|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
1-458 |
0e+00 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 811.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 1 MTLIALNADVLVTMDAQRREIKDGALVADGPALLWVGATAELPAQYrrmadegqARVLDMRGKVVTPGLVNTHHHMYQSL 80
Cdd:PRK08203 1 TTLWIKNPLAIVTMDAARREIADGGLVVEGGRIVEVGPGGALPQPA--------DEVFDARGHVVTPGLVNTHHHFYQTL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 81 TRAVPAAQDAELFSWLQNLYMLWSHLTPEMIHVSTQTAMAELMLSGCTTTSDHLYLFPNGSR--LDDSIAAAQQMGMRFH 158
Cdd:PRK08203 73 TRALPAAQDAELFPWLTTLYPVWARLTPEMVRVATQTALAELLLSGCTTSSDHHYLFPNGLRdaLDDQIEAAREIGMRFH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 159 AARGSMSLGRSKGGLPPDVVVEEEEAILRDSLRLIQQYHDGSRHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHT 238
Cdd:PRK08203 153 ATRGSMSLGESDGGLPPDSVVEDEDAILADSQRLIDRYHDPGPGAMLRIALAPCSPFSVSRELMRESAALARRLGVRLHT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 239 HLAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDA 318
Cdd:PRK08203 233 HLAETLDEEAFCLERFGMRPVDYLEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 319 GVSVALGVDGSASNDGAHMLGEARQAMLLQRVGYGPAAMSAREALEIATLGGARVLNRDDIGALAPGMSADFVAFDMEDV 398
Cdd:PRK08203 313 GVPVGLGVDGSASNDGSNLIGEARQALLLQRLRYGPDAMTAREALEWATLGGARVLGRDDIGSLAPGKLADLALFDLDEL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 399 GYAGAgHDPVAALVFCTPANVSSSVINGRVVVEDGRLLTADLPVVLGQHRHLARSLFERA 458
Cdd:PRK08203 393 RFAGA-HDPVAALVLCGPPRADRVMVGGRWVVRDGQLTTLDLAALIARHRAAARRLAAGA 451
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
9-436 |
1.25e-169 |
|
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: 482.86 E-value: 1.25e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 9 DVLVTMDAQRREIKDGALVADGPALLWVGATAELPAQYRrmadegqARVLDMRGKVVTPGLVNTHHHMYQSLTRAVPAaq 88
Cdd:cd01298 5 NGTIVTTDPRRVLEDGDVLVEDGRIVAVGPALPLPAYPA-------DEVIDAKGKVVMPGLVNTHTHLAMTLLRGLAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 89 DAELFSWLQNLYMLW-SHLTPEMIHVSTQTAMAELMLSGCTTTSDHLYLFPngsrlDDSIAAAQQMGMRFHAARGSMSLG 167
Cdd:cd01298 76 DLPLMEWLKDLIWPLeRLLTEEDVYLGALLALAEMIRSGTTTFADMYFFYP-----DAVAEAAEELGIRAVLGRGIMDLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 168 RSkgglppdvVVEEEEAILRDSLRLIQQYHDGsRHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHTHLAENDNDV 247
Cdd:cd01298 151 TE--------DVEETEEALAEAERLIREWHGA-ADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 248 AFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVD 327
Cdd:cd01298 222 EESLEKYGKRPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 328 GSASNDGAHMLGEARQAMLLQRVGYGPA-AMSAREALEIATLGGARVLNRDDIGALAPGMSADFVAFDMEDVGYAGAgHD 406
Cdd:cd01298 302 GAASNNNLDMFEEMRLAALLQKLAHGDPtALPAEEALEMATIGGAKALGLDEIGSLEVGKKADLILIDLDGPHLLPV-HD 380
|
410 420 430
....*....|....*....|....*....|.
gi 692381278 407 PVAALVF-CTPANVSSSVINGRVVVEDGRLL 436
Cdd:cd01298 381 PISHLVYsANGGDVDTVIVNGRVVMEDGELL 411
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-432 |
3.97e-158 |
|
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: 453.90 E-value: 3.97e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 4 IALNADVLVTMDAQRREIKDGALVADGPALLWVGATAELPAQYRrmadegQARVLDMRGKVVTPGLVNTHHHMYQSLTRA 83
Cdd:COG0402 2 LLIRGAWVLTMDPAGGVLEDGAVLVEDGRIAAVGPGAELPARYP------AAEVIDAGGKLVLPGLVNTHTHLPQTLLRG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 84 VpaAQDAELFSWLQNL-YMLWSHLTPEMIHVSTQTAMAELMLSGCTTTSDHLYLFPngSRLDDSIAAAQQMGMRFHAARG 162
Cdd:COG0402 76 L--ADDLPLLDWLEEYiWPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHP--ESADALAEAAAEAGIRAVLGRG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 163 SMSLGRskgglpPDVVVEEEEAILRDSLRLIQQYHdGSRHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHTHLAE 242
Cdd:COG0402 152 LMDRGF------PDGLREDADEGLADSERLIERWH-GAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 243 NDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSV 322
Cdd:COG0402 225 TRDEVEWVLELYGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 323 ALGVDGSASNDGAHMLGEARQAMLLQRVGYG-PAAMSAREALEIATLGGARVLNRDD-IGALAPGMSADFVAFDMEDVGY 400
Cdd:COG0402 305 GLGTDGAASNNSLDMFEEMRLAALLQRLRGGdPTALSAREALEMATLGGARALGLDDeIGSLEPGKRADLVVLDLDAPHL 384
|
410 420 430
....*....|....*....|....*....|...
