|
Name |
Accession |
Description |
Interval |
E-value |
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
31-398 |
2.64e-174 |
|
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: 491.00 E-value: 2.64e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 31 DGTIAWTGRASDVPAGYVHWPRE-DLRGAWVTPGLVDCHTHLVYGGQRADEFAQRLAGVSYEEIARRGGGIVSTVRATRD 109
Cdd:cd01296 5 DGRIAAVGPAASLPAPGPAAAEEiDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVRATRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 110 ASEATLFEQAAARLRPLLAEGVTAIEIKSGYGLELASERRMLRVARQLGERFPVSVYTTFLGAHALPPEYAGRaDEYVDE 189
Cdd:cd01296 85 ASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGR-EEYIDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 190 VCERMLPALADEGLVDAVDVFCERIGFTLAQSERVFEAAARRGLPVKMHAEQLSGGGGAALAARYRALSADHLEYLDEAG 269
Cdd:cd01296 164 VIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHTSDEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 270 VAAMRASGTTAVLLPGAYYFIRETKqPPIDLLRRHGVPIALATDHNPGTSPLTSLLLTMNMGCTLFKLTVQEALLGVTRH 349
Cdd:cd01296 244 IAALAEAGTVAVLLPGTAFSLRETY-PPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTAATIN 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497575932 350 AAAALGAGDRHGSLAPGRQADFAVWSAATLAELAYWFGRPLCERVVKGG 398
Cdd:cd01296 323 AAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
21-398 |
6.72e-157 |
|
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: 447.24 E-value: 6.72e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 21 IADAAIAVNGdGTIAWTGRASDVPaGYVHWPREDLRGAWVTPGLVDCHTHLVYGGQRADEFAQRLAGVSYEEIARRGGGI 100
Cdd:TIGR01224 1 IEDAVILIHG-GKIVWIGQLAALP-GEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 101 VSTVRATRDASEATLFEQAAARLRPLLAEGVTAIEIKSGYGLELASERRMLRVARQLGERFPVSVYTTFLGAHALPPEYA 180
Cdd:TIGR01224 79 LSTVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 181 GRADEYVDEVCERMLPALADEGLVDAVDVFCERIGFTLAQSERVFEAAARRGLPVKMHAEQLSGGGGAALAARYRALSAD 260
Cdd:TIGR01224 159 GRPDDYVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 261 HLEYLDEAGVAAMRASGTTAVLLPGAYYFIRETKqPPIDLLRRHGVPIALATDHNPGTSPLTSLLLTMNMGCTLFKLTVQ 340
Cdd:TIGR01224 239 HLEHASDAGIKALAEAGTVAVLLPGTTFYLRETY-PPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPE 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 497575932 341 EALLGVTRHAAAALGAGDRHGSLAPGRQADFAVWSAATLAELAYWFGRPLCERVVKGG 398
Cdd:TIGR01224 318 EALHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNG 375
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-402 |
5.31e-78 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 246.03 E-value: 5.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 1 MKSTLWHNLKLcAHGDPNDTIADAAIAVNgDGTIAWTGRASDV--PAGYVhwpREDLRGAWVTPGLVDCHTHLVYGGQRA 78
Cdd:COG1228 7 AGTLLITNATL-VDGTGGGVIENGTVLVE-DGKIAAVGPAADLavPAGAE---VIDATGKTVLPGLIDAHTHLGLGGGRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 79 DEFAQrlagvsyeeiarrGGGIVSTVratrdaseaTLFEQAAARLRPLLAEGVTAIEIKSGYGLEL-----ASERRMLRV 153
Cdd:COG1228 82 VEFEA-------------GGGITPTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPLGLrdaiiAGESKLLPG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 154 ARQLGERFPVSVyttFLGAHAlppeyagradEYVDEvCERMLPALADEGlVDAVDVFCE--RIGFTLAQSERVFEAAARR 231
Cdd:COG1228 140 PRVLAAGPALSL---TGGAHA----------RGPEE-ARAALRELLAEG-ADYIKVFAEggAPDFSLEELRAILEAAHAL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 232 GLPVKMHAEQLSGGGGAALAARYralSADHLEYLDEAGVAAMRASGTTaVLLPGAYYF-----------------IRETK 294
Cdd:COG1228 205 GLPVAAHAHQADDIRLAVEAGVD---SIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFlallegaaapvaakarkVREAA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 295 QPPIDLLRRHGVPIALATDHNPGTSPLTSLLLTMNMGCtLFKLTVQEALLGVTRHAAAALGAGDRHGSLAPGRQADFAVW 374
Cdd:COG1228 281 LANARRLHDAGVPVALGTDAGVGVPPGRSLHRELALAV-EAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLL 359
|
410 420
....*....|....*....|....*...
