|
Name |
Accession |
Description |
Interval |
E-value |
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
48-393 |
4.38e-153 |
|
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: 436.34 E-value: 4.38e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 48 QVVDAEGGTILPGMIDTHVHMMMEFSPVAERLETPFSFMYYQAAKYLETTLKAGITSVRDALGTDLG-VKKAVEEGLISG 126
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEYRTIRATRQARAALRAGFTTVRDAGGADYGlLRDAIDAGLIPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 127 PRLQLSINALTITGGHGDGYTVSGRevdllpsDYPGMPSGKCDGVEEVRKKTREMLRAGAEIIKVHATGGVLSATDHPEF 206
Cdd:cd01299 82 PRVFASGRALSQTGGHGDPRGLSGL-------FPAGGLAAVVDGVEEVRAAVREQLRRGADQIKIMATGGVLSPGDPPPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 207 TQFSQEELETIVEEGRFRkGVKVMAHAQGAEGIKNAVRAGVHSIEHGIFLDDEAIDLMIEKGTFLVPTLLAPVAVLETAK 286
Cdd:cd01299 155 TQFSEEELRAIVDEAHKA-GLYVAAHAYGAEAIRRAIRAGVDTIEHGFLIDDETIELMKEKGIFLVPTLATYEALAAEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 287 ETGMPDTAVQKSKEVIEIHKASIAKAHKAGVKIAMGTDAG--VMKHGTNLRELGLMTEAGMTAMEAIVASTKTAAECLGW 364
Cdd:cd01299 234 APGLPADSAEKVALVLEAGRDALRRAHKAGVKIAFGTDAGfpVPPHGWNARELELLVKAGGTPAEALRAATANAAELLGL 313
|
330 340
....*....|....*....|....*....
gi 227296032 365 QDRVGTIEEGKLADIIIVNGNPLDDINLL 393
Cdd:cd01299 314 SDELGVIEAGKLADLLVVDGDPLEDIAVL 342
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-408 |
5.37e-118 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 348.49 E-value: 5.37e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 1 MTTLLIKNGLFIDGNGGEPQKDAVIVVKDNQIAYVGPETAYSSSGEEQVVDAEGGTILPGMIDTHVHMMMEFSPVAERLE 80
Cdd:COG1228 7 AGTLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 81 ----TPFSFMYYQAAKYLETTLKAGITSVRDALGTDLGVKKAVEEG---LISGPRLQLSINALTITGGHGDGytvsgrev 153
Cdd:COG1228 87 gggiTPTVDLVNPADKRLRRALAAGVTTVRDLPGGPLGLRDAIIAGeskLLPGPRVLAAGPALSLTGGAHAR-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 154 dllpsdypgmpsgkcdGVEEVRKKTREMLRAGAEIIKVHATGGVlsatdhpefTQFSQEELETIVEEGRfRKGVKVMAHA 233
Cdd:COG1228 159 ----------------GPEEARAALRELLAEGADYIKVFAEGGA---------PDFSLEELRAILEAAH-ALGLPVAAHA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 234 QGAEGIKNAVRAGVHSIEHGIFLDDEAIDLMIEKG-TFLVPTLLAPVAVLEtaketGMPDTAVQKSKEVIEIHKASIAKA 312
Cdd:COG1228 213 HQADDIRLAVEAGVDSIEHGTYLDDEVADLLAEAGtVVLVPTLSLFLALLE-----GAAAPVAAKARKVREAALANARRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 313 HKAGVKIAMGTDAGV-MKHGTNL-RELGLMTEAGMTAMEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIVNGNPLDDI 390
Cdd:COG1228 288 HDAGVPVALGTDAGVgVPPGRSLhRELALAVEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDI 367
|
410
....*....|....*...
gi 227296032 391 nllANNENITTVIKDGKI 408
Cdd:COG1228 368 ---AYLEDVRAVMKDGRV 382
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
56-408 |
5.59e-54 |
|
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: 182.32 E-value: 5.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 56 TILPGMIDTHVHMMMefsPVAERLETPFSFMYYQAAKYLETTLKAGITSVRDALGT----DLGVKKAVEEgLISGPRLQL 131
Cdd:pfam01979 1 IVLPGLIDAHVHLEM---GLLRGIPVPPEFAYEALRLGITTMLKSGTTTVLDMGATtstgIEALLEAAEE-LPLGLRFLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 132 sinaltitgghgdgytvsgrevdllpsdypGMPSGKCDGVEEVRKKTREMLRAGAEIIKVHATGGVLSATDHPEFTQFSQ 211
Cdd:pfam01979 77 ------------------------------PGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 212 EELETIVEEGRfRKGVKVMAHAQGAEG-IKNAVRAGVHSIEHGIFLDD-------EAIDLMIEKGTFLVPTLLAPVAvlE 283
Cdd:pfam01979 127 DELKAALEEAK-KYGLPVAIHALETKGeVEDAIAAFGGGIEHGTHLEVaesggllDIIKLILAHGVHLSPTEANLLA--E 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 284 TAKETGMPDTAvqKSKEVIEIHKASIAKAHKAGVKIAMGTDAGVMKH-------GTNLRELGLMTEAGMTAMEAIVASTK 356
Cdd:pfam01979 204 HLKGAGVAHCP--FSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNslnmleeLRLALELQFDPEGGLSPLEALRMATI 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 227296032 357 TAAECLGWQDRVGTIEEGKLADIIIVNGNPLDDINLLANNENITTVIKDGKI 408
Cdd:pfam01979 282 NPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-408 |
1.50e-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: 121.47 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 3 TLLIKNGLFIDGNG-GEPQKDAVIVVKDNQIAYVGP-ETAYSSSGEEQVVDAEGGTILPGMIDTHVHM-MMEFSPVAE-- 77
Cdd:COG0402 1 DLLIRGAWVLTMDPaGGVLEDGAVLVEDGRIAAVGPgAELPARYPAAEVIDAGGKLVLPGLVNTHTHLpQTLLRGLADdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 78 -----------RLETPFS--FMYYQAAKYLETTLKAGITSVRD----ALGTDLGVKKAVEEgliSGPRLQLsinaltitg 140
Cdd:COG0402 81 plldwleeyiwPLEARLDpeDVYAGALLALAEMLRSGTTTVADfyyvHPESADALAEAAAE---AGIRAVL--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 141 ghgdGYTVSGRevdllpsdypGMPSGKCDGVEEVRKKTREMLR----AGAEIIKVHATG-GVLSATDhpeftqfsqEELE 215
Cdd:COG0402 149 ----GRGLMDR----------GFPDGLREDADEGLADSERLIErwhgAADGRIRVALAPhAPYTVSP---------ELLR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 216 TIVEEGRfRKGVKVMAH-AQGAEGIKNAVRA-GVHSIE---------------HGIFLDDEAIDLMIEKGTFLV--PT-- 274
Cdd:COG0402 206 AAAALAR-ELGLPLHTHlAETRDEVEWVLELyGKRPVEyldelgllgprtllaHCVHLTDEEIALLAETGASVAhcPTsn 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 275 -LLApvavletakeTGMPDtavqkskevieihkasIAKAHKAGVKIAMGTDAG----------VMKHGTNLRELGLMTEA 343
Cdd:COG0402 285 lKLG----------SGIAP----------------VPRLLAAGVRVGLGTDGAasnnsldmfeEMRLAALLQRLRGGDPT 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227296032 344 GMTAMEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIVN---------GNPLDDINLLANNENITTVIKDGKI 408
Cdd:COG0402 339 ALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDldaphlaplHDPLSALVYAADGRDVRTVWVAGRV 412
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
4-408 |
3.05e-25 |
|
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: 106.13 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 4 LLIKNGLFIDGNGGEPQKDAVIVVKDNQIAYVGPETAYSSSGEEQVVDAEGGTILPGMIDTHVHMMMEFS---------- 73
Cdd:cd01298 1 ILIRNGTIVTTDPRRVLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 74 -------PVAERLETPFSFmyYQAAK--YLEtTLKAGITSVRDALGTDL-GVKKAVEEgliSGPRLQLsinaltitgghg 143
