|
Name |
Accession |
Description |
Interval |
E-value |
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
5-416 |
1.20e-62 |
|
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: 207.76 E-value: 1.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 5 TLSLGARYVFPV--EGPPIADGVVAIEGGRIAWVGPARERTAD------LDLGNVAIIPGLVNAHTHLELGRLAddGAAP 76
Cdd:COG0402 1 DLLIRGAWVLTMdpAGGVLEDGAVLVEDGRIAAVGPGAELPARypaaevIDAGGKLVLPGLVNTHTHLPQTLLR--GLAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 77 PASPEnevEWLRRVMAQRRAGSSEEAYRENVGRNLRESIEAGTTLVAD-TTTAGLSWDAIAAA----PVRAVVFAEVLGL 151
Cdd:COG0402 79 DLPLL---DWLEEYIWPLEARLDPEDVYAGALLALAEMLRSGTTTVADfYYVHPESADALAEAaaeaGIRAVLGRGLMDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 152 KRYRGLQTNEAAW---------KWLGSIKPeaqvaaNARAGLSPHAPYSTAGWLYHA----AASSRLPLSTHLAEMPEEL 218
Cdd:COG0402 156 GFPDGLREDADEGladserlieRWHGAADG------RIRVALAPHAPYTVSPELLRAaaalARELGLPLHTHLAETRDEV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 219 RLLETRDG--PLRsYLEDLGAWDEewepigprptdyirkgdlrhaDWLVAHGTYIEPSEFWQFRpeassnGHRAAIAYCP 296
Cdd:COG0402 230 EWVLELYGkrPVE-YLDELGLLGP---------------------RTLLAHCVHLTDEEIALLA------ETGASVAHCP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 297 RTNARFGHDAHPYRALLAKGAIVCLGTDSLASSPSLGVLDEARF------LHARDGS-LSGELLLTMATLFGAWALRAET 369
Cdd:COG0402 282 TSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLaallqrLRGGDPTaLSAREALEMATLGGARALGLDD 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1015456696 370 AVGSIRAGKSADLAVVRLPDRDEDDPHRLLF-----ETDEPVVATLFEGQFV 416
Cdd:COG0402 362 EIGSLEPGKRADLVVLDLDAPHLAPLHDPLSalvyaADGRDVRTVWVAGRVV 413
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
31-388 |
1.43e-49 |
|
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: 172.25 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 31 GRIAWVGPARERT-------ADLDLGNVaIIPGLVNAHTHLELGRLADDGaappaSPENEVEWLRRVMAQRRAgSSEEAY 103
Cdd:cd01312 1 DKILEVGDYEKLEkrypgakHEFFPNGV-LLPGLINAHTHLEFSANVAQF-----TYGRFRAWLLSVINSRDE-LLKQPW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 104 RENVGRNLRESIEAGTTLVADTTTAGLSWDAIAAAPVRAVVFAEVLGlkryrglqTNEAAWKWLGSIKPEAQVAANA--- 180
Cdd:cd01312 74 EEAIRQGIRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIG--------SNPSAIDFKGETFLERFKRSKSfes 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 181 ---RAGLSPHAPYSTAGWLYHA----AASSRLPLSTHLAEMPEELRLLEtrdgplrsylEDLGAWDEEWE--------PI 245
Cdd:cd01312 146 qlfIPAISPHAPYSVHPELAQDlidlAKKLNLPLSTHFLESKEEREWLE----------ESKGWFKHFWEsflklpkpKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 246 GPRPTDYIRKGDLRHADWLVAHGTYIEPSEfwqfRPEASSNGHraAIAYCPRTNARFGHDAHPYRALLAKGAIVCLGTDS 325
Cdd:cd01312 216 LATAIDFLDMLGGLGTRVSFVHCVYANLEE----AEILASRGA--SIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDG 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015456696 326 LASSPSLGVLDEAR---FLHARDG--SLSGELLLtMATLFGAWALraETAVGSIRAGKSADLAVVRLP 388
Cdd:cd01312 290 LSSNISLSLLDELRallDLHPEEDllELASELLL-MATLGGARAL--GLNNGEIEAGKRADFAVFELP 354
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
21-411 |
6.14e-36 |
|
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: 136.56 E-value: 6.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 21 IADGVVAIEGGRIAWVGPARERTAD-----LDLGNVAIIPGLVNAHTHL--ELGR-LADDgaappaspENEVEWLRRVMA 92
Cdd:cd01298 17 LEDGDVLVEDGRIVAVGPALPLPAYpadevIDAKGKVVMPGLVNTHTHLamTLLRgLADD--------LPLMEWLKDLIW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 93 QRRAGSSEEAYRENVGRNLRESIEAGTTLVADTttAGLSWDAIAAAP----VRAVVFAEVLGL------KRYRGLQTNEA 162
Cdd:cd01298 89 PLERLLTEEDVYLGALLALAEMIRSGTTTFADM--YFFYPDAVAEAAeelgIRAVLGRGIMDLgtedveETEEALAEAER 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 163 AW-KWLGsiKPEAQVaanaRAGLSPHAPYSTAGWLYHAAAS-SR---LPLSTHLAEMPEELRLLETRDG--PLRsYLEDL 235
Cdd:cd01298 167 LIrEWHG--AADGRI----RVALAPHAPYTCSDELLREVAElAReygVPLHIHLAETEDEVEESLEKYGkrPVE-YLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 236 GAWDEewepigprptdyirkgdlrhaDWLVAHGTYIEPSEFwqfrpeASSNGHRAAIAYCPRTNARFGHDAHPYRALLAK 315
Cdd:cd01298 240 GLLGP---------------------DVVLAHCVWLTDEEI------ELLAETGTGVAHNPASNMKLASGIAPVPEMLEA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 316 GAIVCLGTDSLASSPSLGVLDEARF------LHARDGS-LSGELLLTMATLFGAWALRAEtAVGSIRAGKSADLAVVRLp 388
Cdd:cd01298 293 GVNVGLGTDGAASNNNLDMFEEMRLaallqkLAHGDPTaLPAEEALEMATIGGAKALGLD-EIGSLEVGKKADLILIDL- 370
|
410 420
....*....|....*....|...
gi 1015456696 389 drdeDDPHrlLFETDEPVVATLF 411
Cdd:cd01298 371 ----DGPH--LLPVHDPISHLVY 387
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
8-389 |
6.03e-31 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 122.77 E-value: 6.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 8 LGARYVF-PVEGPPI-ADGVVAIEGgRIAWVGPARERT-----ADLDLG-NVAIIPGLVNAHTHLELGrladdgaAPPAS 79
Cdd:PRK08418 4 IGASYIFtCDENFEIlEDGAVVFDD-KILEIGDYENLKkkypnAKIQFFkNSVLLPAFINPHTHLEFS-------ANKTT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 80 PE--NEVEWLRRVMAQRRAgSSEEAYRENVGRNLRESIEAGTTLVADTTTAGLSWDAIAAAPVRAVVFAEVLGlkryrgl 157
Cdd:PRK08418 76 LDygDFIPWLGSVINHRED-LLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILG------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 158 qTNEAA----WK-WLGSIKpEAQVAANAR--AGLSPHAPYSTAGWLYHA----AASSRLPLSTHLAEMPEELRLLETRDG 226
Cdd:PRK08418 148 -SNASAvdelYQdFLARFE-ESKKFKSKKfiPAIAIHSPYSVHPILAKKalqlAKKENLLVSTHFLESKAEREWLEESKG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 227 PLRSYLEDLGAwdeewepiGPRPT----DYIrkGDLRHADWLVAHGTYIEPSEFWQFrpeaSSNGHraAIAYCPRTNARF 302
Cdd:PRK08418 226 WFKKFFEKFLK--------EPKPLytpkEFL--ELFKGLRTLFTHCVYASEEELEKI----KSKNA--SITHCPFSNRLL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 303 GHDAHPYRALLAKGAIVCLGTDSLASSPSLGVLDEAR---FLHARDG--SLSGELLLtMATLFGAWALRAETavGSIRAG 377
Cdd:PRK08418 290 SNKALDLEKAKKAGINYSIATDGLSSNISLSLLDELRaalLTHANMPllELAKILLL-SATRYGAKALGLNN--GEIKEG 366
|
410
....*....|..
