|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
1-471 |
0e+00 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 834.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 1 MSLIIKNAHAILSGLPGEAARLAGPDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQGLN 80
Cdd:PRK12393 2 PSLLIRNAAAIMTGLPGDAARLGGPDIRIRDGRIAAIGALTPLPGERVIDATDCVVYPGWVNTHHHLFQSLLKGVPAGIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 81 QSLTAWLSATPYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADHNYLYWPDMPFDTSEIVFSEGEALGMRIVLCRGGAT 160
Cdd:PRK12393 82 QSLTAWLAAVPYRFRARFDEDLFRLAARIGLVELLRSGCTTVADHHYLYHPGMPFDTGDILFDEAEALGMRFVLCRGGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 161 QGRAVEQDLPVALRPETFDSYMADVERLVSRYHDPRPESLRRVVMAPTTVLHSAPGAQLREMAKLARQLRIRLHSHLSET 240
Cdd:PRK12393 162 QTRGDHPGLPTALRPETLDQMLADVERLVSRYHDASPDSLRRVVVAPTTPTFSLPPELLREVARAARGMGLRLHSHLSET 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 241 VDYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVS 320
Cdd:PRK12393 242 VDYVDFCREKYGMTPVQFVAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 321 LGVDGAASNEAADMQSEAHAAWLLQRArkgmlaqpryaggtfEGGADAATVEDVVRWGCAGGAQILGLAQSGTLQVGMQA 400
Cdd:PRK12393 322 LGVDGAASNESADMLSEAHAAWLLHRA---------------EGGADATTVEDVVHWGTAGGARVLGLDAIGTLAVGQAA 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460622887 401 DLAIYRLDDPRYFGLHDMAIGPVACGGRAALKALLLNGRPIVEDDAIPGLDLDAMRHDALAAVRTLQQRAA 471
Cdd:PRK12393 387 DLAIYDLDDPRFFGLHDPAIAPVACGGPAPVKALLVNGRPVVENGAIPGLDLAELRHDARAAVRRLLQRAA 457
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
3-448 |
3.98e-138 |
|
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: 403.12 E-value: 3.98e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 3 LIIKNAHAILsglPGEAARLAGPDIRIRDGKIAAIGSLTPLPE---ERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQGL 79
Cdd:cd01298 1 ILIRNGTIVT---TDPRRVLEDGDVLVEDGRIVAVGPALPLPAypaDEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 80 NqsLTAWLSATPYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADHNYLYwpdmpfdtSEIVFSEGEALGMRIVLCRGGA 159
Cdd:cd01298 78 P--LMEWLKDLIWPLERLLTEEDVYLGALLALAEMIRSGTTTFADMYFFY--------PDAVAEAAEELGIRAVLGRGIM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 160 TQGRAVEQDLPVALrpetfdsymADVERLVSRYHDPrPESLRRVVMAPTTVLhSAPGAQLREMAKLARQLRIRLHSHLSE 239
Cdd:cd01298 148 DLGTEDVEETEEAL---------AEAERLIREWHGA-ADGRIRVALAPHAPY-TCSDELLREVAELAREYGVPLHIHLAE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 240 TVDYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPV 319
Cdd:cd01298 217 TEDEVEESLEKYGKRPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 320 SLGVDGAASNEAADMQSEAHAAWLLQRARKGMlaqpryaggtfeggADAATVEDVVRWGCAGGAQILGLAQSGTLQVGMQ 399
Cdd:cd01298 297 GLGTDGAASNNNLDMFEEMRLAALLQKLAHGD--------------PTALPAEEALEMATIGGAKALGLDEIGSLEVGKK 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1460622887 400 ADLAIYRLDDPRYFGLHDMAIGPVACGGRAALKALLLNGRPIVEDDAIP 448
Cdd:cd01298 363 ADLILIDLDGPHLLPVHDPISHLVYSANGGDVDTVIVNGRVVMEDGELL 411
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
1-470 |
4.03e-138 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 404.62 E-value: 4.03e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 1 MSLIIKNAHAILSGlPGEAARLAGPDIRIRDGKIAAIG--SLTPLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQG 78
Cdd:PRK08203 1 TTLWIKNPLAIVTM-DAARREIADGGLVVEGGRIVEVGpgGALPQPADEVFDARGHVVTPGLVNTHHHFYQTLTRALPAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 79 LNQSLTAWLSATpYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADHNYLYwPDMPFDTSEIVFSEGEALGMRIVLCRG- 157
Cdd:PRK08203 80 QDAELFPWLTTL-YPVWARLTPEMVRVATQTALAELLLSGCTTSSDHHYLF-PNGLRDALDDQIEAAREIGMRFHATRGs 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 158 ---GATQG----RAVEQDLPVALrpetfdsymADVERLVSRYHDPRPESLRRVVMAP------TTVLhsapgaqLREMAK 224
Cdd:PRK08203 158 mslGESDGglppDSVVEDEDAIL---------ADSQRLIDRYHDPGPGAMLRIALAPcspfsvSREL-------MRESAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 225 LARQLRIRLHSHLSETVDYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGS 304
Cdd:PRK08203 222 LARRLGVRLHTHLAETLDEEAFCLERFGMRPVDYLEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLAS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 305 GIADLLALEQAGVPVSLGVDGAASNEAADMQSEAHAAWLLQRARkgmlaqpryaggtfeGGADAATVEDVVRWGCAGGAQ 384
Cdd:PRK08203 302 GIAPVRELRAAGVPVGLGVDGSASNDGSNLIGEARQALLLQRLR---------------YGPDAMTAREALEWATLGGAR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 385 ILGLAQSGTLQVGMQADLAIYRLDDPRYFGLHDmaigPVAC---GGRAALKALLLNGRPIVEDDAIPGLDLDAMRHDALA 461
Cdd:PRK08203 367 VLGRDDIGSLAPGKLADLALFDLDELRFAGAHD----PVAAlvlCGPPRADRVMVGGRWVVRDGQLTTLDLAALIARHRA 442
|
....*....