gi 497575932 375 SAATLAELAYWfgrPLCERVVKGGVTVF 402
Cdd:COG1228 360 DGDPLEDIAYL---EDVRAVMKDGRVVD 384
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
14-380 |
8.50e-28 |
|
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: 113.77 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 14 HGDPNDT-IADAAIAVNgDGTIAWTGRASDVPAGYVHWPREDLRGAWVTPGLVDCHTHLVYGGQRA----DEFAQRLAGV 88
Cdd:COG0402 11 TMDPAGGvLEDGAVLVE-DGRIAAVGPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGladdLPLLDWLEEY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 89 SYEEIARRgggivsTVRATRDASEATLFEqaaarlrpLLAEGVTAI-EIksgYGLELASERRMLRVARQLGERFpvsVYT 167
Cdd:COG0402 90 IWPLEARL------DPEDVYAGALLALAE--------MLRSGTTTVaDF---YYVHPESADALAEAAAEAGIRA---VLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 168 TFLGAHALPPEYAGRADEYVDEvCERMLPALADEGLvdavdvfcERIGFTLA----------QSERVFEAAARRGLPVKM 237
Cdd:COG0402 150 RGLMDRGFPDGLREDADEGLAD-SERLIERWHGAAD--------GRIRVALAphapytvspeLLRAAAALARELGLPLHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 238 H-AEQLsggggAALAARYRALSADHLEYLDEAGV------------------AAMRASGTTAVLLPGAYYF----Iretk 294
Cdd:COG0402 221 HlAETR-----DEVEWVLELYGKRPVEYLDELGLlgprtllahcvhltdeeiALLAETGASVAHCPTSNLKlgsgI---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 295 qPPIDLLRRHGVPIALATDhNPGTSPLTSLLLTMNMGCTLFK--------LTVQEALLGVTRHAAAALGAGDRHGSLAPG 366
Cdd:COG0402 292 -APVPRLLAAGVRVGLGTD-GAASNNSLDMFEEMRLAALLQRlrggdptaLSAREALEMATLGGARALGLDDEIGSLEPG 369
|
410
....*....|....
gi 497575932 367 RQADFAVWSAATLA 380
Cdd:COG0402 370 KRADLVVLDLDAPH 383
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
15-405 |
2.26e-16 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 80.61 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 15 GDPNDTIADAaIAVNgDGTIAWTGRASDVPAGYVHWPRE-DLRGAWVTPGLVDCHTHLVYGGQRA-----------DEFA 82
Cdd:COG1574 20 MDPAQPVAEA-VAVR-DGRIVAVGSDAEVRALAGPATEViDLGGKTVLPGFIDAHVHLLGGGLALlgvdlsgarslDELL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 83 QRLA-------------GVSYEE------------------------IARRGG--GIVSTV--------RAT-------- 107
Cdd:COG1574 98 ARLRaaaaelppgewilGRGWDEslwpegrfptradldavspdrpvvLTRVDGhaAWVNSAalelagitADTpdpeggei 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 108 -RDAS-EAT--LFEQAAARLRPLLAEgVTAIEIKSGYglelaseRRMLRVARQLG---------ERFPVSVYTTFLGAHA 174
Cdd:COG1574 178 eRDADgEPTgvLREAAMDLVRAAIPP-PTPEELRAAL-------RAALRELASLGitsvhdaglGPDDLAAYRELAAAGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 175 LPPE---YAGRADEYVDEVCER-MLPALADEGL-VDAVDVF----------------CERIG------FTLAQSERVFEA 227
Cdd:COG1574 250 LPLRvvlYLGADDEDLEELLALgLRTGYGDDRLrVGGVKLFadgslgsrtaallepyADDPGnrglllLDPEELRELVRA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 228 AARRGLPVKMHA-------------EQLSGGGGAalaaryralsAD------HLEYLDEAGVAAMRASGTTAVLLPG-AY 287
Cdd:COG1574 330 ADAAGLQVAVHAigdaavdevldayEAARAANGR----------RDrrhrieHAQLVDPDDLARFAELGVIASMQPThAT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 288 YFI----------RETKQPPIDLLRRHGVPIALATDhnpgtSPLTSL--LLTM-------NMGCTLF----KLTVQEALL 344
Cdd:COG1574 400 SDGdwaedrlgpeRAARAYPFRSLLDAGAPLAFGSD-----APVEPLdpLLGIyaavtrrTPSGRGLgpeeRLTVEEALR 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497575932 345 GVTRHAAAALGAGDRHGSLAPGRQADFAVWS-------AATLAELAywfgrplCERVVKGGVTVFARD 405
Cdd:COG1574 475 AYTIGAAYAAFEEDEKGSLEPGKLADFVVLDrdpltvpPEEIKDIK-------VLLTVVGGRVVYEAE 535
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
59-401 |
1.31e-14 |
|
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: 74.46 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 59 WVTPGLVDCHTHLVYGGQRADefaqrlagvsyeeiarrgggivstvratrDASEATLFEQAAARLRPLLAEGVTAIeIKS 138
