|
Name |
Accession |
Description |
Interval |
E-value |
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
57-415 |
2.37e-111 |
|
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: 331.57 E-value: 2.37e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 57 YHYLDGTGKIVMPGLINAHTHLFSQGKPLNPKLATPKGqrmvatfahsplgkpYMAATVKHNATTLLESGVTTIRTLGDV 136
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVE---------------YRTIRATRQARAALRAGFTTVRDAGGA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 137 GYEVvtLRDQIDAGQILGPRILASGPLMAIPEGHGAPL----------IALTSGTPEEARTAVAQNLKAGVNAIKIAATG 206
Cdd:cd01299 66 DYGL--LRDAIDAGLIPGPRVFASGRALSQTGGHGDPRglsglfpaggLAAVVDGVEEVRAAVREQLRRGADQIKIMATG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 207 GVtdAQEIGEAGSPQMSVEQMRAICDEAHQYGVIVGAHAQSPEGVRRSLLAGVDTIEHGSVLDDELIGMfrhnpnALRGY 286
Cdd:cd01299 144 GV--LSPGDPPPDTQFSEEELRAIVDEAHKAGLYVAAHAYGAEAIRRAIRAGVDTIEHGFLIDDETIEL------MKEKG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 287 SALIPTLSAGLPLtLLGQDVTGITDIQLENSKNVVGGMVSGARQAHEAGLMIGVGTDTGMTFVPQYATWRELELLVAYaG 366
Cdd:cd01299 216 IFLVPTLATYEAL-AAEGAAPGLPADSAEKVALVLEAGRDALRRAHKAGVKIAFGTDAGFPVPPHGWNARELELLVKA-G 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1469299500 367 FSPAEALHAATAVNASILGADAETGSLEVGKSADLLVLNANPLDDLRAL 415
Cdd:cd01299 294 GTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDPLEDIAVL 342
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
10-431 |
1.97e-97 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 297.64 E-value: 1.97e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 10 EPFALAHATIVTGDkAGTILRNMTIVVgADGRIEQVAPSIETSIPAEYHYLDGTGKIVMPGLINAHTHLFSQGKPLNPKL 89
Cdd:COG1228 8 GTLLITNATLVDGT-GGGVIENGTVLV-EDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 90 ATPKGQRMVATFAHSplgkpymaatvKHNATTLLESGVTTIRTLGdvGYEVvTLRDQIDAGQ---ILGPRILASGPLMAI 166
Cdd:COG1228 86 AGGGITPTVDLVNPA-----------DKRLRRALAAGVTTVRDLP--GGPL-GLRDAIIAGEsklLPGPRVLAAGPALSL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 167 PEGHGAplialtsGTPEEARTAVAQNLKAGVNAIKIAATGGVtdaqeigeagsPQMSVEQMRAICDEAHQYGVIVGAHAQ 246
Cdd:COG1228 152 TGGAHA-------RGPEEARAALRELLAEGADYIKVFAEGGA-----------PDFSLEELRAILEAAHALGLPVAAHAH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 247 SPEGVRRSLLAGVDTIEHGSVLDDELIGMFRHNpnalrGYSALIPTLSAGLPLTLLGQDVtgitdiQLENSKNVVGGMVS 326
Cdd:COG1228 214 QADDIRLAVEAGVDSIEHGTYLDDEVADLLAEA-----GTVVLVPTLSLFLALLEGAAAP------VAAKARKVREAALA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 327 GARQAHEAGLMIGVGTDTGMTFVPQYATWRELELLVAYaGFSPAEALHAATAVNASILGADAETGSLEVGKSADLLVLNA 406
Cdd:COG1228 283 NARRLHDAGVPVALGTDAGVGVPPGRSLHRELALAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDG 361
|
410 420
....*....|....*....|....*
gi 1469299500 407 NPLDDLRALEHPALVIAAGHPVWRP 431
Cdd:COG1228 362 DPLEDIAYLEDVRAVMKDGRVVDRS 386
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
66-428 |
8.61e-37 |
|
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: 137.63 E-value: 8.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 66 IVMPGLINAHTHLFS---QGKPLNPKLAtpkgqrmvatfahsplgkpymAATVKHNATTLLESGVTTIRTLGDVG-YEVV 141