gi 1015456696 378 KSADLAVVRLPD 389
Cdd:PRK08418 367 KDADLSVFELPE 378
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
6-389 |
1.97e-23 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 101.53 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 6 LSLGARYVFPVE--GPPIADGVVAIEGGRIAWVGPARERTAD------LDLGNVAIIPGLVNAHTH--LELGR-LADDGA 74
Cdd:PRK09045 9 LLIEARWIVPVEpaGVVLEDHAVAIRDGRIVAILPRAEARARyaaaetVELPDHVLIPGLINAHTHaaMSLLRgLADDLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 75 AppaspeneVEWLRRVM--AQRRAgSSEEAYRENVGRNLRESIEAGTTLVADT-----TTAglswDAIAAAPVRAVVFAE 147
Cdd:PRK09045 89 L--------MTWLQDHIwpAEGAW-VSEEFVRDGTLLAIAEMLRGGTTCFNDMyffpeAAA----EAAHQAGMRAQIGMP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 148 VL--------GLKRY--RGLQTNEaawKWLGSikpeaqvaANARAGLSPHAPYSTA-GWLYHAAASSR---LPLSTHLAE 213
Cdd:PRK09045 156 VLdfptawasDADEYlaKGLELHD---QWRHH--------PLISTAFAPHAPYTVSdENLERIRTLAEqldLPIHIHLHE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 214 MPEELRLLETRDG--PLrSYLEDLGAwdeewepIGPRptdyirkgdlrhadWLVAHGTYIEPSEFwqfrpeASSNGHRAA 291
Cdd:PRK09045 225 TAQEIADSLKQHGqrPL-ARLARLGL-------LGPR--------------LIAVHMTQLTDAEI------ALLAETGCS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 292 IAYCPRTNARFGHDAHPYRALLAKGAIVCLGTDSLASSPSLGVLDEARF--LHARDGSLSGELL-----LTMATLFGAWA 364
Cdd:PRK09045 277 VVHCPESNLKLASGFCPVAKLLQAGVNVALGTDGAASNNDLDLFGEMRTaaLLAKAVAGDATALpahtaLRMATLNGARA 356
|
410 420
....*....|....*....|....*
gi 1015456696 365 LRAETAVGSIRAGKSADLAVVRLPD 389
Cdd:PRK09045 357 LGLDDEIGSLEPGKQADLVAVDLSG 381
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
23-386 |
2.60e-23 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 101.24 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 23 DGVVAIEGGRIAWVGPARER-----TADLDLGNVAIIPGLVNAHTHLELGRLA---DDgaappaspENEVEWLRRVMAQR 94
Cdd:PRK06687 21 DGILAVKDSQIVYVGQDKPAfleqaEQIIDYQGAWIMPGLVNCHTHSAMTGLRgirDD--------SNLHEWLNDYIWPA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 95 RAGSSEEAYRENVGRNLRESIEAGTTLVADT-TTAGLSWDAIAAApVRAVvfaevlGLKRYRG--LQTNEAAWKWLGSIK 171
Cdd:PRK06687 93 ESEFTPDMTTNAVKEALTEMLQSGTTTFNDMyNPNGVDIQQIYQV-VKTS------KMRCYFSptLFSSETETTAETISR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 172 PEAQVAA-------NARAGLSPHAPYSTAGWLYHA----AASSRLPLSTHLAEMPEELRLLETRDG--PLrSYLEDLGAW 238
Cdd:PRK06687 166 TRSIIDEilkyknpNFKVMVAPHSPYSCSRDLLEAslemAKELNIPLHVHVAETKEESGIILKRYGkrPL-AFLEELGYL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 239 DeewepigpRPTdyirkgdlrhadwLVAHGTYIEPSEFWQFrpeASSnghRAAIAYCPRTNARFGHDAHPYRALLAKGAI 318
Cdd:PRK06687 245 D--------HPS-------------VFAHGVELNEREIERL---ASS---QVAIAHNPISNLKLASGIAPIIQLQKAGVA 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015456696 319 VCLGTDSLASSPSLGVLDEAR----FLHARDGSLSG---ELLLTMATLFGAWALRAETAVGSIRAGKSADLAVVR 386
Cdd:PRK06687 298 VGIATDSVASNNNLDMFEEGRtaalLQKMKSGDASQfpiETALKVLTIEGAKALGMENQIGSLEVGKQADFLVIQ 372
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
53-388 |
3.54e-21 |
|
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: 93.72 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 53 IIPGLVNAHTHLELGRLaddgaappaspenevewlrrvmaqRRAGSSEEAYRENVGRNLRESIEAGTTLVADT-TTAGLS 131
Cdd:pfam01979 2 VLPGLIDAHVHLEMGLL------------------------RGIPVPPEFAYEALRLGITTMLKSGTTTVLDMgATTSTG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 132 WDAIAAAP------VRAVVFAEVLGLKR--YRGLQTNEAAWKWLGSIKPEAQVAANAraGLSPHAPYS-TAGWLYHAAAS 202
Cdd:pfam01979 58 IEALLEAAeelplgLRFLGPGCSLDTDGelEGRKALREKLKAGAEFIKGMADGVVFV--GLAPHGAPTfSDDELKAALEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 203 SR---LPLSTHLAEMPEELrlletrdgplrSYLEDLGAWDEEWepiGPRPTDYIRKGDLRHADWLVAHGTYIEPSEFWQF 279
Cdd:pfam01979 136 AKkygLPVAIHALETKGEV-----------EDAIAAFGGGIEH---GTHLEVAESGGLLDIIKLILAHGVHLSPTEANLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 280 RPEASSNGhraaIAYCPRTNARFGHDAHPYRALLAKGAIVCLGTDSLASSPSLGVLDEARF---LHARD-GSLSGELLLT 355
Cdd:pfam01979 202 AEHLKGAG----VAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLaleLQFDPeGGLSPLEALR 277
|
330 340 350
....*....|....*....|....*....|...