gi 692381278 401 AGAgHDPVAALVFC-TPANVSSSVINGRVVVED 432
Cdd:COG0402 385 APL-HDPLSALVYAaDGRDVRTVWVAGRVVVRD 416
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
21-459 |
9.35e-130 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 383.26 E-value: 9.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 21 IKDGALVADGPallwvgataeLPAQyrrmADEgqaRVLDMRGKVVTPGLVNTHHHMYQSLTRAVPAAQDAELFSWLQNL- 99
Cdd:PRK12393 30 IRDGRIAAIGA----------LTPL----PGE---RVIDATDCVVYPGWVNTHHHLFQSLLKGVPAGINQSLTAWLAAVp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 100 YMLWSHLTPEMIHVSTQTAMAELMLSGCTTTSDHLYLFPNGSRLDDSIA---AAQQMGMRFHAARGSMSLGRS-KGGLPP 175
Cdd:PRK12393 93 YRFRARFDEDLFRLAARIGLVELLRSGCTTVADHHYLYHPGMPFDTGDIlfdEAEALGMRFVLCRGGATQTRGdHPGLPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 176 DVVVEEEEAILRDSLRLIQQYHDGSRHSMLRVVLAPCSP-FSVTRDLMRESAVLARAHGVSLHTHLAENDNDVAFSREKF 254
Cdd:PRK12393 173 ALRPETLDQMLADVERLVSRYHDASPDSLRRVVVAPTTPtFSLPPELLREVARAARGMGLRLHSHLSETVDYVDFCREKY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 255 GLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVDGSASNDG 334
Cdd:PRK12393 253 GMTPVQFVAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNES 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 335 AHMLGEARQAMLLQRVGYGPAAMSAREALEIATLGGARVLNRDDIGALAPGMSADFVAFDMEDVGYAGAgHDPVAALVFC 414
Cdd:PRK12393 333 ADMLSEAHAAWLLHRAEGGADATTVEDVVHWGTAGGARVLGLDAIGTLAVGQAADLAIYDLDDPRFFGL-HDPAIAPVAC 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 692381278 415 -TPANVSSSVINGRVVVEDGRLLTADLPVVLGQHRHLARSLFERAA 459
Cdd:PRK12393 412 gGPAPVKALLVNGRPVVENGAIPGLDLAELRHDARAAVRRLLQRAA 457
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-460 |
1.18e-95 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 295.37 E-value: 1.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 1 MTLIALNADVlVTMDAQRrEIKDGALVADGPALLWVGATAELpaqyrrmadEGQARVLDMRGKVVTPGLVNTHHHMYQSL 80
Cdd:PRK07228 1 MTILIKNAGI-VTMNAKR-EIVDGDVLIEDDRIAAVGDRLDL---------EDYDDHIDATGKVVIPGLIQGHIHLCQTL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 81 TRAVpaAQDAELFSWLQN--LYMLWSHlTPEMIHVSTQTAMAELMLSGCTTTSDHLYLfpngSRLDDSIAAAQQMGMRFH 158
Cdd:PRK07228 70 FRGI--ADDLELLDWLKDriWPLEAAH-DAESMYYSALLGIGELIESGTTTIVDMESV----HHTDSAFEAAGESGIRAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 159 AARGSMSLGRSKgglpPDVVVEEEEAILRDSLRLIQQYHdGSRHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHT 238
Cdd:PRK07228 143 LGKVMMDYGDDV----PEGLQEDTEASLAESVRLLEKWH-GADNGRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 239 HLAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDA 318
Cdd:PRK07228 218 HASENRGEIETVEEETGMRNIHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLER 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 319 GVSVALGVDGSASNDGAHMLGEARQAMLLQRVG-YGPAAMSAREALEIATLGGARVLN-RDDIGALAPGMSADFVAFDME 396
Cdd:PRK07228 298 GINVALGADGAPCNNTLDPFTEMRQAALIQKVDrLGPTAMPARTVFEMATLGGAKAAGfEDEIGSLEEGKKADLAILDLD 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692381278 397 DV-GYAGAGHDPVAALVFC-TPANVSSSVINGRVVVEDGRLLTADLPVVLGQHRHLARSLFERAAA 460
Cdd:PRK07228 378 GLhATPSHGVDVLSHLVYAaHGSDVETTMVDGKIVMEDGELTTIDADAVRREANRSIKRLLKRAGL 443
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
3-460 |
5.55e-76 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 244.27 E-value: 5.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 3 LIALNADVLvTMDAQrrEIKDGALVADGPALLWVGATAELPAQyrrmadegqaRVLDMRGKVVTPGLVNTHHHMYQSLTR 82
Cdd:PRK06038 4 IIIKNAYVL-TMDAG--DLKKGSVVIEDGTITEVSESTPGDAD----------TVIDAKGSVVMPGLVNTHTHAAMTLFR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 83 AVpaAQDAELFSWLQNlyMLW---SHLTPEMIHVSTQTAMAELMLSGCTTTSDhLYLFpngsrLDDSIAAAQQMGMRFHA 159
Cdd:PRK06038 71 GY--ADDLPLAEWLND--HIWpaeAKLTAEDVYAGSLLACLEMIKSGTTSFAD-MYFY-----MDEVAKAVEESGLRAAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 160 ARGSMSLGRSkgglppdvvvEEEEAILRDSLRLIQQYHdGSRHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHTH 239
Cdd:PRK06038 141 SYGMIDLGDD----------EKGEAELKEGKRFVKEWH-GAADGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIH 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 240 LAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAG 319
Cdd:PRK06038 210 VLETEAELNQMKEQYGMCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 320 VSVALGVDGSASNDGAHMLGEARQAMLLQRVGYG-PAAMSAREALEIATLGGARVLNRDDiGALAPGMSADFVAFDMeDV 398
Cdd:PRK06038 290 VNVSLGTDGCASNNNLDMFEEMKTAALLHKVNTMdPTALPARQVLEMATVNGAKALGINT-GMLKEGYLADIIIVDM-NK 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 692381278 399 GYAGAGHDPVAALVF-CTPANVSSSVINGRVVVEDGRLLTADLPVVLGQHRHLARSLFERAAA 460
Cdd:PRK06038 368 PHLTPVRDVPSHLVYsASGSDVDTTIVDGRILMEDYKVLCMDEQDVMEDAKKAAEELVSRVNA 430
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
6-444 |
7.93e-74 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 239.04 E-value: 7.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 6 LNADVLVTMDAQRREIKDGALVADGPALLWVGATAELPAQYRrmadegQARVLDMRGKVVTPGLVNTHHHMYQSLTRAVp 85
Cdd:PRK09045 11 IEARWIVPVEPAGVVLEDHAVAIRDGRIVAILPRAEARARYA------AAETVELPDHVLIPGLINAHTHAAMSLLRGL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 86 aAQDAELFSWLQNlyMLW----SHLTPEMIHVSTQTAMAELMLSGCTTTSDHlYLFPngsrlDDSIAAAQQMGMRFHAar 161
Cdd:PRK09045 84 -ADDLPLMTWLQD--HIWpaegAWVSEEFVRDGTLLAIAEMLRGGTTCFNDM-YFFP-----EAAAEAAHQAGMRAQI-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 162 gsmslgrskgGLP----PDVVVEEEEAILRDSLRLIQQYHDgsrHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLH 237
Cdd:PRK09045 153 ----------GMPvldfPTAWASDADEYLAKGLELHDQWRH---HPLISTAFAPHAPYTVSDENLERIRTLAEQLDLPIH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 238 THLAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRD 317
Cdd:PRK09045 220 IHLHETAQEIADSLKQHGQRPLARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 318 AGVSVALGVDGSASNDGAHMLGEARQAMLLQRVGYG-PAAMSAREALEIATLGGARVLNRDD-IGALAPGMSADFVAFDM 395
Cdd:PRK09045 300 AGVNVALGTDGAASNNDLDLFGEMRTAALLAKAVAGdATALPAHTALRMATLNGARALGLDDeIGSLEPGKQADLVAVDL 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 692381278 396 EDVGYAGAgHDPVAALVF-CTPANVSSSVINGRVVVEDGRLLTADLPVVL 444
Cdd:PRK09045 380 SGLETQPV-YDPVSQLVYaAGREQVSHVWVAGKQLLDDRELTTLDEAELL 428
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
47-439 |
4.24e-66 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 218.13 E-value: 4.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 47 RRMADEgqarVLDMRGKVVTPGLVNTHHHMYQSLTRAVpaAQDAELFSWLQNlyMLW---SHLTPEMIHVSTQTAMAELM 123
Cdd:PRK08393 38 NKPADT----VIDASGSVVSPGFINAHTHSPMVLLRGL--ADDVPLMEWLQN--YIWpreRKLKRKDIYWGAYLGLLEMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 124 LSGCTTTSDhLYLFpngsrLDDSIAAAQQMGMRFHAARGSMSLGRSkgglppdvvvEEEEAILRDSLRLIQqYHDGSRHS 203
Cdd:PRK08393 110 KSGTTTFVD-MYFH-----MEEVAKATLEVGLRGYLSYGMVDLGDE----------EKREKEIKETEKLME-FIEKLNSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 204 MLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHTHLAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPE 283
Cdd:PRK08393 173 RVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYGKSPVVLLDEIGFLNEDVIAAHGVWLSSR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 284 GIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVDGSASNDGAHMLGEARQAMLLQRVGY-GPAAMSAREA 362
Cdd:PRK08393 253 DIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDMLREMKLAALLHKVHNlDPTIADAETV 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 692381278 363 LEIATLGGARVLnRDDIGALAPGMSADFVAFDMEDvGYAGAGHDPVAALVFCTPAN-VSSSVINGRVVVEDGRLLTAD 439
Cdd:PRK08393 333 FRMATQNGAKAL-GLKAGVIKEGYLADIAVIDFNR-PHLRPINNPISHLVYSANGNdVETTIVDGKIVMLDGEVLTLD 408
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
11-440 |
7.28e-65 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 214.87 E-value: 7.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 11 LVTMDAQRREIKDGALVADGPALLWVGataelpaQYRRMADEGQARVLDMRGKVVTPGLVNTHHHMYQSLTRAVpaAQDA 90
Cdd:PRK06687 9 IVTCDQDFHVYLDGILAVKDSQIVYVG-------QDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRGI--RDDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 91 ELFSWLQNlyMLW---SHLTPEMIHVSTQTAMAELMLSGCTTTSDhLYlFPNGSRLDDSIAAAQQMGMRFHAargSMSLG 167
Cdd:PRK06687 80 NLHEWLND--YIWpaeSEFTPDMTTNAVKEALTEMLQSGTTTFND-MY-NPNGVDIQQIYQVVKTSKMRCYF---SPTLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 168 RSkgglpPDVVVEEEEAILRDSLRLIQQYHDGSrhsmLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHTHLAENDNDV 247
Cdd:PRK06687 153 SS-----ETETTAETISRTRSIIDEILKYKNPN----FKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEES 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 248 AFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVD 327
Cdd:PRK06687 224 GIILKRYGKRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 328 GSASNDGAHMLGEARQAMLLQRVGYGPAA-MSAREALEIATLGGARVLNRDD-IGALAPGMSADFVAFDMEDVGYAGAGH 405
Cdd:PRK06687 304 SVASNNNLDMFEEGRTAALLQKMKSGDASqFPIETALKVLTIEGAKALGMENqIGSLEVGKQADFLVIQPQGKIHLQPQE 383
|
410 420 430
....*....|....*....|....*....|....*.
