------ALGTDGIGS----DMFEEMKFAFF--KHRDAGGPLWP-DSFAKALA-NGN 349
Cdd:PRK06687 273 HNPISNLKLASG----IAPIIQLqkagvavGIATDSVASnnnlDMFEEGRTAALlqKMKSGDASQFPiETALKVLTiEGA 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535277512 350 ELMSRNfgAKFGLLEAGYKADLTICDYNSPTPLLA-DNIAGHIAFGMGSGSVHSVMVNGVMVYEDRQ 415
Cdd:PRK06687 349 KALGME--NQIGSLEVGKQADFLVIQPQGKIHLQPqENMLSHLVYAVKSSDVDDVYIAGEQVVKQGQ 413
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
167-437 |
8.79e-14 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 73.15 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 167 QEGVEENIRFARQIDEAKKAatepyLVEahiGAHAPFTVPDAGLEMLRE---AVKSTGRGLHIHAAEDLYDVSYSHHWYG 243
Cdd:PRK06151 185 LAGLEEAIAFIKRVDGAHNG-----LVR---GMLAPDRIETCTVDLLRRtaaAARELGCPVRLHCAQGVLEVETVRRLHG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 244 KDLLARLAQFDLIDSKTLVAHGLYLS---------KDDIALLNQRDAFLVHnARSNMNNHVGYNHHLSDIR----NLALG 310
Cdd:PRK06151 257 TTPLEWLADVGLLGPRLLIPHATYISgsprlnysgGDDLALLAEHGVSIVH-CPLVSARHGSALNSFDRYReagiNLALG 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 311 TDGIGSDMFEEMKFAFFKHRDAGGPLwPDSFAKALANGNELMsrnfGAKF------GLLEAGYKADLTICDYNSP--TPL 382
Cdd:PRK06151 336 TDTFPPDMVMNMRVGLILGRVVEGDL-DAASAADLFDAATLG----GARAlgrddlGRLAPGAKADIVVFDLDGLhmGPV 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 535277512 383 LaDNIAGHIAFGMGSgSVHSVMVNGVMVYEDRQFN-FDCDSIYAQARKAAASMWRR 437
Cdd:PRK06151 411 F-DPIRTLVTGGSGR-DVRAVFVDGRVVMEDGRLPgVDLAALRAQAQQQFDKLVAD 464
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
207-409 |
5.92e-12 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 66.99 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 207 DAGLEMLREAVKSTGRGLHIHAAEDLYDVSYSHHWYGKDLLARLaqFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHN 286
Cdd:PRK07213 178 DEELKFICKECKREKKIFSIHAAEHKGSVEYSLEKYGMTEIERL--INLGFKPDFIVHATHPSNDDLELLKENNIPVVVC 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 287 ARSNMNNHVG----YNHHLSDIrNLALGTDGI---GSDMFEEMKFAF-FKHRDAggplwPDSFAKALANGNELMSRNfga 358
Cdd:PRK07213 256 PRANASFNVGlpplNEMLEKGI-LLGIGTDNFmanSPSIFREMEFIYkLYHIEP-----KEILKMATINGAKILGLI--- 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 535277512 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 |
6.32e-12 |
|
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: 67.10 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 14 PAKVQEGVDIAI-ENDVIVAIDdaltqryPDASYKEMH--GRIVMPGIVCSHNHFYSGLSRGIMANIAPCPDFISTLKNL 90
Cdd:cd01313 4 PEGWERNVRIEVdADGRIAAVN-------PDTATEAVAllGGALLPGMPNLHSHAFQRAMAGLTEYRGSAADSFWTWREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 91 WWRLDRALDEESLYYSGLICSLEAIKSGCTSVID----HH-------ASPAYID------GSLSTLRNAFLKVgLRAMTC 153
Cdd:cd01313 77 MYRFAARLTPEQIEAIARQLYIEMLLAGITAVGEfhyvHHdpdgtpyADPAELAqrviaaASDAGIGITLLPV-LYARAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 154 FETTDRNNGIKELQEGVEEnirFARQIDEAKKAATEPYLVEAHIGAHAPFTVPDAGLEMLREAVKSTGRgLHIHAAEDLY 233
Cdd:cd01313 156 FGGPAPNPGQRRFINGYED---FLGLLEKALRAVKEHAAARIGVAPHSLRAVPAEQLAALAALASEKAP-VHIHLAEQPK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 234 DVSYSHHWYGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAF--LVHNARSNMNNHVG-YNHHLSDIRNLALG 310
Cdd:cd01313 232 EVDDCLAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVvgLCPTTEANLGDGIFpAAALLAAGGRIGIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 311 TDG-IGSDMFEEMKFAFFKHR---------DAGGPLWPDS-FAKALANGNELMSRNFGAkfglLEAGYKADLTICDYNSP 379
Cdd:cd01313 312 SDSnARIDLLEELRQLEYSQRlrdrarnvlATAGGSSARAlLDAALAGGAQALGLATGA----LEAGARADLLSLDLDHP 387
|
410 420 430
....*....|....*....|....*....|.