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGI-----------------------------PVPPEFAYEALRLGITTMLKSGTTTV-LDM 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 139 GYGLELASErRMLRVARQ--LGERFPVS-VYTTFLGAHALPPEYAGRADEYVDEVCermlpALADEGLVDAVDVFcERIG 215
Cdd:pfam01979 51 GATTSTGIE-ALLEAAEElpLGLRFLGPgCSLDTDGELEGRKALREKLKAGAEFIK-----GMADGVVFVGLAPH-GAPT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 216 FTLAQSERVFEAAARRGLPVKMHA-EQLSGGGGAALAARYRALSADHLEYLDEAG----VAAMRASGTTA---------- 280
Cdd:pfam01979 124 FSDDELKAALEEAKKYGLPVAIHAlETKGEVEDAIAAFGGGIEHGTHLEVAESGGlldiIKLILAHGVHLspteanllae 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 281 -------VLLPGAYYFIRETKQPPIDLLRRhGVPIALATDHNPGTSPLTSLLLTMNMGCTLF----KLTVQEALLGVTRH 349
Cdd:pfam01979 204 hlkgagvAHCPFSNSKLRSGRIALRKALED-GVKVGLGTDGAGSGNSLNMLEELRLALELQFdpegGLSPLEALRMATIN 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 497575932 350 AAAALGAGDRHGSLAPGRQADFAVWSAATLAELAYWFGRPLCERVVKGGVTV 401
Cdd:pfam01979 283 PAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
7-401 |
3.59e-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: 73.44 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 7 HNLKLcahGDPNDTIADAAIAvngDGTIAWTGRASDVPAGYVHWpreDLRGAWVTPGLVDCHTHL--VYGGQRadefaqr 84
Cdd:cd01293 3 RNARL---ADGGTALVDIAIE---DGRIAAIGPALAVPPDAEEV---DAKGRLVLPAFVDPHIHLdkTFTGGR------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 85 lagVSYEEIARRGGGIVSTVRATRDASEATLFEQAAARLRPLLAEGVTAI----EIKSGYGLELASErrMLRVARQLGER 160
Cdd:cd01293 67 ---WPNNSGGTLLEAIIAWEERKLLLTAEDVKERAERALELAIAHGTTAIrthvDVDPAAGLKALEA--LLELREEWADL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 161 -------FPVSVYTTFLGAHAL----------------PPEYAGRADEYVDEVCErmlpaLADEGLVDaVDVFC----ER 213
Cdd:cd01293 142 idlqivaFPQHGLLSTPGGEELmrealkmgadvvggipPAEIDEDGEESLDTLFE-----LAQEHGLD-IDLHLdetdDP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 214 IGFTLaqsERVFEAAARRGLPVKM---HAEQLSGGGGAALAARyralsadhLEYLDEAGVAAMrASGTTAVLLPGA-YYF 289
Cdd:cd01293 216 GSRTL---EELAEEAERRGMQGRVtcsHATALGSLPEAEVSRL--------ADLLAEAGISVV-SLPPINLYLQGReDTT 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 290 IRETKQPPIDLLRRHGVPIALATDH--NPgTSPLTS--LLLTMNMGCTLFKLTVQE----ALLGVTRHAAAALGAGDrhG 361
Cdd:cd01293 284 PKRRGVTPVKELRAAGVNVALGSDNvrDP-WYPFGSgdMLEVANLAAHIAQLGTPEdlalALDLITGNAARALGLED--Y 360
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 497575932 362 SLAPGRQADFAVWSAATLAELAYwfGRPLCERVVKGGVTV 401
Cdd:cd01293 361 GIKVGCPADLVLLDAEDVAEAVA--RQPPRRVVIRKGRVV 398
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
25-373 |
4.64e-14 |
|
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: 73.50 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 25 AIAVnGDGTIAWTGRASDVPAgYVHWPRE--DLRGAWVTPGLVDCHTHLVYGGQ------------------------RA 78
Cdd:cd01300 1 AVAV-RDGRIVAVGSDAEAKA-LKGPATEviDLKGKTVLPGFIDSHSHLLLGGLsllwldlsgvtskeealariredaAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 79 DEFAQRLAGVSYEEIARRGG--------------------------GIVSTV--------RATRDASEATLFEQAAARLR 124
Cdd:cd01300 79 APPGEWILGFGWDESLLGEGryptraeldavspdrpvlllrrdghsAWVNSAalrlagitRDTPDPPGGEIVRDADGEPT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 125 PLLAEGVTAIEIKSGYGLELASERRMLRVARQ--------------LGERFPVSVYTTFLGAHALP------PEYAGRAD 184
Cdd:cd01300 159 GVLVEAAAALVLEAVPPPTPEERRAALRAAARelaslgvttvhdagGGAADDIEAYRRLAAAGELTlrvrvaLYVSPLAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 185 EYVDEVCERMLPALADEGLVDAVDVF----------------------CERIGFTLAQSERVFEAAARRGLPVKMHA--- 239
Cdd:cd01300 239 DLLEELGARKNGAGDDRLRLGGVKLFadgslgsrtaalsepyldspgtGGLLLISPEELEELVRAADEAGLQVAIHAigd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 240 ----------EQLsgggGAALAARYRALSADHLEYLDEAGVAAMRASGTTAVLLPGAYYFI------------RETKQPP 297
