|
Name |
Accession |
Description |
Interval |
E-value |
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
21-397 |
2.34e-175 |
|
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: 493.85 E-value: 2.34e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 21 VEDAALVTDGPLIHWIGPRAELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGGNRSGEFEQRLEGVSYAEIAAAGGGIAS 100
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQLAALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGILS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 101 TVRATREASEEELLASARKRLEPLLRDGVTALEIKSGYGLDLASERKMLRVIRRLGERLPATVRSTCLAAHALPPEYAGR 180
Cdd:TIGR01224 81 TVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 181 ADDYIEHICSTMLPALAGEGLVDAVDAFCEHLAFSPAQVERVFIAARELGLPVKLHAEQLSSLHGSSLAARYRALSADHL 260
Cdd:TIGR01224 161 PDDYVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 261 EYMTEDDARAMGEAGTVAVLLPGAFYLLRETQlPPIDALRRHGVAMAIASDLNPGTSPALSLRLMLNMACTLFRLTPEET 340
Cdd:TIGR01224 241 EHASDAGIKALAEAGTVAVLLPGTTFYLRETY-PPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600285 341 LAGVTLHAARALGLEASHGSLEVGKLADFVAWDIERPAELAYWLGGDLPKRVIRHAE 397
Cdd:TIGR01224 320 LHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNGN 376
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
26-394 |
6.48e-173 |
|
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: 487.15 E-value: 6.48e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 26 LVTDGpLIHWIGPRAELPPGDYA--ERIDLGGAWLTPGLIDCHTHAVFGGNRSGEFEQRLEGVSYAEIAAAGGGIASTVR 103
Cdd:cd01296 2 AIRDG-RIAAVGPAASLPAPGPAaaEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 104 ATREASEEELLASARKRLEPLLRDGVTALEIKSGYGLDLASERKMLRVIRRLGERLPATVRSTCLAAHALPPEYAGRaDD 183
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGR-EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 184 YIEHICSTMLPALAGEGLVDAVDAFCEHLAFSPAQVERVFIAARELGLPVKLHAEQLSSLHGSSLAARYRALSADHLEYM 263
Cdd:cd01296 160 YIDLVIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 264 TEDDARAMGEAGTVAVLLPGAFYLLRETQlPPIDALRRHGVAMAIASDLNPGTSPALSLRLMLNMACTLFRLTPEETLAG 343
Cdd:cd01296 240 SDEGIAALAEAGTVAVLLPGTAFSLRETY-PPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15600285 344 VTLHAARALGLEASHGSLEVGKLADFVAWDIERPAELAYWLGGDLPKRVIR 394
Cdd:cd01296 319 ATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIK 369
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-402 |
1.84e-85 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 265.29 E-value: 1.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 4 LWQHCHAATLKGGKysIVEDAALVTDGPLIHWIGPRAELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGGNRSGEFEqrl 83
Cdd:COG1228 11 LITNATLVDGTGGG--VIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFE--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 84 egvsyaeiaaAGGGIASTVratreaseeELLASARKRLEPLLRDGVTALEIKSGYGLDL-----ASERKMLRVIRRLGER 158
Cdd:COG1228 86 ----------AGGGITPTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPLGLrdaiiAGESKLLPGPRVLAAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 159 LPATVrstCLAAHAL-PPEyagraddyiehiCSTMLPALAGEGlVDAVDAFCEH--LAFSPAQVERVFIAARELGLPVKL 235
Cdd:COG1228 147 PALSL---TGGAHARgPEE------------ARAALRELLAEG-ADYIKVFAEGgaPDFSLEELRAILEAAHALGLPVAA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 236 HAEQLSslhGSSLAARYRALSADHLEYMTEDDARAMGEAGTVaVLLPGAFYLL-----------------RETQLPPIDA 298
Cdd:COG1228 211 HAHQAD---DIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLallegaaapvaakarkvREAALANARR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 299 LRRHGVAMAIASDLNPGTSPALSLRLMLNMACtLFRLTPEETLAGVTLHAARALGLEASHGSLEVGKLADFVAWDIERPA 378
Cdd:COG1228 287 LHDAGVPVALGTDAGVGVPPGRSLHRELALAV-EAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLE 365
|
410 420
....*....|....*....|....
gi 15600285 379 ELAYWlggDLPKRVIRHAEEVYRG 402
Cdd:COG1228 366 DIAYL---EDVRAVMKDGRVVDRS 386
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
20-378 |
4.62e-35 |
|
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: 133.80 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 20 IVEDAALVTDGPLIHWIGPRAELPPG-DYAERIDLGGAWLTPGLIDCHTHAVFGGNRS----GEFEQRLEGVSYaeiaaa 94
Cdd:COG0402 18 VLEDGAVLVEDGRIAAVGPGAELPARyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGladdLPLLDWLEEYIW------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 95 gggiastvRATREASEEELLASARKRLEPLLRDGVT-ALEIksgYGLDLASERKMLRVIRRLGERlpATVrSTCLAAHAL 173
Cdd:COG0402 92 --------PLEARLDPEDVYAGALLALAEMLRSGTTtVADF---YYVHPESADALAEAAAEAGIR--AVL-GRGLMDRGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 174 PPEYAGRADDYIEHiCSTMLPALAG--EGLVDAVDAFCEHLAFSPAQVERVFIAARELGLPVKLH-AEQLS------SLH 244
Cdd:COG0402 158 PDGLREDADEGLAD-SERLIERWHGaaDGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHlAETRDevewvlELY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 245 GSSLAARYR---ALSAD----HLEYMTEDDARAMGEAGTVAVLLPGAFYLLRETqLPPIDALRRHGVAMAIASDlNPGTS 317
Cdd:COG0402 237 GKRPVEYLDelgLLGPRtllaHCVHLTDEEIALLAETGASVAHCPTSNLKLGSG-IAPVPRLLAAGVRVGLGTD-GAASN 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600285 318 PALSLRLMLNMACTLFR--------LTPEETLAGVTLHAARALGLEASHGSLEVGKLADFVAWDIERPA 378
Cdd:COG0402 315 NSLDMFEEMRLAALLQRlrggdptaLSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPH 383
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
25-373 |
5.74e-21 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 94.48 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 25 ALVTDGPLIHWIGPRAELPP--GDYAERIDLGGAWLTPGLIDCHTHAVFGGNRSGEFeqRLEGV-SYAEIAAA------- 94
Cdd:COG1574 29 AVAVRDGRIVAVGSDAEVRAlaGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGV--DLSGArSLDELLARlraaaae 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 95 --------GGG------------------------------------IASTV---------------------------- 102
Cdd:COG1574 107 lppgewilGRGwdeslwpegrfptradldavspdrpvvltrvdghaaWVNSAalelagitadtpdpeggeierdadgept 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 103 ------------RATREASEEELLASARKRLEPLLRDGVTALeiksgygLDLASERKMLRVIRRLGE--RLPATVRstcL 168
Cdd:COG1574 187 gvlreaamdlvrAAIPPPTPEELRAALRAALRELASLGITSV-------HDAGLGPDDLAAYRELAAagELPLRVV---L 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 169 AAHALPPEYAGRADDYIEhicstmlPALAGEGL-VDAVDAFCE----------------------HLAFSPAQVERVFIA 225