gi 535277512 380 TPL--LADNIAGHIAFGMGSGSVHSVMVNGV 408
Cdd:cd01313 388 SLAgaLPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
23-375 |
5.62e-10 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 60.75 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 23 IAIEnDVIVAIDD--ALTQRYPDASYKEMHGRIVMPGIVCSHNHF-----YSGLSRGimaniapcpDFISTLKNLWWRLD 95
Cdd:PRK08418 24 VVFD-DKILEIGDyeNLKKKYPNAKIQFFKNSVLLPAFINPHTHLefsanKTTLDYG---------DFIPWLGSVINHRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 96 RALDE--ESLYYSGLICSLeaiKSGCTSVidhhaspayidGSLSTLRN---AFLKVGLRAMTCFETTDRN-NGIKELQEg 169
Cdd:PRK08418 94 DLLEKckGALIQQAINEML---KSGVGTI-----------GAISSFGIdleICAKSPLRVVFFNEILGSNaSAVDELYQ- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 170 veeniRFARQIDEAKKAATEPYLveAHIGAHAPFTV-PDAGLEMLREAvKSTGRGLHIHAAEDLYDVSYSHHWYG--KDL 246
Cdd:PRK08418 159 -----DFLARFEESKKFKSKKFI--PAIAIHSPYSVhPILAKKALQLA-KKENLLVSTHFLESKAEREWLEESKGwfKKF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 247 LAR--------------LAQFDliDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSN--MNNHVgynHHLSDIR----N 306
Cdd:PRK08418 231 FEKflkepkplytpkefLELFK--GLRTLFTHCVYASEEELEKIKSKNASITHCPFSNrlLSNKA---LDLEKAKkagiN 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535277512 307 LALGTDGIGS----DMFEEMKFAFFKHRDAggPLwpDSFAKALAngneLMSRNFGAKF-----GLLEAGYKADLTICD 375
Cdd:PRK08418 306 YSIATDGLSSnislSLLDELRAALLTHANM--PL--LELAKILL----LSATRYGAKAlglnnGEIKEGKDADLSVFE 375
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
188-325 |
1.28e-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: 58.57 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 188 TEPYLVEAHIGAHAPFTVPDAG---LEMLREAVKSTGRGLHIHAAEDlydvsySHHWYGKDLLARLAqfdlIDSKTLVaH 264
Cdd:cd01305 102 TEPDDPEILLEVADGLGLSSANdvdLEDILELLRRRGKLFAIHASET------RESVGMTDIERALD----LEPDLLV-H 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535277512 265 GLYLSKDDIALLNQRDAFLVHNARSNMNNHVG---YNHHLSDIRNLALGTDGIGS---DMFEEMKFA 325
Cdd:cd01305 171 GTHLTDEDLELVRENGVPVVLCPRSNLYFGVGippVAELLKLGIKVLLGTDNVMVnepDMWAEMEFL 237
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
23-385 |
4.93e-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: 54.98 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 23 IAIENDVIVAIDDA---LTQRYPDASYKEMHGRIVMPGIVCSHNHFYSglsrgiMANIAPCPDfiSTLknLWWrLDR-AL 98
Cdd:cd01303 29 IVVVDGNIIAAGAAetlKRAAKPGARVIDSPNQFILPGFIDTHIHAPQ------YANIGSGLG--EPL--LDW-LETyTF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 99 DEESLY---------YSGLICSLeaIKSGCTSVidhhASPAYID-GSLSTLRNAFLKVGLRAMTCFETTDRNNG---IKE 165
Cdd:cd01303 98 PEEAKFadpayarevYGRFLDEL--LRNGTTTA----CYFATIHpESTEALFEEAAKRGQRAIAGKVCMDRNAPeyyRDT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 166 LQEGVEENIRFARQIDEAKKaatepyLVEAHIGAHAPFTVPDAGLEMLREAVKSTgRGLHI--HAAEDLYDVSY--SHHW 241
Cdd:cd01303 172 AESSYRDTKRLIERWHGKSG------RVKPAITPRFAPSCSEELLAALGKLAKEH-PDLHIqtHISENLDEIAWvkELFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 242 YGKDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNHVG---YNHHLSDIRNLALGTD---GIG 315
