|
Name |
Accession |
Description |
Interval |
E-value |
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-404 |
6.92e-165 |
|
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: 467.12 E-value: 6.92e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 35 LVVRGQTIAAVIPEAEIPSGHR---QCVDLDGRLVTPGLIDCHTHLVFGGDRAAEWEQRLNGVSYQTISAQGGGINATVT 111
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPaaaEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 112 ATRNSSPEMLLTVAQQRLQRLMNEGVTTIEIKSGYGLNAQAEEKMLLVARQLSLNNLVDISPTLLAAHAVPAEYRQDpDA 191
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGR-EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 192 YLTLVCEQIMPTLWQKELFEAVDVFCENVGFTPVQTERLFRAAAALGIPVKGHVEQLSNLGGAALVSQYKGLSADHIEYL 271
Cdd:cd01296 160 YIDLVIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 272 DDAGIQAMAQSGTVAVLLPGAFYFLQErQRPPVAQLREQGVPMAVATDYNPGTSPFASLHLAMNMACVQFGLTPEEAWAG 351
Cdd:cd01296 240 SDEGIAALAEAGTVAVLLPGTAFSLRE-TYPPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 556409337 352 VTRHAAQALGRGATHGQLKPGYVADFVVWEANHPVEMVYEPGRNPLYQRVFRG 404
Cdd:cd01296 319 ATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
31-406 |
6.56e-163 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 462.27 E-value: 6.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 31 EQHALVVRGQTIAAVIPEAEIPSGHR-QCVDLDGRLVTPGLIDCHTHLVFGGDRAAEWEQRLNGVSYQTISAQGGGINAT 109
Cdd:TIGR01224 2 EDAVILIHGGKIVWIGQLAALPGEEAtEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGILST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 110 VTATRNSSPEMLLTVAQQRLQRLMNEGVTTIEIKSGYGLNAQAEEKMLLVARQLSLNNLVDISPTLLAAHAVPAEYRQDP 189
Cdd:TIGR01224 82 VRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQGRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 190 DAYLTLVCEQIMPTLWQKELFEAVDVFCENVGFTPVQTERLFRAAAALGIPVKGHVEQLSNLGGAALVSQYKGLSADHIE 269
Cdd:TIGR01224 162 DDYVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 270 YLDDAGIQAMAQSGTVAVLLPGAFYFLQErQRPPVAQLREQGVPMAVATDYNPGTSPFASLHLAMNMACVQFGLTPEEAW 349
Cdd:TIGR01224 242 HASDAGIKALAEAGTVAVLLPGTTFYLRE-TYPPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 556409337 350 AGVTRHAAQALGRGATHGQLKPGYVADFVVWEANHPVEMVYEPGRNPLYQRVFRGQV 406
Cdd:TIGR01224 321 HAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNGNI 377
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
5-406 |
4.75e-84 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 261.82 E-value: 4.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 5 HPDDVIWRNARLATLATGEPepyglKEQHALVVRGQTIAAVIPEAE--IPSGHRQcVDLDGRLVTPGLIDCHTHLVFGGD 82
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGV-----IENGTVLVEDGKIAAVGPAADlaVPAGAEV-IDATGKTVLPGLIDAHTHLGLGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 83 RAAEWEQrlngvsyqtisaqGGGINATVTATRNsspemlltvAQQRLQRLMNEGVTTIEIKSGYGL-----NAQAEEKML 157
Cdd:COG1228 80 RAVEFEA-------------GGGITPTVDLVNP---------ADKRLRRALAAGVTTVRDLPGGPLglrdaIIAGESKLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 158 LVARQLSlnNLVDISPTLLAAHAVPAEyrqdpdayltlvCEQIMPTLWqKELFEAVDVFCE--NVGFTPVQTERLFRAAA 235
Cdd:COG1228 138 PGPRVLA--AGPALSLTGGAHARGPEE------------ARAALRELL-AEGADYIKVFAEggAPDFSLEELRAILEAAH 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 236 ALGIPVKGHVEQLSnlgGAALVSQYKGLSADHIEYLDDAGIQAMAQSGTVaVLLPGAFYFL-----------------QE 298
Cdd:COG1228 203 ALGLPVAAHAHQAD---DIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLallegaaapvaakarkvRE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 299 RQRPPVAQLREQGVPMAVATDYNPGTSPFASLHLAMNMAcVQFGLTPEEAWAGVTRHAAQALGRGATHGQLKPGYVADFV 378
Cdd:COG1228 279 AALANARRLHDAGVPVALGTDAGVGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLV 357
|
410 420
....*....|....*....|....*...
gi 556409337 379 VWEANHPVEMVYepgRNPLYQRVFRGQV 406
Cdd:COG1228 358 LLDGDPLEDIAY---LEDVRAVMKDGRV 382
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
17-405 |
3.71e-30 |
|
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: 120.32 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 17 ATLATGEPEpYGLKEQHALVVRGQTIAAVIPEAEIPSGHR--QCVDLDGRLVTPGLIDCHTHLVFGGDRAA-------EW 87
Cdd:COG0402 7 AWVLTMDPA-GGVLEDGAVLVEDGRIAAVGPGAELPARYPaaEVIDAGGKLVLPGLVNTHTHLPQTLLRGLaddlpllDW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 88 eqrLNGVSYQtisaqggginatvtATRNSSPEMLLTVAQQRLQRLMNEGVTTI-EIksgYGLNAQAEEKMLLVARQLSLN 166
Cdd:COG0402 86 ---LEEYIWP--------------LEARLDPEDVYAGALLALAEMLRSGTTTVaDF---YYVHPESADALAEAAAEAGIR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 167 nLVdISPTLLAaHAVPAEYRQDPDAYLTLVCEQImpTLWQKELFEAVdvfceNVGFTPVQ----TERLFRAAAAL----G 238
Cdd:COG0402 146 -AV-LGRGLMD-RGFPDGLREDADEGLADSERLI--ERWHGAADGRI-----RVALAPHApytvSPELLRAAAALarelG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 239 IPVKGHV-EQLSNLggAALVSQYkGLSAdhIEYLDDAG------------------IQAMAQSGTVAVLLPGAFYFLqER 299
Cdd:COG0402 216 LPLHTHLaETRDEV--EWVLELY-GKRP--VEYLDELGllgprtllahcvhltdeeIALLAETGASVAHCPTSNLKL-GS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 300 QRPPVAQLREQGVPMAVATDY---NPGTSPFASLHLAMNMACVQFG----LTPEEAWAGVTRHAAQALGRGATHGQLKPG 372
Cdd:COG0402 290 GIAPVPRLLAAGVRVGLGTDGaasNNSLDMFEEMRLAALLQRLRGGdptaLSAREALEMATLGGARALGLDDEIGSLEPG 369
|
410 420 430
....*....|....*....|....*....|...