gi 1460622887 462 AVRTLQQRA 470
Cdd:PRK08203 443 AARRLAAGA 451
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-444 |
4.14e-115 |
|
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: 344.50 E-value: 4.14e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 2 SLIIKNAHaILSGLPgEAARLAGPDIRIRDGKIAAIGSLTPL----PEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQ 77
Cdd:COG0402 1 DLLIRGAW-VLTMDP-AGGVLEDGAVLVEDGRIAAVGPGAELparyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 78 GLnqSLTAWLSATPYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADHNYLYWpdmpfDTSEIVFSEGEALGMRIVLCRG 157
Cdd:COG0402 79 DL--PLLDWLEEYIWPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHP-----ESADALAEAAAEAGIRAVLGRG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 158 gatqgrAVEQDLPVALRpETFDSYMADVERLVSRYHDpRPESLRRVVMAPTTvLHSAPGAQLREMAKLARQLRIRLHSHL 237
Cdd:COG0402 152 ------LMDRGFPDGLR-EDADEGLADSERLIERWHG-AADGRIRVALAPHA-PYTVSPELLRAAAALARELGLPLHTHL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 238 SETVDYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGV 317
Cdd:COG0402 223 AETRDEVEWVLELYGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 318 PVSLGVDGAASNEAADMQSEAHAAWLLQRARkgmlaqpryaggtfEGGADAATVEDVVRWGCAGGAQILGLA-QSGTLQV 396
Cdd:COG0402 303 RVGLGTDGAASNNSLDMFEEMRLAALLQRLR--------------GGDPTALSAREALEMATLGGARALGLDdEIGSLEP 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1460622887 397 GMQADLAIYRLDDPRYFGLHDMAIGPVACGGRAALKALLLNGRPIVED 444
Cdd:COG0402 369 GKRADLVVLDLDAPHLAPLHDPLSALVYAADGRDVRTVWVAGRVVVRD 416
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
26-472 |
9.11e-53 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 183.66 E-value: 9.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 26 DIRIRDGKIAAIGSLTPLPE-ERQIDARDCVIYPAWVNTHHHLFQSLLKGepQGLNQSLTAWLSATPYRFRAAFDEHTFR 104
Cdd:PRK07228 23 DVLIEDDRIAAVGDRLDLEDyDDHIDATGKVVIPGLIQGHIHLCQTLFRG--IADDLELLDWLKDRIWPLEAAHDAESMY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 105 LAVRIGLVELLRSGCASVADHNYLYWPDMPFdtseivfsegEAL---GMRIVLcrggatqGRAV---EQDLPVALRPETF 178
Cdd:PRK07228 101 YSALLGIGELIESGTTTIVDMESVHHTDSAF----------EAAgesGIRAVL-------GKVMmdyGDDVPEGLQEDTE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 179 DSyMADVERLVSRYHDPRPESLRRVVmAPTTVLhSAPGAQLREMAKLARQLRIRLHSHLSETVDYLDAARQKFSMTPVQY 258
Cdd:PRK07228 164 AS-LAESVRLLEKWHGADNGRIRYAF-TPRFAV-SCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEEETGMRNIHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 259 CAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVSLGVDGAASNEAADMQSEA 338
Cdd:PRK07228 241 LDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGAPCNNTLDPFTEM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 339 HAAWLLQRARkgmlaqpryaggtfEGGADAATVEDVVRWGCAGGAQILGLAQS-GTLQVGMQADLAIYRLDDPRYFGLHD 417
Cdd:PRK07228 321 RQAALIQKVD--------------RLGPTAMPARTVFEMATLGGAKAAGFEDEiGSLEEGKKADLAILDLDGLHATPSHG 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1460622887 418 MAIGP--VACGGRAALKALLLNGRPIVEDDAIPGLDLDAMRHDALAAVRTLQQRAAV 472
Cdd:PRK07228 387 VDVLShlVYAAHGSDVETTMVDGKIVMEDGELTTIDADAVRREANRSIKRLLKRAGL 443
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
2-470 |
5.63e-44 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 159.92 E-value: 5.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 2 SLIIKNAHAilsgLPGEAARLAGPDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQGLnq 81
Cdd:PRK06038 3 DIIIKNAYV----LTMDAGDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 82 SLTAWLSATPYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADHnYLYWPDmpfdTSEIVfsegEALGMRIVLCRGGATQ 161
Cdd:PRK06038 77 PLAEWLNDHIWPAEAKLTAEDVYAGSLLACLEMIKSGTTSFADM-YFYMDE----VAKAV----EESGLRAALSYGMIDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 162 GRaveqdlpvalrPETFDSYMADVERLVSRYHDpRPESLRRVVMAPTTVlHSAPGAQLREMAKLARQLRIRLHSHLSETV 241
Cdd:PRK06038 148 GD-----------DEKGEAELKEGKRFVKEWHG-AADGRIKVMYGPHAP-YTCSEEFLSKVKKLANKDGVGIHIHVLETE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 242 DYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVSL 321
Cdd:PRK06038 215 AELNQMKEQYGMCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 322 GVDGAASNEAADMQSEAHAAWLLQRARKgmlaqpryaggtfeGGADAATVEDVVRWGCAGGAQILGLaQSGTLQVGMQAD 401
Cdd:PRK06038 295 GTDGCASNNNLDMFEEMKTAALLHKVNT--------------MDPTALPARQVLEMATVNGAKALGI-NTGMLKEGYLAD 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460622887 402 LAIYRLDDPRYFGLHDMAIGPVACGGRAALKALLLNGRPIVEDDAIPGLDLDAMRHDALAAVRTLQQRA 470
Cdd:PRK06038 360 IIIVDMNKPHLTPVRDVPSHLVYSASGSDVDTTIVDGRILMEDYKVLCMDEQDVMEDAKKAAEELVSRV 428
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-466 |
8.84e-42 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 153.80 E-value: 8.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 1 MSLIIKNAHAILsglpGEAARLAGPDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQGLn 80
Cdd:PRK08393 1 MSILIKNGYVIY----GENLKVIRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTHSPMVLLRGLADDV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 81 qSLTAWLSATPYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADhnylywpdMPFDTSEIVFSEGEAlGMRIVLCRGGAT 160
Cdd:PRK08393 76 -PLMEWLQNYIWPRERKLKRKDIYWGAYLGLLEMIKSGTTTFVD--------MYFHMEEVAKATLEV-GLRGYLSYGMVD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 161 QGRavEQDLPVALRpETFDSYMAdVERLVSryhdprpeSLRRVVMAPTTVLHSAPgAQLREMAKLARQLRIRLHSHLSET 240
Cdd:PRK08393 146 LGD--EEKREKEIK-ETEKLMEF-IEKLNS--------PRVHFVFGPHAPYTCSL-ALLKWVREKAREWNKLITIHLSET 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 241 VDYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVS 320
Cdd:PRK08393 213 MDEIKQIREKYGKSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 321 LGVDGAASNEAADMQSEAHAAWLLQRARKgmlAQPRYaggtfeggADAatvEDVVRWGCAGGAQILGLaQSGTLQVGMQA 400
Cdd:PRK08393 293 LGTDGAASNNNLDMLREMKLAALLHKVHN---LDPTI--------ADA---ETVFRMATQNGAKALGL-KAGVIKEGYLA 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460622887 401 DLAIYRLDDPRYFGLHDMAIGPVACGGRAALKALLLNGRPIVEDDAIPGLDLDAMRHDALAAVRTL 466
Cdd:PRK08393 358 DIAVIDFNRPHLRPINNPISHLVYSANGNDVETTIVDGKIVMLDGEVLTLDEEKILDKFLKVIEKL 423
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
29-461 |
8.12e-35 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 135.04 E-value: 8.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 29 IRDGKIAAIG----SLTPLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQGLnqSLTAWLSATPYRFRAAFDEHTF- 103
Cdd:PRK09045 33 IRDGRIVAILpraeARARYAAAETVELPDHVLIPGLINAHTHAAMSLLRGLADDL--PLMTWLQDHIWPAEGAWVSEEFv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 104 RLAVRIGLVELLRSGCASVADhNYLYwpdmpfdtSEIVFSEGEALGMRIVLCrggatqgrAVEQDLPVALrPETFDSYMA 183
Cdd:PRK09045 111 RDGTLLAIAEMLRGGTTCFND-MYFF--------PEAAAEAAHQAGMRAQIG--------MPVLDFPTAW-ASDADEYLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 184 DVERLVSRYHDprpESLRRVVMAPttvlHsAP----GAQLREMAKLARQLRIRLHSHLSETVDYLDAARQKFSMTPVQYC 259
Cdd:PRK09045 173 KGLELHDQWRH---HPLISTAFAP----H-APytvsDENLERIRTLAEQLDLPIHIHLHETAQEIADSLKQHGQRPLARL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 260 AEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVSLGVDGAASNEAADMQSEAH 339