Cdd:cd01303 245 GARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGlfdVRKLLDAGIKVGLGTDvggGTS 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535277512 316 SDMFEEMKFAFF--KHR-DAGGPLWPDSFAKAL----ANGNELMSRnfGAKFGLLEAGYKADLTICDYNSpTPLLAD 385
Cdd:cd01303 325 FSMLDTLRQAYKvsRLLgYELGGHAKLSPAEAFylatLGGAEALGL--DDKIGNFEVGKEFDAVVIDPSA-TPLLAD 398
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
61-349 |
4.80e-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: 51.18 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 61 SHNHFYSGLSRGimaniapcpdfisTLKNLWWRLDRALDEESLYYSGLICSLEAIKSGCTSVID--HHASPAYIDGSLST 138
Cdd:cd01292 4 THVHLDGSALRG-------------TRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDmgSTPPPTTTKAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 139 LRNAFLKV-GLRAMTCFETTDRNNGIKElqEGVEENIRFARQIDEAKKAAtepylveahIGAHAPFTVPDAGLEMLREAV 217
Cdd:cd01292 71 VAEAARASaGIRVVLGLGIPGVPAAVDE--DAEALLLELLRRGLELGAVG---------LKLAGPYTATGLSDESLRRVL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 218 ---KSTGRGLHIHAAEDlydvsyshHWYGKDLLaRLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSNMNNH 294
Cdd:cd01292 140 eeaRKLGLPVVIHAGEL--------PDPTRALE-DLVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLG 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535277512 295 VGYNhHLSDIRNL-------ALGTDG----IGSDMFEEMKFAFFKHRDAGGPLWpdsfAKALANGN 349
Cdd:cd01292 211 RDGE-GAEALRRLlelgirvTLGTDGpphpLGTDLLALLRLLLKVLRLGLSLEE----ALRLATIN 271
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
175-437 |
5.56e-07 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 51.77 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 175 RFARQIDEAKKAATEpyLVEAHIGAhAPFTVPDAGLEMLREAVKSTGRG--LHIHAAEDLYDVSYSHHWYGK---DLLar 249
Cdd:PRK09229 183 GFLRLLEALRRALAA--LPGARLGL-APHSLRAVTPDQLAAVLALAAPDgpVHIHIAEQTKEVDDCLAWSGArpvEWL-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 250 LAQFDLIDSKTLVaHGLYLSKDDIALLNQRDA---------------------FLVHNARsnmnnhvgynhhlsdirnLA 308
Cdd:PRK09229 258 LDHAPVDARWCLV-HATHLTDAETARLARSGAvaglcptteanlgdgifpavdYLAAGGR------------------FG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 309 LGTDG-IGSDMFEEMK---------------FAffkhRDAGGPLWPDSFAKALANGNelmsRNFGAKFGLLEAGYKADLT 372
Cdd:PRK09229 319 IGSDShVSIDLVEELRlleygqrlrdrrrnvLA----AAAQPSVGRRLFDAALAGGA----QALGRAIGGLAVGARADLV 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535277512 373 ICDYNSptPLLA----DNIAGHIAFGMGSGSVHSVMVNGVMVYEDRQfNFDCDSIYAQARKAAASMWRR 437
Cdd:PRK09229 391 VLDLDH--PALAgregDALLDRWVFAGGDAAVRDVWVAGRWVVRDGR-HRLREAIAAAFRAALAALLAA 456
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
22-83 |
5.63e-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: 42.30 E-value: 5.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535277512 22 DIAIENDVIVAI---DDALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIAPCPDF 83
Cdd:cd01300 1 AVAVRDGRIVAVgsdAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSK 65