gi 556409337 373 YVADFVVWEANHPvemVYEPGRNPLYQRVFRGQ 405
Cdd:COG0402 370 KRADLVVLDLDAP---HLAPLHDPLSALVYAAD 399
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
34-379 |
1.29e-17 |
|
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: 84.28 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 34 ALVVRGQTIAAVIPEAEIP---SGHRQCVDLDGRLVTPGLIDCHTHLVFGG-----------------------DRAA-- 85
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKalkGPATEVIDLKGKTVLPGFIDSHSHLLLGGlsllwldlsgvtskeealarireDAAAap 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 86 --EWEQ----------------------------------------------RLNGVSYQTISAQGGGI----------- 106
Cdd:cd01300 81 pgEWILgfgwdesllgegryptraeldavspdrpvlllrrdghsawvnsaalRLAGITRDTPDPPGGEIvrdadgeptgv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 107 ---NATVTATRN---SSPEMLLTVAQQRLQRLMNEGVTTIEIKSGYGLNAQAEEKMLLVARQLSL---NNLVDISPTLLA 177
Cdd:cd01300 161 lveAAAALVLEAvppPTPEERRAALRAAARELASLGVTTVHDAGGGAADDIEAYRRLAAAGELTLrvrVALYVSPLAEDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 178 AHAVPAEYRQDPDAYLTLVCEQI----MP---TLWQKELFEAVDVFCENVGFTPVQTERLFRAAAALGIPVKGH------ 244
Cdd:cd01300 241 LEELGARKNGAGDDRLRLGGVKLfadgSLgsrTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAIHaigdra 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 245 -------VEQLSNLGGAALVSqykgLSADHIEYLDDAGIQAMAQSGTVAVLLPG-AFYFLQERQR-----------PPVA 305
Cdd:cd01300 321 vdtvldaLEAALKDNPRADHR----HRIEHAQLVSPDDIPRFAKLGVIASVQPNhLYSDGDAAEDrrlgeerakrsYPFR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 306 QLREQGVPMAVATDYNPGT-SPFASLHLAMN--------MACVQFGLTPEEAWAGVTRHAAQALGRGATHGQLKPGYVAD 376
Cdd:cd01300 397 SLLDAGVPVALGSDAPVAPpDPLLGIWAAVTrktpgggvLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLAD 476
|
...
gi 556409337 377 FVV 379
Cdd:cd01300 477 FVV 479
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
8-383 |
5.55e-17 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 82.54 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 8 DVIWRNARLATLATGEPEPyglkeqHALVVRGQTIAAVIPEAEIPS---GHRQCVDLDGRLVTPGLIDCHTHLVFGG--- 81
Cdd:COG1574 9 DLLLTNGRIYTMDPAQPVA------EAVAVRDGRIVAVGSDAEVRAlagPATEVIDLGGKTVLPGFIDAHVHLLGGGlal 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 82 -------------------DRAAE-----------WEQ----------------------------------------RL 91
Cdd:COG1574 83 lgvdlsgarsldellarlrAAAAElppgewilgrgWDEslwpegrfptradldavspdrpvvltrvdghaawvnsaalEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 92 NGVSYQTISAQGGGI--------------NATVTATRN---SSPEMLLTvAQQRLQRLMNE-GVTTIeiksgygLNAQAE 153
Cdd:COG1574 163 AGITADTPDPEGGEIerdadgeptgvlreAAMDLVRAAippPTPEELRA-ALRAALRELASlGITSV-------HDAGLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 154 EKMLLVARQLSLNNLvdisptlLAAHAVPAEYRQDPDayLTLVCEQIMPTLWQKELFE--AVDVFC-------------- 217
Cdd:COG1574 235 PDDLAAYRELAAAGE-------LPLRVVLYLGADDED--LEELLALGLRTGYGDDRLRvgGVKLFAdgslgsrtaallep 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 218 -----ENVG---FTPVQTERLFRAAAALGIPVKGHVeqlsnLGGAA---LVSQYKGLSAD-----------HIEYLDDAG 275
Cdd:COG1574 306 yaddpGNRGlllLDPEELRELVRAADAAGLQVAVHA-----IGDAAvdeVLDAYEAARAAngrrdrrhrieHAQLVDPDD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 276 IQAMAQSGTVAVLLPGAFYFLQERQRP-----------PVAQLREQGVPMAVATDYnPGTS--PFASLHLAMN---MACV 339
Cdd:COG1574 381 LARFAELGVIASMQPTHATSDGDWAEDrlgperaarayPFRSLLDAGAPLAFGSDA-PVEPldPLLGIYAAVTrrtPSGR 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 556409337 340 QFG----LTPEEAWAGVTRHAAQALGRGATHGQLKPGYVADFVVWEAN 383
Cdd:COG1574 460 GLGpeerLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRD 507
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
70-359 |
7.86e-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: 80.07 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 70 LIDCHTHLVFGGDRAAEWEQRLNGVSYQTisaqggginatvtatrnssPEMLLTVAQQRLQRLMNEGVTTIEIKSGYGLN 149
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELS-------------------PEDLYEDTLRALEALLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 150 AQAEEKMLLVARQLSLNNLVDISPTLLAAHAVPAEYRQDPD---AYLTLVCEQIMPTLwqkelfeAVDVFCENVGFTPVQ 226
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEAlllELLRRGLELGAVGL-------KLAGPYTATGLSDES 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 227 TERLFRAAAALGIPVKGHVEQLSNLGGA-----ALVSQYKGLSADHIEYLDDAGIQAMAQSGTVAVLLPGAFYFLQER-- 299
Cdd:cd01292 135 LRRVLEEARKLGLPVVIHAGELPDPTRAledlvALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDge 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556409337 300 QRPPVAQLREQGVPMAVATDYNPGTS---PFASLHLAMNMAcvQFGLTPEEAWAGVTRHAAQA 359
Cdd:cd01292 215 GAEALRRLLELGIRVTLGTDGPPHPLgtdLLALLRLLLKVL--RLGLSLEEALRLATINPARA 275
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-392 |
1.16e-16 |
|
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: 81.14 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 12 RNARLATlatGEPEPYglkeqhALVVRGQTIAAVIPEAEIPsGHRQCVDLDGRLVTPGLIDCHTHL--VFGGDRaaeweq 89
Cdd:cd01293 3 RNARLAD---GGTALV------DIAIEDGRIAAIGPALAVP-PDAEEVDAKGRLVLPAFVDPHIHLdkTFTGGR------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 90 rlngVSYQTISAQGGGINATVTATRNSSPEMLLTVAQQRLQRLMNEGVTTI----EIKSGYGLNAQaeEKMLLVARQLSl 165
Cdd:cd01293 67 ----WPNNSGGTLLEAIIAWEERKLLLTAEDVKERAERALELAIAHGTTAIrthvDVDPAAGLKAL--EALLELREEWA- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 166 nNLVDIS----PTL----------LAAHAV-----------PAEYRQDPDAYLTLVCEqimptLWQKelFEA-VDVFCEN 219
Cdd:cd01293 140 -DLIDLQivafPQHgllstpggeeLMREALkmgadvvggipPAEIDEDGEESLDTLFE-----LAQE--HGLdIDLHLDE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 220 VGFTPVQT-ERLFRAAAALGIPVK---GHVEQLSNLGGAALvsqykglsADHIEYLDDAGIQAMAqSGTVAVLLPGAFY- 294
Cdd:cd01293 212 TDDPGSRTlEELAEEAERRGMQGRvtcSHATALGSLPEAEV--------SRLADLLAEAGISVVS-LPPINLYLQGREDt 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 295 FLQERQRPPVAQLREQGVPMAVATD-----YNP-GT-SPFASLHLAMNMAcvqfGLTPEE----AWAGVTRHAAQALgrG 363
Cdd:cd01293 283 TPKRRGVTPVKELRAAGVNVALGSDnvrdpWYPfGSgDMLEVANLAAHIA----QLGTPEdlalALDLITGNAARAL--G 356
|
410 420
....*....|....*....|....*....