gi 1015456696 356 MATLFGAWALRAETAVGSIRAGKSADLAVVRLP 388
Cdd:pfam01979 278 MATINPAKALGLDDKVGSIEVGKDADLVVVDLD 310
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
12-396 |
3.96e-21 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 94.82 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 12 YVFPVEGPPIADGVVAIEGGRIAWVGPARERTAD--LDLGNVAIIPGLVNAHTHLELGRL---ADDgaappaspENEVEW 86
Cdd:PRK06038 10 YVLTMDAGDLKKGSVVIEDGTITEVSESTPGDADtvIDAKGSVVMPGLVNTHTHAAMTLFrgyADD--------LPLAEW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 87 LRRVMAQRRAG-SSEEAYRenvGRNLR--ESIEAGTTLVADT-----TTAglswDAIAAAPVRAVVfaeVLGLKRYRGLQ 158
Cdd:PRK06038 82 LNDHIWPAEAKlTAEDVYA---GSLLAclEMIKSGTTSFADMyfymdEVA----KAVEESGLRAAL---SYGMIDLGDDE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 159 TNEAAWKWLGSIKPEAQVAANAR--AGLSPHAPYSTAGWLY----HAAASSRLPLSTHLAEMPEELRLLETRDGPLR-SY 231
Cdd:PRK06038 152 KGEAELKEGKRFVKEWHGAADGRikVMYGPHAPYTCSEEFLskvkKLANKDGVGIHIHVLETEAELNQMKEQYGMCSvNY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 232 LEDLGAWDEewepigprptdyirkgdlrhaDWLVAHGTYIEPSEFWQFRpeassnGHRAAIAYCPRTNARFGHDAHPYRA 311
Cdd:PRK06038 232 LDDIGFLGP---------------------DVLAAHCVWLSDGDIEILR------ERGVNVSHNPVSNMKLASGIAPVPK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 312 LLAKGAIVCLGTDSLASSPSLGVLDE---ARFLHARDG----SLSGELLLTMATLFGAWALRAETavGSIRAGKSADLAV 384
Cdd:PRK06038 285 LLERGVNVSLGTDGCASNNNLDMFEEmktAALLHKVNTmdptALPARQVLEMATVNGAKALGINT--GMLKEGYLADIII 362
|
410
....*....|..
gi 1015456696 385 VrlpdrDEDDPH 396
Cdd:PRK06038 363 V-----DMNKPH 369
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
26-387 |
5.90e-21 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 94.10 E-value: 5.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 26 VAIEGGRIAWVGPARERTAD--LDLGNVAIIPGLVNAHTHLELG---RLADDGAAppaspeneVEWLRRVMAQRRAGSSE 100
Cdd:PRK08393 23 VLIEGNKIVEVKRNINKPADtvIDASGSVVSPGFINAHTHSPMVllrGLADDVPL--------MEWLQNYIWPRERKLKR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 101 EAYRENVGRNLRESIEAGTTLVADTTtagLSWDAIAAAPVRAvvfaevlGLKRYRG-----LQTNEAAWKWLGSIKPEAQ 175
Cdd:PRK08393 95 KDIYWGAYLGLLEMIKSGTTTFVDMY---FHMEEVAKATLEV-------GLRGYLSygmvdLGDEEKREKEIKETEKLME 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 176 VAANARAG-----LSPHAPYSTA----GWLYHAAASSRLPLSTHLAEMPEELRLLEtrdgplrsyledlgawdeewEPIG 246
Cdd:PRK08393 165 FIEKLNSPrvhfvFGPHAPYTCSlallKWVREKAREWNKLITIHLSETMDEIKQIR--------------------EKYG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 247 PRPTDYIRKGDLRHADWLVAHGTYIEPSEFwqfRPEASSNghrAAIAYCPRTNARFGHDAHPYRALLAKGAIVCLGTDSL 326
Cdd:PRK08393 225 KSPVVLLDEIGFLNEDVIAAHGVWLSSRDI---RILASAG---VTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGA 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015456696 327 ASSPSLGVLDEARF------LHARDGSLS-GELLLTMATLFGAWALRAETAVgsIRAGKSADLAVVRL 387
Cdd:PRK08393 299 ASNNNLDMLREMKLaallhkVHNLDPTIAdAETVFRMATQNGAKALGLKAGV--IKEGYLADIAVIDF 364
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
9-385 |
4.00e-17 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 82.32 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 9 GARYVFPVEGPPIADGVVAIEGGRIAWVGPARERTAD-----LDLGNVAIIPGLVNAHTHLELGRLADDGAAPPASPENE 83
Cdd:COG1228 14 NATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPagaevIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGGITPT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 84 VEWLRRVMaqrragsseeayrenvgRNLRESIEAGTTLVADTTTAGLSW-DAIAAAPVRAV----VFAEVLGLKRYRGLQ 158
Cdd:COG1228 94 VDLVNPAD-----------------KRLRRALAAGVTTVRDLPGGPLGLrDAIIAGESKLLpgprVLAAGPALSLTGGAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 159 TN--EAAWKWLgsikpEAQVAANARA------GLSPHAPYSTAGWLYHAAASSRLPLSTHlAEMPEELRLLeTRDGpLRS 230
Cdd:COG1228 157 ARgpEEARAAL-----RELLAEGADYikvfaeGGAPDFSLEELRAILEAAHALGLPVAAH-AHQADDIRLA-VEAG-VDS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 231 yLEDLGAWDEEwepigprptdyirkgdlrHADWLVAHGTYIEPSEFWQFRPEASSNGHRAAIAYCPRTNARFghdaHPYR 310
Cdd:COG1228 229 -IEHGTYLDDE------------------VADLLAEAGTVVLVPTLSLFLALLEGAAAPVAAKARKVREAAL----ANAR 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015456696 311 ALLAKGAIVCLGTDSLA-SSPSLGVLDEARFLHArdGSLSGELLLTMATLFGAWALRAETAVGSIRAGKSADLAVV 385
Cdd:COG1228 286 RLHDAGVPVALGTDAGVgVPPGRSLHRELALAVE--AGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLL 359
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
46-385 |
6.70e-16 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 79.33 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 46 LDLGNVAIIPGLVNAHTHLELGRLADDGAAPPASP--ENEVEWLRRVMAQRRAGSSEEAyrenvgrNLRESIEAGTTLVA 123
Cdd:PRK15493 50 IDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPwlETRIWPLESQFTPELAVASTEL-------GLLEMVKSGTTSFS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 124 DT-TTAGLSWDAIAAAPVRAVVFAEVLGLKRYRGLQTNEA-----AWKWLGSIKPEAQVAANAragLSPHAPYSTAGWLY 197
Cdd:PRK15493 123 DMfNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKEDEKkaieeAEKYVKRYYNESGMLTTM---VAPHSPYTCSTELL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 198 HAAASSRLPLST----HLAEMPEELRLLETRdgplrsyledlgawdeewepIGPRPTDYIRKGDLRHADWLVAHGTYIEP 273
Cdd:PRK15493 200 EECARIAVENQTmvhiHLSETEREVRDIEAQ--------------------YGKRPVEYAASCGLFKRPTVIAHGVVLND 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 274 SEfWQFRPEassngHRAAIAYCPRTNARFGHDAHPYRALLAKGAIVCLGTDSLASSPSLGVLDEARF-------LHARDG 346
Cdd:PRK15493 260 NE-RAFLAE-----HDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIatllqkgIHQDAT 333
|
330 340 350
....*....|....*....|....*....|....*....