gi 692381278 406 DPVAALVFCTP-ANVSSSVINGRVVVEDGRLLTADL 440
Cdd:PRK06687 384 NMLSHLVYAVKsSDVDDVYIAGEQVVKQGQVLTVEL 419
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
11-454 |
5.49e-59 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 199.90 E-value: 5.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 11 LVTMDAQRREIKDGALVADGPALLWVGaTAELPAQYRrmADEgqarVLDMRGKVVTPGLVNTHHHMYQSLTRAVpaAQDA 90
Cdd:PRK15493 10 IVTMNEQNEVIENGYIIVENDQIIDVN-SGEFASDFE--VDE----VIDMKGKWVLPGLVNTHTHVVMSLLRGI--GDDM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 91 ELFSWLQN-LYMLWSHLTPEMIHVSTQTAMAELMLSGCTTTSDHLYlfPNGSRLDDSIAAAQQMGMRFHAARGSMSLGRS 169
Cdd:PRK15493 81 LLQPWLETrIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFN--PIGVDQDAIMETVSRSGMRAAVSRTLFSFGTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 170 kgglppdvvvEEEEAILRDSLRLIQQYHDgsRHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHTHLAENDNDVAF 249
Cdd:PRK15493 159 ----------EDEKKAIEEAEKYVKRYYN--ESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 250 SREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVDGS 329
Cdd:PRK15493 227 IEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 330 ASNDGAHMLGEARQAMLLQR-VGYGPAAMSAREALEIATLGGARVLNRDDIGALAPGMSADFVAFDMEDVGYAGAGHDPV 408
Cdd:PRK15493 307 ASNNNLDMFEEMRIATLLQKgIHQDATALPVETALTLATKGAAEVIGMKQTGSLEVGKCADFITIDPSNKPHLQPADEVL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 692381278 409 AALVFCTPA-NVSSSVINGRVVVEDGRLLTADLPVVLGQHRHLARSL 454
Cdd:PRK15493 387 SHLVYAASGkDISDVIINGKRVVWNGECKTLDEERIIFEASRYKRGL 433
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-429 |
2.50e-52 |
|
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: 179.23 E-value: 2.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 64 VVTPGLVNTHHHMYQSLTRAVPaaqdaelfswlqnlymlwshLTPEMIHVSTQTAMAELMLSGCTTTSDHLYLFPNGSRL 143
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIP--------------------VPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 144 DDSIAAAQQMGMRFHAARGSMSLGRSkgglppDVVVEEEEAILRDSLRLIQQYHDGsrhsMLRVVLAPCSPFSVTRDLMR 223
Cdd:pfam01979 61 LLEAAEELPLGLRFLGPGCSLDTDGE------LEGRKALREKLKAGAEFIKGMADG----VVFVGLAPHGAPTFSDDELK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 224 ESAVLARAHGVSLHTHLAENDNDVAFSREKFG-----LTPAQYAEDLGWVGR-DVWHAHCVKLDPEGIALFART--GTGV 295
Cdd:pfam01979 131 AALEEAKKYGLPVAIHALETKGEVEDAIAAFGggiehGTHLEVAESGGLLDIiKLILAHGVHLSPTEANLLAEHlkGAGV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 296 AHCPCSNMRLASGIAPIRSMRDAGVSVALGVDGSASNDGAHMLGEARQAMLLQRVGYGpaAMSAREALEIATLGGARVLN 375
Cdd:pfam01979 211 AHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEG--GLSPLEALRMATINPAKALG 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 692381278 376 RDD-IGALAPGMSADFVAFDMedvgyagaghDPVAALVFCTPA-NVSSSVINGRVV 429
Cdd:pfam01979 289 LDDkVGSIEVGKDADLVVVDL----------DPLAAFFGLKPDgNVKKVIVKGKIV 334
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
11-394 |
7.00e-52 |
|
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: 180.94 E-value: 7.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 11 LVTMDAQRREIKDGALVADGPALLWVGATAELPAQYrrmadEGQARVLDMRGKVVTPGLVNTHHHMYQslTRAVPAAQDA 90
Cdd:cd01303 14 LELVEDALRVVEDGLIVVVDGNIIAAGAAETLKRAA-----KPGARVIDSPNQFILPGFIDTHIHAPQ--YANIGSGLGE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 91 ELFSWLQNlymlwsHLTPEMIHVS-----TQTA---MAELMLSGCTTTSDHLYLFPNGSRLDDSIAAAQqmGMRFHAARG 162
Cdd:cd01303 87 PLLDWLET------YTFPEEAKFAdpayaREVYgrfLDELLRNGTTTACYFATIHPESTEALFEEAAKR--GQRAIAGKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 163 SMSLgrskggLPPDVVVEEEEAILRDSLRLIQQYHDgsRHSMLRVVLAPCSPFSVTRDLMRESAVLARAH-GVSLHTHLA 241
Cdd:cd01303 159 CMDR------NAPEYYRDTAESSYRDTKRLIERWHG--KSGRVKPAITPRFAPSCSEELLAALGKLAKEHpDLHIQTHIS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 242 ENDNDVAFSREKFgltPA--QYA---EDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMR 316
Cdd:cd01303 231 ENLDEIAWVKELF---PGarDYLdvyDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 317 DAGVSVALGVDGSASNDGAhMLGEARQAM----LLQRVGYGPAAMSAREALEIATLGGARVLNRDD-IGALAPGMSADFV 391
Cdd:cd01303 308 DAGIKVGLGTDVGGGTSFS-MLDTLRQAYkvsrLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDkIGNFEVGKEFDAV 386
|
...