gi 556409337 364 ATHGQLKPGYVADFVVWEANHPVEMVYEP 392
Cdd:cd01293 357 LEDYGIKVGCPADLVLLDAEDVAEAVARQ 385
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
59-383 |
1.01e-15 |
|
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: 77.72 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 59 VDLDGRLVTPGLIDCHTHLVFGGDRAAEWEQrlNGVSYQTIsaqggginatvtatrnsspemlltVAQQRLQRLMNEGVT 138
Cdd:cd01299 4 IDLGGKTLMPGLIDAHTHLGSDPGDLPLDLA--LPVEYRTI------------------------RATRQARAALRAGFT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 139 TIE--IKSGYGLNAQAEEK------MLLVARQLslnnlvdISPTllAAHAVPAEYRQDPDAY-LTLVCEQI--MPTLWQK 207
Cdd:cd01299 58 TVRdaGGADYGLLRDAIDAglipgpRVFASGRA-------LSQT--GGHGDPRGLSGLFPAGgLAAVVDGVeeVRAAVRE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 208 ELFEAVDVF--------------CENVGFTPVQTERLFRAAAALGIPVKGHVEqlsnlgGAALVSQYKGLSADHIE---Y 270
Cdd:cd01299 129 QLRRGADQIkimatggvlspgdpPPDTQFSEEELRAIVDEAHKAGLYVAAHAY------GAEAIRRAIRAGVDTIEhgfL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 271 LDDAGIQAMAQSGTV---------AVLLPGAFYFL-----------QERQRPPVAQLREQGVPMAVATDYNPGTSPFASL 330
Cdd:cd01299 203 IDDETIELMKEKGIFlvptlatyeALAAEGAAPGLpadsaekvalvLEAGRDALRRAHKAGVKIAFGTDAGFPVPPHGWN 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 556409337 331 HLAMNMAcVQFGLTPEEAWAGVTRHAAQALGRGATHGQLKPGYVADFVVWEAN 383
Cdd:cd01299 283 ARELELL-VKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGD 334
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
34-379 |
1.86e-13 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 71.38 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 34 ALVVRGQTIAAVIPEAEIPSGHRQCV---DLDGRLVTPGLIDCHTHL----VFG--GDRAAEW--------EQRLNGVSY 96
Cdd:PRK09228 33 LLLVEDGRIVAAGPYAELRAQLPADAevtDYRGKLILPGFIDTHIHYpqtdMIAsyGEQLLDWlntytfpeERRFADPAY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 97 qtiSAQGGGI-------NATVTAT-----RNSSPEMLLTVAQQRLQR------LMN----EGVT-TIEikSGYglnaqAE 153
Cdd:PRK09228 113 ---AREVAEFfldellrNGTTTALvfgtvHPQSVDALFEAAEARNMRmiagkvLMDrnapDGLRdTAE--SGY-----DD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 154 EKMLL-----VARqlslnNLVDISP---------TLLAAHAVPAEYrqdPDAYL-TLVCEQIMPTLWQKELF-EA---VD 214
Cdd:PRK09228 183 SKALIerwhgKGR-----LLYAITPrfaptstpeQLEAAGALAREH---PDVWIqTHLSENLDEIAWVKELFpEArdyLD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 215 VFcENVGftpvqterLFRAAAALGipvkghveqlsnlggaalvsqykglsadHIEYLDDAGIQAMAQSGTVAVLLP---- 290
Cdd:PRK09228 255 VY-ERYG--------LLGPRAVFA----------------------------HCIHLEDRERRRLAETGAAIAFCPtsnl 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 291 ----GAFyflqerqrpPVAQLREQGVPMAVATDYNPGTSpFASLHlAMNMAC-VQ----FGLTPEEAWAGVTRHAAQALG 361
Cdd:PRK09228 298 flgsGLF---------DLKRADAAGVRVGLGTDVGGGTS-FSMLQ-TMNEAYkVQqlqgYRLSPFQAFYLATLGGARALG 366
|
410
....*....|....*...
gi 556409337 362 RGATHGQLKPGYVADFVV 379
Cdd:PRK09228 367 LDDRIGNLAPGKEADFVV 384
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
42-394 |
2.84e-13 |
|
Metallo-dependent hydrolases, subgroup C 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: 238634 [Multi-domain] Cd Length: 359 Bit Score: 70.42 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 42 IAAVIPEAEIPSGHrQCVDLDGRLVTPGLIDCHTHLvfGGDRA-AEWEQRLNGVSYQTISAQ---GGGINATVTAtrnss 117
Cdd:cd01309 4 IVAVGAEITTPADA-EVIDAKGKHVTPGLIDAHSHL--GLDEEgGVRETSDANEETDPVTPHvraIDGINPDDEA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 118 pemlltvaqqrLQRLMNEGVTTIEIKSGYG-----------LNAQAEEKMLLVA-RQLSLN---------NLVDISPTll 176
Cdd:cd01309 76 -----------FKRARAGGVTTVQVLPGSAnliggqgvvikTDGGTIEDMFIKApAGLKMAlgenpkrvyGGKGKEPA-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 177 AAHAVPAEYRQ---DPDAYLtlvcEQIMPTLWQKELFEAVDVfcenvgftpvQTERLfrAAAALG-IPVKGHVEQLSNLG 252
Cdd:cd01309 143 TRMGVAALLRDafiKAQEYG----RKYDLGKNAKKDPPERDL----------KLEAL--LPVLKGeIPVRIHAHRADDIL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 253 GA-ALVSQYK-GLSADHIE---YLDDAgiqaMAQSGTVAVLLP--GAFYFLQERQR--PPVAQLRE-QGVPMAVATDYNP 322
Cdd:cd01309 207 TAiRIAKEFGiKITIEHGAegyKLADE----LAKHGIPVIYGPtlTLPKKVEEVNDaiDTNAYLLKkGGVAFAISSDHPV 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556409337 323 GTSPFASLHLAMnmaCVQFGLTPEEAWAGVTRHAAQALGRGATHGQLKPGYVADFVVWEAnHP------VEMVYEPGR 394
Cdd:cd01309 283 LNIRNLNLEAAK---AVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNG-DPleptskPEQVYIDGR 356
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
65-398 |
3.96e-12 |
|
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: 66.76 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 65 LVTPGLIDCHTHLVFGgdraaewEQRLNGVSYQTISAqggginatvtATRNSSPEMLltvaqqrlqrlmNEGVTTIeIKS 144
Cdd:pfam01979 1 IVLPGLIDAHVHLEMG-------LLRGIPVPPEFAYE----------ALRLGITTML------------KSGTTTV-LDM 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 145 GYGlNAQAEEKMLLVARQLSLNnlvdisPTLLAAHAVPAEyRQDPDAYLTlVCEQIMPtLWQKELFEAVDVFC------E 218
Cdd:pfam01979 51 GAT-TSTGIEALLEAAEELPLG------LRFLGPGCSLDT-DGELEGRKA-LREKLKA-GAEFIKGMADGVVFvglaphG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 219 NVGFTPVQTERLFRAAAALGIPVKGHVeqLSNLGGAALVSQYKGLSADHIEYLDDAG-------IQAMAQSG-----TVA 286
Cdd:pfam01979 121 APTFSDDELKAALEEAKKYGLPVAIHA--LETKGEVEDAIAAFGGGIEHGTHLEVAEsgglldiIKLILAHGvhlspTEA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 287 VLLPGAFY-----------FLQERQRPPVAQLREQGVPMAVATDYNPGTSPFASLHLAMNMACVQF----GLTPEEAWAG 351
Cdd:pfam01979 199 NLLAEHLKgagvahcpfsnSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFdpegGLSPLEALRM 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 556409337 352 VTRHAAQALGRGATHGQLKPGYVADFVVWEANHPVEMVY-EPGRNPLY 398
Cdd:pfam01979 279 ATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGlKPDGNVKK 326
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
59-383 |
1.10e-11 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 66.02 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 59 VDLDGRLVTPGLIDCHTHLVFGGDRAAEweQRLNGVSY-QTISAQ-----------GGGINATVTA------TRN----S 116
Cdd:pfam07969 3 IDAKGRLVLPGFVDPHTHLDGGGLNLRE--LRLPDVLPnAVVKGQagrtpkgrwlvGEGWDEAQFAetrfpyALAdldeV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 117 SPEMLLTVAQQ----------RLQRLMNEGVTTIEI-------KSGYGLNAQAEEKMLLVARQLSLNNLVDISPTLLAAH 179
Cdd:pfam07969 81 APDGPVLLRALhthaavansaALDLAGITKATEDPPggeiardANGEGLTGLLREGAYALPPLLAREAEAAAVAAALAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 180 A-----------VPAEYRQDPDAYLTLVCEQIMPTLWQKE------------LFEAVDVF-------------------- 216