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllRGIPVPPEFA---------------------YEALRLGITTMLKSGTTTVLDMGATTsTGIE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 142 TLRDQIDAgQILGPRILASGPLMAipeghgaplialtSGTPEEARTAVAQNLKAGVNAIKIAATGGVTDAqeIGEAGSPQ 221
Cdd:pfam01979 60 ALLEAAEE-LPLGLRFLGPGCSLD-------------TDGELEGRKALREKLKAGAEFIKGMADGVVFVG--LAPHGAPT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 222 MSVEQMRAICDEAHQYGVIVGAHAQSPEG-VRRSLLAGVDTIEHGSVLDdeligmFRHNPNALRGYSALI-------PTL 293
Cdd:pfam01979 124 FSDDELKAALEEAKKYGLPVAIHALETKGeVEDAIAAFGGGIEHGTHLE------VAESGGLLDIIKLILahgvhlsPTE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 294 SAGLPLTLLGqdvTGITDIQLENSKNVVGgmVSGARQAHEAGLMIGVGTDT-GMTFVPQYatWRELELLV-----AYAGF 367
Cdd:pfam01979 198 ANLLAEHLKG---AGVAHCPFSNSKLRSG--RIALRKALEDGVKVGLGTDGaGSGNSLNM--LEELRLALelqfdPEGGL 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469299500 368 SPAEALHAATAVNASILGADAETGSLEVGKSADLLVLNANPLDDLRALEH---PALVIAAGHPV 428
Cdd:pfam01979 271 SPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPdgnVKKVIVKGKIV 334
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
12-425 |
1.08e-24 |
|
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: 105.29 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 12 FALAHATIVTGDKAGTILRNMTIVVgADGRIEQVAPSIEtsIPAEYHY---LDGTGKIVMPGLINAHTHLF-------SQ 81
Cdd:COG0402 2 LLIRGAWVLTMDPAGGVLEDGAVLV-EDGRIAAVGPGAE--LPARYPAaevIDAGGKLVLPGLVNTHTHLPqtllrglAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 82 GKPLNPKLATpkgqRMVATFAHspLGKPYMAATVKHNATTLLESGVTTIRTLGDVGYEVVtlRDQIDAGQILGPRILASG 161
Cdd:COG0402 79 DLPLLDWLEE----YIWPLEAR--LDPEDVYAGALLALAEMLRSGTTTVADFYYVHPESA--DALAEAAAEAGIRAVLGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 162 PLMaipeGHGAPLIALTSGTP--EEARTAVAQNLKAGVNAIKIAatggvtdaqeIGEAGSPQMSVEQMRAICDEAHQYGV 239
Cdd:COG0402 151 GLM----DRGFPDGLREDADEglADSERLIERWHGAADGRIRVA----------LAPHAPYTVSPELLRAAAALARELGL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 240 IVGAH-AQSPEGVRRSL-LAGVDTIE---------------HGSVLDDELIGMFR-------HNP--NALRGysaliptl 293
Cdd:COG0402 217 PLHTHlAETRDEVEWVLeLYGKRPVEyldelgllgprtllaHCVHLTDEEIALLAetgasvaHCPtsNLKLG-------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 294 saglpltllgqdvTGITDIqlensknvvggmvsgaRQAHEAGLMIGVGTDTGMTFVPQ--YATWRELELL-----VAYAG 366
Cdd:COG0402 289 -------------SGIAPV----------------PRLLAAGVRVGLGTDGAASNNSLdmFEEMRLAALLqrlrgGDPTA 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469299500 367 FSPAEALHAATAVNASILGADAETGSLEVGKSADLLVLNANPLdDLRALEHP--ALVIAAG 425
Cdd:COG0402 340 LSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAP-HLAPLHDPlsALVYAAD 399
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-412 |
6.96e-15 |
|
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: 75.76 E-value: 6.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 35 VVGADGRIEQVAP--SIETSIPAEYHYLDGTGKIVMPGLINAHTHL-FSqgkplnpklatpkGQRmVATFAHSPLGKPYM 111
Cdd:cd01296 1 IAIRDGRIAAVGPaaSLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLvFA-------------GDR-VDEFAARLAGASYE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 112 ---------AATVKH--NATT-------------LLESGVTTIRTLGDVGYEVVTLRDQIDAGQILGprilASGPLMAIP 167
Cdd:cd01296 67 eilaagggiLSTVRAtrAASEdelfasalrrlarMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLK----EEGPVDLVS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 168 EGHGAplialtSGTPEEARTAVAQnlkagVNAI------KIAATGGVTDAQEIGEAGspQMSVEQMRAICDEAHQYGVIV 241