gi 1015456696 347 SLSGELLLTMATLfGAWALRAETAVGSIRAGKSADLAVV 385
Cdd:PRK15493 334 ALPVETALTLATK-GAAEVIGMKQTGSLEVGKCADFITI 371
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
10-387 |
5.48e-15 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 76.43 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 10 ARYVFPVEGP--PIADGVVAIEGGRIAWVGPARERTAD----LDLGNVAIIPGLVNAHTHL--ELGRladdgAAPPASPE 81
Cdd:PRK08203 8 PLAIVTMDAArrEIADGGLVVEGGRIVEVGPGGALPQPadevFDARGHVVTPGLVNTHHHFyqTLTR-----ALPAAQDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 82 NEVEWLR---RVMAqrraGSSEEAYRENVGRNLRESIEAGTTLVAD-----TTTAGLSWDAIAAApvravvfAEVLGLkR 153
Cdd:PRK08203 83 ELFPWLTtlyPVWA----RLTPEMVRVATQTALAELLLSGCTTSSDhhylfPNGLRDALDDQIEA-------AREIGM-R 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 154 Y---RG-LQTNEAAwkwlGSIKPEAQV-------AANARA---------------GLSPHAPYSTAGWLYHAAA----SS 203
Cdd:PRK08203 151 FhatRGsMSLGESD----GGLPPDSVVededailADSQRLidryhdpgpgamlriALAPCSPFSVSRELMRESAalarRL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 204 RLPLSTHLAEMPEELRLLETRDG--PLrSYLEDLGawdeeWepIGPRPtdyirkgdlrhadWLvAHGTYIEPSEFWQFrp 281
Cdd:PRK08203 227 GVRLHTHLAETLDEEAFCLERFGmrPV-DYLEDLG-----W--LGPDV-------------WL-AHCVHLDDAEIARL-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 282 eassnGH-RAAIAYCPRTNARFGHDAHPYRALLAKGAIVCLGTDSLASSPSLGVLDEAR--FLHARDGS----LSGELLL 354
Cdd:PRK08203 283 -----ARtGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNLIGEARqaLLLQRLRYgpdaMTAREAL 357
|
410 420 430
....*....|....*....|....*....|....
gi 1015456696 355 TMATLFGAWAL-RAETavGSIRAGKSADLAVVRL 387
Cdd:PRK08203 358 EWATLGGARVLgRDDI--GSLAPGKLADLALFDL 389
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
28-389 |
7.44e-15 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 75.87 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 28 IEGGRIAWVGPARERTAD--LDLGNVAIIPGLVNAHTHLELGRLADDGAAPPASPEnevEWLRRVMAQRRAGSSEEAYRE 105
Cdd:PRK12393 30 IRDGRIAAIGALTPLPGErvIDATDCVVYPGWVNTHHHLFQSLLKGVPAGINQSLT---AWLAAVPYRFRARFDEDLFRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 106 NVGRNLRESIEAGTTLVADTTTagLSWDAIAAAPvRAVVF--AEVLGLK----RYRGLQTNEAAWKWLGSIKPEA--QVA 177
Cdd:PRK12393 107 AARIGLVELLRSGCTTVADHHY--LYHPGMPFDT-GDILFdeAEALGMRfvlcRGGATQTRGDHPGLPTALRPETldQML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 178 ANARAGLSPHAPYSTAGWLYHAAASSRLPLSTHLAEMPEELRLLETRDGPLRSYL-EDLGAWDEEWEPIGPRPTDYIRKG 256
Cdd:PRK12393 184 ADVERLVSRYHDASPDSLRRVVVAPTTPTFSLPPELLREVARAARGMGLRLHSHLsETVDYVDFCREKYGMTPVQFVAEH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 257 DLRHADWLVAHGTYIEPSEFwqfrpeASSNGHRAAIAYCPRTNARFGHDAHPYRALLAKGAIVCLGTDSLASSPSLGVLD 336
Cdd:PRK12393 264 DWLGPDVWFAHLVKLDAEEI------ALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADMLS 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1015456696 337 EARF---LHARDG---SLSGELLLTMATLFGAWALrAETAVGSIRAGKSADLAVVRLPD 389
Cdd:PRK12393 338 EAHAawlLHRAEGgadATTVEDVVHWGTAGGARVL-GLDAIGTLAVGQAADLAIYDLDD 395
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
28-387 |
1.53e-13 |
|
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: 71.72 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 28 IEGGRIAWVGPARErTADLDLGNVAIIPGLVNAHTHLELGRLAddGAAPPASPENEVEW-LRRVMAQRRAGSSEEAYrEN 106
Cdd:cd01313 16 DADGRIAAVNPDTA-TEAVALLGGALLPGMPNLHSHAFQRAMA--GLTEYRGSAADSFWtWRELMYRFAARLTPEQI-EA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 107 VGRNL-RESIEAGTTLVAD----------------TTTAGLSWDAIAAAPVRAV---VFAEVLGL-------KRYRGLQT 159
Cdd:cd01313 92 IARQLyIEMLLAGITAVGEfhyvhhdpdgtpyadpAELAQRVIAAASDAGIGITllpVLYARAGFggpapnpGQRRFING 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 160 NEAAWKWLGSIKPEAQVAANARAGLSPHAPYS-TAGWLYH--AAASSRLPLSTHLAEMPEElrlletrdgplrsyLEDLG 236
Cdd:cd01313 172 YEDFLGLLEKALRAVKEHAAARIGVAPHSLRAvPAEQLAAlaALASEKAPVHIHLAEQPKE--------------VDDCL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 237 AWDeewepiGPRPTDYIRKGDLRHADWLVAHGTYIEPSEFWQFRPEassnghRAAIAYCPRTNARFGHDAHPYRALLAKG 316
Cdd:cd01313 238 AAH------GRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRS------GAVVGLCPTTEANLGDGIFPAAALLAAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 317 AIVCLGTDSLAsspSLGVLDEARFLH-------------ARDGSLSGELLLTMATLFGAWALRAetAVGSIRAGKSADLA 383
Cdd:cd01313 306 GRIGIGSDSNA---RIDLLEELRQLEysqrlrdrarnvlATAGGSSARALLDAALAGGAQALGL--ATGALEAGARADLL 380
|
....
gi 1015456696 384 VVRL 387
Cdd:cd01313 381 SLDL 384
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
21-387 |
4.01e-13 |
|
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: 70.77 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 21 IADGVVAIEGGRIAWVGPAR-------ERTADLDLGNVAIIPGLVNAHTHlelgrladdgaAPP----ASPENE--VEWL 87
Cdd:cd01303 24 VEDGLIVVVDGNIIAAGAAEtlkraakPGARVIDSPNQFILPGFIDTHIH-----------APQyaniGSGLGEplLDWL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 88 RRVMAQRRAGSSEEAY-RENVGRNLRESIEAGTTLVA-----DTTTAGLSWDAIAAAPVRAV---VFAEVLGLKRYRglQ 158
Cdd:cd01303 93 ETYTFPEEAKFADPAYaREVYGRFLDELLRNGTTTACyfatiHPESTEALFEEAAKRGQRAIagkVCMDRNAPEYYR--D 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 159 TNEAAWK--------WLGsIKPEAQVAANARaglspHAPYSTAGWLYHAAASSR----LPLSTHLAEMPEELRLLETRDG 226
Cdd:cd01303 171 TAESSYRdtkrlierWHG-KSGRVKPAITPR-----FAPSCSEELLAALGKLAKehpdLHIQTHISENLDEIAWVKELFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 227 PLRSYLEDLgawdEEWEPIGPRPtdyirkgdlrhadwLVAHGTYIEPSEFWQFrpeaSSNGhrAAIAYCPRTNARFGHDA 306
Cdd:cd01303 245 GARDYLDVY----DKYGLLTEKT--------------VLAHCVHLSEEEFNLL----KERG--ASVAHCPTSNLFLGSGL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 307 HPYRALLAKGAIVCLGTDSLA-SSPS-LGVLDEA-------RFLHARDGSLSGELLLTMATLFGAWALRAETAVGSIRAG 377
Cdd:cd01303 301 FDVRKLLDAGIKVGLGTDVGGgTSFSmLDTLRQAykvsrllGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVG 380
|
410
....*....|
gi 1015456696 378 KSADLAVVRL 387
Cdd:cd01303 381 KEFDAVVIDP 390
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
21-416 |
7.61e-13 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 69.64 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 21 IADGVVAIEGGRIAWVGP-ARERTAD--LDLGNVAIIPGLVNAHTHL--ELGR-LADDGAAppaspeneVEWLRRVMAQR 94
Cdd:PRK07228 19 IVDGDVLIEDDRIAAVGDrLDLEDYDdhIDATGKVVIPGLIQGHIHLcqTLFRgIADDLEL--------LDWLKDRIWPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 95 RAGSSEEAYRENVGRNLRESIEAGTTLVADTTT---AGLSWDAIAAAPVRAvVFAEVL---GLKRYRGLQ-TNEAAW--- 164
Cdd:PRK07228 91 EAAHDAESMYYSALLGIGELIESGTTTIVDMESvhhTDSAFEAAGESGIRA-VLGKVMmdyGDDVPEGLQeDTEASLaes 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 165 -----KWLGSIKPEAQVAANARAGLSphapySTAGWLYHAAASSR---LPLSTHLAEMPEELRLLETRDGpLRS--YLED 234
Cdd:PRK07228 170 vrlleKWHGADNGRIRYAFTPRFAVS-----CTEELLRGVRDLADeygVRIHTHASENRGEIETVEEETG-MRNihYLDE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 235 LGawdeewepigprptdyirkgdLRHADWLVAHGTYIEPSEfwqFRPEASSNGHraaIAYCPRTNARFGHDAHPYRALLA 314
Cdd:PRK07228 244 VG---------------------LTGEDLILAHCVWLDEEE---REILAETGTH---VTHCPSSNLKLASGIAPVPDLLE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 315 KGAIVCLGTDSLASSPSLGVLDEAR---FLHARDG----SLSGELLLTMATLFGAWALRAETAVGSIRAGKSADLAVVRL 387
Cdd:PRK07228 297 RGINVALGADGAPCNNTLDPFTEMRqaaLIQKVDRlgptAMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDL 376
|
410 420 430
....*....|....*....|....*....|....*.