Cdd:cd01298 81 ewlkdliWPLERLLTEEDV--YLGALlaLAE-MIRSGTTTFADMYFFYPdAVAEAAEE---LGIRAVL------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 144 dGYTVsgreVDLLPSDYPGMPSGKCDGVEEVRK---KTREMLRAgaeIIKVHATGGVlsatdhpeftqfSQEELETIVEE 220
Cdd:cd01298 143 -GRGI----MDLGTEDVEETEEALAEAERLIREwhgAADGRIRV---ALAPHAPYTC------------SDELLREVAEL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 221 GRfRKGVKVMAH-AQGAEGIKNAVRA-GVHSIE---------------HGIFLDDEAIDLMIEKGTFLVPtllAPVAVLE 283
Cdd:cd01298 203 AR-EYGVPLHIHlAETEDEVEESLEKyGKRPVEyleelgllgpdvvlaHCVWLTDEEIELLAETGTGVAH---NPASNMK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 284 TAKETgmpdtavqkskevieihkASIAKAHKAGVKIAMGTD----------AGVMKHGTNLRELGLMTEAGMTAMEAIVA 353
Cdd:cd01298 279 LASGI------------------APVPEMLEAGVNVGLGTDgaasnnnldmFEEMRLAALLQKLAHGDPTALPAEEALEM 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227296032 354 STKTAAECLGWqDRVGTIEEGKLADIIIVNGN-----PLDDINLL----ANNENITTVIKDGKI 408
Cdd:cd01298 341 ATIGGAKALGL-DEIGSLEVGKKADLILIDLDgphllPVHDPISHlvysANGGDVDTVIVNGRV 403
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
25-406 |
1.62e-22 |
|
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: 98.10 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 25 IVVKDNQIAYVGPETAYSSSGEE--QVVDAEGGTILPGMIDTHVHMMMEFSPVAErletpFSfMYYQAAKYLETtLKAG- 101
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPAaaEEIDAGGRAVTPGLVDCHTHLVFAGDRVDE-----FA-ARLAGASYEEI-LAAGg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 102 --ITSVRDalgtdlgVKKAVEEGLISG--PRLQ--LSINALTITGGHGDGYTVSG--------------REVDLLPSdYP 161
Cdd:cd01296 74 giLSTVRA-------TRAASEDELFASalRRLArmLRHGTTTVEVKSGYGLDLETelkmlrvirrlkeeGPVDLVST-FL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 162 GM---PSGKCDGVEEVRKKTREML-----RAGAEIIKVHATGGVlsatdhpeftqFSQEELETIVEEGRFRkGVKVMAHA 233
Cdd:cd01296 146 GAhavPPEYKGREEYIDLVIEEVLpavaeENLADFCDVFCEKGA-----------FSLEQSRRILEAAKEA-GLPVKIHA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 234 Q---GAEGIKNAVRAGVHSIEHGIFLDDEAIDLMIEKGTflVPTLLaPVAVLETaketgmpdtavqkskevieihKASIA 310
Cdd:cd01296 214 DelsNIGGAELAAELGALSADHLEHTSDEGIAALAEAGT--VAVLL-PGTAFSL---------------------RETYP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 311 KAHK---AGVKIAMGTDAGVMKHGTNlrELGLM-----TEAGMTAMEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIV 382
Cdd:cd01296 270 PARKlidAGVPVALGTDFNPGSSPTS--SMPLVmhlacRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVIL 347
|
410 420
....*....|....*....|....
gi 227296032 383 NGNPLDDINLLANNENITTVIKDG 406
Cdd:cd01296 348 DAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
1-408 |
1.63e-22 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 99.49 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 1 MTTLLIKNGLFIDGNGGEPQKDAViVVKDNQIAYVGPETAYSS--SGEEQVVDAEGGTILPGMIDTHVHMMM-------- 70
Cdd:COG1574 7 AADLLLTNGRIYTMDPAQPVAEAV-AVRDGRIVAVGSDAEVRAlaGPATEVIDLGGKTVLPGFIDAHVHLLGgglallgv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 71 EFSPVA------ERLETpfsfmyYQAAK----------YLETTLK----------------------------------- 99
Cdd:COG1574 86 DLSGARsldellARLRA------AAAELppgewilgrgWDESLWPegrfptradldavspdrpvvltrvdghaawvnsaa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 100 ---AGITS----------VRDALGTDLGVkkaVEEG-------LISGPRLQLSINALT----------ITGGHGDGytVS 149
Cdd:COG1574 160 lelAGITAdtpdpeggeiERDADGEPTGV---LREAamdlvraAIPPPTPEELRAALRaalrelaslgITSVHDAG--LG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 150 GREVDL---------LPSDYPGMPSGKCDGVEEVRKKTR------EMLRAGAeiIKVHATGGVLSAT--------DHPEF 206
Cdd:COG1574 235 PDDLAAyrelaaageLPLRVVLYLGADDEDLEELLALGLrtgygdDRLRVGG--VKLFADGSLGSRTaallepyaDDPGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 207 T---QFSQEELETIVEEGRfRKGVKVMAHAQGAEGIKNAVRA--------GV----HSIEHGIFLDDEAIDLMIEkgtfl 271
Cdd:COG1574 313 RgllLLDPEELRELVRAAD-AAGLQVAVHAIGDAAVDEVLDAyeaaraanGRrdrrHRIEHAQLVDPDDLARFAE----- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 272 vptlLAPVAVLETAKETGMPDTAvqksKEVIEIHKAS----IAKAHKAGVKIAMGTDAGV--------MKHGTNLREL-- 337
Cdd:COG1574 387 ----LGVIASMQPTHATSDGDWA----EDRLGPERAAraypFRSLLDAGAPLAFGSDAPVepldpllgIYAAVTRRTPsg 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227296032 338 -GLMTEAGMTAMEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIVNGNPLD-DINLLANNENITTVIkDGKI 408
Cdd:COG1574 459 rGLGPEERLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTvPPEEIKDIKVLLTVV-GGRV 530
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
25-381 |
1.10e-15 |
|
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: 78.50 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 25 IVVKDNQIAYVGPETAYS--SSGEEQVVDAEGGTILPGMIDTHVHMMM--------EFSPV-----------AERLETP- 82
Cdd:cd01300 2 VAVRDGRIVAVGSDAEAKalKGPATEVIDLKGKTVLPGFIDSHSHLLLgglsllwlDLSGVtskeealarirEDAAAAPp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 83 ------FSFMYYQAAKYLETTLK------------------------------AGITS----------VRDALGTDLGV- 115
Cdd:cd01300 82 gewilgFGWDESLLGEGRYPTRAeldavspdrpvlllrrdghsawvnsaalrlAGITRdtpdppggeiVRDADGEPTGVl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 116 -------------KKAVEEGLISGPRLQLSINALTITGGH------GDGYTV----SGREVDLLPSDYPGMPSGKCDG-- 170
Cdd:cd01300 162 veaaaalvleavpPPTPEERRAALRAAARELASLGVTTVHdagggaADDIEAyrrlAAAGELTLRVRVALYVSPLAEDll 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 171 VEEVRKKTRE---MLRAGAeiIKVHATG--GVLSA---------TDHPEFTQFSQEELETIVEEGrFRKGVKVMAHAQGA 236
Cdd:cd01300 242 EELGARKNGAgddRLRLGG--VKLFADGslGSRTAalsepyldsPGTGGLLLISPEELEELVRAA-DEAGLQVAIHAIGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 237 EGIKNAVRA------------GVHSIEHGIFLDDEAIDLMIEKGTFLV--PTLLAPVAVLETAKETGMpdtavQKSKEVi 302
Cdd:cd01300 319 RAVDTVLDAleaalkdnpradHRHRIEHAQLVSPDDIPRFAKLGVIASvqPNHLYSDGDAAEDRRLGE-----ERAKRS- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 303 eihkASIAKAHKAGVKIAMGTDAGV--------MKHGTNLRELGLMTEAG----MTAMEAIVASTKTAAECLGWQDRVGT 370
Cdd:cd01300 393 ----YPFRSLLDAGVPVALGSDAPVappdpllgIWAAVTRKTPGGGVLGNpeerLSLEEALRAYTIGAAYAIGEEDEKGS 468
|
490
....*....|.