Cdd:cd01296 143 TFLGA------HAVPPEYKGREEY-----IDLVieevlpAVAEENLADFCDVFCEKG--AFSLEQSRRILEAAKEAGLPV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 242 GAHAQSPE---GVRRSLLAGVDTIEHGSVLDDEligmfrhnpnalrGYSALIptlSAGLPLTLLGqdvtgITDIQLENSK 318
Cdd:cd01296 210 KIHADELSnigGAELAAELGALSADHLEHTSDE-------------GIAALA---EAGTVAVLLP-----GTAFSLRETY 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 319 NVvggmvsgARQAHEAGLMIGVGTD--------TGMTFVpqyatwreLELLVAYAGFSPAEALHAATAVNASILGADAET 390
Cdd:cd01296 269 PP-------ARKLIDAGVPVALGTDfnpgssptSSMPLV--------MHLACRLMRMTPEEALTAATINAAAALGLGETV 333
|
410 420
....*....|....*....|..
gi 1469299500 391 GSLEVGKSADLLVLNANPLDDL 412
Cdd:cd01296 334 GSLEVGKQADLVILDAPSYEHL 355
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
16-428 |
2.43e-14 |
|
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: 74.55 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 16 HATIVTGDkAGTILRNMTIVVgADGRIEQVAPSIE-TSIPAEYHyLDGTGKIVMPGLINAHTHLFS-------QGKPLNP 87
Cdd:cd01298 5 NGTIVTTD-PRRVLEDGDVLV-EDGRIVAVGPALPlPAYPADEV-IDAKGKVVMPGLVNTHTHLAMtllrglaDDLPLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 88 KLatpkgQRMVATFAhSPLGKPYMAATVKHNATTLLESGVTTIrtlGDVGYEVVTlrDQIDAGQILGPRILAsgplmaip 167
Cdd:cd01298 82 WL-----KDLIWPLE-RLLTEEDVYLGALLALAEMIRSGTTTF---ADMYFFYPD--AVAEAAEELGIRAVL-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 168 eGHGapLIALTSGTPEEARTAVAQNLKAgVNAIKIAATGGVTDAqeIGEAGSPQMSVEQMRAICDEAHQYGVIVGAHAQS 247
Cdd:cd01298 143 -GRG--IMDLGTEDVEETEEALAEAERL-IREWHGAADGRIRVA--LAPHAPYTCSDELLREVAELAREYGVPLHIHLAE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 248 PEG-VRRSL---------------LAGVDTI-EHGSVLDDELIGMFR-------HNPNAlrgysaliptlsaglpltllg 303
Cdd:cd01298 217 TEDeVEESLekygkrpveyleelgLLGPDVVlAHCVWLTDEEIELLAetgtgvaHNPAS--------------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 304 qdvtgitdiqleNSKNVVGgmVSGARQAHEAGLMIGVGTDTG-------MtfvpqyatWRELEL--LVAYAGFSPAEALH 374
Cdd:cd01298 276 ------------NMKLASG--IAPVPEMLEAGVNVGLGTDGAasnnnldM--------FEEMRLaaLLQKLAHGDPTALP 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469299500 375 AATAV-NASILGADA----ETGSLEVGKSADLLVLnanpldDLRALEHPALVIAAGHPV 428
Cdd:cd01298 334 AEEALeMATIGGAKAlgldEIGSLEVGKKADLILI------DLDGPHLLPVHDPISHLV 386
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
215-430 |
2.11e-12 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 69.06 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 215 GEAGSPQMSVEQMRAICDEAHQYGVIVGAHAQSPEGVRRSL------LAGV------DTIEHGSVLDDELIGMFRhnpnA 282
Cdd:COG1574 311 GNRGLLLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLdayeaaRAANgrrdrrHRIEHAQLVDPDDLARFA----E 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 283 LRGYSALIP---TLSAGLPLTLLGQDvtgitdiQLENSknvvggmvSGARQAHEAGLMIGVGTDTGMTFV-P----QYAT 354
Cdd:COG1574 387 LGVIASMQPthaTSDGDWAEDRLGPE-------RAARA--------YPFRSLLDAGAPLAFGSDAPVEPLdPllgiYAAV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 355 WRELELLVAYA---GFSPAEALHAATAVNASILGADAETGSLEVGKSADLLVLNANPL----DDLRALEhPALVIAAGHP 427
Cdd:COG1574 452 TRRTPSGRGLGpeeRLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLtvppEEIKDIK-VLLTVVGGRV 530
|
...