Cdd:PRK09045 245 ARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDGAASNNDLDLFGEMR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 340 AAWLLQrarKGMlaqpryaggtfEGGADAATVEDVVRWGCAGGAQILGL-AQSGTLQVGMQADLAIYRLDDPRYFGLHDM 418
Cdd:PRK09045 325 TAALLA---KAV-----------AGDATALPAHTALRMATLNGARALGLdDEIGSLEPGKQADLVAVDLSGLETQPVYDP 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1460622887 419 AIGPVACGGRAALKALLLNGRPIVEDDAIPGLDLDAMRHDALA 461
Cdd:PRK09045 391 VSQLVYAAGREQVSHVWVAGKQLLDDRELTTLDEAELLARARQ 433
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
29-402 |
1.60e-34 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 133.59 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 29 IRDGKIAAIGSLTPL---PEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQGLNqsLTAWLSATPYRFRAAFDEHTFRL 105
Cdd:PRK06687 26 VKDSQIVYVGQDKPAfleQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSN--LHEWLNDYIWPAESEFTPDMTTN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 106 AVRIGLVELLRSGCASVADhnyLYWPDmPFDTSEIvFSEGEALGMRivlCRGGATQGRAveqdlPVALRPETFDSYMADV 185
Cdd:PRK06687 104 AVKEALTEMLQSGTTTFND---MYNPN-GVDIQQI-YQVVKTSKMR---CYFSPTLFSS-----ETETTAETISRTRSII 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 186 ERLVSrYHDPRpeslRRVVMAPttvlHSaPGAQLREMAK----LARQLRIRLHSHLSETVDYLDAARQKFSMTPVQYCAE 261
Cdd:PRK06687 171 DEILK-YKNPN----FKVMVAP----HS-PYSCSRDLLEasleMAKELNIPLHVHVAETKEESGIILKRYGKRPLAFLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 262 HDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVSLGVDGAASNEAADMQSEAHAA 341
Cdd:PRK06687 241 LGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVASNNNLDMFEEGRTA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1460622887 342 WLLQRARKGMLAQpryagGTFEGGADAATVEdvvrwgcagGAQILGLA-QSGTLQVGMQADL 402
Cdd:PRK06687 321 ALLQKMKSGDASQ-----FPIETALKVLTIE---------GAKALGMEnQIGSLEVGKQADF 368
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
27-404 |
1.32e-31 |
|
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: 125.85 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 27 IRIRDGKIAAIGSLTPL-----PEERQIDARDCVIYPAWVNTHHHLFQSLLKGepQGLNQSLTAWLSATPY----RFR-A 96
Cdd:cd01303 29 IVVVDGNIIAAGAAETLkraakPGARVIDSPNQFILPGFIDTHIHAPQYANIG--SGLGEPLLDWLETYTFpeeaKFAdP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 97 AFDEHTFRLAVRiglvELLRSGCASVAdhnylYWPDMPFDTSEIVFSEGEALGMRIVLcrggatqGRAV-EQDLPVALRp 175
Cdd:cd01303 107 AYAREVYGRFLD----ELLRNGTTTAC-----YFATIHPESTEALFEEAAKRGQRAIA-------GKVCmDRNAPEYYR- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 176 ETFDSYMADVERLVSRYHDPRPeslrRV--VMAPTTVLHSAPGaQLREMAKLARQLR-IRLHSHLSETVDYLDAARQKF- 251
Cdd:cd01303 170 DTAESSYRDTKRLIERWHGKSG----RVkpAITPRFAPSCSEE-LLAALGKLAKEHPdLHIQTHISENLDEIAWVKELFp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 252 ---SMTPVqYcaEH-DWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVSLGVDGAA 327
Cdd:cd01303 245 garDYLDV-Y--DKyGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGG 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460622887 328 SNeAADMQSEAHAAWLLQRARkgmlaqpryagGTFEGGADAATVEDVVRWGCAGGAQILGLA-QSGTLQVGMQADLAI 404
Cdd:cd01303 322 GT-SFSMLDTLRQAYKVSRLL-----------GYELGGHAKLSPAEAFYLATLGGAEALGLDdKIGNFEVGKEFDAVV 387
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
55-428 |
1.84e-31 |
|
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: 123.38 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 55 VIYPAWVNTHHHLFQSLLKGEPqglnqsltawlsatpyrfraaFDEHTFRLAVRIGLVELLRSGCASVADHNYLYWPDMP 134
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIP---------------------VPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 135 FDTSEIvfsEGEALGMRIVLCRGGATQGRAVEQDLPVALRPETFdsymADVERLVSryhdprpESLRRVVMAPttvlHSA 214
Cdd:pfam01979 60 ALLEAA---EELPLGLRFLGPGCSLDTDGELEGRKALREKLKAG----AEFIKGMA-------DGVVFVGLAP----HGA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 215 PG---AQLREMAKLARQLRIRLHSHLSETVDYLDAARQKF-----SMTPVQYCAE-HDWLGNDVWYAHLVKLLPEEIALL 285
Cdd:pfam01979 122 PTfsdDELKAALEEAKKYGLPVAIHALETKGEVEDAIAAFgggieHGTHLEVAESgGLLDIIKLILAHGVHLSPTEANLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 286 GRT--GTGIAHCPQSNGRLGSGIADLLALEQAGVPVSLGVDGAASNEAADMqseahaawlLQRARKGMLAQPRYAGGtfe 363
Cdd:pfam01979 202 AEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNM---------LEELRLALELQFDPEGG--- 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460622887 364 ggadaATVEDVVRWGCAGGAQILGLA-QSGTLQVGMQADLAIYRLD-DPRYFGL-HDMAIGPVACGGR 428
Cdd:pfam01979 270 -----LSPLEALRMATINPAKALGLDdKVGSIEVGKDADLVVVDLDpLAAFFGLkPDGNVKKVIVKGK 332
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
4-471 |
9.98e-31 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 123.57 E-value: 9.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 4 IIKNAHaILSgLPGEAARLAGPDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGepQGLNQSL 83
Cdd:PRK08204 5 LIRGGT-VLT-MDPAIGDLPRGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRHTWQSVLRG--IGADWTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 84 TAWLSATPYRFRAAFDEHTFRLAVRIGLVELLRSGCASVAD--HNYLywpdMPFDTSEIVFSEGEAlGMRIVLCRGGAtq 161
Cdd:PRK08204 81 QTYFREIHGNLGPMFRPEDVYIANLLGALEALDAGVTTLLDwsHINN----SPEHADAAIRGLAEA-GIRAVFAHGSP-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 162 graveQDLPVALRPETFDSyMADVERLVSRYHdPRPESLRRVVMAPTTVLHSAPGAQLREMAkLARQLRIRLHSHLSetv 241
Cdd:PRK08204 154 -----GPSPYWPFDSVPHP-REDIRRVKKRYF-SSDDGLLTLGLAIRGPEFSSWEVARADFR-LARELGLPISMHQG--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 242 dyLDAARQKFSMtpVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVSL 321
Cdd:PRK08204 223 --FGPWGATPRG--VEQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 322 GVDGAASNeAADMQSEAHAAWLLQRARKGmlAQPRYAGGTfEGGADAATVEDVVRWGCAGGAQILGLA-QSGTLQVGMQA 400
Cdd:PRK08204 299 GVDVVTST-GGDMFTQMRFALQAERARDN--AVHLREGGM-PPPRLTLTARQVLEWATIEGARALGLEdRIGSLTPGKQA 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460622887 401 DLAIYRLDDPRYFGLHDMAIGPVACGGRAALKALLLNGRPIVEDDAIPGLDLDAMRHDALAAVRTLQQRAA 471
Cdd:PRK08204 375 DLVLIDATDLNLAPVHDPVGAVVQSAHPGNVDSVMVAGRAVKRNGKLLGVDLERLRRLAAASRDRLLSRRA 445
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
49-402 |
1.06e-30 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 123.24 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 49 IDARDCVIYPAWVNTHHHLFQSLLKGepQGLNQSLTAWLSATPYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADhnyL 128
Cdd:PRK15493 50 IDMKGKWVLPGLVNTHTHVVMSLLRG--IGDDMLLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSD---M 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 129 YWPdMPFDTSEIVFSEGEAlGMRIVLCRGGATQGraVEQDLPVALRpetfdsymaDVERLVSRYHdpRPESLRRVVMAPT 208
Cdd:PRK15493 125 FNP-IGVDQDAIMETVSRS-GMRAAVSRTLFSFG--TKEDEKKAIE---------EAEKYVKRYY--NESGMLTTMVAPH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 209 TVlHSAPGAQLREMAKLARQLRIRLHSHLSETVDYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRT 288
Cdd:PRK15493 190 SP-YTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEH 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 289 GTGIAHCPQSNGRLGSGIADLLALEQAGVPVSLGVDGAASNEAADMQSEAHAAWLLQRArkgmlaqpryaggtFEGGADA 368
Cdd:PRK15493 269 DVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLQKG--------------IHQDATA 334
|
330 340 350
....*....|....*....|....*....|....