gi 227296032 371 IEEGKLADIII 381
Cdd:cd01300 469 LEPGKLADFVV 479
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
1-408 |
5.71e-15 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 76.33 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 1 MTTLLIKNGLFIDGNGGEPQKdAVIVVKDNQIAYVGPETAYSSSgeeQVVDAEGGTILPGMIDTHVHMMMEF-------S 73
Cdd:PRK06038 1 MADIIIKNAYVLTMDAGDLKK-GSVVIEDGTITEVSESTPGDAD---TVIDAKGSVVMPGLVNTHTHAAMTLfrgyaddL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 74 PVAERLEtpfSFMYYQAAK------YLETTL------KAGITSVRDALGTDLGVKKAVEEgliSGPRLQLSinaltitgg 141
Cdd:PRK06038 77 PLAEWLN---DHIWPAEAKltaedvYAGSLLaclemiKSGTTSFADMYFYMDEVAKAVEE---SGLRAALS--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 142 HGdgytvsgrEVDLlpsdypgmpsgkcdGVEEvrkKTREMLRAGAEIIKV--HATGGVLSATDHPEFTQFSQEELETIVE 219
Cdd:PRK06038 142 YG--------MIDL--------------GDDE---KGEAELKEGKRFVKEwhGAADGRIKVMYGPHAPYTCSEEFLSKVK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 220 EGRFRKGVKVMAHAQGAEGIKNAV--RAGVHSIE---------------HGIFLDDEAIDLMIEKGtflVPTLLAPVAVL 282
Cdd:PRK06038 197 KLANKDGVGIHIHVLETEAELNQMkeQYGMCSVNylddigflgpdvlaaHCVWLSDGDIEILRERG---VNVSHNPVSNM 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 283 ETAKETgmpdtavqkskevieihkASIAKAHKAGVKIAMGTDA----------GVMKHGTNLRELGLMTEAGMTAMEAIV 352
Cdd:PRK06038 274 KLASGI------------------APVPKLLERGVNVSLGTDGcasnnnldmfEEMKTAALLHKVNTMDPTALPARQVLE 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227296032 353 ASTKTAAECLGWQdrVGTIEEGKLADIIIVNGN-----PLDDI--NLL--ANNENITTVIKDGKI 408
Cdd:PRK06038 336 MATVNGAKALGIN--TGMLKEGYLADIIIVDMNkphltPVRDVpsHLVysASGSDVDTTIVDGRI 398
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-410 |
2.83e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 71.19 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 1 MTTLLIKNGLFI--DGNGGEPQKdAVIVVKDNQIAYVGPETaysSSGEEQVVDAEGGTILPGMIDTHVH----------- 67
Cdd:PRK08204 1 MKRTLIRGGTVLtmDPAIGDLPR-GDILIEGDRIAAVAPSI---EAPDAEVVDARGMIVMPGLVDTHRHtwqsvlrgiga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 68 ---MMMEFSPVAERLETPFSFMYYQAAKYLET--TLKAGITSVRDALGTDLGVKKAVEeglisgprlqlSINALTITG-- 140
Cdd:PRK08204 77 dwtLQTYFREIHGNLGPMFRPEDVYIANLLGAleALDAGVTTLLDWSHINNSPEHADA-----------AIRGLAEAGir 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 141 ---GHGDgytvSGREVDLLPSDYPGMPsgkcDGVEEVRKktrEMLRAGAEIIkvhaTGGVlsATDHPEFTQfsqeeLETI 217
Cdd:PRK08204 146 avfAHGS----PGPSPYWPFDSVPHPR----EDIRRVKK---RYFSSDDGLL----TLGL--AIRGPEFSS-----WEVA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 218 VEEGRFRK--GVKVMAHAQG------AEGIKNAVRAGV----HSIEHGIFLDDEAIDLMIEKGTFLVPTllapvAVLETA 285
Cdd:PRK08204 204 RADFRLARelGLPISMHQGFgpwgatPRGVEQLHDAGLlgpdLNLVHGNDLSDDELKLLADSGGSFSVT-----PEIEMM 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 286 KETGMPDTAvqkskevieihkasiaKAHKAGVKIAMGTDA---------GVMKH---------GTNLRELGLMT--EAGM 345
Cdd:PRK08204 279 MGHGYPVTG----------------RLLAHGVRPSLGVDVvtstggdmfTQMRFalqaerardNAVHLREGGMPppRLTL 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227296032 346 TAMEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIVNGnplDDINLL------------ANNENITTVIKDGKIEK 410
Cdd:PRK08204 343 TARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDA---TDLNLApvhdpvgavvqsAHPGNVDSVMVAGRAVK 416
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
2-408 |
3.15e-13 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 70.80 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 2 TTLLIKNGLFIDGNGGEPQKDAVIVVKDNQIAYVGPETAysSSGEEQVVDAEGGTILPGMIDTHVHMMME-FSPVAERLE 80
Cdd:PRK07228 1 MTILIKNAGIVTMNAKREIVDGDVLIEDDRIAAVGDRLD--LEDYDDHIDATGKVVIPGLIQGHIHLCQTlFRGIADDLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 81 ----------------TPFSfMYYqAAK--YLEtTLKAGITSVRDALG---TDLGVKKAVEEGlisgprlqlsINALtit 139
Cdd:PRK07228 79 lldwlkdriwpleaahDAES-MYY-SALlgIGE-LIESGTTTIVDMESvhhTDSAFEAAGESG----------IRAV--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 140 gghgdgytvsgrevdllpsdypgmpSGKC--DGVEEV----RKKTREMLRAGAEII-KVH-ATGGVLSATDHPEFTQFSQ 211
Cdd:PRK07228 143 -------------------------LGKVmmDYGDDVpeglQEDTEASLAESVRLLeKWHgADNGRIRYAFTPRFAVSCT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 212 EELETIVEEGRFRKGVKVMAHAQGAEGIKNAVRA--GVHSIE---------------HGIFLDDEAIDLMIEKGTFLVPt 274
Cdd:PRK07228 198 EELLRGVRDLADEYGVRIHTHASENRGEIETVEEetGMRNIHyldevgltgedlilaHCVWLDEEEREILAETGTHVTH- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 275 llAPVAVLETAkeTGMpdtavqkskevieihkASIAKAHKAGVKIAMGTDA----GVMKHGTNLRELGLMTEAG------ 344
Cdd:PRK07228 277 --CPSSNLKLA--SGI----------------APVPDLLERGINVALGADGapcnNTLDPFTEMRQAALIQKVDrlgpta 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227296032 345 MTAMEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIVNGN-----PLDDINLL------ANNENITTVIKDGKI 408
Cdd:PRK07228 337 MPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDLDglhatPSHGVDVLshlvyaAHGSDVETTMVDGKI 411
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
29-388 |
2.90e-12 |
|
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: 67.34 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 29 DNQIAYVGPETAYSSSGeeQVVDAEGGTILPGMIDTHVHMMM-------EFSPVAERLE--TPF---SFMYYQAAKYLET 96
Cdd:cd01309 1 DGKIVAVGAEITTPADA--EVIDAKGKHVTPGLIDAHSHLGLdeeggvrETSDANEETDpvTPHvraIDGINPDDEAFKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 97 TLKAGITSVrdalgtdlgvkkAVEEGLisgprlqlsinALTItGGHGDGYTVSGREVDllpSDYPGMPSGKCDGVEEVRK 176
Cdd:cd01309 79 ARAGGVTTV------------QVLPGS-----------ANLI-GGQGVVIKTDGGTIE---DMFIKAPAGLKMALGENPK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 177 KT------------------REMLRAGAEIIKVHATGgvLSATDHPEFTQFsqeELETIVEegRFRKGVKVMAHAQGAEG 238
Cdd:cd01309 132 RVyggkgkepatrmgvaallRDAFIKAQEYGRKYDLG--KNAKKDPPERDL---KLEALLP--VLKGEIPVRIHAHRADD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 239 IKNAVRagvhsiehgiFLDDEAIDLMIEKGT---FLVPTLL---APVAVletaketGMPDTAVQKSKEVIEIHKASIAKA 312
Cdd:cd01309 205 ILTAIR----------IAKEFGIKITIEHGAegyKLADELAkhgIPVIY-------GPTLTLPKKVEEVNDAIDTNAYLL 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227296032 313 HKAGVKIAMGTD-AGVMKHGTNLrELGLMTEAGMTAMEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIVNGNPLD 388
Cdd:cd01309 268 KKGGVAFAISSDhPVLNIRNLNL-EAAKAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLE 343
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
4-394 |
5.16e-11 |
|
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: 63.75 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 4 LLIKNGLFIDGNGgepQKDAVIVVKDNQIAYVGPETAYSSsgEEQVVDAEGGTILPGMIDTHVH-----MMMEFSPvaER 78
Cdd:cd00854 1 LIIKNARILTPGG---LEDGAVLVEDGKIVAIGPEDELEE--ADEIIDLKGQYLVPGFIDIHIHggggaDFMDGTA--EA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 79 LETPFSFMY-YQAAKYLETTLKAGITSVRDALGTdlgVKKAVEEGLIS--------GPrlQLSINAltiTGGHGDGYtvs 149
Cdd:cd00854 74 LKTIAEALAkHGTTSFLPTTVTAPPEEIAKALAA---IAEAIAEGQGAeilgihleGP--FISPEK---KGAHPPEY--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 150 grevdLLPSDypgmpsgkcdgVEEVRKktreMLRAGAEIIKVhatggvlsATDHPEfTQFSQEELETIVEegrfrKGVKV 229
Cdd:cd00854 143 -----LRAPD-----------PEELKK----WLEAAGGLIKL--------VTLAPE-LDGALELIRYLVE-----RGIIV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 230 MA-HAQG-AEGIKNAVRAGVHSIEH--------------------------------GIFLDDEAIDLMIE----KGTFL 271