Cdd:COG1574 257 YLGADDEDLEELLALGLR-------TGYGDDRLrVGGVKLFADgslgsrtaallepyaddpgnrgLLLLDPEELRELVRA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 226 ARELGLPVKLHA-------------EQLSSLHGSSlAARYRAlsaDHLEYMTEDDARAMGEAGTVAVLLPG-AFYLL--- 288
Cdd:COG1574 330 ADAAGLQVAVHAigdaavdevldayEAARAANGRR-DRRHRI---EHAQLVDPDDLARFAELGVIASMQPThATSDGdwa 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 289 -------RETQLPPIDALRRHGVAMAIASDlnpgtSPALSLRLMLNMACTLFR-------------LTPEETLAGVTLHA 348
Cdd:COG1574 406 edrlgpeRAARAYPFRSLLDAGAPLAFGSD-----APVEPLDPLLGIYAAVTRrtpsgrglgpeerLTVEEALRAYTIGA 480
|
490 500
....*....|....*....|....*
gi 15600285 349 ARALGLEASHGSLEVGKLADFVAWD 373
Cdd:COG1574 481 AYAAFEEDEKGSLEPGKLADFVVLD 505
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
25-370 |
8.79e-19 |
|
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: 87.75 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 25 ALVTDGPLIHWIGPRAELPP--GDYAERIDLGGAWLTPGLIDCHTHAVFGG------------------------NRSGE 78
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKAlkGPATEVIDLKGKTVLPGFIDSHSHLLLGGlsllwldlsgvtskeealariredAAAAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 79 FEQRLEGVSYAE---------------------------------------IAAAG---------GGI------------ 98
Cdd:cd01300 81 PGEWILGFGWDEsllgegryptraeldavspdrpvlllrrdghsawvnsaaLRLAGitrdtpdppGGEivrdadgeptgv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 99 ------ASTVRATREASEEELLASARKRLEPLLRDGVTALEIKSGYGLDlaserkMLRVIRRLGERLPATVRStclaAHA 172
Cdd:cd01300 161 lveaaaALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAAD------DIEAYRRLAAAGELTLRV----RVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 173 LPPEYAGRADDYIEHicsTMLPALAGEGL-VDAVDAF----------------------CEHLAFSPAQVERVFIAAREL 229
Cdd:cd01300 231 LYVSPLAEDLLEELG---ARKNGAGDDRLrLGGVKLFadgslgsrtaalsepyldspgtGGLLLISPEELEELVRAADEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 230 GLPVKLHA-------------EQLSSLHGSSlAARYRAlsaDHLEYMTEDDARAMGEAGTVAVLLPG-AFYLL------- 288
Cdd:cd01300 308 GLQVAIHAigdravdtvldalEAALKDNPRA-DHRHRI---EHAQLVSPDDIPRFAKLGVIASVQPNhLYSDGdaaedrr 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 289 ----RETQLPPIDALRRHGVAMAIASDLNPGT-SPALSLRLMLN--------MACTLFRLTPEETLAGVTLHAARALGLE 355
Cdd:cd01300 384 lgeeRAKRSYPFRSLLDAGVPVALGSDAPVAPpDPLLGIWAAVTrktpgggvLGNPEERLSLEEALRAYTIGAAYAIGEE 463
|
490
....*....|....*
gi 15600285 356 ASHGSLEVGKLADFV 370
Cdd:cd01300 464 DEKGSLEPGKLADFV 478
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
57-399 |
4.33e-17 |
|
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: 81.78 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 57 WLTPGLIDCHTHAVFGGNRSgefeqrlegvsyaeiaaagggiastvratREASEEELLASARKRLEPLLRDGVTALeIKS 136
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRG-----------------------------IPVPPEFAYEALRLGITTMLKSGTTTV-LDM 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 137 GYGLDLASERkMLRVIRRLGERLPATVRSTCLAA---HALPPEYAGRADDYIEHICSTmlpalaGEGLVDAVDAFCEHLA 213
Cdd:pfam01979 51 GATTSTGIEA-LLEAAEELPLGLRFLGPGCSLDTdgeLEGRKALREKLKAGAEFIKGM------ADGVVFVGLAPHGAPT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 214 FSPAQVERVFIAARELGLPVKLHA-EQLSSLHGSSLAARYRALSADHLEYMTE----DDARAMGEAG-----TVAVLLPG 283
Cdd:pfam01979 124 FSDDELKAALEEAKKYGLPVAIHAlETKGEVEDAIAAFGGGIEHGTHLEVAESggllDIIKLILAHGvhlspTEANLLAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 284 AFYLLR-----------ETQLPPIDALRRHGVAMAIASDLNPGTSPALSLRLMLNMACTLFR----LTPEETLAGVTLHA 348
Cdd:pfam01979 204 HLKGAGvahcpfsnsklRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDpeggLSPLEALRMATINP 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15600285 349 ARALGLEASHGSLEVGKLADFVAWDIERPAELAYWLGGDLPKRVIRHAEEV 399
Cdd:pfam01979 284 AKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
48-373 |
1.89e-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: 76.95 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 48 AERIDLGGAWLTPGLIDCHTHavFGGNRSGEFEQRLEGVSYAEIAAAG-------GGIaSTVR--------ATREASEEE 112
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTH--LGSDPGDLPLDLALPVEYRTIRATRqaraalrAGF-TTVRdaggadygLLRDAIDAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 113 LLASARkrlepLLRDGvTALEIKSGYGlDLASERKMLRVIRRLG-----ERLPATVRstclaahalppEYAGRADDYIEh 187
Cdd:cd01299 78 LIPGPR-----VFASG-RALSQTGGHG-DPRGLSGLFPAGGLAAvvdgvEEVRAAVR-----------EQLRRGADQIK- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 188 ICSTMLPALAGEGLvdavdafcEHLAFSPAQVERVFIAARELGLPVKLHAEqlsSLHGSSLAARYRALSADHLEYMTEDD 267
Cdd:cd01299 139 IMATGGVLSPGDPP--------PDTQFSEEELRAIVDEAHKAGLYVAAHAY---GAEAIRRAIRAGVDTIEHGFLIDDET 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 268 ARAMGEAGTVAVLLPGAFYLL----RETQLPP-------------IDALRR---HGVAMAIASDL----NPGTSPALSLR 323
Cdd:cd01299 208 IELMKEKGIFLVPTLATYEALaaegAAPGLPAdsaekvalvleagRDALRRahkAGVKIAFGTDAgfpvPPHGWNARELE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15600285 324 LMLNMActlfrLTPEETLAGVTLHAARALGLEASHGSLEVGKLADFVAWD 373
Cdd:cd01299 288 LLVKAG-----GTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
6-377 |
2.35e-15 |
|
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: 77.24 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 6 QHCHAATLKGGKysIVEDAALVTDGPLIHWIGPRAELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGGNRS----GEFEQ 81
Cdd:cd01298 4 RNGTIVTTDPRR--VLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGladdLPLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 82 RLEGVsyaeiaaagggiasTVRATREASEEELLASARKRLEPLLRDGVT-ALEIKSGYGLDLAserkmlRVIRRLGERlp 160
Cdd:cd01298 82 WLKDL--------------IWPLERLLTEEDVYLGALLALAEMIRSGTTtFADMYFFYPDAVA------EAAEELGIR-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 161 atvrstCLAAHA---LPPEYAGRADDYIEHiCSTMLPA--LAGEGLVDAVDAFCEHLAFSPAQVERVFIAARELGLPVKL 235
Cdd:cd01298 140 ------AVLGRGimdLGTEDVEETEEALAE-AERLIREwhGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 236 HA-----EQLSSL--HGSS---LAARYRALSAD----HLEYMTEDDARAMGEAGTVAVLLPGAFYLLrETQLPPIDALRR 301
Cdd:cd01298 213 HLaetedEVEESLekYGKRpveYLEELGLLGPDvvlaHCVWLTDEEIELLAETGTGVAHNPASNMKL-ASGIAPVPEMLE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 302 HGVAMAIASDlnpGTSPALSLRLM--LNMACTLFR--------LTPEETLAGVTLHAARALGLEAShGSLEVGKLADFVA 371
Cdd:cd01298 292 AGVNVGLGTD---GAASNNNLDMFeeMRLAALLQKlahgdptaLPAEEALEMATIGGAKALGLDEI-GSLEVGKKADLIL 367
|
....*.