gi 1460622887 369 ATVEDVVRWGCAGGAQILGLAQSGTLQVGMQADL 402
Cdd:PRK15493 335 LPVETALTLATKGAAEVIGMKQTGSLEVGKCADF 368
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
29-459 |
3.59e-28 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 116.68 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 29 IRDG-------KIAAIGSLTPLPEERQIDARDCVIYPAWVNTH-----HHLFQSLLKGEPQGLNQSLTA-WLSATPyrfR 95
Cdd:PRK06151 21 LRDGevvfegdRILFVGHRFDGEVDRVIDAGNALVGPGFIDLDalsdlDTTILGLDNGPGWAKGRVWSRdYVEAGR---R 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 96 AAFDEHTFRLAVRIGLVELLRSGCAS---VADHNYLYWPDMpFDTSEIVFSEGEALGMRIVLCRGGATQGRAVEQD--LP 170
Cdd:PRK06151 98 EMYTPEELAFQKRYAFAQLLRNGITTampIASLFYRQWAET-YAEFAAAAEAAGRLGLRVYLGPAYRSGGSVLEADgsLE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 171 VALRPETFDSYMADVERLVSRyHDPRPESLRRVVMAPTTVLHSAPgAQLREMAKLARQLRIRLHSHLSETVDYLDAARQK 250
Cdd:PRK06151 177 VVFDEARGLAGLEEAIAFIKR-VDGAHNGLVRGMLAPDRIETCTV-DLLRRTAAAARELGCPVRLHCAQGVLEVETVRRL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 251 FSMTPVQYCAEHDWLGNDVWYAH---------LVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVSL 321
Cdd:PRK06151 255 HGTTPLEWLADVGLLGPRLLIPHatyisgsprLNYSGGDDLALLAEHGVSIVHCPLVSARHGSALNSFDRYREAGINLAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 322 GVDGAAsneaADMqseahaawlLQRARKGMlaqprYAGGTFEGGADAATVEDVVRWGCAGGAQILGLAQSGTLQVGMQAD 401
Cdd:PRK06151 335 GTDTFP----PDM---------VMNMRVGL-----ILGRVVEGDLDAASAADLFDAATLGGARALGRDDLGRLAPGAKAD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460622887 402 LAIYRLDDPRYFGLHDMAIGPVACGGRAALKALLLNGRPIVEDDAIPGLDLDAMRHDA 459
Cdd:PRK06151 397 IVVFDLDGLHMGPVFDPIRTLVTGGSGRDVRAVFVDGRVVMEDGRLPGVDLAALRAQA 454
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
28-428 |
3.49e-27 |
|
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: 112.93 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 28 RIRDGKIAAIgslTPLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQGL---NQSLTAWLSATpYRFRAAFDEHTFR 104
Cdd:cd01313 15 VDADGRIAAV---NPDTATEAVALLGGALLPGMPNLHSHAFQRAMAGLTEYRgsaADSFWTWRELM-YRFAARLTPEQIE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 105 LAVRIGLVELLRSGCASVADHNYLYW-PD-----MPFDTSEIVFSEGEALGMRIVLCRGGATQGRAVEQdlPVALRPETF 178
Cdd:cd01313 91 AIARQLYIEMLLAGITAVGEFHYVHHdPDgtpyaDPAELAQRVIAAASDAGIGITLLPVLYARAGFGGP--APNPGQRRF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 179 DSYMADVERLVSRYHDPRPESLRRVVMAPTTVLHSAPGAQLREMAKLARQlRIRLHSHLSETVDYLDAARQKFSMTPVQY 258
Cdd:cd01313 169 INGYEDFLGLLEKALRAVKEHAAARIGVAPHSLRAVPAEQLAALAALASE-KAPVHIHLAEQPKEVDDCLAAHGRRPVEL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 259 CAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVSLGVDgaaSNEAADMQSEA 338
Cdd:cd01313 248 LLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSD---SNARIDLLEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 339 HAAWLLQRAR---KGMLAQPryAGGTFEGGADAATvedvvrwgcAGGAQILGLAqSGTLQVGMQADLAIYRLDDPRY--- 412
Cdd:cd01313 325 RQLEYSQRLRdraRNVLATA--GGSSARALLDAAL---------AGGAQALGLA-TGALEAGARADLLSLDLDHPSLaga 392
|
410 420
....*....|....*....|....*.
gi 1460622887 413 ----------FGLHDMAIGPVACGGR 428
Cdd:cd01313 393 lpdtlldawvFAAGDREVRDVVVGGR 418
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
29-404 |
9.38e-24 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 102.96 E-value: 9.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 29 IRDGKIAAIGS----LTPLPEERQI-DARDCVIYPAWVNTHHHLFQSLLKGEPqglNQSLTAWLSAtpYRF----RAAFD 99
Cdd:PRK09228 36 VEDGRIVAAGPyaelRAQLPADAEVtDYRGKLILPGFIDTHIHYPQTDMIASY---GEQLLDWLNT--YTFpeerRFADP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 100 EHTFRLAvRIGLVELLRSGCASVadhnylywpdMPFDTS-----EIVFSEGEALGMRIVlcrGGATqgrAVEQDLPVALR 174
Cdd:PRK09228 111 AYAREVA-EFFLDELLRNGTTTA----------LVFGTVhpqsvDALFEAAEARNMRMI---AGKV---LMDRNAPDGLR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 175 PETFDSYmADVERLVSRYHD---------PRpeslrrvvMAPTtvlhSAPgAQLREMAKLARQL-RIRLHSHLSETVDYL 244
Cdd:PRK09228 174 DTAESGY-DDSKALIERWHGkgrllyaitPR--------FAPT----STP-EQLEAAGALAREHpDVWIQTHLSENLDEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 245 DAARQKF----SMTPVqYcAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVS 320
Cdd:PRK09228 240 AWVKELFpearDYLDV-Y-ERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 321 LGVD-GAAS--------NEA---ADMQSE----AHAAWLlqrarkgmlaqpryaggtfeggadaATvedvvrwgcAGGAQ 384
Cdd:PRK09228 318 LGTDvGGGTsfsmlqtmNEAykvQQLQGYrlspFQAFYL-------------------------AT---------LGGAR 363
|
410 420
....*....|....*....|.
gi 1460622887 385 ILGLAQS-GTLQVGMQADLAI 404
Cdd:PRK09228 364 ALGLDDRiGNLAPGKEADFVV 384
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
32-410 |
4.46e-23 |
|
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: 100.60 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 32 GKIAAIGSLTPL----PEERQIDARDCVIYPAWVNTHHHL-FQSLLKgepQGLNQSLTAWLSATpYRFRAAFDEHTFRLA 106
Cdd:cd01312 1 DKILEVGDYEKLekryPGAKHEFFPNGVLLPGLINAHTHLeFSANVA---QFTYGRFRAWLLSV-INSRDELLKQPWEEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 107 VRIGLVELLRSGCASVAD-HNYLywpdmpfdtseivfSEGEAL---GMRIVLCRggatqgRAVEQDlPVALRpetfDSYM 182
Cdd:cd01312 77 IRQGIRQMLESGTTSIGAiSSDG--------------SLLPALassGLRGVFFN------EVIGSN-PSAID----FKGE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 183 ADVERLVSR--YHDPRPeSLRRVVMAPTTVlHSAPGAQLREmakLARQLRIRLHSHLSETVD------------------ 242
Cdd:cd01312 132 TFLERFKRSksFESQLF-IPAISPHAPYSV-HPELAQDLID---LAKKLNLPLSTHFLESKEerewleeskgwfkhfwes 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 243 YLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAGVPVSLG 322
Cdd:cd01312 207 FLKLPKPKKLATAIDFLDMLGGLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 323 VDGAASNEAADMQSEAHAAWLLQRaRKGMLAQPRYAggtfeggadaatvedvVRWGCAGGAQILGLAqSGTLQVGMQADL 402
Cdd:cd01312 287 TDGLSSNISLSLLDELRALLDLHP-EEDLLELASEL----------------LLMATLGGARALGLN-NGEIEAGKRADF 348
|
....*...