Cdd:cd01300 319 ravdtvldalEAA----LKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDgdaaedrrlgeeRAKRSYP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 298 IDLLRRHGVPIALATDHNPGT-SPLTSLLLTMN--------MGCTLFKLTVQEALLGVTRHAAAALGAGDRHGSLAPGRQ 368
Cdd:cd01300 395 FRSLLDAGVPVALGSDAPVAPpDPLLGIWAAVTrktpgggvLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKL 474
|
....*
gi 497575932 369 ADFAV 373
Cdd:cd01300 475 ADFVV 479
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
64-353 |
1.06e-12 |
|
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: 67.74 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 64 LVDCHTHLVYGGQRADEFAQRLAGVSYeeiarrgggivstvratrdASEATLFEQAAARLRPLLAEGVTAIEIKSGYGLE 143
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEE-------------------LSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 144 LASERRMLRVARQLGERFPVSVYTtFLGAHALPPEYAGRADEYVDEVCERMLPALADeglVDAVDVFCERIGFTLAQSER 223
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRVVL-GLGIPGVPAAVDEDAEALLLELLRRGLELGAV---GLKLAGPYTATGLSDESLRR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 224 VFEAAARRGLPVKMHAEQLSGGGGA-----ALAARYRALSADHLEYLDEAGVAAMRASGTTAVLLPG--AYYFIRETKQP 296
Cdd:cd01292 138 VLEEARKLGLPVVIHAGELPDPTRAledlvALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLsnYLLGRDGEGAE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 497575932 297 PIDLLRRHGVPIALATDHNPGTSPLTsLLLTMNMGCTLFKL--TVQEALLGVTRHAAAA 353
Cdd:cd01292 218 ALRRLLELGIRVTLGTDGPPHPLGTD-LLALLRLLLKVLRLglSLEEALRLATINPARA 275
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
31-402 |
2.14e-11 |
|
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: 64.64 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 31 DGTIAWTGRASDVPAGYVhwpREDLRGAWVTPGLVDCHTHL-------VYGGQRADEF-----AQRLAGVSYE------E 92
Cdd:cd01309 1 DGKIVAVGAEITTPADAE---VIDAKGKHVTPGLIDAHSHLgldeeggVRETSDANEEtdpvtPHVRAIDGINpddeafK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 93 IARRGGgiVSTVRATrdASEATLFEQAAARLRplLAEGVTAIEIKSGY-GLELASERRMLRVARQlGERFPvsvyTTFLG 171
Cdd:cd01309 78 RARAGG--VTTVQVL--PGSANLIGGQGVVIK--TDGGTIEDMFIKAPaGLKMALGENPKRVYGG-KGKEP----ATRMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 172 AHALPPEYAGRADEYVdevcERMLPALADEGLVDAVDVFCERIGftlaqservfeAAARRGLPVKMHAEQLSGGGGAALA 251
Cdd:cd01309 147 VAALLRDAFIKAQEYG----RKYDLGKNAKKDPPERDLKLEALL-----------PVLKGEIPVRIHAHRADDILTAIRI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 252 ARYRA--LSADHleYLDEAGVA-AMRASGTTAVLLP--GAYYFIRETKQP---PIDLLRRHGVPIALATDHNpgTSPLTS 323
Cdd:cd01309 212 AKEFGikITIEH--GAEGYKLAdELAKHGIPVIYGPtlTLPKKVEEVNDAidtNAYLLKKGGVAFAISSDHP--VLNIRN 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497575932 324 LLLTMNMGCTlFKLTVQEALLGVTRHAAAALGAGDRHGSLAPGRQADFAVWSAATLAELAYwfgrplCERVVKGGVTVF 402
Cdd:cd01309 288 LNLEAAKAVK-YGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSK------PEQVYIDGRLVY 359
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
54-402 |
6.18e-11 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 63.70 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 54 DLRGAWVTPGLVDCHTHLVYGGQRADEFA--------------------QRLAGVSYEEI---------------ARRGG 98
Cdd:pfam07969 4 DAKGRLVLPGFVDPHTHLDGGGLNLRELRlpdvlpnavvkgqagrtpkgRWLVGEGWDEAqfaetrfpyaladldEVAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 99 GIV--------STVRATR-----DASEATLFEQAAARLRPLLAEGVTAI-EIKSGYGLELASERRMLRVARQLGERFPVS 164
Cdd:pfam07969 84 GPVllralhthAAVANSAaldlaGITKATEDPPGGEIARDANGEGLTGLlREGAYALPPLLAREAEAAAVAAALAALPGF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 165 VYTTFLGAHAL---PPEY--------AGRADEYVDEVCERMLPALADEGLVDAVDVF---------------------CE 212