gi 1015456696 388 ------PDRDEDDPHRLLFE-TDEPVVATLFEGQFV 416
Cdd:PRK07228 377 dglhatPSHGVDVLSHLVYAaHGSDVETTMVDGKIV 412
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
21-396 |
1.09e-10 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 63.14 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 21 IADGVVAIEGGRIAWVGPARERTAD--LDLGNVAIIPGLVNA-------HTHLELGRlADDGAAPPASPENEVEWLRRVM 91
Cdd:PRK06151 21 LRDGEVVFEGDRILFVGHRFDGEVDrvIDAGNALVGPGFIDLdalsdldTTILGLDN-GPGWAKGRVWSRDYVEAGRREM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 92 AQRragsSEEA--YRENVGRNLRESIeagTTLVADTTTAGLSWDAIAAAPVRAVVFAEVLGLKRYRG--LQTNEAAWKWL 167
Cdd:PRK06151 100 YTP----EELAfqKRYAFAQLLRNGI---TTAMPIASLFYRQWAETYAEFAAAAEAAGRLGLRVYLGpaYRSGGSVLEAD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 168 GSIKPEAQvAANARAGLSPH-------------------AP----YSTAGWLYHAAASSR---LPLSTHLAEMPEELRLL 221
Cdd:PRK06151 173 GSLEVVFD-EARGLAGLEEAiafikrvdgahnglvrgmlAPdrieTCTVDLLRRTAAAARelgCPVRLHCAQGVLEVETV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 222 ETRDG--PLRsYLEDLGAwdeewepIGPRptdyirkgdlrhadWLVAHGTYI---EPSEFWQFRPEASSNGHRAAIAYCP 296
Cdd:PRK06151 252 RRLHGttPLE-WLADVGL-------LGPR--------------LLIPHATYIsgsPRLNYSGGDDLALLAEHGVSIVHCP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 297 RTNARFGHDAHPYRALLAKGAIVCLGTDS----LASSPSLGvLDEARFLHARDGSLSGELLLTMATLFGAWALRaETAVG 372
Cdd:PRK06151 310 LVSARHGSALNSFDRYREAGINLALGTDTfppdMVMNMRVG-LILGRVVEGDLDAASAADLFDAATLGGARALG-RDDLG 387
|
410 420
....*....|....*....|....
gi 1015456696 373 SIRAGKSADLAVVRLpdrdeDDPH 396
Cdd:PRK06151 388 RLAPGAKADIVVFDL-----DGLH 406
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
21-388 |
1.68e-10 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 62.52 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 21 IADGVVAIEGGRIAWVGPARERTADL-------DLGNVAIIPGLVNAHTHLelgrladdgaapP-----ASP-ENEVEWL 87
Cdd:PRK09228 29 IEDGLLLVEDGRIVAAGPYAELRAQLpadaevtDYRGKLILPGFIDTHIHY------------PqtdmiASYgEQLLDWL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 88 RRVM--AQRRAGSSEEAyRENVGRNLRESIEAGTT--LVADTTTAGlSWDAIAAApvravvfAEVLGLKRYRG------- 156
Cdd:PRK09228 97 NTYTfpEERRFADPAYA-REVAEFFLDELLRNGTTtaLVFGTVHPQ-SVDALFEA-------AEARNMRMIAGkvlmdrn 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 157 -----LQTNEAAW--------KWLGsiKPEAQVAANAR-AGLSPHAPYSTAGWLYHAAASSRLplSTHLAEMPEELRLLE 222
Cdd:PRK09228 168 apdglRDTAESGYddskalieRWHG--KGRLLYAITPRfAPTSTPEQLEAAGALAREHPDVWI--QTHLSENLDEIAWVK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 223 TRDGPLRSYLEDlgawdeewepigprptdYIRKGDLRHADwLVAHGTYIEPSEFWQFRpeassnGHRAAIAYCPRTNARF 302
Cdd:PRK09228 244 ELFPEARDYLDV-----------------YERYGLLGPRA-VFAHCIHLEDRERRRLA------ETGAAIAFCPTSNLFL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 303 GHDAHPYRALLAKGAIVCLGTDSLA-SSPS-LGVLDEARFLHARDG-SLSGELLLTMATLFGAWALRAETAVGSIRAGKS 379
Cdd:PRK09228 300 GSGLFDLKRADAAGVRVGLGTDVGGgTSFSmLQTMNEAYKVQQLQGyRLSPFQAFYLATLGGARALGLDDRIGNLAPGKE 379
|
....*....