Cdd:pfam07969 161 PgfgitsvdgggGNVHSLDDYEPLRELTAAEKLKELLDAPerlglphsiyelRIGAMKLFadgvlgsrtaaltepyfdap 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 217 -CENVGFTPVQTERLFRAAAALGIPVKGHV---EQLSN-LGGAALVSQYKGL----SADH---IEYLDDAGIQAMAQSGT 284
Cdd:pfam07969 241 gTGWPDFEDEALAELVAAARERGLDVAIHAigdATIDTaLDAFEAVAEKLGNqgrvRIEHaqgVVPYTYSQIERVAALGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 285 VA----VLLPGAFYFLQERQR-------PPVAQLREQGVPMAVATDYNPGT-SPFASLHLA------MNMACVQFG--LT 344
Cdd:pfam07969 321 AAgvqpVFDPLWGDWLQDRLGaerarglTPVKELLNAGVKVALGSDAPVGPfDPWPRIGAAvmrqtaGGGEVLGPDeeLS 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 556409337 345 PEEAWAGVTRHAAQALGRGATHGQLKPGYVADFVVWEAN 383
Cdd:pfam07969 401 LEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDD 439
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
12-406 |
3.50e-11 |
|
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: 64.53 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 12 RNARLATLATGEPEPYGlkeqhALVVRGQTIAAVIPEAEIPSGHR-QCVDLDGRLVTPGLIDCHTHLVFGGDRA------ 84
Cdd:cd01298 4 RNGTIVTTDPRRVLEDG-----DVLVEDGRIVAVGPALPLPAYPAdEVIDAKGKVVMPGLVNTHTHLAMTLLRGladdlp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 85 -AEW--------EQRLNGVSyQTISAQGGGInatvtatrnsspEMLLTvaqqrlqrlmneGVTTIEIKSGYGLNAQAEek 155
Cdd:cd01298 79 lMEWlkdliwplERLLTEED-VYLGALLALA------------EMIRS------------GTTTFADMYFFYPDAVAE-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 156 mllVARQLSLNNLvdISPTLLAahaVPAEYRQDPDAYLTLVCEQImpTLWQKELFEAVdvfceNVGFTPVQ----TERLF 231
Cdd:cd01298 132 ---AAEELGIRAV--LGRGIMD---LGTEDVEETEEALAEAERLI--REWHGAADGRI-----RVALAPHApytcSDELL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 232 RAAAAL----GIPVKGH-------------------VEQLSNLGgaaLVSqyKGLSADHIEYLDDAGIQAMAQSGTVAVL 288
Cdd:cd01298 197 REVAELareyGVPLHIHlaetedeveeslekygkrpVEYLEELG---LLG--PDVVLAHCVWLTDEEIELLAETGTGVAH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 289 LPGAfyflqeRQR-----PPVAQLREQGVPMAVATD---YNPGTSPFASLHLAMNMACVQFG----LTPEEAWAGVTRHA 356
Cdd:cd01298 272 NPAS------NMKlasgiAPVPEMLEAGVNVGLGTDgaaSNNNLDMFEEMRLAALLQKLAHGdptaLPAEEALEMATIGG 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 556409337 357 AQALGRGAThGQLKPGYVADFVVWEANHPvEM--VYEPGRNPLYQrVFRGQV 406
Cdd:cd01298 346 AKALGLDEI-GSLEVGKKADLILIDLDGP-HLlpVHDPISHLVYS-ANGGDV 394
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
12-382 |
6.01e-11 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 63.85 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 12 RNARL-ATLATGEPEPYGLKEQHALV----VRGQtIAAVIPEAEIPSGHRQcVDLDGRLVTPGLIDCHTHLvfggDRAAE 86
Cdd:PRK07583 16 KNARVpAALLEGGVPPGDTLEGLVLVdieiADGK-IAAILPAGGAPDELPA-VDLKGRMVWPCFVDMHTHL----DKGHI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 87 WEQRLN--GVSYQTISAqggginATVTATRNSSPEMLLtvaqqrlqRLMNegvttieiksgYGLN-AQAEEKMLLVARQL 163
Cdd:PRK07583 90 WPRSPNpdGTFPGALDA------VTADREAHWSAEDLY--------RRME-----------FGLRcAYAHGTSAIRTHLD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 164 SLNNLVDIS--------------PTLLAAHAVPAEYRQDpDAYLTLvceqimptlwqkelfeaVDVFCENVG-------F 222
Cdd:PRK07583 145 SFAPQAAISwevfaelreawagrIALQAVSLVPLDAYLT-DAGERL-----------------ADLVAEAGGllggvtyM 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 223 TP---VQTERLFRAAAALGIPVKGHVEQ--------LSNLGGAALVSQYKG-LSADHIEYLD-------DAGIQAMAQSG 283
Cdd:PRK07583 207 NPdldAQLDRLFRLARERGLDLDLHVDEtgdpasrtLKAVAEAALRNGFEGkVTCGHCCSLAvqpeeqaQATIALVAEAG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 284 TVAVLLPGAFYFLQERQRP---------PVAQLREQGVPMAVATDyNpGTSPFAS----------------LHLAmnmac 338
Cdd:PRK07583 287 IAIVSLPMCNLYLQDRQPGrtprwrgvtLVHELKAAGIPVAVASD-N-CRDPFYAygdhdmlevfreavriLHLD----- 359
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 556409337 339 vqfglTPEEAW-AGVTRHAAQALGRgATHGQLKPGYVADFVVWEA 382
Cdd:PRK07583 360 -----HPYDDWpAAVTTTPADIMGL-PDLGRIAVGAPADLVLFKA 398
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
55-385 |
2.23e-10 |
|
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: 61.70 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 55 HRQCVdldgrlVTPGLIDCHTHLVFGGDRAAeweqrlngVSYQTISAQGGGINATVTATRNSSPEmllTVAQQRLQRLMN 134
Cdd:cd01312 24 FPNGV------LLPGLINAHTHLEFSANVAQ--------FTYGRFRAWLLSVINSRDELLKQPWE---EAIRQGIRQMLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 135 EGVTTI-EIKS-GYGLNAQAEEKM---------------------LLVARQLSLNNLVdiSPTLLAAHAVPAEYRQDPDA 191
Cdd:cd01312 87 SGTTSIgAISSdGSLLPALASSGLrgvffnevigsnpsaidfkgeTFLERFKRSKSFE--SQLFIPAISPHAPYSVHPEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 192 Y---LTLVCEQIMP--TLWQKELFEAvDVFCENVGFTPVQTERLFRAA-AALGIPVKGHVEQLSNLGGAalvsqykgLSA 265
Cdd:cd01312 165 AqdlIDLAKKLNLPlsTHFLESKEER-EWLEESKGWFKHFWESFLKLPkPKKLATAIDFLDMLGGLGTR--------VSF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 266 DHIEYLDDAGIQAMAQSGTVAVLLPGAFYFLQErQRPPVAQLREQGVPMAVATDynpGTSPFASLHLAMNM-----ACVQ 340
Cdd:cd01312 236 VHCVYANLEEAEILASRGASIALCPRSNRLLNG-GKLDVSELKKAGIPVSLGTD---GLSSNISLSLLDELralldLHPE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 556409337 341 FGL--TPEEAWAGVTRHAAQALgrGATHGQLKPGYVADFVVWEANHP 385
Cdd:cd01312 312 EDLleLASELLLMATLGGARAL--GLNNGEIEAGKRADFAVFELPGP 356
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
34-380 |
3.04e-10 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 61.79 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 34 ALVVRGQTIAAVIPEAEIPSGHRQCVDLDGRLVTPGLIDCHTHLvfggdraaeweqrlngvsYQTIS-AQGGGINAT--- 109
Cdd:PRK08203 25 GLVVEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHHF------------------YQTLTrALPAAQDAElfp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 110 -------VTAtrNSSPEMLLTVAQQRLQRLMNEGVTTIE-------IKSGYGLNAQAEEkmllvARQLSL---------- 165
Cdd:PRK08203 87 wlttlypVWA--RLTPEMVRVATQTALAELLLSGCTTSSdhhylfpNGLRDALDDQIEA-----AREIGMrfhatrgsms 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 166 ----------NNLVDISPTLLAA-HAVPAEYRQ-DPDAYLTL---------VCEQIM---PTLWQKE-------LFEAVD 214
Cdd:PRK08203 160 lgesdgglppDSVVEDEDAILADsQRLIDRYHDpGPGAMLRIalapcspfsVSRELMresAALARRLgvrlhthLAETLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 215 --VFC-ENVGFTPVQterlfraaaalgipvkgHVEQLSNLGgaalvsqykglsAD----HIEYLDDAGIQAMAQSGT-VA 286
Cdd:PRK08203 240 eeAFClERFGMRPVD-----------------YLEDLGWLG------------PDvwlaHCVHLDDAEIARLARTGTgVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 287 -------VLLPGAfyflqerqrPPVAQLREQGVPMAVATD---YNPGTSPFASLHLAMNMACVQFG---LTPEEA--WAg 351
Cdd:PRK08203 291 hcpcsnmRLASGI---------APVRELRAAGVPVGLGVDgsaSNDGSNLIGEARQALLLQRLRYGpdaMTAREAleWA- 360
|
410 420
....*....|....*....|....*....