Cdd:pfam07969 164 GITSVDGGGGNvhsLDDYeplreltaAEKLKELLDAPERLGLPHSIYELRIGAMKLFadgvlgsrtaaltepyfdapgTG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 213 RIGFTLAQSERVFEAAARRGLPVKMHAEQ--------LSGGGGAALAARYRALSADH---LEYLDEAGVAAMRASGTTAV 281
Cdd:pfam07969 244 WPDFEDEALAELVAAARERGLDVAIHAIGdatidtalDAFEAVAEKLGNQGRVRIEHaqgVVPYTYSQIERVAALGGAAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 282 LLPGAYYFIRETKQ-----------PPIDLLRRHGVPIALATDHNPGT----SPLTSLL-LTMNMGCTLF----KLTVQE 341
Cdd:pfam07969 324 VQPVFDPLWGDWLQdrlgaerarglTPVKELLNAGVKVALGSDAPVGPfdpwPRIGAAVmRQTAGGGEVLgpdeELSLEE 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497575932 342 ALLGVTRHAAAALGAGDRHGSLAPGRQADFAVWSAATL----AELAYwfgrPLCERVVKGGVTVF 402
Cdd:pfam07969 404 ALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLtvdpPAIAD----IRVRLTVVDGRVVY 464
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
261-373 |
9.95e-11 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 62.90 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 261 HLEYLDEAGVAAMRASGTTAVLLP------GAYYFiretkqpPIDLLRRHGVPIALATDHNPGTSplTSLLLTMNMG--- 331
Cdd:PRK09228 270 HCIHLEDRERRRLAETGAAIAFCPtsnlflGSGLF-------DLKRADAAGVRVGLGTDVGGGTS--FSMLQTMNEAykv 340
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 497575932 332 CTL--FKLTVQEALLGVTRHAAAALGAGDRHGSLAPGRQADFAV 373
Cdd:PRK09228 341 QQLqgYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVV 384
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
11-374 |
2.64e-08 |
|
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: 55.29 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 11 LCAHGDPNDTIADAAIAVNgDGTIAWTGRASDVPAgyvhWPRE---DLRGAWVTPGLVDCHTHLVYGGQRA----DEFAQ 83
Cdd:cd01298 7 TIVTTDPRRVLEDGDVLVE-DGRIVAVGPALPLPA----YPADeviDAKGKVVMPGLVNTHTHLAMTLLRGladdLPLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 84 RLAGVsYEEIARRgggivSTVRATRDASEATLFEqaaarlrpLLAEGVT-AIEIKSGYGLELAserrmlRVARQLGERFP 162
Cdd:cd01298 82 WLKDL-IWPLERL-----LTEEDVYLGALLALAE--------MIRSGTTtFADMYFFYPDAVA------EAAEELGIRAV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 163 VSvYTTFlgahALPPEYAGRADEYVDEvCERMLPA--LADEGLVDAVdvFCERIGFTL--AQSERVFEAAARRGLPVKMH 238
Cdd:cd01298 142 LG-RGIM----DLGTEDVEETEEALAE-AERLIREwhGAADGRIRVA--LAPHAPYTCsdELLREVAELAREYGVPLHIH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 239 -AEqlSGGGGAALAARYRALSADHLE---------------YLDEAGVAAMRASGTTAVLLPGAYYfiretKQ----PPI 298
Cdd:cd01298 214 lAE--TEDEVEESLEKYGKRPVEYLEelgllgpdvvlahcvWLTDEEIELLAETGTGVAHNPASNM-----KLasgiAPV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 299 DLLRRHGVPIALATDHNPGTSPLtSLLLTMNMGCTLFK--------LTVQEALLGVTRHAAAALGAGDRhGSLAPGRQAD 370
Cdd:cd01298 287 PEMLEAGVNVGLGTDGAASNNNL-DMFEEMRLAALLQKlahgdptaLPAEEALEMATIGGAKALGLDEI-GSLEVGKKAD 364
|
....
gi 497575932 371 FAVW 374
Cdd:cd01298 365 LILI 368
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
261-396 |
3.12e-08 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 55.36 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 261 HLEYLDEAGVAAMRASGTTAVLLP--------GAYyfiretkqpPIDLLRRHGVPIALATDHNPGTSPltSLLLTM---- 328
Cdd:cd01303 267 HCVHLSEEEFNLLKERGASVAHCPtsnlflgsGLF---------DVRKLLDAGIKVGLGTDVGGGTSF--SMLDTLrqay 335
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497575932 329 ------NMGCT-LFKLTVQEALLGVTRHAAAALGAGDRHGSLAPGRQADFAV--WSAATLAELAYWFGRPLCERVVK 396
Cdd:cd01303 336 kvsrllGYELGgHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVidPSATPLLADRMFRVESLEEALFK 412
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
54-373 |
1.02e-07 |
|
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: 53.45 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 54 DLRGAWVTPGLVDCHTHLvyGGQRADEFAQRLAGVSYEEI---------ARRGggiVSTVR--------ATRDASEATLF 116