Cdd:cd00854 189 SIgHSDAtYEQAVAAFEAGATHVTHlfnamsplhhrepgvvgaalsdddvyaeliadGIHVHPAAVRLAYRakgaDKIVL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 272 VPTLLAPvavletakeTGMPDTAVQKSKEVIEIhkasiakaHKAGVKIAMGTDAGV---MKHGT-NLRELGLMTEAgmta 347
Cdd:cd00854 269 VTDAMAA---------AGLPDGEYELGGQTVTV--------KDGVARLADGTLAGStltMDQAVrNMVKWGGCPLE---- 327
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 227296032 348 mEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIVNgnplDDINLLA 394
Cdd:cd00854 328 -EAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD----DDLNVKA 369
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
21-382 |
9.98e-11 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 63.10 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 21 KDAVIVVKDNQIAYVGPETAYSSSGEEQVVDAEGGTILPGMIDTHVHMMMEF-------SPVAERLETpfsfmYYQAAky 93
Cdd:PRK06687 20 LDGILAVKDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGlrgirddSNLHEWLND-----YIWPA-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 94 lETTLKAGITSVrdalgtdlGVKKAVEEGLISGprlqlsinaltiTGGHGDGYTVSGREVDLLPSDY----------PGM 163
Cdd:PRK06687 93 -ESEFTPDMTTN--------AVKEALTEMLQSG------------TTTFNDMYNPNGVDIQQIYQVVktskmrcyfsPTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 164 PSGKCDGVEEVRKKTREMLRagaEIIKVHATGGVLSATDHPEFTqFSQEELETIVEEGRfrkGVKVMAHAQGAEgIKNav 243
Cdd:PRK06687 152 FSSETETTAETISRTRSIID---EILKYKNPNFKVMVAPHSPYS-CSRDLLEASLEMAK---ELNIPLHVHVAE-TKE-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 244 ragvhsiEHGIFLD---DEAIDLMIEKGTFLVPTLLAPVAVLETAKETGMPDTAVQKSKEVIEIHK-----ASIAKAHKA 315
Cdd:PRK06687 222 -------ESGIILKrygKRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKlasgiAPIIQLQKA 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227296032 316 GVKIAMGTDAGVMKHGTNLRELGlMTEAGMTAM-----------EAIVASTKTAAECLGWQDRVGTIEEGKLADIIIV 382
Cdd:PRK06687 295 GVAVGIATDSVASNNNLDMFEEG-RTAALLQKMksgdasqfpieTALKVLTIEGAKALGMENQIGSLEVGKQADFLVI 371
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-67 |
1.15e-09 |
|
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: 59.62 E-value: 1.15e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227296032 4 LLIKNGLFIDGNGGEPQKdAVIVVKDNQIAYVGPETaySSSGEEqVVDAEGGTILPGMIDTHVH 67
Cdd:cd01297 2 LVIRNGTVVDGTGAPPFT-ADVGIRDGRIAAIGPIL--STSARE-VIDAAGLVVAPGFIDVHTH 61
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
48-408 |
1.29e-09 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 59.85 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 48 QVVDAEGGTILPGMIDTHVHM----------------------------------------------------MMEFSPV 75
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLdggglnlrelrlpdvlpnavvkgqagrtpkgrwlvgegwdeaqfaetrfpyaLADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 76 AERLETPFSFMYYQAAkYLETTL--KAGITS----------VRDALGTDL----------GVKKAVEEGLISGPRLQLS- 132
Cdd:pfam07969 81 APDGPVLLRALHTHAA-VANSAAldLAGITKatedppggeiARDANGEGLtgllregayaLPPLLAREAEAAAVAAALAa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 133 INALTITGGHGDGYTVSGREvdllpsDYPGM----PSGKCDGVEEVRKKTREML---RAGAEIIKVHA--TGGVLSATDH 203
Cdd:pfam07969 160 LPGFGITSVDGGGGNVHSLD------DYEPLreltAAEKLKELLDAPERLGLPHsiyELRIGAMKLFAdgVLGSRTAALT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 204 PEF--------TQFSQEELETIVEEGRfRKGVKVMAHAQGAEGIKNAVRA-----------GVHSIEHGiflddEAIDLM 264
Cdd:pfam07969 234 EPYfdapgtgwPDFEDEALAELVAAAR-ERGLDVAIHAIGDATIDTALDAfeavaeklgnqGRVRIEHA-----QGVVPY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 265 IEKgtflvptLLAPVAVLETAK--ETGMPDTAVQKSKEVIEIHKAS----IAKAHKAGVKIAMGTDAGV--------MKH 330
Cdd:pfam07969 308 TYS-------QIERVAALGGAAgvQPVFDPLWGDWLQDRLGAERARgltpVKELLNAGVKVALGSDAPVgpfdpwprIGA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 331 GTNLRELGLMTEAGM----TAMEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIVNGNPL--DDINLLanNENITTVIK 404
Cdd:pfam07969 381 AVMRQTAGGGEVLGPdeelSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLtvDPPAIA--DIRVRLTVV 458
|
....
gi 227296032 405 DGKI 408
Cdd:pfam07969 459 DGRV 462
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
5-104 |
1.31e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 59.34 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 5 LIKNGLFIDGNGgePQKDAVIVVKDNQIAYVGPEtaysSSGEEQVVDAEGGTILPGMIDTHVH-----MMMEFSPvaERL 79
Cdd:COG1820 1 AITNARIFTGDG--VLEDGALLIEDGRIAAIGPG----AEPDAEVIDLGGGYLAPGFIDLHVHggggvDFMDGTP--EAL 72
|
90 100
....*....|....*....|....*
gi 227296032 80 ETpfsfmyyqAAKYLettLKAGITS 104
Cdd:COG1820 73 RT--------IARAH---ARHGTTS 86
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-408 |
2.09e-09 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 59.34 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 4 LLIKNGLFIDGNGGEPQKDAvIVVKDNQIAYVGPetaYSSSGEEqVVDAEGGTILPGMIDTHVHM---MMefspvaerle 80
Cdd:COG1001 7 LVIKNGRLVNVFTGEILEGD-IAIAGGRIAGVGD---YIGEATE-VIDAAGRYLVPGFIDGHVHIessMV---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 81 TPFSFmyyqaAKyleTTLKAGITSV-------RDALGTDlGVKKAVEEGLisgpRLQLSINAltitgghgdgytvsgrev 153
Cdd:COG1001 72 TPAEF-----AR---AVLPHGTTTViadpheiANVLGLE-GVRYMLEAAE----GLPLDIFV------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 154 dLLPSDYPGMP----SGKCDGVEEVrkktREMLRAGaeiiKVHATG------GVLSATdhpeftqfsqEELETIVEEGRf 223
Cdd:COG1001 121 -MLPSCVPATPgletAGAVLGAEDL----AELLDHP----RVIGLGevmnfpGVLNGD----------PRMLAKIAAAL- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 224 RKGVKVMAHAQGAEGIK-NA-VRAGVHSiEHGIFLDDEAID-------LMIEKGTF--LVPTLLApvAVLETAKETGM-- 290
Cdd:COG1001 181 AAGKVIDGHAPGLSGKDlNAyAAAGIRS-DHECTTAEEALEklrrgmyVMIREGSAakDLPALLP--AVTELNSRRCAlc 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 291 -----PDTAVQKskevieihkasiakahkagvkiamgtdaGVMKHgtNLRELglmTEAGMTAMEAIVASTKTAAECLGwQ 365
Cdd:COG1001 258 tddrhPDDLLEE----------------------------GHIDH--VVRRA---IELGLDPVTAIQMATLNAAEHFG-L 303
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 227296032 366 DRVGTIEEGKLADIIIvngnpLDDINLLanneNITTVIKDGKI 408
Cdd:COG1001 304 KDLGAIAPGRRADIVL-----LDDLEDF----KVEKVYADGKL 337
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
20-383 |
2.88e-09 |
|
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: 58.44 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 20 QKDAVIVVKDNQIAYVGPETAYSSSGEEQ--VVDAEGGTILPGMIDTHVH-----MMMEF--SPVAERLET---P----F 83
Cdd:cd01303 24 VEDGLIVVVDGNIIAAGAAETLKRAAKPGarVIDSPNQFILPGFIDTHIHapqyaNIGSGlgEPLLDWLETytfPeeakF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 84 SFMYYQ---AAKYLETTLKAGITSVRdALGT-DLGVKKA-VEEGLISGPRlqlsinALTitgghgdGYTVSGRevdLLPs 158
Cdd:cd01303 104 ADPAYArevYGRFLDELLRNGTTTAC-YFATiHPESTEAlFEEAAKRGQR------AIA-------GKVCMDR---NAP- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 159 dypgmpsgkcdgvEEVRKKTREMLRAGAEIIK-VHATGGVLS----------------------ATDHPEF---TQFSQE 212
Cdd:cd01303 166 -------------EYYRDTAESSYRDTKRLIErWHGKSGRVKpaitprfapscseellaalgklAKEHPDLhiqTHISEN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 213 ELETIVEEGRFrKGVKVMAHAQGAEGI--KNAVRAgvhsieHGIFLDDEAIDLMIEKGTFLV--PTLlapvavlETAKET 288
Cdd:cd01303 233 LDEIAWVKELF-PGARDYLDVYDKYGLltEKTVLA------HCVHLSEEEFNLLKERGASVAhcPTS-------NLFLGS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 289 GMPDtavqkskevieihkasIAKAHKAGVKIAMGTDAG---------VMKHG---TNLRELGLMTEAGMTAMEAIVASTK 356
Cdd:cd01303 299 GLFD----------------VRKLLDAGIKVGLGTDVGggtsfsmldTLRQAykvSRLLGYELGGHAKLSPAEAFYLATL 362
|
410 420
....*....|....*....|....*..