gi 1015456696 380 ADLAVVRLP 388
Cdd:PRK09228 380 ADFVVLDPA 388
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
300-416 |
4.01e-10 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 61.35 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 300 ARFGHD----AHPYRALLAKGAIVCLGTDSLASSPS-LGVLDEARFLHARDGS-------LSGELLLTMATLFGAWALRA 367
Cdd:COG1574 407 DRLGPEraarAYPFRSLLDAGAPLAFGSDAPVEPLDpLLGIYAAVTRRTPSGRglgpeerLTVEEALRAYTIGAAYAAFE 486
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1015456696 368 ETAVGSIRAGKSADLAVVrlpDRD--EDDPHRLLfetDEPVVATLFEGQFV 416
Cdd:COG1574 487 EDEKGSLEPGKLADFVVL---DRDplTVPPEEIK---DIKVLLTVVGGRVV 531
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
19-386 |
7.74e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 60.40 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 19 PPIADgvVAIEGGRIAWVGPARER--TADLDLGNVAIIPGLVNAHTHLELGRLAddGAAPPASPENEVEWLRRVMAQRRa 96
Cdd:PRK08204 21 LPRGD--ILIEGDRIAAVAPSIEApdAEVVDARGMIVMPGLVDTHRHTWQSVLR--GIGADWTLQTYFREIHGNLGPMF- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 97 gSSEEAYREN-VGrnLRESIEAGTTLVADTTT-------AGLSWDAIAAAPVRAVvFAevlglkryRGLQTNEAAWKWLG 168
Cdd:PRK08204 96 -RPEDVYIANlLG--ALEALDAGVTTLLDWSHinnspehADAAIRGLAEAGIRAV-FA--------HGSPGPSPYWPFDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 169 SIKPEAQVAANARAglsphaPYSTAGWLYHAAASSRLPLSTHLAEMPEELRLLETRDGPLRSYLeDLGAWDEewepiGPR 248
Cdd:PRK08204 164 VPHPREDIRRVKKR------YFSSDDGLLTLGLAIRGPEFSSWEVARADFRLARELGLPISMHQ-GFGPWGA-----TPR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 249 PTDYIRKGDLRHADWLVAHGTYIEPSEFWQFRPEASSnghraaIAYCPRTNARFGHDAHPYRALLAKGAIVCLGTDSLAS 328
Cdd:PRK08204 232 GVEQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGS------FSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTS 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015456696 329 SPSlGVLDEARFLH----ARDG--------------SLSGELLLTMATLFGAWALRAETAVGSIRAGKSADLAVVR 386
Cdd:PRK08204 306 TGG-DMFTQMRFALqaerARDNavhlreggmppprlTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLID 380
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
57-362 |
1.97e-09 |
|
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: 58.11 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 57 LVNAHTHLelgrlaDDGAAPPASPENEVEWLRRVmaqrragsSEEAYRENVGRNLRESIEAGTTLVAD------TTTAGL 130
Cdd:cd01292 1 FIDTHVHL------DGSALRGTRLNLELKEAEEL--------SPEDLYEDTLRALEALLAGGVTTVVDmgstppPTTTKA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 131 SWDAIAAAPVRAVVFAEVLGLKRYRGlqTNEAAWKWLGSIKPEAQVAANARA-GLSPHAPYSTAGW-------LYHAAAS 202
Cdd:cd01292 67 AIEAVAEAARASAGIRVVLGLGIPGV--PAAVDEDAEALLLELLRRGLELGAvGLKLAGPYTATGLsdeslrrVLEEARK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 203 SRLPLSTHLAEMPEELRLLETrdgplrsyledlgawdeewepigprptdyIRKGDLRHADWLVAHGTYIEPSEFWQFRPe 282
Cdd:cd01292 145 LGLPVVIHAGELPDPTRALED-----------------------------LVALLRLGGRVVIGHVSHLDPELLELLKE- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 283 assngHRAAIAYCPRTNARF---GHDAHPYRALLAKGAIVCLGTDSLASSPSLGVLDEARFLHARDGS-LSGELLLTMAT 358
Cdd:cd01292 195 -----AGVSLEVCPLSNYLLgrdGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLgLSLEEALRLAT 269
|
....
gi 1015456696 359 LFGA 362
Cdd:cd01292 270 INPA 273
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
21-392 |
3.42e-09 |
|
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: 58.19 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 21 IADGVVAIEGGRIAWVG-----PARERTADLDLGNVAIIPGLVNAHTHLELG--RLADDGAAPPASPENEVEW-----LR 88
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGqlaalPGEEATEIIDCGGGLVTPGLVDPHTHLVFAgdRVNEFEMKLQGASYLEILAqgggiLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 89 RVMAQRRAgsSEEAYRENVGRNLRESIEAGTTLVADTTTAGLSWD-------AIAAA----PVRaVVFAEVLGLKRYRGL 157
Cdd:TIGR01224 81 TVRATRAA--SEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLEtelkmlrAAKALheeqPVD-VVTTFLGAHAVPPEF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 158 QTNEAAW--KWLGSIKPEAQVAANARA--------GLSPHAPYStagwLYHAAASSRLPLSTHlAEMPEELRLLE-TRDG 226
Cdd:TIGR01224 158 QGRPDDYvdGICEELIPQVAEEGLASFadvfceagVFSVEQSRR----ILQAAQEAGLPVKLH-AEELSNLGGAElAAKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 227 PLRSYledlgawdeewepigprptDYIRKGDLRHADWLVAHGTyiepsefwqfrpeassnghraAIAYCPRTNARFGHDA 306
Cdd:TIGR01224 233 GAVSA-------------------DHLEHASDAGIKALAEAGT---------------------VAVLLPGTTFYLRETY 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 307 HPYRALLAKGAIVCLGTDslaSSPSLGVLDEARF---LHARDGSLSGELLLTMATLFGAWAL-RAETAvGSIRAGKSADL 382
Cdd:TIGR01224 273 PPARQLIDYGVPVALATD---LNPGSSPTLSMQLimsLACRLMKMTPEEALHAATVNAAYALgLGEER-GTLEAGRDADL 348
|
410
....*....|
gi 1015456696 383 AVVRLPDRDE 392
Cdd:TIGR01224 349 VILSAPSYAE 358
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
26-392 |
2.93e-08 |
|
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: 55.34 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 26 VAIEGGRIAWVGPA-------RERTADLDLGNVAIIPGLVNAHTHLELGrladdgaappASPENEVEW------------ 86
Cdd:cd01296 1 IAIRDGRIAAVGPAaslpapgPAAAEEIDAGGRAVTPGLVDCHTHLVFA----------GDRVDEFAArlagasyeeila 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 87 -----LRRVMAQRRAgsSEEAYRENVGRNLRESIEAGTTLVADTTTAGLSWD-------AIAAA----PVRAV------- 143
Cdd:cd01296 71 agggiLSTVRATRAA--SEDELFASALRRLARMLRHGTTTVEVKSGYGLDLEtelkmlrVIRRLkeegPVDLVstflgah 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 144 -VFAEVLGLKRYRGLQTNEaawkWLGSIKPEAQVAA-----NARAGlsphaPYSTAGWLYHAAASSRLPLSTHlaemPEE 217
Cdd:cd01296 149 aVPPEYKGREEYIDLVIEE----VLPAVAEENLADFcdvfcEKGAF-----SLEQSRRILEAAKEAGLPVKIH----ADE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 218 LrlleTRDGPLRSYLEdLGAwdeewepigprptdyirkgdlRHADwlvaHGTYIEPSefwQFRPEASSNghrAAIAYCPR 297
Cdd:cd01296 216 L----SNIGGAELAAE-LGA---------------------LSAD----HLEHTSDE---GIAALAEAG---TVAVLLPG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 298 TNARFGHDAHPYRALLAKGAIVCLGTDSLASSPSLGVLDEARFLHARDGSLSGELLLTMATLFGAWALRAETAVGSIRAG 377
Cdd:cd01296 260 TAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVG 339
|
410
....*....|....*
gi 1015456696 378 KSADLAVVRLPDRDE 392
Cdd:cd01296 340 KQADLVILDAPSYEH 354
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
53-362 |
4.32e-08 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 53.94 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 53 IIPGLVNAHTHLELGRLADDGAapPASPENEVEWLRRVMAQRRAGSSEEAYRENVGRNLRESIEAGTTLVADTTTAGLSW 132
Cdd:cd01305 2 LIPALVNAHTHLGDSAIKEVGD--GLPLDDLVAPPDGLKHRLLAQADDRELAEAMRKVLRDMRETGIGAFADFREGGVEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 133 DAI--AAAPVRAVVFAEVLGLkryrglqtneaawkwlgSIKPEAQVAANARA-GLSPHAPYSTAGWLYHAAASSR-LPLS 208
Cdd:cd01305 80 IELlrRALGKLPVPFEVILGR-----------------PTEPDDPEILLEVAdGLGLSSANDVDLEDILELLRRRgKLFA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 209 THLAEmpeelrlleTRDGPLRSYLE---DLGAwdeewepigprptdyirkgdlrhaDWLVaHGTYIEPSEFWQFRPeass 285
Cdd:cd01305 143 IHASE---------TRESVGMTDIEralDLEP------------------------DLLV-HGTHLTDEDLELVRE---- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 286 ngHRAAIAYCPRTNARFGHDAHPYRALLAKGAIVCLGTDSLA-SSPSLgvLDEARFLHAR---DGSLSGELLLTMATLFG 361
Cdd:cd01305 185 --NGVPVVLCPRSNLYFGVGIPPVAELLKLGIKVLLGTDNVMvNEPDM--WAEMEFLAKYsrlQGYLSPLEILRMATVNA 260
|
.