gi 556409337 352 vTRHAAQALGRGAThGQLKPGYVADFVVW 380
Cdd:PRK08203 361 -TLGGARVLGRDDI-GSLAPGKLADLALF 387
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
8-406 |
1.33e-09 |
|
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: 59.61 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 8 DVIWRNARLATlatgepePYGLKEQHALVVRGQtIAAVIPEAEIPSGHRqCVDLDGRLVTPGLIDCHTHLVFGGdrAAEW 87
Cdd:cd01315 1 DLVIKNGRVVT-------PDGVREADIAVKGGK-IAAIGPDIANTEAEE-VIDAGGLVVMPGLIDTHVHINEPG--RTEW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 88 EqrlnGVSYQTISAQGGGINATVTATRNSSPEMLLtvaqqrlqrlmnegVTTIEIKsgygLNAqAEEKML--------LV 159
Cdd:cd01315 70 E----GFETGTKAAAAGGITTIIDMPLNSIPPTTT--------------VENLEAK----LEA-AQGKLHvdvgfwggLV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 160 ArqlslNNLVDISPTLLA---------AHAVPAEYRQDPDAYLtlvcEQIMPTLwqKELFEAVDVFCENVGFT------- 223
Cdd:cd01315 127 P-----GNLDQLRPLDEAgvvgfkcflCPSGVDEFPAVDDEQL----EEAMKEL--AKTGSVLAVHAENPEITealqeqa 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 224 ---------------PVQTE-----RLFRAAAALGIPVkgHVEQLSNLGGAALVSQYKGLSAD-HIE----YLDDAGIQA 278
Cdd:cd01315 196 kakgkrdyrdylasrPVFTEveaiqRILLLAKETGCRL--HIVHLSSAEAVPLIREARAEGVDvTVEtcphYLTFTAEDV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 279 mAQSGTVAVLLPGAfyflqeRQRPPVAQLREQ---GVPMAVATDYNP--------GTSPF-------ASLHLAMNM---- 336
Cdd:cd01315 274 -PDGGTEFKCAPPI------RDAANQEQLWEAlenGDIDMVVSDHSPctpelkllGKGDFfkawggiSGLQLGLPVmlte 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556409337 337 ACVQFGLTPEEAWAGVTRHAAQALGRGATHGQLKPGYVADFVVWEANHPVE-----MVYEPGRNPLYQRVFRGQV 406
Cdd:cd01315 347 AVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPEEEFTvdaedLYYKNKISPYVGRTLKGRV 421
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
267-379 |
1.06e-08 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 56.90 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 267 HIEYLDDAGIQAMAQSGTVAVLLP--------GAFyflqerqrpPVAQLREQGVPMAVATDYNPGTSP----------FA 328
Cdd:cd01303 267 HCVHLSEEEFNLLKERGASVAHCPtsnlflgsGLF---------DVRKLLDAGIKVGLGTDVGGGTSFsmldtlrqayKV 337
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 556409337 329 SLHLAMNMACVQFgLTPEEAWAGVTRHAAQALGRGATHGQLKPGYVADFVV 379
Cdd:cd01303 338 SRLLGYELGGHAK-LSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVV 387
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
12-387 |
2.63e-08 |
|
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: 55.48 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 12 RNARLATlatgepePYGLKEQhALVVRGQTIAAVIPEAEIPSGhRQCVDLDGRLVTPGLIDCHTHL-------------- 77
Cdd:COG0044 3 KNGRVVD-------PGGLERA-DVLIEDGRIAAIGPDLAAPEA-AEVIDATGLLVLPGLIDLHVHLrepglehkedietg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 78 ----VFGG-----------------DRAAEWEQRLNGVSYQTISAQGGginatvtATRNSSPEMlltvaqQRLQRLMNEG 136
Cdd:COG0044 74 traaAAGGvttvvdmpntnpvtdtpEALEFKLARAEEKALVDVGPHGA-------LTKGLGENL------AELGALAEAG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 137 VTTIEIKSGYG-----LNAQAEEKMLLVARQLSLnnlvdisptLLAAHA---------VPAEYRQDPDAYLtlvceqimp 202
Cdd:COG0044 141 AVAFKVFMGSDdgnpvLDDGLLRRALEYAAEFGA---------LVAVHAedpdlirggVMNEGKTSPRLGL--------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 203 tlwqkelfEAVDVFCENvgftpVQTERLFRAAAALGIPVkgHVEQLSNLGGAALVSQYK--GL--SAD----HIeYLDDA 274
Cdd:COG0044 203 --------KGRPAEAEE-----EAVARDIALAEETGARL--HIVHVSTAEAVELIREAKarGLpvTAEvcphHL-TLTDE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 275 giqAMAQSGTVAVLLPgafyflqerqrPP-----VAQLRE---QGVPMAVATDYNPGTS-----PFA-----------SL 330
Cdd:COG0044 267 ---DLERYGTNFKVNP-----------PLrteedREALWEglaDGTIDVIATDHAPHTLeekelPFAeapngipgletAL 332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 556409337 331 HLAMNMACVQFGLTPEEAWAGVTRHAAQALGRgATHGQLKPGYVADFVVWEANHPVE 387
Cdd:COG0044 333 PLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDAEWT 388
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
12-390 |
4.04e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 54.72 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 12 RNARLATlatgepePYGLKEQHALVVRGQTIAAVIPEAEIPSghrQCVDLDGRLVTPGLIDCHTHlvfGgdraaeweqrl 91
Cdd:COG1820 3 TNARIFT-------GDGVLEDGALLIEDGRIAAIGPGAEPDA---EVIDLGGGYLAPGFIDLHVH---G----------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 92 ngvsyqtisaqGGGINATvtatrNSSPEMLLTVAqqrlQRLMNEGVT-----TIeiksgyglnAQAEEKMLLVARQLSln 166
Cdd:COG1820 59 -----------GGGVDFM-----DGTPEALRTIA----RAHARHGTTsflptTI---------TAPPEDLLRALAAIA-- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 167 NLVD----------------ISPTLLAAHavPAEYRQDPDAyltlvcEQImptlwqKELFEA-------VDVFCENVGft 223
Cdd:COG1820 108 EAIEqgggagilgihlegpfLSPEKKGAH--PPEYIRPPDP------EEL------DRLLEAaggliklVTLAPELPG-- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 224 pvqTERLFRAAAALGIPVK-GH-------VEQLSNLG----------------------GAALVSQ--YKGLSADHIeYL 271
Cdd:COG1820 172 ---ALEFIRYLVEAGVVVSlGHtdatyeqARAAFEAGathvthlfnamsplhhrepgvvGAALDDDdvYAELIADGI-HV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 272 DDAGIQ----------------AMAqsgtvAVLLPGAFYFLQERqrpPVaqLREQGVpmAVATDynpGTspFASLHLAMN 335