gi 15600285 372 WDIERP 377
Cdd:cd01298 368 IDLDGP 373
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
62-351 |
5.50e-15 |
|
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: 74.68 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 62 LIDCHTHAVFGGNRSGEFEQRLEGVSYAeiaaagggiastvratreaSEEELLASARKRLEPLLRDGVTALEIKSGYGLD 141
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEEL-------------------SPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 142 LASERKMLRVIRRLGErlPATVRSTCLAAHalPPEYAGRADDYIEHicstmLPALAGEGLVDAVDAF-----CEHLAFSP 216
Cdd:cd01292 62 TTTKAAIEAVAEAARA--SAGIRVVLGLGI--PGVPAAVDEDAEAL-----LLELLRRGLELGAVGLklagpYTATGLSD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 217 AQVERVFIAARELGLPVKLHAEQLSSLHGSSLAARYRALS-----ADHLEYMTEDDARAMGEAG-TVAVLLPGAFYLLR- 289
Cdd:cd01292 133 ESLRRVLEEARKLGLPVVIHAGELPDPTRALEDLVALLRLggrvvIGHVSHLDPELLELLKEAGvSLEVCPLSNYLLGRd 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600285 290 ETQLPPIDALRRHGVAMAIASDLNPGTSPALSLRLMLN-MACTLFRLTPEETLAGVTLHAARA 351
Cdd:cd01292 213 GEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLlLKVLRLGLSLEEALRLATINPARA 275
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
14-374 |
1.49e-14 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 75.08 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 14 KGGKYSIVEDAALVTDGPLIHWIGPRAelpPGDYAERIDLGGAWLTPGLIDCHT-----HAVFG-GNRSGEFEQRLEGVS 87
Cdd:PRK06151 14 DDGDHRLLRDGEVVFEGDRILFVGHRF---DGEVDRVIDAGNALVGPGFIDLDAlsdldTTILGlDNGPGWAKGRVWSRD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 88 YAEiaaagggiastvRATREA-SEEELLASARKRLEPLLRDGVT-ALEIKSGY----GLDLASERKMLRVIRRLGER--L 159
Cdd:PRK06151 91 YVE------------AGRREMyTPEELAFQKRYAFAQLLRNGITtAMPIASLFyrqwAETYAEFAAAAEAAGRLGLRvyL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 160 PATVRSTCLAAHA------LPPEYAG-----RADDYIEHIcstmlpALAGEGLVDAVDAFCEHLAFSPAQVERVFIAARE 228
Cdd:PRK06151 159 GPAYRSGGSVLEAdgslevVFDEARGlagleEAIAFIKRV------DGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 229 LGLPVKLHAEQ-------LSSLHGSS----------LAARyraLSADHLEYMTE---------DDARAMGEAGTVAVLLP 282
Cdd:PRK06151 233 LGCPVRLHCAQgvlevetVRRLHGTTplewladvglLGPR---LLIPHATYISGsprlnysggDDLALLAEHGVSIVHCP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 283 GAFYlLRETQLPPIDALRRHGVAMAIASDlnpgTSPALSLRLML--NMACTLFRLTPEETLAG-----VTLHAARALGLE 355
Cdd:PRK06151 310 LVSA-RHGSALNSFDRYREAGINLALGTD----TFPPDMVMNMRvgLILGRVVEGDLDAASAAdlfdaATLGGARALGRD 384
|
410
....*....|....*....
gi 15600285 356 aSHGSLEVGKLADFVAWDI 374
Cdd:PRK06151 385 -DLGRLAPGAKADIVVFDL 402
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
26-380 |
2.08e-14 |
|
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: 74.21 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 26 LVTDGPlIHWIGPRAELPPGdyAERIDLGGAWLTPGLIDCHTH--AVFGGNRSGEFEQrlegvsyaeiAAAGGGIASTVR 103
Cdd:cd01293 18 AIEDGR-IAAIGPALAVPPD--AEEVDAKGRLVLPAFVDPHIHldKTFTGGRWPNNSG----------GTLLEAIIAWEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 104 ATREASEEELLASARKRLEPLLRDGVTAleIKSGYGLDLASERKMLRVIRRLGERLpatvRSTC-LAAHALPPE---YAG 179
Cdd:cd01293 85 RKLLLTAEDVKERAERALELAIAHGTTA--IRTHVDVDPAAGLKALEALLELREEW----ADLIdLQIVAFPQHgllSTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 180 RADDYIEHicstmlpALA-GEGLVDAVDAFcEHLAFSPAQVERVFIAARELGLPVKLH---AEQLSSLHGSSLAARYRAL 255
Cdd:cd01293 159 GGEELMRE-------ALKmGADVVGGIPPA-EIDEDGEESLDTLFELAQEHGLDIDLHldeTDDPGSRTLEELAEEAERR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 256 S---------ADHLEYMTEDDARA----MGEAG-TVAVLLPGAFYLL-------RETQLPPIDALRRHGVAMAIASD--L 312
Cdd:cd01293 231 GmqgrvtcshATALGSLPEAEVSRladlLAEAGiSVVSLPPINLYLQgredttpKRRGVTPVKELRAAGVNVALGSDnvR 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600285 313 NP----GTSPALSLrlmLNMACTLFRLTPEETLAG----VTLHAARALGLEasHGSLEVGKLADFVAWDIERPAEL 380
Cdd:cd01293 311 DPwypfGSGDMLEV---ANLAAHIAQLGTPEDLALaldlITGNAARALGLE--DYGIKVGCPADLVLLDAEDVAEA 381
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
51-400 |
7.92e-14 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 72.56 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 51 IDLGGAWLTPGLIDCHTHAVFGGnrSGEFEQRLEGVS-------YAEIAAAG------GGIASTVRATREASEEELLASA 117
Cdd:pfam07969 3 IDAKGRLVLPGFVDPHTHLDGGG--LNLRELRLPDVLpnavvkgQAGRTPKGrwlvgeGWDEAQFAETRFPYALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 118 RKRLEPLLRDGVTALEIKSGYGLDLA-----SERKMLRVIRRLGERLPATVRSTCLAAHALPP----------------- 175
Cdd:pfam07969 81 APDGPVLLRALHTHAAVANSAALDLAgitkaTEDPPGGEIARDANGEGLTGLLREGAYALPPLlareaeaaavaaalaal 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 176 ------------EYAGRADDYIEH-------ICSTMLPALAGEGL--------VDAVDAF-------------------- 208
Cdd:pfam07969 161 pgfgitsvdgggGNVHSLDDYEPLreltaaeKLKELLDAPERLGLphsiyelrIGAMKLFadgvlgsrtaaltepyfdap 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 209 -CEHLAFSPAQVERVFIAARELGLPVKLHA---EQLSSLHGS--------SLAARYRALSADHLEYMTEDDARAMGEAGT 276
Cdd:pfam07969 241 gTGWPDFEDEALAELVAAARERGLDVAIHAigdATIDTALDAfeavaeklGNQGRVRIEHAQGVVPYTYSQIERVAALGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 277 VAVLLPGAFYLL-----------RETQLPPIDALRRHGVAMAIASDLN-------PGTSPALSLRLMLNMACTLF--RLT 336
Cdd:pfam07969 321 AAGVQPVFDPLWgdwlqdrlgaeRARGLTPVKELLNAGVKVALGSDAPvgpfdpwPRIGAAVMRQTAGGGEVLGPdeELS 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600285 337 PEETLAGVTLHAARALGLEASHGSLEVGKLADFVAWDIER----PAELAYwlggDLPKRVIRHAEEVY 400
Cdd:pfam07969 401 LEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPltvdPPAIAD----IRVRLTVVDGRVVY 464
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
40-373 |
1.58e-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: 71.19 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 40 AELPPGDYAERIDLGGAWLTPGLIDCHTHA-------VFGGNRSGEF----------------------EQRLEGVSYAE 90
Cdd:cd01309 9 AEITTPADAEVIDAKGKHVTPGLIDAHSHLgldeeggVRETSDANEEtdpvtphvraidginpddeafkRARAGGVTTVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 91 I----AAAGGGIASTVRaTREASEEELLASA-----------------RKRLEPLLRDGVTALEIKSGYGldlaserkml 149
Cdd:cd01309 89 VlpgsANLIGGQGVVIK-TDGGTIEDMFIKApaglkmalgenpkrvygGKGKEPATRMGVAALLRDAFIK---------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 150 rvIRRLGERLPATvrstcLAAHALPPEYAGRADdyiehicsTMLPALAGEGLVdavdaFCEhlAFSPAQVERVFIAAREL 229
Cdd:cd01309 158 --AQEYGRKYDLG-----KNAKKDPPERDLKLE--------ALLPVLKGEIPV-----RIH--AHRADDILTAIRIAKEF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 230 GLPVKL--HAEQLsslhgsslaaryraLSADHLeymteddARAMGEAGTVAVL-LPGAFYLLRETQLPPIDALRRHGVAM 306
Cdd:cd01309 216 GIKITIehGAEGY--------------KLADEL-------AKHGIPVIYGPTLtLPKKVEEVNDAIDTNAYLLKKGGVAF 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600285 307 AIASDlnpgtSPALSLR-LMLNMA-CTLFRLTPEETLAGVTLHAARALGLEASHGSLEVGKLADFVAWD 373
Cdd:cd01309 275 AISSD-----HPVLNIRnLNLEAAkAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
3-371 |
3.70e-13 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 70.42 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 3 RLWQHCHAATLKGGkYSIVEDAALVTDGPLIHWIGPRAELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGGNR----SGE 78
Cdd:PRK06687 2 KVFQHVNIVTCDQD-FHVYLDGILAVKDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRgirdDSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 79 FEQRLEgvSYAEIAAAGGGIASTVRATREASEEELLAsarkrlepllrdGVTAL-EIKSGYGLDLaserkmlrvirrlgE 157
Cdd:PRK06687 81 LHEWLN--DYIWPAESEFTPDMTTNAVKEALTEMLQS------------GTTTFnDMYNPNGVDI--------------Q 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 158 RLPATVRSTCLAAHALPPEYAGRADDYIEHICSTMlpALAGEGLVDAVDAFCEHLA-FSPAQVERVFIA-----ARELGL 231
Cdd:PRK06687 133 QIYQVVKTSKMRCYFSPTLFSSETETTAETISRTR--SIIDEILKYKNPNFKVMVApHSPYSCSRDLLEaslemAKELNI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 232 PVKLHAEQLSSLHGSSLAaRY--RALS-ADHLEYMTEDDARAMG-----------EAGTVAVLLPGAFYLLRETQLPPID 297
Cdd:PRK06687 211 PLHVHVAETKEESGIILK-RYgkRPLAfLEELGYLDHPSVFAHGvelnereierlASSQVAIAHNPISNLKLASGIAPII 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 298 ALRRHGVAMAIASD----------LNPGTSPALsLRLMLNMACTLFrlTPEETLAGVTLHAARALGLEASHGSLEVGKLA 367
Cdd:PRK06687 290 QLQKAGVAVGIATDsvasnnnldmFEEGRTAAL-LQKMKSGDASQF--PIETALKVLTIEGAKALGMENQIGSLEVGKQA 366
|
....