gi 1015456696 362 A 362
Cdd:cd01305 261 A 261
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
308-416 |
4.64e-08 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 54.84 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 308 PYRALLAKGAIVCLGTDslassPSLGVLDEARFLHA--------------RDGSLSGELLLTMATLFGAWALRAETAVGS 373
Cdd:pfam07969 350 PVKELLNAGVKVALGSD-----APVGPFDPWPRIGAavmrqtagggevlgPDEELSLEEALALYTSGPAKALGLEDRKGT 424
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1015456696 374 IRAGKSADLAVVRlPDRDEDDPHRLLfetDEPVVATLFEGQFV 416
Cdd:pfam07969 425 LGVGKDADLVVLD-DDPLTVDPPAIA---DIRVRLTVVDGRVV 463
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
26-384 |
5.03e-08 |
|
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: 55.01 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 26 VAIEGGRIAWVGP-------ARERTADLDLGNVAIIPGLVNAHTHLELGRLADDGA--APPASPENEvewLRRVMAQRRA 96
Cdd:cd01300 2 VAVRDGRIVAVGSdaeakalKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLdlSGVTSKEEA---LARIREDAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 97 GSSEEAYRenvGRNLRESIEAGTTLVadtTTAGLswDAIAaaPVRAVVFAEV---------LGLKRY------------- 154
Cdd:cd01300 79 APPGEWIL---GFGWDESLLGEGRYP---TRAEL--DAVS--PDRPVLLLRRdghsawvnsAALRLAgitrdtpdppgge 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 155 ---------RGLQTNEAAW---KWLGSIKPEAQVAA-------NARAGL----SPHAPYSTAGWLY---HAAASSRLPLS 208
Cdd:cd01300 149 ivrdadgepTGVLVEAAAAlvlEAVPPPTPEERRAAlraaareLASLGVttvhDAGGGAADDIEAYrrlAAAGELTLRVR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 209 THLAEMPEELRLLETRDGPLRSYLED--------------LGAW------------DEEWEPIGPRPT--DYIRKgdLRH 260
Cdd:cd01300 229 VALYVSPLAEDLLEELGARKNGAGDDrlrlggvklfadgsLGSRtaalsepyldspGTGGLLLISPEEleELVRA--ADE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 261 ADWLVA-HGTYIEPSE-----FWQFRPEASSNGHRAAIAYC----PRTNARFGH----------------DAH------- 307
Cdd:cd01300 307 AGLQVAiHAIGDRAVDtvldaLEAALKDNPRADHRHRIEHAqlvsPDDIPRFAKlgviasvqpnhlysdgDAAedrrlge 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 308 -------PYRALLAKGAIVCLGTDSLASSPS---------LGVLDEARFLHARDGSLSGELLLTMATLFGAWALRAETAV 371
Cdd:cd01300 387 erakrsyPFRSLLDAGVPVALGSDAPVAPPDpllgiwaavTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEK 466
|
490
....*....|...
gi 1015456696 372 GSIRAGKSADLAV 384
Cdd:cd01300 467 GSLEPGKLADFVV 479
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
17-385 |
7.26e-08 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 54.12 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 17 EGPPIADGVVAIEGGRIAWVGPARErTAD--LDLGNVAIIPGLVNAHTHLelGRLADDGAAPPASPENEVEWLRRVMAQR 94
Cdd:PRK06380 15 EKREILQGNVYIEGNKIVYVGDVNE-EADyiIDATGKVVMPGLINTHAHV--GMTASKGLFDDVDLEEFLMKTFKYDSKR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 95 ragSSEEAYreNVGR-NLRESIEAGTTLVADTTTaglSWDAIAAApvravvfAEVLGLKRYRGLQT-NEAAWKWLGS--- 169
Cdd:PRK06380 92 ---TREGIY--NSAKlGMYEMINSGITAFVDLYY---SEDIIAKA-------AEELGIRAFLSWAVlDEEITTQKGDpln 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 170 -----IKpEAQVAANARAGLSPHAPYSTAGWLYHAAA--SSRLP--LSTHLAEMPEELrlLETRdgplrsyledlgawde 240
Cdd:PRK06380 157 naenfIR-EHRNEELVTPSIGVQGIYVANDETYLKAKeiAEKYDtiMHMHLSETRKEV--YDHV---------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 241 ewEPIGPRPTDYIRKGDLRHADWLVAHGTYIEPSEFWQFrpeaSSNGHRAAiaYCPRTNARFGHDAH-PYRALLAKGAIV 319
Cdd:PRK06380 218 --KRTGERPVEHLEKIGFLNSKLIAAHCVWATYHEIKLL----SKNGVKVS--WNSVSNFKLGTGGSpPIPEMLDNGINV 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015456696 320 CLGTDSLASSPSLGVLDEARFL-----HAR-DGSL-SGELLLTMATLFGAWALRAETavGSIRAGKSADLAVV 385
Cdd:PRK06380 290 TIGTDSNGSNNSLDMFEAMKFSalsvkNERwDASIiKAQEILDFATINAAKALELNA--GSIEVGKLADLVIL 360
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
170-407 |
5.61e-07 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 51.39 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 170 IKPEAQVAANARAGLSPHapyS----TAGWLYHAAASS--RLPLSTHLAEMPEELrlletrdgplrsylEDLGAWDeewe 243
Cdd:PRK09229 191 LRRALAALPGARLGLAPH---SlravTPDQLAAVLALAapDGPVHIHIAEQTKEV--------------DDCLAWS---- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 244 piGPRPTDYIrkgdLRHAD----WLVAHGTYIEPSEfwqfrpeASSNGHRAAIA-YCPRTNARFGHDAHPYRALLAKGAI 318
Cdd:PRK09229 250 --GARPVEWL----LDHAPvdarWCLVHATHLTDAE-------TARLARSGAVAgLCPTTEANLGDGIFPAVDYLAAGGR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 319 VCLGTDSLAsspSLGVLDEARFL--------HAR------DGSLSGELLLTMATLFGAWALRAetAVGSIRAGKSADLAV 384
Cdd:PRK09229 317 FGIGSDSHV---SIDLVEELRLLeygqrlrdRRRnvlaaaAQPSVGRRLFDAALAGGAQALGR--AIGGLAVGARADLVV 391
|
250 260
....*....|....*....|....*....