Cdd:cd01299 5 DLGGKTLMPGLIDAHTHL--GSDPGDLPLDLALPVEYRTIratrqaraaLRAG---FTTVRdaggadygLLRDAIDAGLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 117 EqaAARLRPllaeGVTAIEIKSGYGlelaserrmlrvarqlgerfpvsvytTFLGAHALPPEYAGRAdeYVDEVCErmLP 196
Cdd:cd01299 80 P--GPRVFA----SGRALSQTGGHG--------------------------DPRGLSGLFPAGGLAA--VVDGVEE--VR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 197 ALADEGLVDAVDVF--------------CERIGFTLAQSERVFEAAARRGLPVKMHAEqlsGGGGAALAARYRALSADHL 262
Cdd:cd01299 124 AAVREQLRRGADQIkimatggvlspgdpPPDTQFSEEELRAIVDEAHKAGLYVAAHAY---GAEAIRRAIRAGVDTIEHG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 263 EYLDEAGVAAMRASGTTAVLLPGAYYFIRETKQPP-----------------IDLLRR---HGVPIALATDHNPGTSPLT 322
Cdd:cd01299 201 FLIDDETIELMKEKGIFLVPTLATYEALAAEGAAPglpadsaekvalvleagRDALRRahkAGVKIAFGTDAGFPVPPHG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 497575932 323 SLLLTMNMgctLFK--LTVQEALLGVTRHAAAALGAGDRHGSLAPGRQADFAV 373
Cdd:cd01299 281 WNARELEL---LVKagGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLV 330
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
32-373 |
9.18e-07 |
|
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: 50.53 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 32 GTIAWTGRASDVPAGYVHWPREDLRGAWVTPGLVDCHTHLvyggqradEFAQRLAGVSYeeiaRRGGGIVSTVRATRDAS 111
Cdd:cd01312 1 DKILEVGDYEKLEKRYPGAKHEFFPNGVLLPGLINAHTHL--------EFSANVAQFTY----GRFRAWLLSVINSRDEL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 112 EATLFEQAAAR-LRPLLAEGVTAIEIKSGYGLELAserrmLRVARQLGERFpvsvYTTFLGAH-----ALPPEYAGRADE 185
Cdd:cd01312 69 LKQPWEEAIRQgIRQMLESGTTSIGAISSDGSLLP-----ALASSGLRGVF----FNEVIGSNpsaidFKGETFLERFKR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 186 YVDEVCERMLPALA--------DEGLVDAVDV-----------FCErigfTLAQSERVFEAAA---------RRGLPVKM 237
Cdd:cd01312 140 SKSFESQLFIPAISphapysvhPELAQDLIDLakklnlplsthFLE----SKEEREWLEESKGwfkhfwesfLKLPKPKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 238 HA------EQLSGGGGAAlaaryralSADHLEYLDEAGVAAMRASGTTAVLLPGAYYfIRETKQPPIDLLRRHGVPIALA 311
Cdd:cd01312 216 LAtaidflDMLGGLGTRV--------SFVHCVYANLEEAEILASRGASIALCPRSNR-LLNGGKLDVSELKKAGIPVSLG 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497575932 312 TD---HNPGTS---PLTSLLLTMNMGCTLFklTVQEALLGVTRHAAAALGAGDrhGSLAPGRQADFAV 373
Cdd:cd01312 287 TDglsSNISLSlldELRALLDLHPEEDLLE--LASELLLMATLGGARALGLNN--GEIEAGKRADFAV 350
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
21-373 |
1.76e-06 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 49.62 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 21 IADAAIAVNGDGTIAWTGRASDVPagyvhwpreDLRGAWVTPGLVDCHTHLVYGGQRADEFAQRLAGVSYEEIARRGGGI 100
Cdd:PRK06687 26 VKDSQIVYVGQDKPAFLEQAEQII---------DYQGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAESEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 101 vsTVRATRDASEATLFEqaaarlrpLLAEGVTAI-EIKSGYGLELaseRRMLRVARQLGERFPVSVyTTFLGAHALPPEY 179
Cdd:PRK06687 97 --TPDMTTNAVKEALTE--------MLQSGTTTFnDMYNPNGVDI---QQIYQVVKTSKMRCYFSP-TLFSSETETTAET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 180 AGRADEYVDEVC-------ERML----PALADEGLVDAVDVFCERIGFTLaqSERVFEAAARRGLPVKMHAEQLSGGGGA 248
Cdd:PRK06687 163 ISRTRSIIDEILkyknpnfKVMVaphsPYSCSRDLLEASLEMAKELNIPL--HVHVAETKEESGIILKRYGKRPLAFLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 249 ALAARYRALSADHLEyLDEAGVAAMRASGTTAVLLPGAYYFIRETKQPPIDLLRRhGVPIALATDHNPGTSPL------- 321
Cdd:PRK06687 241 LGYLDHPSVFAHGVE-LNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKA-GVAVGIATDSVASNNNLdmfeegr 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 497575932 322 -TSLLLTMNMGcTLFKLTVQEALLGVTRHAAAALGAGDRHGSLAPGRQADFAV 373
Cdd:PRK06687 319 tAALLQKMKSG-DASQFPIETALKVLTIEGAKALGMENQIGSLEVGKQADFLV 370
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
1-405 |