Cdd:COG1820 248 HPAAVRlalrakgpdrlilvtdAMA-----AAGLPDGEYELGGL---EV--TVKDGV--ARLAD---GT--LAGSTLTMD 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 336 mACVQF-----GLTPEEAWAGVTRHAAQALGRGATHGQLKPGYVADFVVWEANHPVEMVY 390
Cdd:COG1820 311 -DAVRNlvewtGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATW 369
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
267-385 |
9.76e-08 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 53.70 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 267 HIEYLDDAGIQAMAQSGTVAVLLP--------GAFyflqerqrpPVAQLREQGVPMAVATDYNPGTSPFASL-------- 330
Cdd:PRK09229 271 HATHLTDAETARLARSGAVAGLCPtteanlgdGIF---------PAVDYLAAGGRFGIGSDSHVSIDLVEELrlleygqr 341
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 556409337 331 --HLAMN-MACVQFGLTPEEAWAGVTRHAAQALGRGAthGQLKPGYVADFVVWEANHP 385
Cdd:PRK09229 342 lrDRRRNvLAAAAQPSVGRRLFDAALAGGAQALGRAI--GGLAVGARADLVVLDLDHP 397
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
7-389 |
1.09e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 53.40 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 7 DDVIWRNARLATlatGEPepyglkeqHALVVRGQTIAAVIPEAEIPSGhRQCVDLDGRLVTPGLIDCHTHL--VFGGDRa 84
Cdd:PRK05985 2 TDLLFRNVRPAG---GAA--------VDILIRDGRIAAIGPALAAPPG-AEVEDGGGALALPGLVDGHIHLdkTFWGDP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 85 aeWeqrlngVSYQTISAQGGGINATVTATRNSSPEMLltvaqQRLQRLMNE----GVTTI----EIKSGYGLNAQaeEKM 156
Cdd:PRK05985 69 --W------YPNEPGPSLRERIANERRRRAASGHPAA-----ERALALARAaaaaGTTAMrshvDVDPDAGLRHL--EAV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 157 LLVARQlsLNNLVDI---------------SPTLLAAhAV-----------PAEYRQDPDAYLTLVceqimptlwqkelF 210
Cdd:PRK05985 134 LAARET--LRGLIDIqivafpqsgvlsrpgTAELLDA-ALragadvvggldPAGIDGDPEGQLDIV-------------F 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 211 E-------AVDVFCENVGFTPVQT-ERLFRAAAALGipvkghveqlsnLGGAALVSQYKGLSADHIEYLDDAgIQAMAQS 282
Cdd:PRK05985 198 GlaerhgvGIDIHLHEPGELGAFQlERIAARTRALG------------MQGRVAVSHAFCLGDLPEREVDRL-AERLAEA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 283 GtVAVLL--PGAFYFlqerqrPPVAQLREQGVPMAVATDYNPGT-SPFAS---LHLAMnMACVQFGL-TPEE---AWAGV 352
Cdd:PRK05985 265 G-VAIMTnaPGSVPV------PPVAALRAAGVTVFGGNDGIRDTwWPYGNgdmLERAM-LIGYRSGFrTDDElaaALDCV 336
|
410 420 430
....*....|....*....|....*....|....*..
gi 556409337 353 TRHAAQALGRgATHGqLKPGYVADFVVWEANHPVEMV 389
Cdd:PRK05985 337 THGGARALGL-EDYG-LAVGARADFVLVDAETVAEAV 371
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
25-76 |
2.76e-07 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 52.22 E-value: 2.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 556409337 25 EPYG-LKEQHALVVRGQTIAAVIPEAEIPSGH--RQCVDLDGRLVTPGLIDCHTH 76
Cdd:PRK09045 20 EPAGvVLEDHAVAIRDGRIVAILPRAEARARYaaAETVELPDHVLIPGLINAHTH 74
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
8-83 |
3.42e-07 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 51.71 E-value: 3.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556409337 8 DVIWRNARLATLATGepepygLKEQHALVVRGQTIAAVIPEAEIPSGHRQcVDLDGRLVTPGLIDCHTHLVFGGDR 83
Cdd:COG3964 1 DLLIKGGRVIDPANG------IDGVMDIAIKDGKIAAVAKDIDAAEAKKV-IDASGLYVTPGLIDLHTHVFPGGTD 69
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
9-81 |
7.79e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 50.62 E-value: 7.79e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556409337 9 VIWRNARLATLATGEPEPYglkeqhALVVRGQTIAAVIPEAEiPSGHRQCVDLDGRLVTPGLIDCHTHLVFGG 81
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGVI------DIAIEDGKIAAVAGDID-GSQAKKVIDLSGLYVSPGWIDLHVHVYPGS 66
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
24-84 |
9.53e-07 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 50.47 E-value: 9.53e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556409337 24 PEPYGLKEqhaLVVRGQTIAAVIPEAEIPSGHR-QCVDLDGRLVTPGLIDCHTHLVFGGDRA 84
Cdd:cd01308 12 PEYLGKKD---ILIAGGKILAIEDQLNLPGYENvTVVDLHGKILVPGFIDQHVHIIGGGGEG 70
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
28-390 |
2.31e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 49.11 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 28 GLKEQHALVVRGQTIAAVIPEAEIPSGHRQcVDLDGRLVTPGLIDCHTHlvfGgdraaeweqrlngvsyqtisaqGGGIN 107
Cdd:cd00854 12 GGLEDGAVLVEDGKIVAIGPEDELEEADEI-IDLKGQYLVPGFIDIHIH---G----------------------GGGAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 108 ATvtatrNSSPEMLLTVAqqrlQRLMNEGVT-----TIeiksgyglnAQAEEKMLLVARQLSLNNLVDISPTLLAAH--- 179
Cdd:cd00854 66 FM-----DGTAEALKTIA----EALAKHGTTsflptTV---------TAPPEEIAKALAAIAEAIAEGQGAEILGIHleg 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 180 ---------AVPAEYRQDPDAyltlvcEQIMPTLWQK-----------EL---FEAVDVFCEN-----VGFTpVQTERLF 231
Cdd:cd00854 128 pfispekkgAHPPEYLRAPDP------EELKKWLEAAggliklvtlapELdgaLELIRYLVERgiivsIGHS-DATYEQA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 232 RAAAALGIpvkGHVEQLSN-----------LGGAALVSQ--YKGLSADHIeYLDDAGIQ----------------AMAqs 282
Cdd:cd00854 201 VAAFEAGA---THVTHLFNamsplhhrepgVVGAALSDDdvYAELIADGI-HVHPAAVRlayrakgadkivlvtdAMA-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 283 gtvAVLLPGAFYFLQERQrppvaQLREQGVpmAVATDynpGTspFASLHLAMNmACVQF-----GLTPEEAWAGVTRHAA 357
Cdd:cd00854 275 ---AAGLPDGEYELGGQT-----VTVKDGV--ARLAD---GT--LAGSTLTMD-QAVRNmvkwgGCPLEEAVRMASLNPA 338
|
410 420 430
....*....|....*....|....*....|...