gi 15600285 368 DFVA 371
Cdd:PRK06687 367 DFLV 370
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
18-373 |
1.68e-12 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 68.68 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 18 YSIVEDAALVTDGPLIHWIGPRAELPP--GDYAERIDLGGAWLTPGLIDCHTH----AVFGGnrSGE----------F-- 79
Cdd:PRK09228 26 LRYIEDGLLLVEDGRIVAAGPYAELRAqlPADAEVTDYRGKLILPGFIDTHIHypqtDMIAS--YGEqlldwlntytFpe 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 80 EQRLEGVSYA-EIAA-------AGGGIASTVRAT-REASEEELLASARKR--------------LEPLLRDgvTAleiKS 136
Cdd:PRK09228 104 ERRFADPAYArEVAEffldellRNGTTTALVFGTvHPQSVDALFEAAEARnmrmiagkvlmdrnAPDGLRD--TA---ES 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 137 GYgldlaseRKMLRVIRRLGE--RLpatvrstclaAHALPPEYAgraddyiehICST--MLpALAGEGLVDAVDAFCE-H 211
Cdd:PRK09228 179 GY-------DDSKALIERWHGkgRL----------LYAITPRFA---------PTSTpeQL-EAAGALAREHPDVWIQtH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 212 LAFSPAQVERV---FIAARELgLPVKLHAEQLsslhgsslaaRYRALSAdHLEYMTEDDARAMGEAGTVAVLLP------ 282
Cdd:PRK09228 232 LSENLDEIAWVkelFPEARDY-LDVYERYGLL----------GPRAVFA-HCIHLEDRERRRLAETGAAIAFCPtsnlfl 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 283 --GAFyllretqlpPIDALRRHGVAMAIASDLNPGTSpaLSLRLMLNMA---CTL--FRLTPEETLAGVTLHAARALGLE 355
Cdd:PRK09228 300 gsGLF---------DLKRADAAGVRVGLGTDVGGGTS--FSMLQTMNEAykvQQLqgYRLSPFQAFYLATLGGARALGLD 368
|
410
....*....|....*...
gi 15600285 356 ASHGSLEVGKLADFVAWD 373
Cdd:PRK09228 369 DRIGNLAPGKEADFVVLD 386
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
26-377 |
2.10e-12 |
|
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: 68.19 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 26 LVTDGpLIHWIGPRAELPPGDyaERIDLGGAWLTPGLIDCHTHAvfggnrsgefeqRLEGVSYAE------IAAAGGGIA 99
Cdd:COG0044 19 LIEDG-RIAAIGPDLAAPEAA--EVIDATGLLVLPGLIDLHVHL------------REPGLEHKEdietgtRAAAAGGVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 100 S------TVRATREASE-EELLASARKR---------------------LEPLLRDGVTALEIKSGY--GLDLASERKML 149
Cdd:COG0044 84 TvvdmpnTNPVTDTPEAlEFKLARAEEKalvdvgphgaltkglgenlaeLGALAEAGAVAFKVFMGSddGNPVLDDGLLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 150 RVIRRLGErLPATVrstclAAHAlppEYAGRADDYIEHicstmlpalagEGLVDAVDafceHLAFSPAQVERVFIA---- 225
Cdd:COG0044 164 RALEYAAE-FGALV-----AVHA---EDPDLIRGGVMN-----------EGKTSPRL----GLKGRPAEAEEEAVArdia 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 226 -ARELGlpVKLHAEQLSSLHGSSLAARYRA----LSAD----HLeYMTEDDaraMGEAGTVAVLlpgafyllretqLPPI 296
Cdd:COG0044 220 lAEETG--ARLHIVHVSTAEAVELIREAKArglpVTAEvcphHL-TLTDED---LERYGTNFKV------------NPPL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 297 ------DALRRH---GVAMAIASDLNP----------GTSPA------LSLRLMLNMACTLFRLTPEETLAGVTLHAARA 351
Cdd:COG0044 282 rteedrEALWEGladGTIDVIATDHAPhtleekelpfAEAPNgipgleTALPLLLTELVHKGRLSLERLVELLSTNPARI 361
|
410 420
....*....|....*....|....*.
gi 15600285 352 LGLEaSHGSLEVGKLADFVAWDIERP 377
Cdd:COG0044 362 FGLP-RKGRIAVGADADLVLFDPDAE 386
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
58-399 |
1.52e-11 |
|
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: 65.16 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 58 LTPGLIDCHTHAVFGGNRS----GEFEQRLEGV--SYAEIaaagggiastvraTREASEEELLASARKRLEpllrDGVTA 131
Cdd:cd01312 29 LLPGLINAHTHLEFSANVAqftyGRFRAWLLSVinSRDEL-------------LKQPWEEAIRQGIRQMLE----SGTTS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 132 LEIKSGYGLDL---------------------ASERKMLRVIRRLGERLPATVRSTCLAAHALPPEYAgraddyIEHICS 190
Cdd:cd01312 92 IGAISSDGSLLpalassglrgvffnevigsnpSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYS------VHPELA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 191 TMLPALAGE--GLVDAvdafceHLAFSPAQVERVFIAA--------RELGLP-VKLHAEQLSSLHGssLAARYRALSADH 259
Cdd:cd01312 166 QDLIDLAKKlnLPLST------HFLESKEEREWLEESKgwfkhfweSFLKLPkPKKLATAIDFLDM--LGGLGTRVSFVH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 260 LEYMTEDDARAMGEAGTVAVLLPGAFYLLrETQLPPIDALRRHGVAMAIASDlnpGTSPALSLRLM--LNMACTLFRL-- 335
Cdd:cd01312 238 CVYANLEEAEILASRGASIALCPRSNRLL-NGGKLDVSELKKAGIPVSLGTD---GLSSNISLSLLdeLRALLDLHPEed 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600285 336 ---TPEETLAGVTLHAARALGLEAshGSLEVGKLADFVAWDIERPAElaywlGGDLPKRVIRHAEEV 399
Cdd:cd01312 314 lleLASELLLMATLGGARALGLNN--GEIEAGKRADFAVFELPGPGI-----KEQAPLQFILHAKEV 373
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
20-378 |
6.09e-10 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 60.70 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 20 IVEDAALVTDGPLIHWIGPRAELPPG-DYAERIDLGGAWLTPGLIDCHTHAVFGGNRSGEFEQRLEGVSYAEIAAAGGgi 98
Cdd:PRK09045 25 VLEDHAVAIRDGRIVAILPRAEARARyAAAETVELPDHVLIPGLINAHTHAAMSLLRGLADDLPLMTWLQDHIWPAEG-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 99 astvratREASEE-----ELLASARkrlepLLRDGVTALEIKSGYGlDLASErkmlrVIRRLGERlpATVrstCLAAHAL 173
Cdd:PRK09045 103 -------AWVSEEfvrdgTLLAIAE-----MLRGGTTCFNDMYFFP-EAAAE-----AAHQAGMR--AQI---GMPVLDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 174 PPEYAGRADDYIEHICSTMlPALAGEGLVDAvdAFCEHLAF--SPAQVERVFIAARELGLPVKLH--------AEQLSSl 243
Cdd:PRK09045 160 PTAWASDADEYLAKGLELH-DQWRHHPLIST--AFAPHAPYtvSDENLERIRTLAEQLDLPIHIHlhetaqeiADSLKQ- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 244 HGSSLAARYRALS-------ADHLEYMTEDDARAMGEAGTVAVLLPgafyllrETQLP------PIDALRRHGVAMAIas 310
Cdd:PRK09045 236 HGQRPLARLARLGllgprliAVHMTQLTDAEIALLAETGCSVVHCP-------ESNLKlasgfcPVAKLLQAGVNVAL-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 311 dlnpGTSPALS---LRLMLNM--ACTLFR--------LTPEETLAGVTLHAARALGLEASHGSLEVGKLADFVAWDIERP 377
Cdd:PRK09045 307 ----GTDGAASnndLDLFGEMrtAALLAKavagdataLPAHTALRMATLNGARALGLDDEIGSLEPGKQADLVAVDLSGL 382
|
.