gi 1460622887 403 AIYRLDDP 410
Cdd:cd01312 349 AVFELPGP 356
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
3-469 |
5.53e-22 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 98.08 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 3 LIIKNAHAILSglpgEAAR--LAGPDIRIRDGKIAAIGSLTPL----PEERQIDARDCVIYPAWVNTHHHLFQSLLKG-- 74
Cdd:PRK07203 2 LLIGNGTAITR----DPAKpvIEDGAIAIEGNVIVEIGTTDELkakyPDAEFIDAKGKLIMPGLINSHNHIYSGLARGmm 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 75 ----EPQGLNQSLTA-WlsatpYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADHN--YLYWPDMPFDTSEIVfsegEA 147
Cdd:PRK07203 78 anipPPPDFISILKNlW-----WRLDRALTLEDVYYSALICSLEAIKNGVTTVFDHHasPNYIGGSLFTIADAA----KK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 148 LGMRIVLC-----RGGATQGRA-VEQDLPVAlrpetfdsymadverlvsRYHDPRPESLRRVVM---APTTVlhsaPGAQ 218
Cdd:PRK07203 149 VGLRAMLCyetsdRDGEKELQEgVEENIRFI------------------KHIDEAKDDMVEAMFglhASFTL----SDAT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 219 LREMAKLARQLRIRLHSHLSETVDYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQS 298
Cdd:PRK07203 207 LEKCREAVKETGRGYHIHVAEGIYDVSDSHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPES 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 299 NGRLGSGIADLLALEQAGVPVSLGVDGAASneaaDMQSEAHAAWLLQRarkgmlaqpryaggtFEGGADAATVEDVVRWG 378
Cdd:PRK07203 287 NMGNAVGYNPVLEMIKNGILLGLGTDGYTS----DMFESYKVANFKHK---------------HAGGDPNVGWPESPAML 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 379 CAGGAQILGL---AQSGTLQVGMQADLAI--YR----LDDPRYFGlHdMAIGPvacGGRaALKALLLNGRPIVEDDAIPG 449
Cdd:PRK07203 348 FENNNKIAERyfgAKFGILEEGAKADLIIvdYNpptpLNEDNING-H-ILFGM---NGG-SVDTTIVNGKVVMEDRKFLN 421
|
490 500
....*....|....*....|
gi 1460622887 450 LDLDAMRHDALAAVRTLQQR 469
Cdd:PRK07203 422 FDEESIYARARKAAAKLWKR 441
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-404 |
2.03e-20 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 93.02 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 1 MSLIIKNAHAILSGlpgEAARLAGPDIRIRDGKIAAIGSLTPLPEErQIDARDCVIYPAWVNTHHHLFQSLLKGEPQGLN 80
Cdd:PRK06380 1 MSILIKNAWIVTQN---EKREILQGNVYIEGNKIVYVGDVNEEADY-IIDATGKVVMPGLINTHAHVGMTASKGLFDDVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 81 qsLTAWLSATPYRFRAAFDEHTFRLAvRIGLVELLRSGCASVADhnyLYWpdmpfdTSEIVFSEGEALGMR-----IVLC 155
Cdd:PRK06380 77 --LEEFLMKTFKYDSKRTREGIYNSA-KLGMYEMINSGITAFVD---LYY------SEDIIAKAAEELGIRaflswAVLD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 156 RGGATQ-GRAVEQdlpvalrPETFDSYMaDVERLVsryhdprpeslrrVVMAPTTVLHSAPGAQLREMAKLARQLRIRLH 234
Cdd:PRK06380 145 EEITTQkGDPLNN-------AENFIREH-RNEELV-------------TPSIGVQGIYVANDETYLKAKEIAEKYDTIMH 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 235 SHLSETVDYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGS-GIADLLALE 313
Cdd:PRK06380 204 MHLSETRKEVYDHVKRTGERPVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEML 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 314 QAGVPVSLGVDGAASNEAADM-QSEAHAAWLLQRARkgmlaqpryaggtfeggADAATV--EDVVRWGCAGGAQILGLaQ 390
Cdd:PRK06380 284 DNGINVTIGTDSNGSNNSLDMfEAMKFSALSVKNER-----------------WDASIIkaQEILDFATINAAKALEL-N 345
|
410
....*....|....
gi 1460622887 391 SGTLQVGMQADLAI 404
Cdd:PRK06380 346 AGSIEVGKLADLVI 359
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
15-469 |
9.26e-18 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 85.29 E-value: 9.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 15 LPGEAARlagpDIRIR---DGKIAAIGSLTPLPEERQidARDCVIyPAWVNTHHHLFQSLL------KGEPQGlnqSLTA 85
Cdd:PRK09229 12 LPDGWAR----NVRLTvdaDGRIAAVEPGAAPAGAER--LAGPVL-PGMPNLHSHAFQRAMagltevRGPPQD---SFWS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 86 WLSATpYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADHNYL--------YwpDMPFDTSEIVFSEGEALGMRIVLcrg 157
Cdd:PRK09229 82 WRELM-YRFALRLTPDQLEAIARQLYVEMLEAGYTSVGEFHYLhhdpdgtpY--ADPAEMALRIVAAARAAGIGLTL--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 158 gatqgraveqdLPV----------ALRP------ETFDSYMADVERLVSRYHDprpESLRRVVMAPttvlHS---APGAQ 218
Cdd:PRK09229 156 -----------LPVlyahsgfggqPPNPgqrrfiNDPDGFLRLLEALRRALAA---LPGARLGLAP----HSlraVTPDQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 219 LREMAKLARQlRIRLHSHLSETVDYLDAARQKFSMTPVQYCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQS 298
Cdd:PRK09229 218 LAAVLALAAP-DGPVHIHIAEQTKEVDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 299 NGRLGSGIADLLALEQAGVPVSLGVDgaaSNEAADMQSEAHAAWLLQRARKGmlaqpryAGGTFEGGADAATVEDVVRWG 378
Cdd:PRK09229 297 EANLGDGIFPAVDYLAAGGRFGIGSD---SHVSIDLVEELRLLEYGQRLRDR-------RRNVLAAAAQPSVGRRLFDAA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 379 CAGGAQILGLAqSGTLQVGMQADLAIYRLDDPRYFGLHDMAI--GPVACGGRAALKALLLNGRPIVEDDAIPglDLDAMR 456
Cdd:PRK09229 367 LAGGAQALGRA-IGGLAVGARADLVVLDLDHPALAGREGDALldRWVFAGGDAAVRDVWVAGRWVVRDGRHR--LREAIA 443
|
490
....*....|...
gi 1460622887 457 HDALAAVRTLQQR 469
Cdd:PRK09229 444 AAFRAALAALLAA 456
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
3-449 |
5.91e-13 |
|
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: 70.40 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 3 LIIKNAHaILSGLPGEAARlagPDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHlFQSLLKGEPqglnqs 82
Cdd:cd01297 2 LVIRNGT-VVDGTGAPPFT---ADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTH-YDGQVFWDP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 83 ltawlsatpyrfraafdehtfrlavriGLVELLRSGCASVADHN-----YLYWPDMPFDtseivfsEGEALGMRIVLcrg 157
Cdd:cd01297 71 ---------------------------DLRPSSRQGVTTVVLGNcgvspAPANPDDLAR-------LIMLMEGLVAL--- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 158 gatqgraveqDLPVALRPETFDSYMADVERLvsryhDPRPES--------LRRVVMAPTTVLHSApgAQLREMAKLARQ- 228
Cdd:cd01297 114 ----------GEGLPWGWATFAEYLDALEAR-----PPAVNVaalvghaaLRRAVMGLDAREATE--EELAKMRELLREa 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 229 ----------LRIRLHSHLSETVDYLD----AARQKfsmtpVQYCAEHDWLGNDVWYAhlvklLPEEIALLGRTGTGI-- 292
Cdd:cd01297 177 leagalgistGLAYAPRLYAGTAELVAlarvAARYG-----GVYQTHVRYEGDSILEA-----LDELLRLGRETGRPVhi 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 293 ----AHCPQSNGRLGSGIADLLALEQAGVPVSLGV----DGAASNEAADMQSEAHA----AWLLQRARKGMLAQPRYAGG 360
Cdd:cd01297 247 shlkSAGAPNWGKIDRLLALIEAARAEGLQVTADVypygAGSEDDVRRIMAHPVVMggsdGGALGKPHPRSYGDFTRVLG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 361 TFEGGADAATVEDVVRWGCAGGAQILGLAQSGTLQVGMQADLAIYRLDDpryfgLHDMAIGPVACGGRAALKALLLNGRP 440
Cdd:cd01297 327 HYVRERKLLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVFDPDT-----LADRATFTRPNQPAEGIEAVLVNGVP 401
|
....*....