gi 227296032 357 TAAECLGWQDRVGTIEEGKLADIIIVN 383
Cdd:cd01303 363 GGAEALGLDDKIGNFEVGKEFDAVVID 389
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-67 |
9.08e-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: 56.91 E-value: 9.08e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227296032 4 LLIKNGLFIDGNGGEPqkdAVIVVKDNQIAYVGPETAYSSSgeEQVVDAEGGTILPGMIDTHVH 67
Cdd:cd01315 2 LVIKNGRVVTPDGVRE---ADIAVKGGKIAAIGPDIANTEA--EEVIDAGGLVVMPGLIDTHVH 60
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
62-360 |
1.33e-08 |
|
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: 55.80 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 62 IDTHVHMMM--------EFSPVAERLETPFS--FMYYQAAKYLettLKAGITSVRDALGTDLGVKKAVEEGLIsgprLQL 131
Cdd:cd01292 2 IDTHVHLDGsalrgtrlNLELKEAEELSPEDlyEDTLRALEAL---LAGGVTTVVDMGSTPPPTTTKAAIEAV----AEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 132 SINALTITGGHGDGYtvsgrevdllpSDYPGMPSGkcDGVEEVRKKTREMLRAGAEIIKVHatggvlsatDHPEFTQFSQ 211
Cdd:cd01292 75 ARASAGIRVVLGLGI-----------PGVPAAVDE--DAEALLLELLRRGLELGAVGLKLA---------GPYTATGLSD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 212 EELETIVEEGRfRKGVKVMAHAQGA----EGIKNAVRAGVHS----IEHGIFLDDEAIDLMIEKGTFLVPTLLAPvavle 283
Cdd:cd01292 133 ESLRRVLEEAR-KLGLPVVIHAGELpdptRALEDLVALLRLGgrvvIGHVSHLDPELLELLKEAGVSLEVCPLSN----- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 284 taketgMPDTavqkskeVIEIHKASIAKAHKAGVKIAMGTDAGVMKHGTNL----RELGLMTEAGMTAMEAIVASTKTAA 359
Cdd:cd01292 207 ------YLLG-------RDGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLlallRLLLKVLRLGLSLEEALRLATINPA 273
|
.
gi 227296032 360 E 360
Cdd:cd01292 274 R 274
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
25-408 |
2.54e-08 |
|
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: 55.33 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 25 IVVKDNQIAYVGPetAYSSSGEEQVVDAEGGTILPGMIDTHVHM-----MMEFSP-----------VAERLETPFSF--M 86
Cdd:cd01293 17 IAIEDGRIAAIGP--ALAVPPDAEEVDAKGRLVLPAFVDPHIHLdktftGGRWPNnsggtlleaiiAWEERKLLLTAedV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 87 YYQAAKYLETTLKAGITSVR------DALGTDL--GVKKAVEEgliSGPRLQLSINALTitgghGDGYTVSGREVDLLps 158
Cdd:cd01293 95 KERAERALELAIAHGTTAIRthvdvdPAAGLKAleALLELREE---WADLIDLQIVAFP-----QHGLLSTPGGEELM-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 159 dypgmpsgkcdgveevrkktREMLRAGAEIIkvhatGGVlsatDHPEFTQFSQEELETIVE-EGRFRKGVKVMAHAQGAE 237
Cdd:cd01293 165 --------------------REALKMGADVV-----GGI----PPAEIDEDGEESLDTLFElAQEHGLDIDLHLDETDDP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 238 G-------IKNAVRAGVH---SIEHGIFLDD-------EAIDLMIEKG---TFLVPT-LLAPVAVLETAKETGMPdtavq 296
Cdd:cd01293 216 GsrtleelAEEAERRGMQgrvTCSHATALGSlpeaevsRLADLLAEAGisvVSLPPInLYLQGREDTTPKRRGVT----- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 297 kskevieihkaSIAKAHKAGVKIAMGTDaGVMKH----GTN---------LRELGLMTEAGMTAmeAIVASTKTAAECLG 363
Cdd:cd01293 291 -----------PVKELRAAGVNVALGSD-NVRDPwypfGSGdmlevanlaAHIAQLGTPEDLAL--ALDLITGNAARALG 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 227296032 364 WQDrvGTIEEGKLADIIIVNGNplDDINLLANNENITTVIKDGKI 408
Cdd:cd01293 357 LED--YGIKVGCPADLVLLDAE--DVAEAVARQPPRRVVIRKGRV 397
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
2-67 |
2.85e-08 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 55.20 E-value: 2.85e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227296032 2 TTLLIKNGLFIDGNGGEPQKDavIVVKDNQIAYVGPETAYSssgEEQVVDAEGGTILPGMIDTHVH 67
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDEVAD--VLIDDGKIAAIGENIEAE---GAEVIDATGLVVAPGLVDLHVH 61
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-105 |
4.01e-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: 55.10 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 5 LIKNGLFIDGNGGEPqkdAVIVVKDNQIAYVGPETAYSSsgEEQVVDAEGGTILPGMIDTHVHMMMefsPVAERLETpfs 84
Cdd:COG0044 1 LIKNGRVVDPGGLER---ADVLIEDGRIAAIGPDLAAPE--AAEVIDATGLLVLPGLIDLHVHLRE---PGLEHKED--- 69
|
90 100
....*....|....*....|....*
gi 227296032 85 fmyyqaakyLETTLKA----GITSV 105
Cdd:COG0044 70 ---------IETGTRAaaagGVTTV 85
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-67 |
1.03e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 53.32 E-value: 1.03e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227296032 4 LLIKNGLFID-GNGGEPQKDavIVVKDNQIAYVGPETaySSSGEEQVVDAEGGTILPGMIDTHVH 67
Cdd:PRK09237 1 LLLRGGRVIDpANGIDGVID--IAIEDGKIAAVAGDI--DGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
2-68 |
1.79e-07 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 52.93 E-value: 1.79e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227296032 2 TTLLIKNGLFI--DGNGGEPQKDAVIVVKDNQIAYVGPeTAYSSSGEEQVVDAEGGTILPGMIDTHVHM 68
Cdd:PRK08203 1 TTLWIKNPLAIvtMDAARREIADGGLVVEGGRIVEVGP-GGALPQPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
4-408 |
1.91e-07 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 53.02 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 4 LLIKNGLFIDGNGGEP-QKDAVIVVKDNQIAYVGP----ETAYSssgEEQVVDAEGGTILPGMIDTHVHMMMEFSP-VAE 77
Cdd:PRK07203 2 LLIGNGTAITRDPAKPvIEDGAIAIEGNVIVEIGTtdelKAKYP---DAEFIDAKGKLIMPGLINSHNHIYSGLARgMMA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 78 RLETPFSFM-------------------YYQA-AKYLEtTLKAGITSVRD-------ALGTDLGVKKAVEEglisgprlq 130
Cdd:PRK07203 79 NIPPPPDFIsilknlwwrldraltledvYYSAlICSLE-AIKNGVTTVFDhhaspnyIGGSLFTIADAAKK--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 131 LSINALTItgghgdgYTVSGRevdllpsdypgmpsgkcDGVEEVRKKTREMLRAGAEIIKvhATGGVLSAT--DHPEFTq 208
Cdd:PRK07203 149 VGLRAMLC-------YETSDR-----------------DGEKELQEGVEENIRFIKHIDE--AKDDMVEAMfgLHASFT- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 209 FSQEELETIVEEGrfrKGVKVMAHAQGAEGI-----------KNAVR----AGV---HSIE-HGIFLDDEAIDLMIEKGT 269
Cdd:PRK07203 202 LSDATLEKCREAV---KETGRGYHIHVAEGIydvsdshkkygKDIVErladFGLlgeKTLAaHCIYLSDEEIDLLKETDT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 270 FLVptllapvavleTAKETGMpDTAVQKSKEVIEIHKasiakahkaGVKIAMGTDA-----------GVMKHGTNLRELG 338