gi 15600285 378 A 378
Cdd:PRK09045 383 E 383
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
215-377 |
3.00e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 58.48 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 215 SPAQVERVFIAARELGLPVKLHAEQLSSLHGSSLAARYRA---LSAD----HLEYMTEDDARAMGEAGTVAVLLPgafyl 287
Cdd:PRK08204 199 SWEVARADFRLARELGLPISMHQGFGPWGATPRGVEQLHDaglLGPDlnlvHGNDLSDDELKLLADSGGSFSVTP----- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 288 lrETQL------PPIDALRRHGVAMAIASDLNPGTSPAL--SLRLMLNMACTLFR---------------LTPEETLAGV 344
Cdd:PRK08204 274 --EIEMmmghgyPVTGRLLAHGVRPSLGVDVVTSTGGDMftQMRFALQAERARDNavhlreggmppprltLTARQVLEWA 351
|
170 180 190
....*....|....*....|....*....|...
gi 15600285 345 TLHAARALGLEASHGSLEVGKLADFVAWDIERP 377
Cdd:PRK08204 352 TIEGARALGLEDRIGSLTPGKQADLVLIDATDL 384
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
20-373 |
6.15e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 57.03 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 20 IVEDAALVTDGPLIHWIGPRAELPpgdyAERIDLGGAWLTPGLIDCHTHavfGGNrsgefeqrleGVSYAeiaaagggia 99
Cdd:COG1820 13 VLEDGALLIEDGRIAAIGPGAEPD----AEVIDLGGGYLAPGFIDLHVH---GGG----------GVDFM---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 100 stvratrEASEEELLASARKrlepLLRDGVTALeiksgygldL-----ASERKMLRVIRRLGERLPATVRSTCLAAH--- 171
Cdd:COG1820 66 -------DGTPEALRTIARA----HARHGTTSF---------LpttitAPPEDLLRALAAIAEAIEQGGGAGILGIHleg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 172 ---------ALPPEYAGRAD-DYIEHICS---------TMLPALagEGLVDAVDAFCE--------HLAFSPAQVERVF- 223
Cdd:COG1820 126 pflspekkgAHPPEYIRPPDpEELDRLLEaaggliklvTLAPEL--PGALEFIRYLVEagvvvslgHTDATYEQARAAFe 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 224 ---------------IAARELGLPvklhAEQLSS-------------LHGSSLAARYRALSADHLEYMTedDA-RAMGea 274
Cdd:COG1820 204 agathvthlfnamspLHHREPGVV----GAALDDddvyaeliadgihVHPAAVRLALRAKGPDRLILVT--DAmAAAG-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 275 gtvavLLPGAFyllretQLPPIDALRRHGVAM----AIA-SDLNPGTspalSLRLMLNMActlfRLTPEETLAGVTLHAA 349
Cdd:COG1820 276 -----LPDGEY------ELGGLEVTVKDGVARladgTLAgSTLTMDD----AVRNLVEWT----GLPLEEAVRMASLNPA 336
|
410 420
....*....|....*....|....
gi 15600285 350 RALGLEASHGSLEVGKLADFVAWD 373
Cdd:COG1820 337 RALGLDDRKGSIAPGKDADLVVLD 360
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
21-373 |
1.07e-08 |
|
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: 56.43 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 21 VEDAALVTDGPLIHWIGPRAELPPGDyaERIDLGGAWLTPGLIDCHTHavfggnrsgefeqrlegvsyaeiaaaGGGIAS 100
Cdd:cd00854 14 LEDGAVLVEDGKIVAIGPEDELEEAD--EIIDLKGQYLVPGFIDIHIH--------------------------GGGGAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 101 TVratrEASEEELLASARKrlepLLRDGVTALeiksgygldLA-----SERKMLRVIRRLGERLPATVRSTCLAAH---- 171
Cdd:cd00854 66 FM----DGTAEALKTIAEA----LAKHGTTSF---------LPttvtaPPEEIAKALAAIAEAIAEGQGAEILGIHlegp 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 172 --------ALPPEY--AGRADDYIEHICS--------TMLPALAGEGlvDAVDAFCEH-----LAFSPA---QVERVFIA 225
Cdd:cd00854 129 fispekkgAHPPEYlrAPDPEELKKWLEAaggliklvTLAPELDGAL--ELIRYLVERgiivsIGHSDAtyeQAVAAFEA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 226 A----------------RELGLPvklhAEQLSS-------------LHGSSLAARYRALSADHLEYMTedDA-RAMGeag 275
Cdd:cd00854 207 GathvthlfnamsplhhREPGVV----GAALSDddvyaeliadgihVHPAAVRLAYRAKGADKIVLVT--DAmAAAG--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 276 tvavlLPGAFYLLRETQLppidaLRRHGVAMAIASDLNPGTSPALS-LRLMLNMActlfRLTPEETLAGVTLHAARALGL 354
Cdd:cd00854 278 -----LPDGEYELGGQTV-----TVKDGVARLADGTLAGSTLTMDQaVRNMVKWG----GCPLEEAVRMASLNPAKLLGL 343
|
410
....*....|....*....
gi 15600285 355 EASHGSLEVGKLADFVAWD 373
Cdd:cd00854 344 DDRKGSLKPGKDADLVVLD 362
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
17-399 |
4.15e-08 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 54.98 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 17 KYSIVEDAALVTDGPlIHWIGPRAELP---PGdyAERIDLGGAWLTPGLIDCHTHAVFGGNRS----GEFEQRLEGVSya 89
Cdd:PRK08418 15 NFEILEDGAVVFDDK-ILEIGDYENLKkkyPN--AKIQFFKNSVLLPAFINPHTHLEFSANKTtldyGDFIPWLGSVI-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 90 eiaaagggiastvratreASEEELLASA-----RKRLEPLLRDGVTALEIKSGYGLDL-ASERKMLRVI---RRLGerlp 160
Cdd:PRK08418 90 ------------------NHREDLLEKCkgaliQQAINEMLKSGVGTIGAISSFGIDLeICAKSPLRVVffnEILG---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 161 atvrSTCLAAHALPPEYAGRADDYIEHICSTMLPALAgeglvdavdafcEHLAFS--PAQVERVFIAARELGLPVKLH-- 236
Cdd:PRK08418 148 ----SNASAVDELYQDFLARFEESKKFKSKKFIPAIA------------IHSPYSvhPILAKKALQLAKKENLLVSTHfl 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 237 --AEQLSSLHGSS-------------------------LAARYRALSAdHLEYMTEDDARAMGEAGTVAVLLPGAFYLLR 289
Cdd:PRK08418 212 esKAEREWLEESKgwfkkffekflkepkplytpkefleLFKGLRTLFT-HCVYASEEELEKIKSKNASITHCPFSNRLLS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 290 ETQLPpIDALRRHGVAMAIASDlnpGTSPALSLRLMLNMACTLFRLT--PEETLA-----GVTLHAARALGLEAshGSLE 362
Cdd:PRK08418 291 NKALD-LEKAKKAGINYSIATD---GLSSNISLSLLDELRAALLTHAnmPLLELAkilllSATRYGAKALGLNN--GEIK 364
|
410 420 430
....*....|....*....|....*....|....*...