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
2-76 |
5.95e-04 |
|
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: 41.82 E-value: 5.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535277512 2 LILKNVTAVQlhpAKVQEGVDIAIENDVIVAI----DDALTQRYPDASykemhGRIVMPGIVCSHNHFYSGLSRGIMAN 76
Cdd:cd01314 1 LIIKNGTIVT---ADGSFKADILIEDGKIVAIgpnlEAPGGVEVIDAT-----GKYVLPGGIDPHTHLELPFMGTVTAD 71
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
244-384 |
5.97e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 42.10 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 244 KDLLARLAQFDLIDSKTLVAHGLYLSKDDIALLNQRDAFLVHNARSN---------MNNHVGYNHHlsdirnLALGTD-G 313
Cdd:PRK09228 250 RDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNlflgsglfdLKRADAAGVR------VGLGTDvG 323
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535277512 314 IGS--DMFEEMKFAFFKHRDAGGPLWP-DSFAKALANGNELMSrnFGAKFGLLEAGYKADLTICDYNSpTPLLA 384
Cdd:PRK09228 324 GGTsfSMLQTMNEAYKVQQLQGYRLSPfQAFYLATLGGARALG--LDDRIGNLAPGKEADFVVLDPAA-TPLLA 394
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
361-420 |
7.52e-04 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 41.78 E-value: 7.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535277512 361 GLLEAGYKADLTICDYNSPTPLLADNIAGH--------IAFgmgSGSVHSVMVNGVMVYEDRQFNFDC 420
Cdd:PRK09236 371 GFIREGYWADLVLVDLNSPWTVTKENILYKcgwspfegRTF---RSRVATTFVNGQLVYHNGQLVESC 435
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
2-75 |
9.82e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 41.37 E-value: 9.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535277512 2 LILKNVTAVqlHPAKVQEGV-DIAIENDVIVAIDDALTQRyPDASYKEMHGRIVMPGIVCSHNHFYSGL-SRGIMA 75
Cdd:PRK09237 1 LLLRGGRVI--DPANGIDGViDIAIEDGKIAAVAGDIDGS-QAKKVIDLSGLYVSPGWIDLHVHVYPGStPYGDEP 73
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|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
23-83 |
1.37e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 40.94 E-value: 1.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535277512 23 IAIENDVIVAI---DDALTQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIAPCPDF 83
Cdd:COG1574 30 VAVRDGRIVAVgsdAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDLSGARSL 93
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
21-100 |
2.65e-03 |
|
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: 39.92 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535277512 21 VDIAIENDVIVAIDDALtQRYPDASYKEMHGRIVMPGIVCSHNHFYSGLSRGIMANIAPCPDFISTLKNLWWRLDRALDE 100
Cdd:cd01293 15 VDIAIEDGRIAAIGPAL-AVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFTGGRWPNNSGGTLLEAIIAWEERKLLLTAED 93
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
21-65 |
9.21e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 37.99 E-value: 9.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 535277512 21 VDIAIENDVIVAIDDALtQRYPDASYKEMHGRIVMPGIVCSHNHF 65
Cdd:PRK05985 17 VDILIRDGRIAAIGPAL-AAPPGAEVEDGGGALALPGLVDGHIHL 60
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