Cdd:PRK07203 279 FVV-----------HNPESNM-GNAVGYNPVLEMIKN---------GILLGLGTDGytsdmfesykvANFKHKHAGGDPN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 339 LM-TEAGMTAMEaivASTKTAAECLGwqDRVGTIEEGKLADIIIVNGNPL-----DDIN--LL--ANNENITTVIKDGKI 408
Cdd:PRK07203 338 VGwPESPAMLFE---NNNKIAERYFG--AKFGILEEGAKADLIIVDYNPPtplneDNINghILfgMNGGSVDTTIVNGKV 412
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-67 |
2.45e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 52.35 E-value: 2.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227296032 1 MTTLLIKNGLFIDGNGGEPqkdAVIVVKDNQIAYVGpeTAYSSSGEEQVVDAEGGTILPGMIDTHVH 67
Cdd:PRK02382 1 MRDALLKDGRVYYNNSLQP---RDVRIDGGKITAVG--KDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
252-383 |
4.56e-07 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 51.73 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 252 HGIFLDDEAIDLMIEKGTFLV--PT---LLApvavletakeTGMPDtavqkskevieihkasIAKAHKAGVKIAMGTDAG 326
Cdd:PRK09228 270 HCIHLEDRERRRLAETGAAIAfcPTsnlFLG----------SGLFD----------------LKRADAAGVRVGLGTDVG 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227296032 327 VmkhGTNLRELGLMTEA---------GMTAMEAIVASTKTAAECLGWQDRVGTIEEGKLADIIIVN 383
Cdd:PRK09228 324 G---GTSFSMLQTMNEAykvqqlqgyRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLD 386
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-67 |
8.38e-07 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 51.02 E-value: 8.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227296032 1 MTTLLIKNGLFIdgNGGEpQKDAVIVVKDNQIAYVGPetAYSSSGEEQVVDAEGGTILPGMIDTHVH 67
Cdd:PRK09236 1 MKRILIKNARIV--NEGK-IFEGDVLIENGRIAKIAS--SISAKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
3-410 |
1.07e-06 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 50.65 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 3 TLLIKNGLFIDGNGGEPQKDAVIVVKDNQIAYVGPETAYSssgeEQVVDAEGGTILPGMIDTHVHMMMEFSP-------V 75
Cdd:PRK06380 2 SILIKNAWIVTQNEKREILQGNVYIEGNKIVYVGDVNEEA----DYIIDATGKVVMPGLINTHAHVGMTASKglfddvdL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 76 AERLETPFSF--------MYYQAAKYLETTLKAGITSVRDALGTDLGVKKAVEEglisgprlqLSINALTitgghgdGYT 147
Cdd:PRK06380 78 EEFLMKTFKYdskrtregIYNSAKLGMYEMINSGITAFVDLYYSEDIIAKAAEE---------LGIRAFL-------SWA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 148 VSGREVDllpsdypgmpSGKCDGVEEVRKKTREMlRAGAEIIKVHATGGVLSATDhpeftqfsqeelETIVEEGRFRKGV 227
Cdd:PRK06380 142 VLDEEIT----------TQKGDPLNNAENFIREH-RNEELVTPSIGVQGIYVAND------------ETYLKAKEIAEKY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 228 KVMAHAQGAEGIKNAV----RAGVHSIEHgiflddeaidlmIEKGTFLVPTLLAPVAVLETAKETGM-PDTAVQKSKEVI 302
Cdd:PRK06380 199 DTIMHMHLSETRKEVYdhvkRTGERPVEH------------LEKIGFLNSKLIAAHCVWATYHEIKLlSKNGVKVSWNSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 303 EIHK------ASIAKAHKAGVKIAMGTDAGVMKHGTNLRE------LGLMTE----AGMTAMEAIVASTKTAAECLgwQD 366
Cdd:PRK06380 267 SNFKlgtggsPPIPEMLDNGINVTIGTDSNGSNNSLDMFEamkfsaLSVKNErwdaSIIKAQEILDFATINAAKAL--EL 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 227296032 367 RVGTIEEGKLADIII-----VNGNPLDDINLLAN------NENITTVIKDGKIEK 410
Cdd:PRK06380 345 NAGSIEVGKLADLVIldaraPNMIPTRKNNIVSNivyslnPLNVDHVIVNGKILK 399
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
3-408 |
1.18e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 50.18 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 3 TLLIKNGLFIDGNGGEPQKdAVIVVKDNQIAYVGPETAYSSsgeEQVVDAEGGTILPGMIDTHVHMMM-------EFSPV 75
Cdd:PRK08393 2 SILIKNGYVIYGENLKVIR-ADVLIEGNKIVEVKRNINKPA---DTVIDASGSVVSPGFINAHTHSPMvllrglaDDVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 76 AERLE-------------------------------TPFSFMYYQAAKYLETTLKAGItsvRDALG---TDLGVKKAVEE 121
Cdd:PRK08393 78 MEWLQnyiwprerklkrkdiywgaylgllemiksgtTTFVDMYFHMEEVAKATLEVGL---RGYLSygmVDLGDEEKREK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 122 GLISGPRLQLSINALT------ITGGHGDgYTVSgreVDLLpsdypgmpsgkcdgvEEVRKKTREMlragAEIIKVHatg 195
Cdd:PRK08393 155 EIKETEKLMEFIEKLNsprvhfVFGPHAP-YTCS---LALL---------------KWVREKAREW----NKLITIH--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 196 gvLSATdhpeftqfsQEELETIVEegRFRKGVKVMAHAQGAEGIKNAvragvhsIEHGIFLDDEAIDLMIEKGTFLVPTl 275
Cdd:PRK08393 209 --LSET---------MDEIKQIRE--KYGKSPVVLLDEIGFLNEDVI-------AAHGVWLSSRDIRILASAGVTVAHN- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 276 laPVAVLETAKETgMPdtavqkskevieihkasIAKAHKAGVKIAMGTDAGV----------MKHGTNLRELGLMTEAGM 345
Cdd:PRK08393 268 --PASNMKLGSGV-MP-----------------LRKLLNAGVNVALGTDGAAsnnnldmlreMKLAALLHKVHNLDPTIA 327
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227296032 346 TAMEAIVASTKTAAECLGWqdRVGTIEEGKLADIIIVN---------GNPLDDINLLANNENITTVIKDGKI 408
Cdd:PRK08393 328 DAETVFRMATQNGAKALGL--KAGVIKEGYLADIAVIDfnrphlrpiNNPISHLVYSANGNDVETTIVDGKI 397
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
3-72 |
1.32e-06 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 50.17 E-value: 1.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 3 TLLIKNGLFIDGNGgepQKDAVIVVKDNQIAYVGPETAysssgeEQVVDAEGGTILPGMIDTHVHMMMEF 72
Cdd:PRK08323 2 STLIKNGTVVTADD---TYKADVLIEDGKIAAIGANLG------DEVIDATGKYVMPGGIDPHTHMEMPF 62
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-67 |
2.59e-06 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 49.31 E-value: 2.59e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227296032 1 MTTLLIKNGLFIDgNGGEPQKDavIVVKDNQIAYVGPETaysSSGEEQVVDAEGGTILPGMIDTHVH 67
Cdd:PRK06189 2 MYDLIIRGGKVVT-PEGVYRAD--IGIKNGKIAEIAPEI---SSPAREIIDADGLYVFPGMIDVHVH 62
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
4-67 |
2.96e-06 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 49.15 E-value: 2.96e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227296032 4 LLIKNGLFIDgNGGEPQKDavIVVKDNQIAYVGpETAYSSSGEeqVVDAEGGTILPGMIDTHVH 67
Cdd:PRK09060 7 LILKGGTVVN-PDGEGRAD--IGIRDGRIAAIG-DLSGASAGE--VIDCRGLHVLPGVIDSQVH 64
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
4-67 |
3.40e-06 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 48.60 E-value: 3.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227296032 4 LLIKNGLFIDGNGGEPQKdAVIVVKDNQIAyvgPETAYSSSGEEQVVDAEGGTILPGMIDTHVH 67