gi 15600285 363 VGKLADFVAWDI-ERPAELAywlggDLPKRVIRHAEEV 399
Cdd:PRK08418 365 EGKDADLSVFELpEECTKKE-----QLPLQFILHAKEV 397
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
21-375 |
9.27e-08 |
|
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: 53.83 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 21 VEDAALVTDGPLIHWIGPraELPPGDYAERIDLGGAWLTPGLIDCHTHAvfggNRSGEFEQrlEGVSYAEIAAAGGGIAS 100
Cdd:cd01315 15 VREADIAVKGGKIAAIGP--DIANTEAEEVIDAGGLVVMPGLIDTHVHI----NEPGRTEW--EGFETGTKAAAAGGITT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 101 TV----------------RATREASEEELLASA----------RKRLEPLLRDGVTALE---IKSGYG----LDLASERK 147
Cdd:cd01315 87 IIdmplnsipptttvenlEAKLEAAQGKLHVDVgfwgglvpgnLDQLRPLDEAGVVGFKcflCPSGVDefpaVDDEQLEE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 148 MLRVIRRLGERL-------PATVRSTCLAAHALPPEYAgradDYiehicstmlpaLAGEGLVDAVDAfcehlafspaqVE 220
Cdd:cd01315 167 AMKELAKTGSVLavhaenpEITEALQEQAKAKGKRDYR----DY-----------LASRPVFTEVEA-----------IQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 221 RVFIAARELGlpVKLHAEQLSSLHGSSLAARYRALSAD-------HLEYMTEDDARamgEAGTVAVLLPGafylLRE--T 291
Cdd:cd01315 221 RILLLAKETG--CRLHIVHLSSAEAVPLIREARAEGVDvtvetcpHYLTFTAEDVP---DGGTEFKCAPP----IRDaaN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 292 QLPPIDALRRHGVAMaIASDLNPGT-------------------SPALSLRLMLNMACTLFRLTPEETLAGVTLHAARAL 352
Cdd:cd01315 292 QEQLWEALENGDIDM-VVSDHSPCTpelkllgkgdffkawggisGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLF 370
|
410 420
....*....|....*....|...
gi 15600285 353 GLEASHGSLEVGKLADFVAWDIE 375
Cdd:cd01315 371 GLSHQKGRIAVGYDADFVVWDPE 393
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
259-383 |
1.97e-07 |
|
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: 52.67 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 259 HLEYMTEDDARAMGEAGTVAVLLPGA-FYLlrETQLPPIDALRRHGVAMAIASDLNPGTSPALsLRLM---------LNM 328
Cdd:cd01303 267 HCVHLSEEEFNLLKERGASVAHCPTSnLFL--GSGLFDVRKLLDAGIKVGLGTDVGGGTSFSM-LDTLrqaykvsrlLGY 343
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600285 329 ACT-LFRLTPEETLAGVTLHAARALGLEASHGSLEVGKLADFVAWDIERPAELAYW 383
Cdd:cd01303 344 ELGgHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLADR 399
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
26-376 |
7.49e-07 |
|
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: 51.06 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 26 LVTDGpLIHWIGPRaeLPPGDYAERIDLGGAWLTPGLIDCHTH--AVFGGNRSGE-FEQrlegvsyAEIAAAGGGIASTV 102
Cdd:cd01314 20 LIEDG-KIVAIGPN--LEAPGGVEVIDATGKYVLPGGIDPHTHleLPFMGTVTADdFES-------GTRAAAAGGTTTII 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 103 RATREASEEELLASARKR----------------------------LEPLLRDGVTALEIKSGY-GLDLASERKMLRVIR 153
Cdd:cd01314 90 DFAIPNKGQSLLEAVEKWrgkadgksvidygfhmiitdwtdsvieeLPELVKKGISSFKVFMAYkGLLMVDDEELLDVLK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 154 RLGErLPATVrstclAAHAlppeyagRADDYIEHICSTML---------------PALAGEGLVDA------VDA--FCE 210
Cdd:cd01314 170 RAKE-LGALV-----MVHA-------ENGDVIAELQKKLLaqgktgpeyhalsrpPEVEAEATARAirlaelAGAplYIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 211 HLAfSPAQVERVfIAARELGLPVklHAEQLsslhgsslaARYRALSADHLEYMTEDDARamgeagtvAVLLPGafylLRE 290
Cdd:cd01314 237 HVS-SKEAADEI-ARARKKGLPV--YGETC---------PQYLLLDDSDYWKDWFEGAK--------YVCSPP----LRP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 291 TQLPpiDALRRH---GVAMAIASD-----------------LNPGTSPALSLRLMLnmactLF-------RLTPEETLAG 343
Cdd:cd01314 292 KEDQ--EALWDGlssGTLQTVGSDhcpfnfaqkargkddftKIPNGVPGVETRMPL-----LWsegvakgRITLEKFVEL 364
|
410 420 430
....*....|....*....|....*....|...
gi 15600285 344 VTLHAARALGLEASHGSLEVGKLADFVAWDIER 376
Cdd:cd01314 365 TSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
18-64 |
1.69e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 49.59 E-value: 1.69e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15600285 18 YSIVEDAALVTDGPLIHWIGPRAELPPGdyAERIDLGGAWLTPGLID 64
Cdd:PRK11170 13 HEVLDDHAVVIADGLIEAVCPVAELPPG--IEQRDLNGAILSPGFID 57
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
36-138 |
2.85e-06 |
|
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: 48.93 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 36 IGPRAELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGGNRSGeFEQRLEGVSYAEIAAAGG----GIASTVRATReaSEE 111
Cdd:cd01308 30 IEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGG-PSTRTPEVTLSDLTTAGVttvvGCLGTDGISR--SME 106
|
90 100
....*....|....*....|....*..
gi 15600285 112 ELLASARKrlepLLRDGVTALEIKSGY 138
Cdd:cd01308 107 DLLAKARA----LEEEGITCFVYTGSY 129
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
29-377 |
3.25e-06 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 48.73 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 29 DGPLIHWIGprAELPPGDYAerIDLGGAWLTPGLIDCHTHAVFGGNRsGEFEQrlegVSYAEIaaagggIASTVRATREA 108
Cdd:PRK06380 27 EGNKIVYVG--DVNEEADYI--IDATGKVVMPGLINTHAHVGMTASK-GLFDD----VDLEEF------LMKTFKYDSKR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 109 SEEELLASARKRLEPLLRDGVTALeiksgygLDL-ASERKMLRVIRRLGERlpatvrsTCLAAHALPPEYA---GRADDY 184
Cdd:PRK06380 92 TREGIYNSAKLGMYEMINSGITAF-------VDLyYSEDIIAKAAEELGIR-------AFLSWAVLDEEITtqkGDPLNN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 185 IEHICSTM------LPALAGEGLVDAVDAFCE-------------HLAFSPAQVErVFIAARELGL-PVKlHAEQLSSLH 244
Cdd:PRK06380 158 AENFIREHrneelvTPSIGVQGIYVANDETYLkakeiaekydtimHMHLSETRKE-VYDHVKRTGErPVE-HLEKIGFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 245 GSSLAAryralsadHLEYMTEDDARAMGEAGTVAVLLPGAFYLLRETQLPPIDALRRHGVAMAIASDLNpGTSPALSLRL 324
Cdd:PRK06380 236 SKLIAA--------HCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGGSPPIPEMLDNGINVTIGTDSN-GSNNSLDMFE 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600285 325 MLNMACTLFR--------LTPEETLAGVTLHAARALGLEAshGSLEVGKLADFVAWDIERP 377
Cdd:PRK06380 307 AMKFSALSVKnerwdasiIKAQEILDFATINAAKALELNA--GSIEVGKLADLVILDARAP 365
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
259-393 |
4.15e-06 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 48.69 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 259 HLEYMTEDDARAMGEAGTVAVLLP--------GAFyllretqlpPIDALRRHGVAMAIASDLNPGTSPALSLRlMLNMAC 330
Cdd:PRK09229 271 HATHLTDAETARLARSGAVAGLCPtteanlgdGIF---------PAVDYLAAGGRFGIGSDSHVSIDLVEELR-LLEYGQ 340
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600285 331 TLFRL------TPEETLAGVTLHA------ARALGLEAshGSLEVGKLADFVAWDIERPAeLAYWLGGDLPKRVI 393
Cdd:PRK09229 341 RLRDRrrnvlaAAAQPSVGRRLFDaalaggAQALGRAI--GGLAVGARADLVVLDLDHPA-LAGREGDALLDRWV 412
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
42-380 |
1.71e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 46.57 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 42 LPPGDYAERIDLGGAWLTPGLIDCHTHavFggnRSGEFEQRlEGVSYAEIAAAGGGIASTVR-------ATREASEEELL 114
Cdd:PRK02382 36 LDGSSSEEVIDARGMLLLPGGIDVHVH--F---REPGYTHK-ETWYTGSRSAAAGGVTTVVDqpntdppTVDGESFDEKA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 115 ASARKR-----------------LEPLLRDGVTAL-EI---KS--GYGLDLASERKMLRVIRRLGerLPATVrstclaaH 171
Cdd:PRK02382 110 ELAARKsivdfginggvtgnwdpLESLWERGVFALgEIfmaDStgGMGIDEELFEEALAEAARLG--VLATV-------H 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 172 AlppEYAGRADDYIEhicstmlpALAGEGLVDAvdafceHLAFSPAQ-----VERVFIAARELGlpVKLHAEQLSSLHGS 246
Cdd:PRK02382 181 A---EDEDLFDELAK--------LLKGDADADA------WSAYRPAAaeaaaVERALEVASETG--ARIHIAHISTPEGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 247 SLAARYRAL--SADHLEYMTEDDARAMGEAGTVAvllpgafyllretqlPPI----------DALRRHGVAMaIASDLNP 314
Cdd:PRK02382 242 DAARREGITceVTPHHLFLSRRDWERLGTFGKMN---------------PPLrsekrrealwERLNDGTIDV-VASDHAP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 315 GTS--PALSLR--------------LMLnMACTLFRLTPEETLAGVTLHAARALGLEaSHGSLEVGKLADFVAWDIERPA 378
Cdd:PRK02382 306 HTReeKDADIWdapsgvpgvetmlpLLL-AAVRKNRLPLERVRDVTAANPARIFGLD-GKGRIAEGYDADLVLVDPDAAR 383
|
..