gi 1460622887 441 IVEDDAIPG 449
Cdd:cd01297 402 VVRDGAFTG 410
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-412 |
3.45e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 67.68 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 2 SLIIKNAHAIlsglPGEAARLAGP-DIRIRDGKIAAIG---SLTPLPEERQIDARDCVIYPAWVNTHHHLFQSllkgepQ 77
Cdd:COG1228 9 TLLITNATLV----DGTGGGVIENgTVLVEDGKIAAVGpaaDLAVPAGAEVIDATGKTVLPGLIDAHTHLGLG------G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 78 GLNQSLTAWLSATPYRFRAAFDEHTFRLAVR--IGLVELLRSGCASVADH------NYLYWPDmpfdtseiVFSEGEALG 149
Cdd:COG1228 79 GRAVEFEAGGGITPTVDLVNPADKRLRRALAagVTTVRDLPGGPLGLRDAiiagesKLLPGPR--------VLAAGPALS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 150 MRivlcrGGATQG--RAVEQDLPVALRpetfdsYMADVERLVSRYHDP--RPESLRRVVMApttvlhsapgaqlremakl 225
Cdd:COG1228 151 LT-----GGAHARgpEEARAALRELLA------EGADYIKVFAEGGAPdfSLEELRAILEA------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 226 ARQLRIRLHSHLSETVDYLDAARqkfsmtpvqycaehdwLGNDVWyAHLVKLLPEEIALLGRTGT--------------- 290
Cdd:COG1228 201 AHALGLPVAAHAHQADDIRLAVE----------------AGVDSI-EHGTYLDDEVADLLAEAGTvvlvptlslflalle 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 291 --GIAHCPQSNGRLGSGIADLLALEQAGVPVSLGVDGAASNEAAdmQSEAHAAWLLQRArkGMlaqpryaggtfeggada 368
Cdd:COG1228 264 gaAAPVAAKARKVREAALANARRLHDAGVPVALGTDAGVGVPPG--RSLHRELALAVEA--GL----------------- 322
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1460622887 369 aTVEDVVRWGCAGGAQILGLAQS-GTLQVGMQADLAIYR---LDDPRY 412
Cdd:COG1228 323 -TPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLLDgdpLEDIAY 369
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
31-409 |
3.74e-11 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 64.61 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 31 DGKIAAIGSLTPL----PEERQIDARDCVIYPAWVNTHHHL-FQS----LLKGepqglnqSLTAWLSATpYRFRAAFDEH 101
Cdd:PRK08418 27 DDKILEIGDYENLkkkyPNAKIQFFKNSVLLPAFINPHTHLeFSAnkttLDYG-------DFIPWLGSV-INHREDLLEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 102 TFRLAVRIGLVELLRSGCASV-------ADHNYLywPDMPFDTseIVFSEgeALGmrivlcrggaTQGRAVEQdlpvalr 174
Cdd:PRK08418 99 CKGALIQQAINEMLKSGVGTIgaissfgIDLEIC--AKSPLRV--VFFNE--ILG----------SNASAVDE------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 175 peTFDSYMADVERLVSrYHDPRpeslrrvvMAPTTVLHSaPGAQLREMAK----LARQLRIRLHSHLSETV---DYLDAA 247
Cdd:PRK08418 156 --LYQDFLARFEESKK-FKSKK--------FIPAIAIHS-PYSVHPILAKkalqLAKKENLLVSTHFLESKaerEWLEES 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 248 R-------QKFSMTPVQYCAEHDWL----GNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQAG 316
Cdd:PRK08418 224 KgwfkkffEKFLKEPKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 317 VPVSLGVDGAASNEAADMQSEAHAAW-------LLQRARKGMLAQPRYaggtfeggadaatvedvvrwgcagGAQILGLa 389
Cdd:PRK08418 304 INYSIATDGLSSNISLSLLDELRAALlthanmpLLELAKILLLSATRY------------------------GAKALGL- 358
|
410 420
....*....|....*....|
gi 1460622887 390 QSGTLQVGMQADLAIYRLDD 409
Cdd:PRK08418 359 NNGEIKEGKDADLSVFELPE 378
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
61-341 |
5.95e-11 |
|
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: 63.12 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 61 VNTHHHLFQSLLkgEPQGLNQSLTAWLSATPYRFRAAFDEhtfrlavriGLVELLRSGCASVADHNYLYWPDMPFDTSEI 140
Cdd:cd01292 2 IDTHVHLDGSAL--RGTRLNLELKEAEELSPEDLYEDTLR---------ALEALLAGGVTTVVDMGSTPPPTTTKAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 141 VFSE-GEALGMRIVLCRGGATQGRAVEQDLPVALRPEtfdsyMADVERLVSRYHDPrpeslrrvVMAPTTVLHSAPgaQL 219
Cdd:cd01292 71 VAEAaRASAGIRVVLGLGIPGVPAAVDEDAEALLLEL-----LRRGLELGAVGLKL--------AGPYTATGLSDE--SL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 220 REMAKLARQLRIRLHSHLSETVDYLDAARQkfsmtpvqyCAEHDWLGNDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSN 299
Cdd:cd01292 136 RRVLEEARKLGLPVVIHAGELPDPTRALED---------LVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSN 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1460622887 300 GRLGS---GIADLLALEQAGVPVSLGVDGAASNEAADMQSEAHAA 341
Cdd:cd01292 207 YLLGRdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLL 251
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
55-347 |
1.71e-10 |
|
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: 61.26 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 55 VIYPAWVNTHHHLFQSLLK--GEPQGLNQsLTAWLSATPYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADhnylywpd 132
Cdd:cd01305 1 ILIPALVNAHTHLGDSAIKevGDGLPLDD-LVAPPDGLKHRLLAQADDRELAEAMRKVLRDMRETGIGAFAD-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 133 mpfdtseivFSEGEALGMRIVlcrggatqgRAVEQDLPValrpeTFDSYMADverlvsryhDPRPESLRRVVMAPTTVLH 212
Cdd:cd01305 72 ---------FREGGVEGIELL---------RRALGKLPV-----PFEVILGR---------PTEPDDPEILLEVADGLGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 213 SAPGA-QLREMAKLARQLRIRLHSHLSETvdyldaaRQKFSMTPVQYC--AEHDWLgndvwyAHLVKLLPEEIALLGRTG 289
Cdd:cd01305 120 SSANDvDLEDILELLRRRGKLFAIHASET-------RESVGMTDIERAldLEPDLL------VHGTHLTDEDLELVRENG 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1460622887 290 TGIAHCPQSNGRLGSGIADLLALEQAGVPVSLGVDGAASNEaADMQSEAHAAWLLQRA 347
Cdd:cd01305 187 VPVVLCPRSNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNE-PDMWAEMEFLAKYSRL 243
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
3-69 |
3.06e-08 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 55.56 E-value: 3.06e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1460622887 3 LIIKNAHAIlsglpGEAARLAGP-DIRIRDGKIAAIG-SLTPLPEERQIDARDCVIYPAWVNTHHHLFQ 69
Cdd:COG3964 2 LLIKGGRVI-----DPANGIDGVmDIAIKDGKIAAVAkDIDAAEAKKVIDASGLYVTPGLIDLHTHVFP 65
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-67 |
5.41e-08 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 54.82 E-value: 5.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460622887 1 MSLIIKNAHAI-LSGLPGEAarlagpDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHL 67
Cdd:PRK09357 1 MMILIKNGRVIdPKGLDEVA------DVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-411 |