gi 692381278 392 AFD 394
Cdd:cd01303 387 VID 389
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
11-457 |
2.99e-51 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 179.36 E-value: 2.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 11 LVTMDAQRREIKDGALVADGPALLWVGATAELPAQYRrmadegQARVLDMRGKVVTPGLVNTHHHMYQSLTRAV----PA 86
Cdd:PRK07203 9 AITRDPAKPVIEDGAIAIEGNVIVEIGTTDELKAKYP------DAEFIDAKGKLIMPGLINSHNHIYSGLARGMmaniPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 87 AQDaeLFSWLQNLYmlWS---HLTPEMIHVSTQTAMAELMLSGCTTTSDH--LYLFPNGSrLDDSIAAAQQMGMRfhaar 161
Cdd:PRK07203 83 PPD--FISILKNLW--WRldrALTLEDVYYSALICSLEAIKNGVTTVFDHhaSPNYIGGS-LFTIADAAKKVGLR----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 162 GSMSLGRS-KGGLppdvvvEEEEAILRDSLRLIQqYHDGSRHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHTHL 240
Cdd:PRK07203 153 AMLCYETSdRDGE------KELQEGVEENIRFIK-HIDEAKDDMVEAMFGLHASFTLSDATLEKCREAVKETGRGYHIHV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 241 AENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGV 320
Cdd:PRK07203 226 AEGIYDVSDSHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 321 SVALGVDGSASNdgahMLGEARQAMLLQRVGYGPAAMSAREALEIATLGGARVLNR---DDIGALAPGMSADFVAFD--- 394
Cdd:PRK07203 306 LLGLGTDGYTSD----MFESYKVANFKHKHAGGDPNVGWPESPAMLFENNNKIAERyfgAKFGILEEGAKADLIIVDynp 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692381278 395 ---MEDVGYagAGHdpvaaLVF-CTPANVSSSVINGRVVVEDGRLLTADLPVVLGQHRHLARSLFER 457
Cdd:PRK07203 382 ptpLNEDNI--NGH-----ILFgMNGGSVDTTIVNGKVVMEDRKFLNFDEESIYARARKAAAKLWKR 441
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
11-460 |
8.08e-48 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 170.57 E-value: 8.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 11 LVTMDAQRREIKDGALVADGPALLWVGATAELPAqyrrmadegqARVLDMRGKVVTPGLVNTHHHMYQSLTRAVpaAQDA 90
Cdd:PRK08204 11 VLTMDPAIGDLPRGDILIEGDRIAAVAPSIEAPD----------AEVVDARGMIVMPGLVDTHRHTWQSVLRGI--GADW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 91 ELFSWLQNLY-MLWSHLTPEMIHVSTQTAMAELMLSGCTTTSDHLYLFPNGSRLDDSIAAAQQMGMRFHAARGSmslgrs 169
Cdd:PRK08204 79 TLQTYFREIHgNLGPMFRPEDVYIANLLGALEALDAGVTTLLDWSHINNSPEHADAAIRGLAEAGIRAVFAHGS------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 170 kgGLPPDVVVEEEEAILRDSLRLIQQYHDGSRHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHTHLAendndvaf 249
Cdd:PRK08204 153 --PGPSPYWPFDSVPHPREDIRRVKKRYFSSDDGLLTLGLAIRGPEFSSWEVARADFRLARELGLPISMHQG-------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 250 srekFGLTPAQYA-----EDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVAL 324
Cdd:PRK08204 223 ----FGPWGATPRgveqlHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 325 GVDgSASNDGAHMLGEARQAMLLQRVGYG------------PAAMSAREALEIATLGGARVLNRDD-IGALAPGMSADFV 391
Cdd:PRK08204 299 GVD-VVTSTGGDMFTQMRFALQAERARDNavhlreggmpppRLTLTARQVLEWATIEGARALGLEDrIGSLTPGKQADLV 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 392 AFDMEDVGYAGAgHDPVAALVFCT-PANVSSSVINGRVVVEDGRLLTADLPVVLGQHRHLARSLFERAAA 460
Cdd:PRK08204 378 LIDATDLNLAPV-HDPVGAVVQSAhPGNVDSVMVAGRAVKRNGKLLGVDLERLRRLAAASRDRLLSRRAR 446
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
15-462 |
1.33e-46 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 167.91 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 15 DAQRREIKDGALVADGPALLWVGATAELPAqyrrmadegqARVLDMRGKVVTPGLVNTH-------------HHMYQSLT 81
Cdd:PRK06151 15 DGDHRLLRDGEVVFEGDRILFVGHRFDGEV----------DRVIDAGNALVGPGFIDLDalsdldttilgldNGPGWAKG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 82 RAVPAaqdaelfSWLQNLYmlWSHLTPEMIHVSTQTAMAELMLSGCTTT---SDHLYLFPNGS--RLDDSIAAAQQMGMR 156
Cdd:PRK06151 85 RVWSR-------DYVEAGR--REMYTPEELAFQKRYAFAQLLRNGITTAmpiASLFYRQWAETyaEFAAAAEAAGRLGLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 157 FH---AARGSMSLGRSKGGLppDVVVEEEE--AILRDSLRLIQQyHDGSRHSMLRVVLAPCSPFSVTRDLMRESAVLARA 231
Cdd:PRK06151 156 VYlgpAYRSGGSVLEADGSL--EVVFDEARglAGLEEAIAFIKR-VDGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 232 HGVSLHTHLAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLD---------PEGIALFARTGTGVAHCPCSN 302
Cdd:PRK06151 233 LGCPVRLHCAQGVLEVETVRRLHGTTPLEWLADVGLLGPRLLIPHATYISgsprlnysgGDDLALLAEHGVSIVHCPLVS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 303 MRLASGIAPIRSMRDAGVSVALGVDgSASNDgahMLGEARQAMLLQRVGYG-PAAMSAREALEIATLGGARVLNRDDIGA 381
Cdd:PRK06151 313 ARHGSALNSFDRYREAGINLALGTD-TFPPD---MVMNMRVGLILGRVVEGdLDAASAADLFDAATLGGARALGRDDLGR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 382 LAPGMSADFVAFDMEDVGYaGAGHDPVAALVFC-TPANVSSSVINGRVVVEDGRLLTADLPVVlgqhRHLARSLFERAAA 460
Cdd:PRK06151 389 LAPGAKADIVVFDLDGLHM-GPVFDPIRTLVTGgSGRDVRAVFVDGRVVMEDGRLPGVDLAAL----RAQAQQQFDKLVA 463
|
..