gi 15600285 379 EL 380
Cdd:PRK02382 384 EI 385
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
47-377 |
4.01e-05 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 45.31 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 47 YAERIDLGGAWLTPGLIDCHTHavfggnrSGE--FEQRlEGVSYAEIAAAGGGIASTVratreaseeellasARKRLEPL 124
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVH-------LREpgFEYK-ETLESGAKAAAAGGFTTVV--------------CMPNTNPV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 125 LrDGVTALEiksgYGLDLASERKMLRVI-------RRLGERL-----------------PATVRSTCLAAHALppEYAGR 180
Cdd:cd01317 59 I-DNPAVVE----LLKNRAKDVGIVRVLpigaltkGLKGEELteigelleagavgfsddGKPIQDAELLRRAL--EYAAM 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 181 ADDYIehICSTMLPALAGEGLV-DAVDAFCEHLAFSPAQVERVFIAaRELGL----PVKLHAEQLSSLHGSSLAARYRAL 255
Cdd:cd01317 132 LDLPI--IVHPEDPSLAGGGVMnEGKVASRLGLPGIPPEAETIMVA-RDLELaeatGARVHFQHLSTARSLELIRKAKAK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 256 ----SAD----HLeymTEDDaRAMGEAGTVAVLLPGafylLR--ETQLPPIDALRRhGVAMAIASDLNPGTSP------- 318
Cdd:cd01317 209 glpvTAEvtphHL---LLDD-EALESYDTNAKVNPP----LRseEDREALIEALKD-GTIDAIASDHAPHTDEekdlpfa 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600285 319 -----ALSLRLMLNMACTLFR----LTPEETLAGVTLHAARALGLEAshGSLEVGKLADFVAWDIERP 377
Cdd:cd01317 280 eappgIIGLETALPLLWTLLVkgglLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAE 345
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
2-68 |
8.45e-05 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 44.46 E-value: 8.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600285 2 KRLW--QHCHAATLKGGKYSIvEDAALVTDGPLIHWIGPRAElPPGDYAERIDLGGAWLTPGLIDCHTH 68
Cdd:PRK08203 1 TTLWikNPLAIVTMDAARREI-ADGGLVVEGGRIVEVGPGGA-LPQPADEVFDARGHVVTPGLVNTHHH 67
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
21-377 |
9.59e-05 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 44.31 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 21 VEDAALVTDGPLIHWIGPRAElppGDYAERIDLGGAWLTPGLIDCHTHAvfggNRSGEFEqrLEGVSYAEIA-AAGGG-- 97
Cdd:PRK06189 18 VYRADIGIKNGKIAEIAPEIS---SPAREIIDADGLYVFPGMIDVHVHF----NEPGRTH--WEGFATGSAAlAAGGCtt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 98 --------IASTVraTREASEEELLASARK-----------------RLEPLLRDGVTALE-IKSGYGLD---LASERKM 148
Cdd:PRK06189 89 yfdmplnsIPPTV--TREALDAKAELARQKsavdfalwgglvpgnleHLRELAEAGVIGFKaFMSNSGTDefrSSDDLTL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 149 L---RVIRRLGerlpatvrsTCLAAHAlppeyagRADDYIEHICSTmlpaLAGEGLVDAVDAFCEHLAFSPAQ-VERVFI 224
Cdd:PRK06189 167 YegmKEIAALG---------KILALHA-------ESDALTRHLTTQ----ARQQGKTDVRDYLESRPVVAELEaVQRALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 225 AARELGLPvkLHAEQLSSLHGSSLAARYRALSAD-------HLEYMTEDDARAMGEAGTVAVLLPGafyllRETQLPPID 297
Cdd:PRK06189 227 YAQETGCP--LHFVHISSGKAVALIAEAKKRGVDvsvetcpHYLLFTEEDFERIGAVAKCAPPLRS-----RSQKEELWR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 298 ALRRHGVAMaIASDLNPgTSPAL------------------SLRLMLNMAcTLFRLTPEETLAGVT-LHAARALGLeASH 358
Cdd:PRK06189 300 GLLAGEIDM-ISSDHSP-CPPELkegddfflvwggisggqsTLLVMLTEG-YIERGIPLETIARLLaTNPAKRFGL-PQK 375
|
410
....*....|....*....
gi 15600285 359 GSLEVGKLADFVAWDIERP 377
Cdd:PRK06189 376 GRLEVGADADFVLVDLDET 394
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
40-73 |
1.58e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 43.30 E-value: 1.58e-04
10 20 30
....*....|....*....|....*....|....
gi 15600285 40 AELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGG 73
Cdd:PRK09237 33 GDIDGSQAKKVIDLSGLYVSPGWIDLHVHVYPGS 66
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
13-77 |
2.72e-04 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 42.85 E-value: 2.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600285 13 LKGGKysiVEDAALVTDGPL--------IHWIGPraELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGGNRSG 77
Cdd:COG3964 4 IKGGR---VIDPANGIDGVMdiaikdgkIAAVAK--DIDAAEAKKVIDASGLYVTPGLIDLHTHVFPGGTDYG 71
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
20-376 |
3.58e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 42.68 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 20 IVEDAALVTDGPLIHWIGPRAELPpgDYAERIDLGGAWLTPGLIDCHTHAVfggnrsgefeQRLegvsyaeiaaaGGGIA 99
Cdd:PRK07228 18 EIVDGDVLIEDDRIAAVGDRLDLE--DYDDHIDATGKVVIPGLIQGHIHLC----------QTL-----------FRGIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 100 STVR-----ATR----EAS--EEELLASARKRLEPLLRDGVTA-LEIKSGYGLDLASE-------RKML-RVIRRLGERL 159
Cdd:PRK07228 75 DDLElldwlKDRiwplEAAhdAESMYYSALLGIGELIESGTTTiVDMESVHHTDSAFEaagesgiRAVLgKVMMDYGDDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 160 PATVRSTCLAA----HALPPEYAGRADDYIEHicstmlpalageglvdavdAFCEHLAFS--PAQVERVFIAARELGLPV 233
Cdd:PRK07228 155 PEGLQEDTEASlaesVRLLEKWHGADNGRIRY-------------------AFTPRFAVSctEELLRGVRDLADEYGVRI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 234 KLHA----------EQLSS------LHGSSLAARYRALSadHLEYMTEDDARAMGEAGTVAVLLPGAFYLLrETQLPPID 297
Cdd:PRK07228 216 HTHAsenrgeietvEEETGmrnihyLDEVGLTGEDLILA--HCVWLDEEEREILAETGTHVTHCPSSNLKL-ASGIAPVP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 298 ALRRHGVAMAIASD---LNPGTSPALSLRL--MLNMACTL--FRLTPEETLAGVTLHAARALGLEASHGSLEVGKLADFV 370
Cdd:PRK07228 293 DLLERGINVALGADgapCNNTLDPFTEMRQaaLIQKVDRLgpTAMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLA 372
|
....*.