gi 556409337 358 QALGRGATHGQLKPGYVADFVVWEANHPVEMVY 390
Cdd:cd00854 339 KLLGLDDRKGSLKPGKDADLVVLDDDLNVKATW 371
|
|
| PLN02795 |
PLN02795 |
allantoinase |
34-118 |
3.38e-06 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 49.00 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 34 ALVVRGQTIAAVIPEAEIPS--GHRQCVDLDGRLVTPGLIDCHTHLVFGGdrAAEWEQRLNGvsyqTISAQGGGINATVT 111
Cdd:PLN02795 63 AVEVEGGRIVSVTKEEEAPKsqKKPHVLDYGNAVVMPGLIDVHVHLNEPG--RTEWEGFPTG----TKAAAAGGITTLVD 136
|
....*..
gi 556409337 112 ATRNSSP 118
Cdd:PLN02795 137 MPLNSFP 143
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
35-378 |
3.81e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 48.85 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 35 LVVRGQTIAAVIPEAEIPSGHRqcVDLDGRLVTPGLIDCHTHLVFGGDR--AAEW--EQRLNGV------------SYqt 98
Cdd:PRK08204 26 ILIEGDRIAAVAPSIEAPDAEV--VDARGMIVMPGLVDTHRHTWQSVLRgiGADWtlQTYFREIhgnlgpmfrpedVY-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 99 ISAQGG---GINATVTAT-----RNSSPEMlltvAQQRLQRLMNEGvttIEIKSGYGLNAQAEEKMllvaRQLSLNNLVD 170
Cdd:PRK08204 102 IANLLGaleALDAGVTTLldwshINNSPEH----ADAAIRGLAEAG---IRAVFAHGSPGPSPYWP----FDSVPHPRED 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 171 ISptllaahAVPAEYRQDPDAYLTLVceqiMPTLwqkelfeavdvfceNVGFTPVQTERL-FRAAAALGIPVKGHVEQLS 249
Cdd:PRK08204 171 IR-------RVKKRYFSSDDGLLTLG----LAIR--------------GPEFSSWEVARAdFRLARELGLPISMHQGFGP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 250 NLGGAALVSQYKG---LSAD----HIEYLDDAGIQAMAQSGTVAVLLPgAFYFLQERQRPPVAQLREQGVPMAVATDYNP 322
Cdd:PRK08204 226 WGATPRGVEQLHDaglLGPDlnlvHGNDLSDDELKLLADSGGSFSVTP-EIEMMMGHGYPVTGRLLAHGVRPSLGVDVVT 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556409337 323 GTS--PFASLHLAM---------------NMACVQFGLTPEEAWAGVTRHAAQALGRGATHGQLKPGYVADFV 378
Cdd:PRK08204 305 STGgdMFTQMRFALqaerardnavhlregGMPPPRLTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLV 377
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
6-76 |
1.02e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 47.40 E-value: 1.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556409337 6 PDDVIWRNARLATLATGEPEPyglkeqHALVVRGQTIAAV---IPEAeipsghRQCVDLDGRLVTPGLIDCHTH 76
Cdd:COG1001 4 PADLVIKNGRLVNVFTGEILE------GDIAIAGGRIAGVgdyIGEA------TEVIDAAGRYLVPGFIDGHVH 65
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
33-72 |
2.04e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 46.51 E-value: 2.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 556409337 33 HALVVRGQTIAAVIPEAEIPSGHRQCvDLDGRLVTPGLID 72
Cdd:PRK11170 19 HAVVIADGLIEAVCPVAELPPGIEQR-DLNGAILSPGFID 57
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
9-106 |
2.10e-05 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 46.44 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 9 VIWRNARLATlatgepePYGLKEQHALVVRGqTIAAvIPEAEIPSGHRQCVDLDGRLVTPGLIDCHTHL--VFGGDRAAE 86
Cdd:cd01314 1 LIIKNGTIVT-------ADGSFKADILIEDG-KIVA-IGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLelPFMGTVTAD 71
|
90 100
....*....|....*....|.
gi 556409337 87 -WEQrlngvsyQTISAQGGGI 106
Cdd:cd01314 72 dFES-------GTRAAAAGGT 85
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-381 |
2.47e-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: 45.78 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 34 ALVVRGQTIAAVipEAEI-PSGHRQCVDLDGRLVTPGLIDCHTHlVF-----GGDRAAEWEQRlNGVSyqTISAQGGGIN 107
Cdd:cd01307 1 DVAIENGKIAAV--GAALaAPAATQIVDAGGCYVSPGWIDLHVH-VYqggtrYGDRPDMIGVK-SGVT--TVVDAGSAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 108 ATVTATRNSSPEMlltvAQQRLQRLMNEGVTtieiksgyGLNAQAEekmllvarqlslnnLVDisPTLLAAHAVPAEYRQ 187
Cdd:cd01307 75 DNIDGFRYTVIER----SATRVYAFLNISRV--------GLVAQDE--------------LPD--PDNIDEDAVVAAARE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 188 DPDAYLTLvceqimptlwqkELFEAVDVFCENvGFTPVqtERLFRAAAALGIPVKGHVEQLSnlggaalvsqykGLSADH 267
Cdd:cd01307 127 YPDVIVGL------------KARASKSVVGEW-GIKPL--ELAKKIAKEADLPLMVHIGSPP------------PILDEV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 268 IEYLDDAGIQAMAQSGTvavllPGAFYFLQERQRPPVAQLREQGVPMAVATdynpGTSPF-------------------A 328
Cdd:cd01307 180 VPLLRRGDVLTHCFNGK-----PNGIVDEEGEVLPLVRRARERGVIFDVGH----GTASFsfrvaraaiaagllpdtisS 250
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556409337 329 SLHLAMNMACVQFGLTP------------EEAWAGVTRHAAQALGRgATHGQLKPGYVADFVVWE 381
Cdd:cd01307 251 DIHGRNRTNGPVYALATtlskllalgmplEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFD 314
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
8-118 |
3.27e-05 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 45.85 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 8 DVIWRNARLATlatgepePYGLKEQHALVVRGQtIAAVIPEAEIPSghRQCVDLDGRLVTPGLIDCHTHlvFGGDRAAEW 87
Cdd:PRK06189 4 DLIIRGGKVVT-------PEGVYRADIGIKNGK-IAEIAPEISSPA--REIIDADGLYVFPGMIDVHVH--FNEPGRTHW 71
|
90 100 110
....*....|....*....|....*....|.