gi 1015456696 385 V-----RLPDRDEDD-PHRLLFETDEPVV 407
Cdd:PRK09229 392 LdldhpALAGREGDAlLDRWVFAGGDAAV 420
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
17-138 |
1.45e-05 |
|
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: 46.86 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 17 EGPPIADgvVAIEGGRIAWVGPARERTAD---LDLGNVAIIPGLVNAHTHLELGRLAddGAAPPASPENEVEwLRRVMAQ 93
Cdd:cd01293 10 GGTALVD--IAIEDGRIAAIGPALAVPPDaeeVDAKGRLVLPAFVDPHIHLDKTFTG--GRWPNNSGGTLLE-AIIAWEE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1015456696 94 RRAGSSEEAYRENVGRNLRESIEAGTTLV---AD-TTTAGL-SWDAIAAA 138
Cdd:cd01293 85 RKLLLTAEDVKERAERALELAIAHGTTAIrthVDvDPAAGLkALEALLEL 134
|
|
| PLN02795 |
PLN02795 |
allantoinase |
11-384 |
1.92e-05 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 46.69 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 11 RYVFPvegPPIADGVVAIEGGRIAWVGPARERTAD------LDLGNVAIIPGLVNAHTHL-ELGRladdgaappaspene 83
Cdd:PLN02795 52 RVVTP---AGVIPGAVEVEGGRIVSVTKEEEAPKSqkkphvLDYGNAVVMPGLIDVHVHLnEPGR--------------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 84 VEWLRRVMAQRRAGSSEEAYRENVGRN----------LRESIEA--GTTLVADTTTAGL-SWDAIAAAPVRAVVFAEVLG 150
Cdd:PLN02795 114 TEWEGFPTGTKAAAAGGITTLVDMPLNsfpsttsvetLELKIEAakGKLYVDVGFWGGLvPENAHNASVLEELLDAGALG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 151 LKRY---RGLQTNEAAwkwlgsikpeaqVAANARAGLSPHAPYstagwlyhaaassRLPLSTHlAEMPEELRLLETRDGP 227
Cdd:PLN02795 194 LKSFmcpSGINDFPMT------------TATHIKAALPVLAKY-------------GRPLLVH-AEVVSPVESDSRLDAD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 228 LRSYLEDLGAWDEEWEPIGPR-----PTDYIRKGDLRHADWLVAHGTyiEPSEFWQFRPEASSNGHRAAIAYCPRTNArF 302
Cdd:PLN02795 248 PRSYSTYLKSRPPSWEQEAIRqllevAKDTRPGGVAEGAHVHIVHLS--DAESSLELIKEAKAKGDSVTVETCPHYLA-F 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 303 GHD-----------AHPYR---------ALLAKGAIVCLGTDSLASSPSLGVLDEARFLHARDGSLSGELLL-------- 354
Cdd:PLN02795 325 SAEeipdgdtrykcAPPIRdaanrellwKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLpatwtagr 404
|
410 420 430
....*....|....*....|....*....|....*....
gi 1015456696 355 ----TMATLFGAWALRAETAV-----GSIRAGKSADLAV 384
Cdd:PLN02795 405 ayglTLEQLARWWSERPAKLAgldskGAIAPGKDADIVV 443
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
21-65 |
6.74e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 45.09 E-value: 6.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1015456696 21 IADGVVAIEGGRIAWVGPAR-ERTADLDLGNVAIIPGLVNAHTHLE 65
Cdd:COG1001 22 ILEGDIAIAGGRIAGVGDYIgEATEVIDAAGRYLVPGFIDGHVHIE 67
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
26-64 |
9.16e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 44.54 E-value: 9.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1015456696 26 VAIEGGRIAWVGPARERTAD---LDLGNVAIIPGLVNAHTHL 64
Cdd:PRK05985 19 ILIRDGRIAAIGPALAAPPGaevEDGGGALALPGLVDGHIHL 60
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
8-63 |
1.21e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 43.93 E-value: 1.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1015456696 8 LGARYVFPVEgpPIADGVVAIEGGRIAWVGPARERTAD-LDLGNVAIIPGLVNAHTH 63
Cdd:COG1820 3 TNARIFTGDG--VLEDGALLIEDGRIAAIGPGAEPDAEvIDLGGGYLAPGFIDLHVH 57
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
22-72 |
1.29e-03 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 40.93 E-value: 1.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1015456696 22 ADgvVAIEGGRIAWVGPARERTAdLDLGNVAIIPGLVNAHTHLEL----GRLADD 72
Cdd:PRK08323 19 AD--VLIEDGKIAAIGANLGDEV-IDATGKYVMPGGIDPHTHMEMpfggTVSSDD 70
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
19-77 |
1.90e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 40.30 E-value: 1.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015456696 19 PPIADGVVAIEGGRIAWVGPARERTAD------LDLGNVAIIPGLVNAHTHL--ELGR-LADDGAAPP 77
Cdd:PRK07203 17 PVIEDGAIAIEGNVIVEIGTTDELKAKypdaefIDAKGKLIMPGLINSHNHIysGLARgMMANIPPPP 84
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
9-79 |
1.90e-03 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 40.36 E-value: 1.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015456696 9 GARYVFPVEGPP-IADgvVAIEGGRIAWVGPARERTAD--LDLGNVAIIPGLVNAHTHLELGRLADDGAAPPAS 79
Cdd:cd01297 6 NGTVVDGTGAPPfTAD--VGIRDGRIAAIGPILSTSARevIDAAGLVVAPGFIDVHTHYDGQVFWDPDLRPSSR 77
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
9-65 |
2.18e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 40.16 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1015456696 9 GARYVFPVEgppIADGVVAIEGGRIAWVGPARER-TADLDLGNVAIIPGLVNAHT-HLE 65
Cdd:PRK15446 8 NARLVLPDE---VVDGSLLIEDGRIAAIDPGASAlPGAIDAEGDYLLPGLVDLHTdNLE 63
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
13-66 |
4.53e-03 |
|
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: 39.12 E-value: 4.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1015456696 13 VFPVEGPPIADgvVAIEGGRIAWVGPARERTAD---LDLGNVAIIPGLVNAHTHLEL 66
Cdd:cd01314 8 IVTADGSFKAD--ILIEDGKIVAIGPNLEAPGGvevIDATGKYVLPGGIDPHTHLEL 62
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
295-386 |
4.56e-03 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 38.87 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015456696 295 CPRTNARFGHDAHPYRALLAKGAIVCLGTDSL-ASSPSLgvLDEARF------LHARDgslsgelLLTMATLFGAWALRA 367
Cdd:PRK07213 255 CPRANASFNVGLPPLNEMLEKGILLGIGTDNFmANSPSI--FREMEFiyklyhIEPKE-------ILKMATINGAKILGL 325
|
90
....*....|....*....
gi 1015456696 368 ETaVGSIRAGKSADLAVVR 386
Cdd:PRK07213 326 IN-VGLIEEGFKADFTFIK 343
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
26-65 |
7.21e-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: 38.53 E-value: 7.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1015456696 26 VAIEGGRIAWVGPARERTAD---LDLGNVAIIPGLVNAHTHLE 65
Cdd:COG0044 18 VLIEDGRIAAIGPDLAAPEAaevIDATGLLVLPGLIDLHVHLR 60
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
310-385 |
7.85e-03 |
|
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: 38.04 E-value: 7.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015456696 310 RALLAKGAIVCLGTDSLASSPSLGVL-DEARFLhARDGSLSGELLlTMATLFGAWALRAETAVGSIRAGKSADLAVV 385
Cdd:cd01299 257 RRAHKAGVKIAFGTDAGFPVPPHGWNaRELELL-VKAGGTPAEAL-RAATANAAELLGLSDELGVIEAGKLADLLVV 331
|
|
| |