gi 15600285 371 AWDIER 376
Cdd:PRK07228 373 ILDLDG 378
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
33-69 |
5.18e-04 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 42.08 E-value: 5.18e-04
10 20 30
....*....|....*....|....*....|....*..
gi 15600285 33 IHWIGpraELPPGDYAERIDLGGAWLTPGLIDCHTHA 69
Cdd:COG3653 31 IVAVG---DLAAAEAARVIDATGLVVAPGFIDIHTHY 64
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
40-115 |
9.02e-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: 41.16 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 40 AELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGGNRSGEFEQRL---EGVSyaEIAAAGGGIASTVRATR----EASEEE 112
Cdd:cd01307 14 AALAAPAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYGDRPDMIgvkSGVT--TVVDAGSAGADNIDGFRytviERSATR 91
|
...
gi 15600285 113 LLA 115
Cdd:cd01307 92 VYA 94
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
20-68 |
1.24e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 40.69 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15600285 20 IVEDAALVTDGPLIHWIGPRAELPpGDY--AERIDLGGAWLTPGLIDCHTH 68
Cdd:PRK07203 18 VIEDGAIAIEGNVIVEIGTTDELK-AKYpdAEFIDAKGKLIMPGLINSHNH 67
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
21-68 |
1.44e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.85 E-value: 1.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15600285 21 VEDAALVTDGPLIHWIGPRaelpPGDYAERIDLGGAWLTPGLIDCHTH 68
Cdd:COG1001 22 ILEGDIAIAGGRIAGVGDY----IGEATEVIDAAGRYLVPGFIDGHVH 65
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
21-370 |
1.88e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 40.16 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 21 VEDAALVTDGPLIHWIGPRAELPPGDyaerIDLGGAWLTPGLIDCHTHAvfggnrsgeFEQRLE---GVSY--------- 88
Cdd:PRK15446 17 VVDGSLLIEDGRIAAIDPGASALPGA----IDAEGDYLLPGLVDLHTDN---------LEKHLAprpGVDWpadaalaah 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 89 -AEIAAAggGIASTVRATREASEEEllasARKRLEPLLRDGVTALEiksgygldLASERKMLRVIRRLGERlpatvrstC 167
Cdd:PRK15446 84 dAQLAAA--GITTVFDALSVGDEED----GGLRSRDLARKLIDAIE--------EARARGLLRADHRLHLR--------C 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 168 -LAAHALPPEYAGRADDYIEHICSTM-----------LPALA-----GEGLVDA-VDAFCEHL-----AFSPAQVERVFI 224
Cdd:PRK15446 142 eLTNPDALELFEALLAHPRVDLVSLMdhtpgqrqfrdLEKYReyyagKYGLSDEeFDAFVEERialsaRYAPPNRRAIAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 225 AARELGLPVKLH----AE--QLSSLHGSSLAaryralsadhlEY-MTEDDARAMGEAGtVAVLLpGAFYLLR-ETQLPPI 296
Cdd:PRK15446 222 LARARGIPLASHdddtPEhvAEAHALGVAIA-----------EFpTTLEAARAARALG-MSVLM-GAPNVVRgGSHSGNV 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600285 297 DA--LRRHGVAMAIASDLNPGTspalslrlMLNMACTLFR---LTPEETLAGVTLHAARALGLeASHGSLEVGKLADFV 370
Cdd:PRK15446 289 SAldLAAAGLLDILSSDYYPAS--------LLDAAFRLADdggLDLPQAVALVTANPARAAGL-DDRGEIAPGKRADLV 358
|
|
| YcjU |
COG0637 |
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism]; |
225-358 |
2.57e-03 |
|
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
Pssm-ID: 440402 [Multi-domain] Cd Length: 208 Bit Score: 39.04 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 225 AARELGLPvkLHAEQLSSLHGSSLAaryralsaDHLEYMTEDDARAMGEAGTVAVLLPGAFYLLRETQLPPI-------D 297
Cdd:COG0637 27 AFAELGID--LTEEEYRRLMGRSRE--------DILRYLLEEYGLDLPEEELAARKEELYRELLAEEGLPLIpgvvellE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 298 ALRRHGVAMAIASdlnpgTSPALSLRLMLNMA--CTLF--RLTPEETLAG-----VTLHAARALGLEASH 358
Cdd:COG0637 97 ALKEAGIKIAVAT-----SSPRENAEAVLEAAglLDYFdvIVTGDDVARGkpdpdIYLLAAERLGVDPEE 161
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
26-68 |
3.81e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 39.15 E-value: 3.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15600285 26 LVTDGPLIHwIGPRAELPPGdyAERIDLGGAWLTPGLIDCHTH 68
Cdd:PRK05985 20 LIRDGRIAA-IGPALAAPPG--AEVEDGGGALALPGLVDGHIH 59
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
341-373 |
3.84e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 39.30 E-value: 3.84e-03
10 20 30
....*....|....*....|....*....|...
gi 15600285 341 LAGVTLHAARALGLEASHGSLEVGKLADFVAWD 373
Cdd:PRK13308 406 IAKYTINPAITFGIDDHIGSLEPGKLADIVLWR 438
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
263-373 |
4.77e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 38.92 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 263 MTEDDARAMGEAGTVavllpgafyLLRETQLPPIDALRRHGVamaiasdlnPGTSPALSLRLmlnmactlfrltpEETLA 342
Cdd:PRK13206 363 MIGSDSQAMGRIGEV---------VLRTWQTAHVMKRRRGAL---------PGDGRADNNRA-------------RRYVA 411
|
90 100 110
....*....|....*....|....*....|.
gi 15600285 343 GVTLHAARALGLEASHGSLEVGKLADFVAWD 373
Cdd:PRK13206 412 KYTICPAVAHGIDHEIGSVEVGKLADLVLWE 442
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
295-373 |
4.96e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 39.06 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 295 PIDALRRHGVAMAIASD---LNPGTSPALSLRLMLNMACTLF---RLTPEETLAGVTLHAARALGlEASHGSLEVGKLAD 368
Cdd:PRK08203 305 PVRELRAAGVPVGLGVDgsaSNDGSNLIGEARQALLLQRLRYgpdAMTAREALEWATLGGARVLG-RDDIGSLAPGKLAD 383
|
....*
gi 15600285 369 FVAWD 373
Cdd:PRK08203 384 LALFD 388
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
259-377 |
7.85e-03 |
|
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: 38.21 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600285 259 HLEYMTEDDARAMGEAGTVAVLLPGAFYLLRETqLPPIDALRRHGVAMAIASDLNPGTSPALSLRLM------------- 325
Cdd:cd01313 262 HATHLTDNETLLLGRSGAVVGLCPTTEANLGDG-IFPAAALLAAGGRIGIGSDSNARIDLLEELRQLeysqrlrdrarnv 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15600285 326 LNMACTLfrlTPEETLAGVTLHAARALGLEAshGSLEVGKLADFVAWDIERP 377
Cdd:cd01313 341 LATAGGS---SARALLDAALAGGAQALGLAT--GALEAGARADLLSLDLDHP 387
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
40-97 |
9.30e-03 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 37.84 E-value: 9.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600285 40 AELPPGDYAERIDLGGAWLTPGLIDCHTH--AVFGGNRSGE-FEqrlegvsYAEIAAAGGG 97
Cdd:PRK08323 29 AAIGANLGDEVIDATGKYVMPGGIDPHTHmeMPFGGTVSSDdFE-------TGTRAAACGG 82
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
341-378 |
9.64e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 38.23 E-value: 9.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15600285 341 LAGVTLHAARALGLeaSH--GSLEVGKLADFVAWdieRPA 378
Cdd:PRK13207 405 IAKYTINPAIAHGI--SHevGSVEVGKLADLVLW---KPA 439
|
|
| |