2.68e-06 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 49.16 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 1 MKSTLWHNLKLcahgdPNDTIADAAIAvngDGTIAWTGRASDVPAGYvhwPREDLRGAWVTPGLVDCHTHL---VYGG-- 75
Cdd:PRK05985 1 MTDLLFRNVRP-----AGGAAVDILIR---DGRIAAIGPALAAPPGA---EVEDGGGALALPGLVDGHIHLdktFWGDpw 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 76 ---QRADEFAQRLAGvsyeeiarrgggivstVRATRDASEATLFEQAAARLRPLLAEGVTAI----EIKSGYGleLASER 148
Cdd:PRK05985 70 ypnEPGPSLRERIAN----------------ERRRRAASGHPAAERALALARAAAAAGTTAMrshvDVDPDAG--LRHLE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 149 RMLRVARQLGER-------FPVSVYTTFLGAHALppeyagrADEYVDEVCER---MLPALAD---EGLVDAVDVFCERIG 215
Cdd:PRK05985 132 AVLAARETLRGLidiqivaFPQSGVLSRPGTAEL-------LDAALRAGADVvggLDPAGIDgdpEGQLDIVFGLAERHG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 216 ------------FTLAQSERVFEAAARRGLPVKM---HAEQLSGGGGAALAARyralsadhLEYLDEAGVAAMrasgTTA 280
Cdd:PRK05985 205 vgidihlhepgeLGAFQLERIAARTRALGMQGRVavsHAFCLGDLPEREVDRL--------AERLAEAGVAIM----TNA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 281 vllPGAYYFiretkqPPIDLLRRHGVPIALATDHNPGT-SPLTS-------LLLTMNMGctlfkLTVQEALLG----VTR 348
Cdd:PRK05985 273 ---PGSVPV------PPVAALRAAGVTVFGGNDGIRDTwWPYGNgdmleraMLIGYRSG-----FRTDDELAAaldcVTH 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 497575932 349 HAAAALGAgDRHGsLAPGRQADFAVWSAATLAELAywFGRPLCERVVKGGVTVfARD 405
Cdd:PRK05985 339 GGARALGL-EDYG-LAVGARADFVLVDAETVAEAV--VAVPVRRLVVRGGRIV-ARD 390
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-88 |
3.64e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 48.69 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 5 LWHNLKLCAHGDPNDTIADAAIAvngDGTIAWTGRASDVPAGYVHWpreDLRGAWVTPGLVDCHTHLVYG----GQRADE 80
Cdd:PRK09237 2 LLRGGRVIDPANGIDGVIDIAIE---DGKIAAVAGDIDGSQAKKVI---DLSGLYVSPGWIDLHVHVYPGstpyGDEPDE 75
|
....*...
gi 497575932 81 FAQRlAGV 88
Cdd:PRK09237 76 VGVR-SGV 82
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
19-88 |
3.88e-05 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 45.54 E-value: 3.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497575932 19 DTIADAAIAvngDGTIAWTGRASDVPAGYVhwpREDLRGAWVTPGLVDCHTHLVYGGQ----RADEFAQRlAGV 88
Cdd:COG3964 17 DGVMDIAIK---DGKIAAVAKDIDAAEAKK---VIDASGLYVTPGLIDLHTHVFPGGTdygvDPDGVGVR-SGV 83
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
16-70 |
4.78e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 45.09 E-value: 4.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 497575932 16 DPNDTIADAAIAVNgDGTIAWTGRASDVPAgyvhwPREDLRGAWVTPGLVDCHTH 70
Cdd:COG1820 9 TGDGVLEDGALLIE-DGRIAAIGPGAEPDA-----EVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
225-371 |
1.00e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 44.22 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 225 FEAAARRGLPVKMHAEQLSGGGGAALAARYRAL---SAD----HLEYLDEAGVAAMRASGTTAVLLPGAyyfirETKQ-- 295
Cdd:PRK08204 207 FRLARELGLPISMHQGFGPWGATPRGVEQLHDAgllGPDlnlvHGNDLSDDELKLLADSGGSFSVTPEI-----EMMMgh 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 296 --PPIDLLRRHGVPIALATDHNPGTS--PLTS--LLLTMN---MGCTLF----------KLTVQEALLGVTRHAAAALGA 356
Cdd:PRK08204 282 gyPVTGRLLAHGVRPSLGVDVVTSTGgdMFTQmrFALQAErarDNAVHLreggmppprlTLTARQVLEWATIEGARALGL 361
|
170
....*....|....*
gi 497575932 357 GDRHGSLAPGRQADF 371
Cdd:PRK08204 362 EDRIGSLTPGKQADL 376
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
297-373 |
1.01e-04 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 44.19 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 297 PIDLLRRHGVPIALATDhnpGTSPLTSLLLTMNMGCTLFKLT-------VQEALLGVTRHAAAALGAGDrhGSLAPGRQA 369
Cdd:PRK08418 295 DLEKAKKAGINYSIATD---GLSSNISLSLLDELRAALLTHAnmpllelAKILLLSATRYGAKALGLNN--GEIKEGKDA 369
|
....