gi 556409337 88 EqrlnGVSYQTISAQGGGINATVTATRNSSP 118
Cdd:PRK06189 72 E----GFATGSAALAAGGCTTYFDMPLNSIP 98
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
12-77 |
3.88e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 45.57 E-value: 3.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556409337 12 RNARLAtlatgepEPYGLKEQHALVVRGQTIAAVIPEAEIPSGHRqcVDLDGRLVTPGLIDCHTHL 77
Cdd:PRK09357 6 KNGRVI-------DPKGLDEVADVLIDDGKIAAIGENIEAEGAEV--IDATGLVVAPGLVDLHVHL 62
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
267-385 |
5.26e-05 |
|
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: 45.14 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 267 HIEYLDDAGIQAMAQSGTVAVLLPGAFYFLQErQRPPVAQLREQGVPMAVATDYNPGTSPFASL----------HLAMNM 336
Cdd:cd01313 262 HATHLTDNETLLLGRSGAVVGLCPTTEANLGD-GIFPAAALLAAGGRIGIGSDSNARIDLLEELrqleysqrlrDRARNV 340
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 556409337 337 ACVQFGLTPEEAWAGVTRHAAQALGRGAthGQLKPGYVADFVVWEANHP 385
Cdd:cd01313 341 LATAGGSSARALLDAALAGGAQALGLAT--GALEAGARADLLSLDLDHP 387
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
60-390 |
5.59e-05 |
|
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: 44.91 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 60 DLDGRLVTPGLIDCHTHLvfggdraaewEQRLNgvsyqtisaqggginatvtatrnsSPEMLLTVAQQRlqrlmneGVTT 139
Cdd:cd01295 1 DAEGKYIVPGFIDAHLHI----------ESSML------------------------TPSEFAKAVLPH-------GTTT 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 140 I-----EIKSGYGLnaQAEEKMLLVARQLSLNNLVDISPTllaahaVPAEYRQDPDAYLTLvcEQImptlwqKELFEAVD 214
Cdd:cd01295 40 ViadphEIANVAGV--DGIEFMLEDAKKTPLDIFWMLPSC------VPATPFETSGAELTA--EDI------KELLEHPE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 215 VFC--ENVGFTPVQT--ERLF---RAAAALGIPVKGHVEQLSNLGGAALVsqYKGLSADH----IEYLDD---AGIQAMA 280
Cdd:cd01295 104 VVGlgEVMDFPGVIEgdDEMLakiQAAKKAGKPVDGHAPGLSGEELNAYM--AAGISTDHeamtGEEALEklrLGMYVML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 281 QSGTVA----VLLPGAFYFLQERqrppvaqlreqgvpMAVATDynpGTSPFASLHLAMNMACV----QFGLTPEEAWAGV 352
Cdd:cd01295 182 REGSIAknleALLPAITEKNFRR--------------FMFCTD---DVHPDDLLSEGHLDYIVrraiEAGIPPEDAIQMA 244
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 556409337 353 TRHAAQALGRGaTHGQLKPGYVADFVVWE--ANHPVEMVY 390
Cdd:cd01295 245 TINPAECYGLH-DLGAIAPGRIADIVILDdlENFNITTVL 283
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
8-81 |
6.04e-05 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 44.75 E-value: 6.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556409337 8 DVIWRNARLATLATGEpepyglKEQHALVVRGQTIAaviPEAEIPS-GHRQCVDLDGRLVTPGLIDCHTHLVFGG 81
Cdd:PRK12394 4 DILITNGHIIDPARNI------NEINNLRIINDIIV---DADKYPVaSETRIIHADGCIVTPGLIDYHAHVFYDG 69
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
37-97 |
9.73e-05 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 44.39 E-value: 9.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556409337 37 VRGQTIAAVipeAEIPSGH-RQCVDLDGRLVTPGLIDCHTHlvfgGDRAAEWEQRLNGVSYQ 97
Cdd:COG3653 26 IKGGRIVAV---GDLAAAEaARVIDATGLVVAPGFIDIHTH----YDLQLLWDPRLEPSLRQ 80
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
34-75 |
5.69e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 41.70 E-value: 5.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556409337 34 ALVVRGQTIAAVIPEaeiPSGHRQCVDLDGRLVTPGLIDCHT 75
Cdd:PRK15446 21 SLLIEDGRIAAIDPG---ASALPGAIDAEGDYLLPGLVDLHT 59
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
35-91 |
9.37e-04 |
|
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: 41.13 E-value: 9.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 556409337 35 LVVRGQTIAAVIPEAEIPSghRQCVDLDGRLVTPGLIDCHTHlvfgGDRAAEWEQRL 91
Cdd:cd01297 22 VGIRDGRIAAIGPILSTSA--REVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL 72
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
59-385 |
1.30e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 40.80 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 59 VDLDGRLVTPGLIDCHT-----HLVFGGDRAAEWEQ-RLNGVSYqtisaqggginatVTATRNS--SPEMLLTVAQQRLQ 130
Cdd:PRK06151 48 IDAGNALVGPGFIDLDAlsdldTTILGLDNGPGWAKgRVWSRDY-------------VEAGRREmyTPEELAFQKRYAFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 131 RLMNEGVTT-IEIKSGYgLNAQAE-----EKMLLVARQLSLNnlVDISPTLLAAHAVpaeyrQDPDAYLTLVCEqimPTL 204
Cdd:PRK06151 115 QLLRNGITTaMPIASLF-YRQWAEtyaefAAAAEAAGRLGLR--VYLGPAYRSGGSV-----LEADGSLEVVFD---EAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 205 WQKELFEAVDvFCENV------------------GFTPVQTERLFRAAAALGIPVKGHVEQlsNLGGAALVSQYKGLSAd 266
Cdd:PRK06151 184 GLAGLEEAIA-FIKRVdgahnglvrgmlapdrieTCTVDLLRRTAAAARELGCPVRLHCAQ--GVLEVETVRRLHGTTP- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 267 hIEYLDDAG---------------------------IQAMAQSGTVAVLLPGAFyFLQERQRPPVAQLREQGVPMAVATD 319
Cdd:PRK06151 260 -LEWLADVGllgprlliphatyisgsprlnysggddLALLAEHGVSIVHCPLVS-ARHGSALNSFDRYREAGINLALGTD 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556409337 320 ynpgTSP---FASLHLAMNMACVQFGLTPEEAWAGVTRHA----AQALGRGAThGQLKPGYVADFVVWEANHP 385
Cdd:PRK06151 338 ----TFPpdmVMNMRVGLILGRVVEGDLDAASAADLFDAAtlggARALGRDDL-GRLAPGAKADIVVFDLDGL 405
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
37-86 |
2.34e-03 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 39.77 E-value: 2.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 556409337 37 VRGQTIAAVIP--EAEIpsghrqcVDLDGRLVTPGLIDCHTHLV--FGGDRAAE 86
Cdd:PRK08323 23 IEDGKIAAIGAnlGDEV-------IDATGKYVMPGGIDPHTHMEmpFGGTVSSD 69
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
34-78 |
3.28e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 39.60 E-value: 3.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 556409337 34 ALVVRGQTIAAVIPEAEIPsGHRQCVDLDGRLVTPGLIDCHTHLV 78
Cdd:PRK07228 23 DVLIEDDRIAAVGDRLDLE-DYDDHIDATGKVVIPGLIQGHIHLC 66
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
31-77 |
3.77e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 39.44 E-value: 3.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 556409337 31 EQHALV-VRGQTIAAVIPEAEIPSGHRqCVDLDGRLVTPGLIDCHTHL 77
Cdd:PLN02942 20 QELADVyVEDGIIVAVAPNLKVPDDVR-VIDATGKFVMPGGIDPHTHL 66
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
8-77 |
3.98e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 39.23 E-value: 3.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 8 DVIWRNARLatlatgepePYGlKEQHALVVRGQTIAAVipEAEIPSGHRQCVDLDGRLVTPGLIDCHTHL 77
Cdd:PRK07572 3 DLIVRNANL---------PDG-RTGIDIGIAGGRIAAV--EPGLQAEAAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
8-77 |
7.36e-03 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 38.53 E-value: 7.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556409337 8 DVIWRNARLATlATGepepyglKEQHALVVRGQTIAAVipEAEIPSGHRQcVDLDGRLVTPGLIDCHTHL 77
Cdd:PRK13404 5 DLVIRGGTVVT-ATD-------TFQADIGIRGGRIAAL--GEGLGPGARE-IDATGRLVLPGGVDSHCHI 63
|
|
| |