gi 692381278 461 GH 462
Cdd:PRK06151 464 DY 465
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-439 |
1.04e-44 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 161.20 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 1 MTLIALNAdvLVTMDAQRREIKDGALVADGPALLWVGaTAELPAQYrrmadegqarVLDMRGKVVTPGLVNTHHHMYQSL 80
Cdd:PRK06380 1 MSILIKNA--WIVTQNEKREILQGNVYIEGNKIVYVG-DVNEEADY----------IIDATGKVVMPGLINTHAHVGMTA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 81 TRAVpaAQDAELFSWLQNLYMLWSHLTPEMIHVSTQTAMAELMLSGCTTTSDHLYLfpngsrlDDSIA-AAQQMGMRfhA 159
Cdd:PRK06380 68 SKGL--FDDVDLEEFLMKTFKYDSKRTREGIYNSAKLGMYEMINSGITAFVDLYYS-------EDIIAkAAEELGIR--A 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 160 ARGSMSLGR---SKGGLPpdvvVEEEEAILRDslrliqqyHDGSRhsMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSL 236
Cdd:PRK06380 137 FLSWAVLDEeitTQKGDP----LNNAENFIRE--------HRNEE--LVTPSIGVQGIYVANDETYLKAKEIAEKYDTIM 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 237 HTHLAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLAS-GIAPIRSM 315
Cdd:PRK06380 203 HMHLSETRKEVYDHVKRTGERPVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEM 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 316 RDAGVSVALGVDGSASNDGAHMLGEAR-QAMLLQRVGYGPAAMSAREALEIATLGGARVLNRDDiGALAPGMSADFVAFD 394
Cdd:PRK06380 283 LDNGINVTIGTDSNGSNNSLDMFEAMKfSALSVKNERWDASIIKAQEILDFATINAAKALELNA-GSIEVGKLADLVILD 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 692381278 395 MEDV-GYAGAGHDPVAALVFC-TPANVSSSVINGRVVVEDGRLLTAD 439
Cdd:PRK06380 362 ARAPnMIPTRKNNIVSNIVYSlNPLNVDHVIVNGKILKENGRLNGFN 408
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
19-395 |
9.19e-42 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 153.81 E-value: 9.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 19 REIKDGALVADGPALLWVGATAELPAQYRrmadeGQARVLDMRGKVVTPGLVNTHHHMYQSLTRAVPAAQdaeLFSWLQN 98
Cdd:PRK09228 27 RYIEDGLLLVEDGRIVAAGPYAELRAQLP-----ADAEVTDYRGKLILPGFIDTHIHYPQTDMIASYGEQ---LLDWLNT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 99 lymlwsHLTPE------MIHvSTQTA---MAELMLSGCTT----TSDHlylfpnGSRLDDSIAAAQQMGMRFHAARGSMS 165
Cdd:PRK09228 99 ------YTFPEerrfadPAY-AREVAeffLDELLRNGTTTalvfGTVH------PQSVDALFEAAEARNMRMIAGKVLMD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 166 LgrskggLPPDVVVEEEEAILRDSLRLIQQYHDGSRhsmLRVVLAPCSPFSVTRDLMRESAVLARAH-GVSLHTHLAEND 244
Cdd:PRK09228 166 R------NAPDGLRDTAESGYDDSKALIERWHGKGR---LLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 245 NDVAFSREKFgltPAQ------YaEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDA 318
Cdd:PRK09228 237 DEIAWVKELF---PEArdyldvY-ERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 319 GVSVALGVD--GSASNDGAHMLGEARQAMLLQRVgygpaAMSAREALEIATLGGARVLNRDD-IGALAPGMSADFVAFDM 395
Cdd:PRK09228 313 GVRVGLGTDvgGGTSFSMLQTMNEAYKVQQLQGY-----RLSPFQAFYLATLGGARALGLDDrIGNLAPGKEADFVVLDP 387
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
21-395 |
9.55e-40 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 147.40 E-value: 9.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 21 IKDGALVADGPALLWVGATAELPAQYRRmadegQARVLDMRGKVVTPGLVNTHHHMYQSltrAVPAAQDAELFSWLQNlY 100
Cdd:TIGR02967 4 FEDGLLVVENGRIVAVGDYAELKETLPA-----GVEIDDYRGHLIMPGFIDTHIHYPQT---EMIASYGEQLLEWLEK-Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 101 M---------------LWSHLTPEMIHVSTQTAMAElmlsgCT---TTSDHLYlfpngsrlddsiAAAQQMGMRFHAARG 162
Cdd:TIGR02967 75 TfptearfadpdhaeeVAEFFLDELLRNGTTTALVF-----ATvhpESVDALF------------EAALKRGMRMIAGKV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 163 SMSLGrskgglPPDVVVEEEEAILRDSLRLIQQYHDGSRhsmLRVVLAP-----CSPfsvtrDLMRESAVLARAH-GVSL 236
Cdd:TIGR02967 138 LMDRN------APDYLRDTAESSYDESKALIERWHGKGR---LLYAVTPrfaptSSP-----EQLAAAGELAKEYpDVYV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 237 HTHLAENDNDVAFSREKFGLTPAqYA---EDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIR 313
Cdd:TIGR02967 204 QTHLSENKDEIAWVKELFPEAKD-YLdvyDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 314 SMRDAGVSVALGVDGSASNDGA--HMLGEARQAMLLQRvgygpAAMSAREALEIATLGGARVLNRDD-IGALAPGMSADF 390
Cdd:TIGR02967 283 KALEHGVRVGLGTDVGGGTSFSmlQTLREAYKVSQLQG-----ARLSPFEAFYLATLGGARALDLDDrIGNFEPGKEADF 357
|
....*
gi 692381278 391 VAFDM 395
Cdd:TIGR02967 358 VVLDP 362
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
59-427 |
7.24e-36 |
|
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: 137.20 E-value: 7.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 59 DMRGKVVTPGLVNTHHHMYQ----SLTRAVPAAQDAeLFSWLQNLYMLWSHLTPEMIHVSTQTAMAELMLSGCTTTSDHL 134
Cdd:cd01313 34 ALLGGALLPGMPNLHSHAFQramaGLTEYRGSAADS-FWTWRELMYRFAARLTPEQIEAIARQLYIEMLLAGITAVGEFH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 135 YLF--PNGSRLDDS-------IAAAQQMGMRFHAARgSMSLGRSKGGLPPDVVVEEEEAILRDSLRLIQQYHDGSR-HSM 204
Cdd:cd01313 113 YVHhdPDGTPYADPaelaqrvIAAASDAGIGITLLP-VLYARAGFGGPAPNPGQRRFINGYEDFLGLLEKALRAVKeHAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 205 LRVVLAPCSPFSVTRDLMResAVLARAHG-VSLHTHLAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCVKLDPE 283
Cdd:cd01313 192 ARIGVAPHSLRAVPAEQLA--ALAALASEkAPVHIHLAEQPKEVDDCLAAHGRRPVELLLDHGHLDARWCLVHATHLTDN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 284 GIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVDgsaSNDGAHMLGEARQAMLLQR-------VGYGPAA 356
Cdd:cd01313 270 ETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSD---SNARIDLLEELRQLEYSQRlrdrarnVLATAGG 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 692381278 357 MSAREALEIATLGGARVLNRdDIGALAPGMSADFVAFDMEDVGYAGAGHDPVA-ALVFC-TPANVSSSVINGR 427
Cdd:cd01313 347 SSARALLDAALAGGAQALGL-ATGALEAGARADLLSLDLDHPSLAGALPDTLLdAWVFAaGDREVRDVVVGGR 418
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
33-427 |
8.20e-32 |
|
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: 125.25 E-value: 8.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 33 LLWVGATAELPAQYrrmadeGQARVLDMRGKVVTPGLVNTHHHMYQSltrAVPAAQDAELFS-WLQNLYMLWSHLTPEMI 111
Cdd:cd01312 3 ILEVGDYEKLEKRY------PGAKHEFFPNGVLLPGLINAHTHLEFS---ANVAQFTYGRFRaWLLSVINSRDELLKQPW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 112 HVSTQTAMAELMLSGCTTTSDHLylfpnGSRLDDSIAAAQQMGMR-FHAARGSmslgrskgglPPDVVVEEEEAILRDSL 190
Cdd:cd01312 74 EEAIRQGIRQMLESGTTSIGAIS-----SDGSLLPALASSGLRGVfFNEVIGS----------NPSAIDFKGETFLERFK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 191 RLiQQYHDGsrhsMLRVVLAPCSPFSVTRDLMRESAVLARAHGVSLHTHLAENDNDVAF------------------SRE 252
Cdd:cd01312 139 RS-KSFESQ----LFIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWleeskgwfkhfwesflklPKP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 253 KFGLTPAQYAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVDGSASN 332
Cdd:cd01312 214 KKLATAIDFLDMLGGLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 333 DGAHMLGEARQAMLLQRvgyGPAAMS-AREALEIATLGGARVLNRdDIGALAPGMSADFVAFDMEdvgyaGAGHDPVAAL 411
Cdd:cd01312 294 ISLSLLDELRALLDLHP---EEDLLElASELLLMATLGGARALGL-NNGEIEAGKRADFAVFELP-----GPGIKEQAPL 364
|
410
....*....|....*..