Cdd:PRK12394 5 ILITNGHIIDPARNINEI-NNLRIINDIIV---DADKYPVASETRIIHADGCIVTPGLIDYHAH 64
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
4-73 |
4.44e-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: 48.75 E-value: 4.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 4 LLIKNGLFIDGNGgepQKDAVIVVKDNQIAYVGPETAysSSGEEQVVDAEGGTILPGMIDTHVHMMMEFS 73
Cdd:cd01314 1 LIIKNGTIVTADG---SFKADILIEDGKIVAIGPNLE--APGGVEVIDATGKYVLPGGIDPHTHLELPFM 65
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-72 |
9.25e-06 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 47.53 E-value: 9.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227296032 2 TTLLIKNGLFIDGNggePQKDAVIVVKDNQIAYVGPETAYSSsgEEQVVDAEGGTILPGMIDTHVHMMMEF 72
Cdd:PLN02942 5 TKILIKGGTVVNAH---HQELADVYVEDGIIVAVAPNLKVPD--DVRVIDATGKFVMPGGIDPHTHLAMPF 70
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-67 |
1.27e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 46.98 E-value: 1.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227296032 1 MTTLLIKNGLFIDGNGgEPQKDAVIVvKDNQIAYVGPETaySSSGEEQVVDAEGGTILPGMIDTHVH 67
Cdd:PRK07575 2 MMSLLIRNARILLPSG-ELLLGDVLV-EDGKIVAIAPEI--SATAVDTVIDAEGLTLLPGVIDPQVH 64
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
307-383 |
2.34e-05 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 46.44 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 307 ASIAKAHKAGVKIAMGTDA----------GVMKHGTNLRELGLMTEAGMTAMEAIVASTKTAAECLGWQDRVGTIEEGKL 376
Cdd:PRK09045 292 CPVAKLLQAGVNVALGTDGaasnndldlfGEMRTAALLAKAVAGDATALPAHTALRMATLNGARALGLDDEIGSLEPGKQ 371
|
....*..
gi 227296032 377 ADIIIVN 383
Cdd:PRK09045 372 ADLVAVD 378
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
53-381 |
5.11e-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: 238637 [Multi-domain] Cd Length: 381 Bit Score: 45.13 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 53 EGGTILPGMIDTHVHMmmEFSpvaeRLETPFSFMYYQAakyletTLKAGITSVRDALGTdlGVKKAVEEGLisgpRLQL- 131
Cdd:cd01312 25 PNGVLLPGLINAHTHL--EFS----ANVAQFTYGRFRA------WLLSVINSRDELLKQ--PWEEAIRQGI----RQMLe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 132 ----SINALTITGGHGDGYTVSGREV----DLLPSDYPG-MPSGKcdgVEEVRKKTREMLRAGAEI--IKVHATGGVlsa 200
Cdd:cd01312 87 sgttSIGAISSDGSLLPALASSGLRGvffnEVIGSNPSAiDFKGE---TFLERFKRSKSFESQLFIpaISPHAPYSV--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 201 tdHPEFTQF------------------SQEELETIVEEG--------RFRKGVKVMAHAQGAEGIKNAVRAGVH-SIEHG 253
Cdd:cd01312 161 --HPELAQDlidlakklnlplsthfleSKEEREWLEESKgwfkhfweSFLKLPKPKKLATAIDFLDMLGGLGTRvSFVHC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 254 IFLDDEAIDLMIEKGTFLVptlLAPvavletaketgmpdtavqKSKEVIEIHKASIAKAHKAGVKIAMGTDAgvmKHGTN 333
Cdd:cd01312 239 VYANLEEAEILASRGASIA---LCP------------------RSNRLLNGGKLDVSELKKAGIPVSLGTDG---LSSNI 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 334 lrELGLMTEAGM------------TAMEAIVASTKTAAECLGWQdrVGTIEEGKLADIII 381
Cdd:cd01312 295 --SLSLLDELRAlldlhpeedlleLASELLLMATLGGARALGLN--NGEIEAGKRADFAV 350
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
20-67 |
1.26e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 44.03 E-value: 1.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 227296032 20 QKDAVIVVKDNQIAYVGPETAYSSS--GEEQVVDAEGGTILPGMIDTHVH 67
Cdd:PRK09228 29 IEDGLLLVEDGRIVAAGPYAELRAQlpADAEVTDYRGKLILPGFIDTHIH 78
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
4-105 |
1.62e-04 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 43.66 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 4 LLIKNGLFIDG-NGGEpqKDAVIVVKDNQIAYVGPEtaYSSSGEEQVVDAEGGTILPGMIDTHVHM---MMefspvaerl 79
Cdd:PRK10027 32 YIIDNVSILDLiNGGE--ISGPIVIKGRYIAGVGAE--YADAPALQRIDARGATAVPGFIDAHLHIessMM--------- 98
|
90 100
....*....|....*....|....*.
gi 227296032 80 eTPFSFMyyqaakylETTLKAGITSV 105
Cdd:PRK10027 99 -TPVTFE--------TATLPRGLTTV 115
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
342-406 |
1.70e-04 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 43.37 E-value: 1.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227296032 342 EAGMTAMEAIVASTKTAAECLGWQDrVGTIEEGKLADIIIvngnpLDDInllaNNENITTVIKDG 406
Cdd:cd01295 232 EAGIPPEDAIQMATINPAECYGLHD-LGAIAPGRIADIVI-----LDDL----ENFNITTVLAKG 286
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
4-68 |
2.17e-04 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 43.31 E-value: 2.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227296032 4 LLIKNGLFIDGNGgepQKDAVIVVKDNQIAYVGPETAYSssgeEQVVDAEGGTILPGMIDTHVHM 68
Cdd:PRK08044 5 LIIKNGTVILENE---ARVVDIAVKGGKIAAIGQDLGDA----KEVMDASGLVVSPGMVDAHTHI 62
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-382 |
2.43e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 42.86 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 1 MTTLLIKNGLFIDGNGGEpqkDAVIVVKDNQIAYVGPETayssSGEEQVVDAEGGTILPGMIDTHV-HMMMEFSPVAE-R 78
Cdd:PRK15446 1 MMEMILSNARLVLPDEVV---DGSLLIEDGRIAAIDPGA----SALPGAIDAEGDYLLPGLVDLHTdNLEKHLAPRPGvD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 79 LETPFSFMYYQAAkyletTLKAGITSVRDALgtdlgvkkAVEEGLISGPRLQLSINALTitgghgdgytvsgrevdllps 158
Cdd:PRK15446 74 WPADAALAAHDAQ-----LAAAGITTVFDAL--------SVGDEEDGGLRSRDLARKLI--------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 159 dypgmpsgkcDGVEEVRkkTREMLRAGAeiiKVHATGGVLSATDHPEFtqfsqeelETIVEEGRFRKgVKVMAHA--QGA 236
Cdd:PRK15446 120 ----------DAIEEAR--ARGLLRADH---RLHLRCELTNPDALELF--------EALLAHPRVDL-VSLMDHTpgQRQ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 237 EGIKNAVRAGVHSIEHgifLDDEAIDLMIEK----GTFLVPTLLAPVAvlETAKETGMP-----DTAVQKSKEVIEiHKA 307
Cdd:PRK15446 176 FRDLEKYREYYAGKYG---LSDEEFDAFVEErialSARYAPPNRRAIA--ALARARGIPlashdDDTPEHVAEAHA-LGV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 308 SIA----------KAHKAGVKIAMGtdA-GVMK---HGTNLR-----ELGLMT--------------------EAGMTAM 348
Cdd:PRK15446 250 AIAefpttleaarAARALGMSVLMG--ApNVVRggsHSGNVSaldlaAAGLLDilssdyypaslldaafrladDGGLDLP 327
|
410 420 430
....*....|....*....|....*....|....