5.09e-07 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 52.02 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 4 IIKNAHAILSGLPGEAarlagpDIRIRDGKIAAIGS-LTPLPEERQIDARDCVIYPAWVNTHHHLfqsllkGEPqGLNQS 82
Cdd:COG0044 1 LIKNGRVVDPGGLERA------DVLIEDGRIAAIGPdLAAPEAAEVIDATGLLVLPGLIDLHVHL------REP-GLEHK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 83 LTaWLSATpyrfRAA--------FD--------------EHTFRLA-----VRIGLV---------------ELLRSGCA 120
Cdd:COG0044 68 ED-IETGT----RAAaaggvttvVDmpntnpvtdtpealEFKLARAeekalVDVGPHgaltkglgenlaelgALAEAGAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 121 SVADHnylywpdMPFDTSEIVFSEGEalgMRIVLcrggatqGRAVEQDLPVALRPEtfDSYMADV----ERLVS-RYHDP 195
Cdd:COG0044 143 AFKVF-------MGSDDGNPVLDDGL---LRRAL-------EYAAEFGALVAVHAE--DPDLIRGgvmnEGKTSpRLGLK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 196 -RPEslrrvvmapttvlhSAPGAQLREMAKLARQLRIRLH-SHLS--ETVDYLDAARQK----FSMTPVQYCA--EHDWL 265
Cdd:COG0044 204 gRPA--------------EAEEEAVARDIALAEETGARLHiVHVStaEAVELIREAKARglpvTAEVCPHHLTltDEDLE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 266 GNDVWYahlvKLLP-----EEI-ALLG--RTGT--GIA--HCPQS------------NGrlGSGIADLLALeqagvpvsl 321
Cdd:COG0044 270 RYGTNF----KVNPplrteEDReALWEglADGTidVIAtdHAPHTleekelpfaeapNG--IPGLETALPL--------- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 322 gvdgaasneaadMQSEAHaawllqraRKGMLaqpryaggtfeggadaaTVEDVVRWGCAGGAQILGLAQSGTLQVGMQAD 401
Cdd:COG0044 335 ------------LLTELV--------HKGRL-----------------SLERLVELLSTNPARIFGLPRKGRIAVGADAD 377
|
490
....*....|
gi 1460622887 402 LAIYRLDDPR 411
Cdd:COG0044 378 LVLFDPDAEW 387
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
3-69 |
7.69e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.00 E-value: 7.69e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460622887 3 LIIKNAHAILSGLPGEAARlagpDIRIRDGKIAAIGSLTPLPEERQ-IDARDCVIYPAWVNTHHHLFQ 69
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGVI----DIAIEDGKIAAVAGDIDGSQAKKvIDLSGLYVSPGWIDLHVHVYP 64
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
27-416 |
1.40e-06 |
|
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: 50.33 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 27 IRIRDGKIAAIGSLTPLPE-----ERQIDARDCVIYPAWVNTHHHL---------FQSLLKGEPQ--------GLNQSLT 84
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPApgpaaAEEIDAGGRAVTPGLVDCHTHLvfagdrvdeFAARLAGASYeeilaaggGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 85 AWLSATPYRFRAAFdehTFRL--AVRIG--LVELlRSGcasvadhnylYWPDMpfdtseivfsEGEALGMRIVlcrggat 160
Cdd:cd01296 81 ATRAASEDELFASA---LRRLarMLRHGttTVEV-KSG----------YGLDL----------ETELKMLRVI------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 161 qgRAVEQDLPVALRPeTF-------DSYMADVE--RLVSRYHDPRPESLRRV----VMAPTTVLHSAPGAQLREMAKlAR 227
Cdd:cd01296 130 --RRLKEEGPVDLVS-TFlgahavpPEYKGREEyiDLVIEEVLPAVAEENLAdfcdVFCEKGAFSLEQSRRILEAAK-EA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 228 QLRIRLHshlsetvdyldaARQKFSMTPVQYCAEhdwLGNdVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIA 307
Cdd:cd01296 206 GLPVKIH------------ADELSNIGGAELAAE---LGA-LSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 308 DLLALEQAGVPVSLGVD-GAASNEAADMQSEAHAAWLLQRarkgMlaqpryaggtfeggadaaTVEDVVRWGCAGGAQIL 386
Cdd:cd01296 270 PARKLIDAGVPVALGTDfNPGSSPTSSMPLVMHLACRLMR----M------------------TPEEALTAATINAAAAL 327
|
410 420 430
....*....|....*....|....*....|....*
gi 1460622887 387 GLAQS-GTLQVGMQADLAIYRLDDPRY----FGLH 416
Cdd:cd01296 328 GLGETvGSLEVGKQADLVILDAPSYEHlayrFGVN 362
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
15-404 |
1.44e-06 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 50.42 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 15 LPGEAARLAGPDIRIRDGKIAAIGSltPLPEERQIDARDCVIyPAWVNTHHHLFQSLLKGEpqGLNQSLTAwLSATP--- 91
Cdd:PRK07213 10 LYGEDFEPKKGNLVIEDGIIKGFTN--EVHEGNVIDAKGLVI-PPLINAHTHIGDSSIKDI--GIGKSLDE-LVKPPngl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 92 -YRFRAAFDEHTFRLAVRIGLVELLRSGCASVADhnylywpdmpfdtseivFSEGEALGMRIVlcrggatqgRAVEQDLP 170
Cdd:PRK07213 84 kHKFLNSCSDKELVEGMKEGLYDMYNNGIKAFCD-----------------FREGGIKGINLL---------KKASSDLP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 171 VAL----RPETFDSYMADVErlvsryhdprpesLRRVvmapttvLHSAPG-----------AQLREMAKLARQLRIRLHS 235
Cdd:PRK07213 138 IKPiilgRPTEADENELKKE-------------IREI-------LKNSDGiglsganeysdEELKFICKECKREKKIFSI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 236 HLSETVDYLDAARQKFSMTPVQYCAEhdwLG-NDVWYAHLVKLLPEEIALLGRTGTGIAHCPQSNGRLGSGIADLLALEQ 314
Cdd:PRK07213 198 HAAEHKGSVEYSLEKYGMTEIERLIN---LGfKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 315 AGVPVSLGVDGAASNeAADMQSEahaawlLQRARKGMLAQPRyaggtfeggadaatveDVVRWGCAGGAQILGLAQSGTL 394
Cdd:PRK07213 275 KGILLGIGTDNFMAN-SPSIFRE------MEFIYKLYHIEPK----------------EILKMATINGAKILGLINVGLI 331
|
410
....*....|
gi 1460622887 395 QVGMQADLAI 404
Cdd:PRK07213 332 EEGFKADFTF 341
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
78-408 |
4.89e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 48.68 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 78 GLNQSLTAWLSATPYRFRAAFDEHTFRLAVRIGLVELLRSGCASVADHNYLYWPDMPFDTSEIVFSEGEALGMRIVLCRG 157
Cdd:pfam07969 124 ANGEGLTGLLREGAYALPPLLAREAEAAAVAAALAALPGFGITSVDGGGGNVHSLDDYEPLRELTAAEKLKELLDAPERL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 158 GATQGRAVEQDLPVALrpetfdsyMADVERLVSRYHDPRPESlrrvvMAPTTVLHSAPGAQLREMAKLARQ--LRIRLHS 235
Cdd:pfam07969 204 GLPHSIYELRIGAMKL--------FADGVLGSRTAALTEPYF-----DAPGTGWPDFEDEALAELVAAARErgLDVAIHA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 236 HLSETVDYLD----AARQKFSMTPVQYCaEHDwLGNDVWYAHLVKLLPeeiALLGRTGTGIAHCPQSNGRL--------G 303
Cdd:pfam07969 271 IGDATIDTALdafeAVAEKLGNQGRVRI-EHA-QGVVPYTYSQIERVA---ALGGAAGVQPVFDPLWGDWLqdrlgaerA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 304 SGIADLLALEQAGVPVSLGVDgaASNEAADMQSEAHAAWLLQRARKGMLAQPRyaggtfeggaDAATVEDVVRWGCAGGA 383
Cdd:pfam07969 346 RGLTPVKELLNAGVKVALGSD--APVGPFDPWPRIGAAVMRQTAGGGEVLGPD----------EELSLEEALALYTSGPA 413
|
330 340
....*....|....*....|....*.