gi 692381278 412 VFCTPA-NVSSSVINGR 427
Cdd:cd01312 365 QFILHAkEVRHLFISGK 381
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
64-434 |
9.61e-28 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 114.95 E-value: 9.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 64 VVTPGLVNTHHHMYQ----SLTRAVPAAQDAeLFSWLQNLYMLWSHLTPEMIHVSTQTAMAELMLSGCTTTSDHLYLF-- 137
Cdd:PRK09229 48 PVLPGMPNLHSHAFQramaGLTEVRGPPQDS-FWSWRELMYRFALRLTPDQLEAIARQLYVEMLEAGYTSVGEFHYLHhd 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 138 PNGSRLDDS-------IAAAQQMGMR------FHAARGSmslgrskGGLPPDVV----VEEEEAILR--DSLRliqqyHD 198
Cdd:PRK09229 127 PDGTPYADPaemalriVAAARAAGIGltllpvLYAHSGF-------GGQPPNPGqrrfINDPDGFLRllEALR-----RA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 199 GSRHSMLRVVLAPCSPFSVTRDLMRESAVLARAHGvSLHTHLAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVWHAHCV 278
Cdd:PRK09229 195 LAALPGARLGLAPHSLRAVTPDQLAAVLALAAPDG-PVHIHIAEQTKEVDDCLAWSGARPVEWLLDHAPVDARWCLVHAT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 279 KLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVDGSASNDgahMLGEARQAMLLQR-------VG 351
Cdd:PRK09229 274 HLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGSDSHVSID---LVEELRLLEYGQRlrdrrrnVL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 352 YGPAAMS-AREALEIATLGGARVLNRDdIGALAPGMSADFVAFDMEDVGYAGA-GHDPVAALVFCTPAN-VSSSVINGRV 428
Cdd:PRK09229 351 AAAAQPSvGRRLFDAALAGGAQALGRA-IGGLAVGARADLVVLDLDHPALAGReGDALLDRWVFAGGDAaVRDVWVAGRW 429
|
....*.
gi 692381278 429 VVEDGR 434
Cdd:PRK09229 430 VVRDGR 435
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
11-432 |
4.87e-23 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 100.42 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 11 LVTMDAQRReIKDGALVADGPALLWVGATAELPAqyrrmadEGQARVLDMRGKVVTPGLVNTHHHMYQSLTRAVPAAQDa 90
Cdd:COG1228 17 LVDGTGGGV-IENGTVLVEDGKIAAVGPAADLAV-------PAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 91 elfswlqnlymlwSHLTPEMIHVSTQTAMAELMLS-GCTTTSDHL-YLFPNGSRLDDSIAAAQQMGMRFHAARG-SMSLG 167
Cdd:COG1228 88 -------------GGITPTVDLVNPADKRLRRALAaGVTTVRDLPgGPLGLRDAIIAGESKLLPGPRVLAAGPAlSLTGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 168 RSKGGlppdvvVEEEEAILRDSLR----LIQQYHDGSRHSMlrvvlapcspfsvTRDLMResAVLARAHG----VSLHTH 239
Cdd:COG1228 155 AHARG------PEEARAALRELLAegadYIKVFAEGGAPDF-------------SLEELR--AILEAAHAlglpVAAHAH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 240 LAENDNDVAfsreKFGLTPAqyaedlgwvgrdvwhAHCVKLDPEGIALFARTGTgVAHCP------------------CS 301
Cdd:COG1228 214 QADDIRLAV----EAGVDSI---------------EHGTYLDDEVADLLAEAGT-VVLVPtlslflallegaaapvaaKA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 302 NMRLASGIAPIRSMRDAGVSVALGVDGSASND-GAHMLGEARQAmllqrVGYGpaaMSAREALEIATLGGARVLNRDD-I 379
Cdd:COG1228 274 RKVREAALANARRLHDAGVPVALGTDAGVGVPpGRSLHRELALA-----VEAG---LTPEEALRAATINAAKALGLDDdV 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 692381278 380 GALAPGMSADFVAFDmedvgyagagHDPVAALvfCTPANVSSSVINGRVVVED 432
Cdd:COG1228 346 GSLEPGKLADLVLLD----------GDPLEDI--AYLEDVRAVMKDGRVVDRS 386
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
69-372 |
2.97e-17 |
|
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: 81.61 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 69 LVNTHHHMYQSLTRAVPAAQdaelfsWLQNLYMLWSHLTPEMIHvstqTAMAELMLSGCTTTSDHLYLFPNGSRLDDSIA 148
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNL------ELKEAEELSPEDLYEDTL----RALEALLAGGVTTVVDMGSTPPPTTTKAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 149 AAQqmgmrfhAARGSMSLGRSKGGLPPDVVVEEEEAILRDSLRLIQQYHDGSRHSMLRVVLAPCSPFSVtrDLMRESAVL 228
Cdd:cd01292 71 VAE-------AARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSD--ESLRRVLEE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 229 ARAHGVSLHTHLAENDNDVAFSREkfgltpaqyAEDLGWVGRDVWHAHCVKLDPEGIALFARTGTGVAHCPCSNMRLAS- 307
Cdd:cd01292 142 ARKLGLPVVIHAGELPDPTRALED---------LVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRd 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692381278 308 --GIAPIRSMRDAGVSVALGVDGSASNDGAHMLGEARQAMLLQRVGygpaaMSAREALEIATLGGAR 372
Cdd:cd01292 213 geGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG-----LSLEEALRLATINPAR 274
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
1-397 |
3.31e-16 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 80.40 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 1 MTLIAlnADVLVTMDAQRREIKDGALVADGpALLWVGATAELPAQYrrmadeGQARVLDMRGKVVTPGLVNTHHHMYQSl 80
Cdd:PRK08418 1 MKIIG--ASYIFTCDENFEILEDGAVVFDD-KILEIGDYENLKKKY------PNAKIQFFKNSVLLPAFINPHTHLEFS- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 81 travpaAQDAEL-----FSWLQNLYM----LWSHLTPEMIhvstQTAMAELMLSGCTT---TSDHlylfpnGSRLDdSIA 148
Cdd:PRK08418 71 ------ANKTTLdygdfIPWLGSVINhredLLEKCKGALI----QQAINEMLKSGVGTigaISSF------GIDLE-ICA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 149 AAQQMGMRFHAARGSMslgrskgglpPDVVVEEEEAILRdSLRLIQQYHDgsrhSMLRVVLAPCSPFSVTRDLMRESAVL 228
Cdd:PRK08418 134 KSPLRVVFFNEILGSN----------ASAVDELYQDFLA-RFEESKKFKS----KKFIPAIAIHSPYSVHPILAKKALQL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 229 ARAHGVSLHTH----------LAENDNDVA------FSREKFGLTPAQYAEDLGwvGRDVWHAHCVKLDPEGIALFARTG 292
Cdd:PRK08418 199 AKKENLLVSTHfleskaerewLEESKGWFKkffekfLKEPKPLYTPKEFLELFK--GLRTLFTHCVYASEEELEKIKSKN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 293 TGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVDGSASNDGAHMLGEARQAMLLQRvgYGPAAMSAREALEIATLGGAR 372