gi 497575932 370 DFAV 373
Cdd:PRK08418 370 DLSV 373
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
3-71 |
1.72e-04 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 43.69 E-value: 1.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497575932 3 STLW--HNLKLCAHGDPNDTIADAAIAVNGdGTIAWTGRASDVPAGYVHwpREDLRGAWVTPGLVDCHTHL 71
Cdd:PRK08203 1 TTLWikNPLAIVTMDAARREIADGGLVVEG-GRIVEVGPGGALPQPADE--VFDARGHVVTPGLVNTHHHF 68
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
21-70 |
4.52e-04 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 42.47 E-value: 4.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 497575932 21 IADAAIAvngDGTIAWTGRASDVPAGyvhwpRE-DLRGAWVTPGLVDCHTH 70
Cdd:COG3653 21 RADVAIK---GGRIVAVGDLAAAEAA-----RViDATGLVVAPGFIDIHTH 63
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
22-83 |
6.03e-04 |
|
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: 41.82 E-value: 6.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497575932 22 ADAAIAvngDGTIAWTGRASDVPAGYvhwPREDLRGAWVTPGLVDCHTHL---VYGGQRADEFAQ 83
Cdd:cd01314 17 ADILIE---DGKIVAIGPNLEAPGGV---EVIDATGKYVLPGGIDPHTHLelpFMGTVTADDFES 75
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
15-71 |
7.77e-04 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 41.51 E-value: 7.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 497575932 15 GDPNDTIADAAIAVNgDGTIAWTGRASDVPAGYvhwPREDLRGAWVTPGLVDCHTHL 71
Cdd:PRK07583 32 GDTLEGLVLVDIEIA-DGKIAAILPAGGAPDEL---PAVDLKGRMVWPCFVDMHTHL 84
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
337-375 |
8.02e-04 |
|
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: 41.41 E-value: 8.02e-04
10 20 30
....*....|....*....|....*....|....*....
gi 497575932 337 LTVQEALLGVTRHAAAALGAGDRHGSLAPGRQADFAVWS 375
Cdd:cd00854 324 CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD 362
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
53-140 |
8.90e-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: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 53 EDLRGAWVTPGLVDCHTHLVYGGQRADeFAQRLAGVSYEEIARRGG----GIVSTVRATRDASEatLFEQAAArlrpLLA 128
Cdd:cd01308 45 VDLHGKILVPGFIDQHVHIIGGGGEGG-PSTRTPEVTLSDLTTAGVttvvGCLGTDGISRSMED--LLAKARA----LEE 117
|
90
....*....|..
gi 497575932 129 EGVTAIEIKSGY 140
Cdd:cd01308 118 EGITCFVYTGSY 129
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
297-371 |
1.04e-03 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 41.05 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 297 PIDLLRRHGVPIALATDHNPGTSPLtSLLLTMNMGCTLFK--------LTVQEALLGVTRHAAAALGAGDRHGSLAPGRQ 368
Cdd:PRK09045 293 PVAKLLQAGVNVALGTDGAASNNDL-DLFGEMRTAALLAKavagdataLPAHTALRMATLNGARALGLDDEIGSLEPGKQ 371
|
...
gi 497575932 369 ADF 371
Cdd:PRK09045 372 ADL 374
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
19-71 |
1.50e-03 |
|
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: 40.46 E-value: 1.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 497575932 19 DTIADAAIAVNgDGTIAWTGRASDVPAGyvhwpRE--DLRGAWVTPGLVDCHTHL 71
Cdd:COG0044 11 GGLERADVLIE-DGRIAAIGPDLAAPEA-----AEviDATGLLVLPGLIDLHVHL 59
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
297-384 |
1.91e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 40.22 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 297 PIDLLRRHGVPIALATD---HNPGTSPLTSL---LLTMNMGCTLFKLTVQEALLGVTRHAAAALGAGDRhGSLAPGRQAD 370
Cdd:PRK08203 305 PVRELRAAGVPVGLGVDgsaSNDGSNLIGEArqaLLLQRLRYGPDAMTAREALEWATLGGARVLGRDDI-GSLAPGKLAD 383
|
90
....*....|....
gi 497575932 371 FAVWsaaTLAELAY 384
Cdd:PRK08203 384 LALF---DLDELRF 394
|
|
| TatD_DNase |
pfam01026 |
TatD related DNase; This family of proteins are related to a large superfamily of ... |
116-240 |
6.66e-03 |
|
TatD related DNase; This family of proteins are related to a large superfamily of metalloenzymes. TatD, a member of this family has been shown experimentally to be a DNase enzyme.
Pssm-ID: 425997 [Multi-domain] Cd Length: 253 Bit Score: 38.01 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497575932 116 FEQAAARLRpllAEGVTAIeIKSGygLELASERRMLRVArqlgERFPVSVYTTFlGAHalpPEYAgraDEYVDEVCERML 195
Cdd:pfam01026 16 RDEVIERAR---EAGVTGV-VVVG--TDLEDFLRVLELA----EKYPDRVYAAV-GVH---PHEA---DEASEDDLEALE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 497575932 196 pALADEGLVDAV-----DVFCERIGfTLAQSERVFEA----AARRGLPVKMHAE 240
Cdd:pfam01026 79 -KLAEHPKVVAIgeiglDYYYVDES-PKEAQEEVFRRqlelAKELGLPVVIHTR 130
|
|
| |