gi 227296032 349 EAIVASTKTAAECLGWQDRvGTIEEGKLADIIIV 382
Cdd:PRK15446 328 QAVALVTANPARAAGLDDR-GEIAPGKRADLVRV 360
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
1-68 |
3.86e-04 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 42.36 E-value: 3.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227296032 1 MTTLLIKNGLFI-DGNGGEPQKD--AVIVVKDNQIAYVGPETAyssSGEEQVVDAEGGTILPGMIDTHVHM 68
Cdd:PRK12393 1 MPSLLIRNAAAImTGLPGDAARLggPDIRIRDGRIAAIGALTP---LPGERVIDATDCVVYPGWVNTHHHL 68
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
25-74 |
6.08e-04 |
|
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: 41.55 E-value: 6.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 227296032 25 IVVKDNQIAYVGPETAysSSGEEQVVDAEGGTILPGMIDTHVHMMMEFSP 74
Cdd:cd01307 2 VAIENGKIAAVGAALA--APAATQIVDAGGCYVSPGWIDLHVHVYQGGTR 49
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
21-407 |
6.50e-04 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 41.58 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 21 KDAVIVVKDNQIAYVGPETAYSSSGEEQVVDAEGGTILPGMIDTHVHMMMEFspvaerLETPFSFMYYQAakYLET---T 97
Cdd:PRK15493 21 ENGYIIVENDQIIDVNSGEFASDFEVDEVIDMKGKWVLPGLVNTHTHVVMSL------LRGIGDDMLLQP--WLETriwP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 98 LKAGITSVRDALGTDLGVKKAVEEGlisgprlqlsinaltiTGGHGDGYTVSGREVDLLPSDY--PGMPSGKCD-----G 170
Cdd:PRK15493 93 LESQFTPELAVASTELGLLEMVKSG----------------TTSFSDMFNPIGVDQDAIMETVsrSGMRAAVSRtlfsfG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 171 VEEVRKKTREmlRAGAEIIKVHATGGVLSATDHPEFTQFSQEELetIVEEGRFRKGVKVMAHAQGAEGIKNavragVHSI 250
Cdd:PRK15493 157 TKEDEKKAIE--EAEKYVKRYYNESGMLTTMVAPHSPYTCSTEL--LEECARIAVENQTMVHIHLSETERE-----VRDI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 251 EHGifLDDEAIDLMIEKGTFLVPTLLAPVAVLETAKETGMPDTAVQ-----KSKEVIEIHKASIAKAHKAGVKIAMGTDA 325
Cdd:PRK15493 228 EAQ--YGKRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRvahnpNSNLKLGSGIANVKAMLEAGIKVGIATDS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 326 GVMKHGTNLRE---------LGLMTEAGMTAME-AIVASTKTAAECLGWQdRVGTIEEGKLADIIIVNG------NPLDD 389
Cdd:PRK15493 306 VASNNNLDMFEemriatllqKGIHQDATALPVEtALTLATKGAAEVIGMK-QTGSLEVGKCADFITIDPsnkphlQPADE 384
|
410 420
....*....|....*....|..
gi 227296032 390 I--NLL--ANNENITTVIKDGK 407
Cdd:PRK15493 385 VlsHLVyaASGKDISDVIINGK 406
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
25-112 |
7.96e-04 |
|
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: 41.22 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 25 IVVKDNQIAYVGPETAYSSSGEEQVVDAEGGTILPGMIDTHVHMMMEFSPVAERLETPfsfmyyqaakylETTL----KA 100
Cdd:cd01308 20 ILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTP------------EVTLsdltTA 87
|
90
....*....|..
gi 227296032 101 GITSVRDALGTD 112
Cdd:cd01308 88 GVTTVVGCLGTD 99
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
1-68 |
1.25e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 40.84 E-value: 1.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227296032 1 MTTLLIKNgLFIDGNGGEPQkdavIVVKDNQIAYVGPETAYSSSGEEqVVDAEGGTILPGMIDTHVHM 68
Cdd:PRK09230 3 NALMTIKN-ARLPGKEGLWQ----ITIEDGKISAIEPQSEASLEAGE-VLDAEGGLAIPPFIEPHIHL 64
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
4-80 |
1.28e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 40.83 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 4 LLIKNGLFIDGNGGepqKDAV--IVVKDNQIAYVGpetaySSSGE-EQVVDAEGGTILPGMIDTHVHMMmefSPVAERLE 80
Cdd:PRK09061 21 LVIRNGRVVDPETG---LDAVrdVGIKGGKIAAVG-----TAAIEgDRTIDATGLVVAPGFIDLHAHGQ---SVAAYRMQ 89
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
309-408 |
1.49e-03 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 40.34 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 309 IAKAHKAGVKIAMGTDAGVMKHGTNL-REL--GLMTEAGMT----AMEAIVASTKTAAECLGWQDrvGTIEEGKLADIII 381
Cdd:PRK08418 296 LEKAKKAGINYSIATDGLSSNISLSLlDELraALLTHANMPllelAKILLLSATRYGAKALGLNN--GEIKEGKDADLSV 373
|
90 100 110
....*....|....*....|....*....|...
gi 227296032 382 VNGNP-LDDINLLA-----NNENITTVIKDGKI 408
Cdd:PRK08418 374 FELPEeCTKKEQLPlqfilHAKEVKKLFIGGKE 406
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
252-381 |
1.71e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 40.22 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 252 HGIFLDDEAIDLMIEKGTFLV--PT---LLApvavletakeTGMpdtavqkskevieihkASIAKAHKAGVKIAMGTDAG 326
Cdd:PRK08203 270 HCVHLDDAEIARLARTGTGVAhcPCsnmRLA----------SGI----------------APVRELRAAGVPVGLGVDGS 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227296032 327 VMKHGTNL----RELGLMTEAG-----MTAMEAIVASTKTAAECLGWQDrVGTIEEGKLADIII 381
Cdd:PRK08203 324 ASNDGSNLigeaRQALLLQRLRygpdaMTAREALEWATLGGARVLGRDD-IGSLAPGKLADLAL 386
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
4-72 |
2.12e-03 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 40.06 E-value: 2.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227296032 4 LLIKNGLFIDGNGgepQKDAVIVVKDNQIAYVGPETaySSSGEEQVVDAEGGTILPGMIDTHVHMMMEF 72
Cdd:TIGR02033 1 LLIKGGTVVNADD---VFQADVLIEGGKIVAVGDNL--IPPDAVEVIDATGKYVLPGGIDVHTHLEMPF 64
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
1-67 |
2.66e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 39.53 E-value: 2.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227296032 1 MTTLLIKNGLFIDGnggepqkDAV-IVVKDNQIAYVGPETAysSSGEEQVVDAEGGTILPGMIDTHVH 67
Cdd:PRK05985 1 MTDLLFRNVRPAGG-------AAVdILIRDGRIAAIGPALA--APPGAEVEDGGGALALPGLVDGHIH 59
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
270-406 |
2.76e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 39.64 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227296032 270 FLVPTLLAPVAVL----ETAKETGMPDTAVQKSKEVIEIH---------KA--SIAKAHKAGVKIAMGTDAGV------M 328
Cdd:PRK06151 268 LLGPRLLIPHATYisgsPRLNYSGGDDLALLAEHGVSIVHcplvsarhgSAlnSFDRYREAGINLALGTDTFPpdmvmnM 347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227296032 329 KHGTNLRELGLMTEAGMTAMEAIVASTKTAAECLGWQDrVGTIEEGKLADIIIVNgnpLDDINLLANNENITTVIKDG 406
Cdd:PRK06151 348 RVGLILGRVVEGDLDAASAADLFDAATLGGARALGRDD-LGRLAPGAKADIVVFD---LDGLHMGPVFDPIRTLVTGG 421
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-68 |
5.37e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 38.85 E-value: 5.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227296032 1 MTTLLIKNGLFIDGnggepQKDAVIVVKDNQIAYVGPETAYSSsgeEQVVDAEGGTILPGMIDTHVHM 68
Cdd:PRK07572 1 MFDLIVRNANLPDG-----RTGIDIGIAGGRIAAVEPGLQAEA---AEEIDAAGRLVSPPFVDPHFHM 60
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
22-67 |
9.56e-03 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 37.81 E-value: 9.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 227296032 22 DAVIVVKDNQIAYVGpetAYSSSGEEQVVDAEGGTILPGMIDTHVH 67
Cdd:TIGR00857 5 EVDILVEGGRIKKIG---KLRIPPDAEVIDAKGLLVLPGFIDLHVH 47
|
|
| |