Cdd:PRK08418 277 ASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISLSLLDELRAALLTHA--NMPLLELAKILLLSATRYGAK 354
|
410 420
....*....|....*....|....*
gi 692381278 373 VLNRDDiGALAPGMSADFVAFDMED 397
Cdd:PRK08418 355 ALGLNN-GEIKEGKDADLSVFELPE 378
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
276-397 |
2.11e-14 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 74.22 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 276 HCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVDgsaSNDGAHMLGEARQAMLLQRVGYGpa 355
Cdd:cd01296 235 HLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTD---FNPGSSPTSSMPLVMHLACRLMR-- 309
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 692381278 356 aMSAREALEIATLGGARVLNR-DDIGALAPGMSADFVAFDMED 397
Cdd:cd01296 310 -MTPEEALTAATINAAAALGLgETVGSLEVGKQADLVILDAPS 351
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
209-373 |
1.88e-12 |
|
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: 67.43 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 209 LAPCSPFSVTRDLMREsavLARAHGVSLHTHLAENDNDVafsrekfGLTPAQYAEDLGwvgRDVWhAHCVKLDPEGIALF 288
Cdd:cd01305 117 LGLSSANDVDLEDILE---LLRRRGKLFAIHASETRESV-------GMTDIERALDLE---PDLL-VHGTHLTDEDLELV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 289 ARTGTGVAHCPCSNMRLASGIAPIRSMRDAGVSVALGVDGSASNDgAHMLGEARQAMLLQRVgygPAAMSAREALEIATL 368
Cdd:cd01305 183 RENGVPVVLCPRSNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNE-PDMWAEMEFLAKYSRL---QGYLSPLEILRMATV 258
|
....*
gi 692381278 369 GGARV 373
Cdd:cd01305 259 NAAEF 263
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
20-429 |
7.51e-12 |
|
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: 66.89 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 20 EIKDGALVADGPALlwvgataelpaqyrrmADEGQARVLDMRGKVVTPGLVNTHHHMYQSLT----RAV-PAAQDAELFS 94
Cdd:cd01293 18 AIEDGRIAAIGPAL----------------AVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFTggrwPNNsGGTLLEAIIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 95 WLQnlymLWSHLTPEMIHVSTQTAMAELMLSGCTTTSDHLYLFP-NGSRLDDSIAAAQQmgmrfhaargsmslgRSKGGL 173
Cdd:cd01293 82 WEE----RKLLLTAEDVKERAERALELAIAHGTTAIRTHVDVDPaAGLKALEALLELRE---------------EWADLI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 174 PPDVVV---------EEEEAILRDSLRLiqqyhdGSRhsmlrvVLAPCSPFSVTRDLMRESAV---LARAHGVSLHTHLA 241
Cdd:cd01293 143 DLQIVAfpqhgllstPGGEELMREALKM------GAD------VVGGIPPAEIDEDGEESLDTlfeLAQEHGLDIDLHLD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 242 ENDNDVAFSREKFgltpAQYAEDLGWVGRdVWHAHCVKLD--PEG-----IALFARTGTGVAHCPCSNMRLAS------- 307
Cdd:cd01293 211 ETDDPGSRTLEEL----AEEAERRGMQGR-VTCSHATALGslPEAevsrlADLLAEAGISVVSLPPINLYLQGredttpk 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 308 --GIAPIRSMRDAGVSVALGVD---------GSASndgahMLGEARQAMLLQRVGyGPAAMSAreALEIATLGGARVLNR 376
Cdd:cd01293 286 rrGVTPVKELRAAGVNVALGSDnvrdpwypfGSGD-----MLEVANLAAHIAQLG-TPEDLAL--ALDLITGNAARALGL 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 692381278 377 DDIGaLAPGMSADFVAFDMEDVgyagaghdpvaALVFCTPANVSSSVINGRVV 429
Cdd:cd01293 358 EDYG-IKVGCPADLVLLDAEDV-----------AEAVARQPPRRVVIRKGRVV 398
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
1-394 |
6.49e-11 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 64.43 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 1 MTLIALNADVLV------TMDAQRREIkdGALVADGPALLWVGATAELPAQYRRmadegQARVLDMRGKVVTPGLVNTHH 74
Cdd:COG1574 1 MKLAAAAADLLLtngriyTMDPAQPVA--EAVAVRDGRIVAVGSDAEVRALAGP-----ATEVIDLGGKTVLPGFIDAHV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 75 HMYQS---------------------LTRAVPAAQDAEL---FSWLQNLYMLWSHLTPE------------MIHVSTQTA 118
Cdd:COG1574 74 HLLGGglallgvdlsgarsldellarLRAAAAELPPGEWilgRGWDESLWPEGRFPTRAdldavspdrpvvLTRVDGHAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 119 MAE---LMLSGCTTTSDhlylFPNGSRL----------------------------DDSIAAAQQMGMRFHAARG----- 162
Cdd:COG1574 154 WVNsaaLELAGITADTP----DPEGGEIerdadgeptgvlreaamdlvraaippptPEELRAALRAALRELASLGitsvh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 163 SMSLG----------RSKGGLPPDVVV------EEEEAILRDSLRliqqyhDGSRHSMLRV-----------------VL 209
Cdd:COG1574 230 DAGLGpddlaayrelAAAGELPLRVVLylgaddEDLEELLALGLR------TGYGDDRLRVggvklfadgslgsrtaaLL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 210 AP-------CSPFSVTRDLMRESAVLARAHGVSLHTH----LAendNDV---AFsrekfgltpAQYAEDLGWvgRDVWH- 274
Cdd:COG1574 304 EPyaddpgnRGLLLLDPEELRELVRAADAAGLQVAVHaigdAA---VDEvldAY---------EAARAANGR--RDRRHr 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 275 -AHCVKLDPEGIALFARTGTGV----AHC----PCSNMRL----ASGIAPIRSMRDAGVSVALGVDGSASNdgAHMLGEA 341
Cdd:COG1574 370 iEHAQLVDPDDLARFAELGVIAsmqpTHAtsdgDWAEDRLgperAARAYPFRSLLDAGAPLAFGSDAPVEP--LDPLLGI 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 692381278 342 RQAMLLQR---VGYGPA-AMSAREALEIATLGGARVLNRDD-IGALAPGMSADFVAFD 394
Cdd:COG1574 448 YAAVTRRTpsgRGLGPEeRLTVEEALRAYTIGAAYAAFEEDeKGSLEPGKLADFVVLD 505
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
239-426 |
2.30e-10 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 61.98 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 239 HLAENDNDVAFSREKFGLTPAQYAEDLGWVGRDVwhAHCVKLDPEGIALFARTGTGVAHCPCSNMRLASGIAPIRSMRDA 318
Cdd:PRK07213 198 HAAEHKGSVEYSLEKYGMTEIERLINLGFKPDFI--VHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 319 GVSVALGVDGSASNDgAHMLgeaRQAMLLQRVGYgpaaMSAREALEIATLGGARVLNRDDIGALAPGMSADFVAFDMEDV 398
Cdd:PRK07213 276 GILLGIGTDNFMANS-PSIF---REMEFIYKLYH----IEPKEILKMATINGAKILGLINVGLIEEGFKADFTFIKPTNI 347
|
170 180
....*....|....*....|....*....