gi 1460622887 384 QILGLAQS-GTLQVGMQADLAIYRLD 408
Cdd:pfam07969 414 KALGLEDRkGTLGVGKDADLVVLDDD 439
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-67 |
9.86e-06 |
|
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: 47.98 E-value: 9.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460622887 3 LIIKNAHAILSGLPGEAarlagpDIRIRDGKIAAIG-SLTPLPEERQIDARDCVIYPAWVNTHHHL 67
Cdd:cd01314 1 LIIKNGTIVTADGSFKA------DILIEDGKIVAIGpNLEAPGGVEVIDATGKYVLPGGIDPHTHL 60
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
26-69 |
1.02e-05 |
|
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: 47.32 E-value: 1.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1460622887 26 DIRIRDGKIAAIGSLTPLPE-ERQIDARDCVIYPAWVNTHHHLFQ 69
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAaTQIVDAGGCYVSPGWIDLHVHVYQ 45
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
1-66 |
1.42e-05 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 47.49 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460622887 1 MSLIIKNAHAI--LSGLPGEAArlagpDIRIRDGKIAAigSLTPLPEERQIDARDCVIYPAWVNTHHH 66
Cdd:COG1229 1 MELIIKNGRVYdpANGIDGEVM-----DIAIKDGKIVE--EPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-84 |
1.52e-05 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 47.32 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460622887 1 MSLIIKNAHailsgLPGEAArlaGPDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQgLN 80
Cdd:PRK07572 2 FDLIVRNAN-----LPDGRT---GIDIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHMDATLSYGLPR-VN 72
|
....
gi 1460622887 81 QSLT 84
Cdd:PRK07572 73 ASGT 76
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
3-67 |
5.88e-05 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 45.36 E-value: 5.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460622887 3 LIIKNAHAILSGLPGEAarlagpDIRIRDGKIAAIGSLTPLPE-ERQIDARDCVIYPAWVNTHHHL 67
Cdd:cd01315 2 LVIKNGRVVTPDGVREA------DIAVKGGKIAAIGPDIANTEaEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
4-76 |
1.12e-04 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 44.16 E-value: 1.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460622887 4 IIKNAHailsgLPGEAARLAgpDIRIRDGKIAAIG-SLTPLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGEP 76
Cdd:cd01293 1 LLRNAR-----LADGGTALV--DIAIEDGRIAAIGpALAVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFTGGRW 67
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
3-67 |
2.02e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 43.76 E-value: 2.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460622887 3 LIIKNAHAILSGlpGEAARlagpDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHL 67
Cdd:PRK09060 7 LILKGGTVVNPD--GEGRA----DIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVHF 65
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
21-66 |
2.40e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 43.49 E-value: 2.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1460622887 21 RLAGPDIRIRDGKIAAIG-SLTPLPEERQIDARDCVIYPAWVNTHHH 66
Cdd:PRK02382 16 SLQPRDVRIDGGKITAVGkDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-67 |
7.38e-04 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 41.70 E-value: 7.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1460622887 1 MSLIIKNAHAILSGLPGEAarlagpDIRIRDGKIAAIGsltPLPEERQIDARDCVIYPAWVNTHHHL 67
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKA------DVLIEDGKIAAIG---ANLGDEVIDATGKYVMPGGIDPHTHM 58
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
370-408 |
7.84e-04 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 41.89 E-value: 7.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1460622887 370 TVEDVVRWGCAGGAQILGL-AQSGTLQVGMQADLAIYRLD 408
Cdd:cd01315 354 SLEDIARLMCENPAKLFGLsHQKGRIAVGYDADFVVWDPE 393
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-68 |
9.60e-04 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 41.28 E-value: 9.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460622887 1 MSLIIKNAHAIlsglPGEAARLAGPDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHLF 68
Cdd:PRK12394 3 NDILITNGHII----DPARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAHVF 66
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
370-417 |
1.21e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 40.99 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1460622887 370 TVEDVVRWGCAGGAQILGLAQSGTLQVGMQADLAIYRLDDPRyFGLHD 417
Cdd:PRK09237 297 PLEEVIAAVTKNAADALRLPELGRLQVGSDADLTLFTLKDGP-FTLTD 343
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
372-410 |
2.10e-03 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 40.46 E-value: 2.10e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1460622887 372 EDVVRWGCAGGAQILGLAQSGTLQVGMQADLAIYRLDDP 410
Cdd:PRK06189 356 ETIARLLATNPAKRFGLPQKGRLEVGADADFVLVDLDET 394
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-58 |
3.23e-03 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 39.85 E-value: 3.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460622887 1 MSLIIKNAHAILSGLPGEAarlagpDIRIRDGKIAAIG-SLTPLPEERQIDARDCVIYP 58
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEG------DVLIENGRIAKIAsSISAKSADTVIDAAGRYLLP 54
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
370-411 |
3.49e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 39.66 E-value: 3.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1460622887 370 TVEDVVRWGCAGGAQILGLAQSGTLQVGMQADLAIYRLDDPR 411
Cdd:PRK07575 343 TVAQVVRWMSTAVARAYGIPNKGRIAPGYDADLVLVDLNTYR 384
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
3-67 |
4.78e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 39.45 E-value: 4.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460622887 3 LIIKNAHAILSGlpgeAARLAgpDIRIRDGKIAAIGSLTPLPeERQIDARDCVIYPAWVNTHHHL 67
Cdd:PRK08044 5 LIIKNGTVILEN----EARVV--DIAVKGGKIAAIGQDLGDA-KEVMDASGLVVSPGMVDAHTHI 62
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
20-84 |
5.05e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 39.30 E-value: 5.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460622887 20 ARLAGPD----IRIRDGKIAAIGSLT--PLPEERQIDARDCVIYPAWVNTHHHLFQSLLKGEPQgLNQSLT 84
Cdd:PRK09230 11 ARLPGKEglwqITIEDGKISAIEPQSeaSLEAGEVLDAEGGLAIPPFIEPHIHLDTTQTAGEPN-WNQSGT 80
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
343-417 |
7.02e-03 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 38.47 E-value: 7.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460622887 343 LLQRARKGMLaqpryaggtfeggadaaTVEDVVRWGCAGGAQILGLAQSGTLQVGMQADLAIYRLDDPRYFGLHD 417
Cdd:cd01318 278 MLTLVNKGIL-----------------SLSRVVRLTSHNPARIFGIKNKGRIAEGYDADLTVVDLKEERTIRAEE 335
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
3-67 |
7.54e-03 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 38.53 E-value: 7.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460622887 3 LIIKNAHAILsglPGEAARLagpDIRIRDGKIAAIGSLTPLPEERQIDARDCVIYPAWVNTHHHL 67
Cdd:PRK06189 5 LIIRGGKVVT---PEGVYRA---DIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHF 63
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
380-408 |
9.56e-03 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 38.55 E-value: 9.56e-03
10 20
....*....|....*....|....*....
gi 1460622887 380 AGGAQILGLAQSGTLQVGMQADLAIYRLD 408
Cdd:cd01304 438 AGPAKLLGLSDKGHLGVGADADIAIYDDD 466
|
|
| |