gi 692381278 399 GYAGaghDPVAALVF-CTPANVSSSVING 426
Cdd:PRK07213 348 KFSK---NPYASIITrCESGDIVNKILKG 373
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
228-433 |
1.49e-09 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 59.56 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 228 LARAHGVSLHTHLAENDNDVAFSREKFgltpAQYAEDLGWVGR-DVWHAHCVKLDPEG-----IALFARTGTGVAhcpcS 301
Cdd:PRK05985 199 LAERHGVGIDIHLHEPGELGAFQLERI----AARTRALGMQGRvAVSHAFCLGDLPERevdrlAERLAEAGVAIM----T 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 302 NMRLASGIAPIRSMRDAGVSVALGVDG-----SASNDGaHMLGearQAMLLqrvGYGPAAMSARE---ALEIATLGGARV 373
Cdd:PRK05985 271 NAPGSVPVPPVAALRAAGVTVFGGNDGirdtwWPYGNG-DMLE---RAMLI---GYRSGFRTDDElaaALDCVTHGGARA 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 374 LNRDDIGaLAPGMSADFVAFDMEDVGYAGAGHdPVAALVfctpanvsssVINGRVVVEDG 433
Cdd:PRK05985 344 LGLEDYG-LAVGARADFVLVDAETVAEAVVAV-PVRRLV----------VRGGRIVARDG 391
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
55-394 |
9.62e-09 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 56.92 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 55 ARVLDMRGKVVTPGLVNTHHHMYQSLTRAVPAAQdaelfswlqnlymlwshlTPEMIHVSTQTAMAELML-SGCTT---- 129
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLA------------------LPVEYRTIRATRQARAALrAGFTTvrda 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 130 -TSDHLYL-------FPNGSRLddsIAAAQQMGMRF-HAARGSMSLGRSKGGLPPdVVVEEEEAI------LRDSLRLIQ 194
Cdd:cd01299 63 gGADYGLLrdaidagLIPGPRV---FASGRALSQTGgHGDPRGLSGLFPAGGLAA-VVDGVEEVRaavreqLRRGADQIK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 195 QYHDGSRHSMLRVVLAPCSPFSVTRDLMREsavlARAHGVSLHTHlaendndvAFSREKfgltpAQYAEDLGwVgRDVwh 274
Cdd:cd01299 139 IMATGGVLSPGDPPPDTQFSEEELRAIVDE----AHKAGLYVAAH--------AYGAEA-----IRRAIRAG-V-DTI-- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 275 AHCVKLDPEGIALFARTGTGVahCPC-SNMR----------------------LASGIAPIRSMRDAGVSVALGVD-GSA 330
Cdd:cd01299 198 EHGFLIDDETIELMKEKGIFL--VPTlATYEalaaegaapglpadsaekvalvLEAGRDALRRAHKAGVKIAFGTDaGFP 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692381278 331 SNDGAHMLGEARqamLLQRVGygpaaMSAREALEIATLGGARVLNR-DDIGALAPGMSADFVAFD 394
Cdd:cd01299 276 VPPHGWNARELE---LLVKAG-----GTPAEALRAATANAAELLGLsDELGVIEAGKLADLLVVD 332
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
303-391 |
3.94e-07 |
|
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: 52.31 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 303 MRLASGIAPIRSMRDAGVSVALGVD----GSASNDGAHmlgeA---RQAMLLQRVGYGPAAMSAREALEIATLGGARVLN 375
Cdd:cd01300 386 EERAKRSYPFRSLLDAGVPVALGSDapvaPPDPLLGIW----AavtRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIG 461
|
90
....*....|....*..
gi 692381278 376 RDD-IGALAPGMSADFV 391
Cdd:cd01300 462 EEDeKGSLEPGKLADFV 478
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
306-430 |
1.80e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 50.22 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 306 ASGIAPIRSMRDAGVSVALGVDGS-ASNDGAHMLGEA--RQAMLLQRVGYGPAAMSAREALEIATLGGARVLNRDD-IGA 381
Cdd:pfam07969 345 ARGLTPVKELLNAGVKVALGSDAPvGPFDPWPRIGAAvmRQTAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDrKGT 424
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 692381278 382 LAPGMSADFVAFDMEDVgyagagHDPVAALVfctPANVSSSVINGRVVV 430
Cdd:pfam07969 425 LGVGKDADLVVLDDDPL------TVDPPAIA---DIRVRLTVVDGRVVY 464
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
362-436 |
2.62e-06 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 49.71 E-value: 2.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692381278 362 ALEIATLGGARVLNRDDIGALAPGMSADFVAF-DMEDVgyagaghdpVAALVFctpanvsssvINGRVVVEDGRLL 436
Cdd:COG1001 289 AIQMATLNAAEHFGLKDLGAIAPGRRADIVLLdDLEDF---------KVEKVY----------ADGKLVAEDGKLL 345
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
361-434 |
9.29e-05 |
|
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: 44.60 E-value: 9.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692381278 361 EALEIATLGGARVLNRDDIGALAPGMSADFVAFDMEDVgyagagHDPVAALVFCTPAN-VSSSVINGRVVVEDGR 434
Cdd:cd01297 339 EAVRKMTGLPARVFGLADRGRIAPGYRADIVVFDPDTL------ADRATFTRPNQPAEgIEAVLVNGVPVVRDGA 407
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
357-431 |
9.84e-04 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 41.44 E-value: 9.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692381278 357 MSAREALEIATLGGARVLNRDDIGALAPGMSADFVAF-DMEDVgyagaghdpvaalvfctpaNVSSSVINGRVVVE 431
Cdd:cd01295 235 IPPEDAIQMATINPAECYGLHDLGAIAPGRIADIVILdDLENF-------------------NITTVLAKGIAVVE 291
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
361-394 |
2.81e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 39.70 E-value: 2.81e-03
10 20 30
....*....|....*....|....*....|....*
gi 692381278 361 EALEIATLGGARVLNRDD-IGALAPGMSADFVAFD 394
Cdd:COG1820 326 EAVRMASLNPARALGLDDrKGSIAPGKDADLVVLD 360
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
228-393 |
5.72e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 38.81 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 228 LARAHGVSLHTHLAENDNDVAFSREKFgltpAQYAEDLGWVGRdVWHAHCVKLD-------PEGIALFARTGTGVAHCPC 300
Cdd:PRK07583 220 LARERGLDLDLHVDETGDPASRTLKAV----AEAALRNGFEGK-VTCGHCCSLAvqpeeqaQATIALVAEAGIAIVSLPM 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692381278 301 SNMRLAS----------GIAPIRSMRDAGVSVALGVDGSasND-----GAH-MLGEARQAMllqRVG-----YGPAAmsa 359
Cdd:PRK07583 295 CNLYLQDrqpgrtprwrGVTLVHELKAAGIPVAVASDNC--RDpfyayGDHdMLEVFREAV---RILhldhpYDDWP--- 366
|
170 180 190
....*....|....*....|....*....|....
gi 692381278 360 realEIATLGGARVLNRDDIGALAPGMSADFVAF 393
Cdd:PRK07583 367 ----AAVTTTPADIMGLPDLGRIAVGAPADLVLF 396
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
357-397 |
6.97e-03 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 38.46 E-value: 6.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 692381278 357 MSAREALEIATLGGARVLNRDDIGALAPGMSADFVAFDMED 397
Cdd:cd01307 277 MPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFDLKD 317
|
|
| |