gi 1469299500 428 VWR 430
Cdd:COG1574 531 VYE 533
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
40-425 |
3.81e-12 |
|
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: 67.44 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 40 GRIEQVAPSIETSIPAEYHYLDGTGKIVMPGLINAHTHL-FS-----------QGKPLNPKLATPKGQR--MVATFAHSp 105
Cdd:TIGR01224 11 GKIVWIGQLAALPGEEATEIIDCGGGLVTPGLVDPHTHLvFAgdrvnefemklQGASYLEILAQGGGILstVRATRAAS- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 106 lgKPYMAATVKHNATTLLESGVTTIRTLGDVGYEVVTLRDQIDAGQILGPrilaSGPLMAIPEGHGAPLIAL-TSGTPEE 184
Cdd:TIGR01224 90 --EEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHE----EQPVDVVTTFLGAHAVPPeFQGRPDD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 185 ARTAVAQNLKAgvnaiKIAATGGVTDAQEIGEAGSpqMSVEQMRAICDEAHQYGVIVGAHAQSPEGVRRSLLAG------ 258
Cdd:TIGR01224 164 YVDGICEELIP-----QVAEEGLASFADVFCEAGV--FSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAklgavs 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 259 VDTIEHgsvLDDELIgmfrhnpnALRGYSALIPTLsagLPLTLLgqdvtgitdiqlensknVVGGMVSGARQAHEAGLMI 338
Cdd:TIGR01224 237 ADHLEH---ASDAGI--------KALAEAGTVAVL---LPGTTF-----------------YLRETYPPARQLIDYGVPV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 339 GVGTDTGMTFVPQYATWRELELLVAYAGFSPAEALHAATAVNASILGADAETGSLEVGKSADLLVLNANPLDDLR---AL 415
Cdd:TIGR01224 286 ALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEALHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPyhyGV 365
|
410
....*....|
gi 1469299500 416 EHPALVIAAG 425
Cdd:TIGR01224 366 NHVHAVIKNG 375
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-410 |
1.19e-09 |
|
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: 59.63 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 39 DGRIEQVAPSIETsiPAEYHYLDGTGKIVMPGLINAHTHLFSQGKPLNPklATPKGQRMVATFAhsplgkPYMAATVKHN 118
Cdd:cd01309 1 DGKIVAVGAEITT--PADAEVIDAKGKHVTPGLIDAHSHLGLDEEGGVR--ETSDANEETDPVT------PHVRAIDGIN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 119 AT-----TLLESGVTTIRTL----GDVGYEVVTLRDQidagqilgprilASGPLMAIPEGHGAPLIALtsgtpeeartav 189
Cdd:cd01309 71 PDdeafkRARAGGVTTVQVLpgsaNLIGGQGVVIKTD------------GGTIEDMFIKAPAGLKMAL------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 190 aqnlkaGVNAIKIAATGGVTDAQEIGEAGspqmsveQMRAICDEAHQYG-VIVGAHAQSPEGVRRSL----LAGVDTIE- 263
Cdd:cd01309 127 ------GENPKRVYGGKGKEPATRMGVAA-------LLRDAFIKAQEYGrKYDLGKNAKKDPPERDLkleaLLPVLKGEi 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 264 ----HGSVLDDELIGM-----FRHNPNALRGYSA--LIPTLSA-GLPLtLLGQDVTGITDIQLensknVVGGMVSGARQA 331
Cdd:cd01309 194 pvriHAHRADDILTAIriakeFGIKITIEHGAEGykLADELAKhGIPV-IYGPTLTLPKKVEE-----VNDAIDTNAYLL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 332 HEAGLMIGVGTDTgmTFVPQyatwRELELLVAYA---GFSPAEALHAATAVNASILGADAETGSLEVGKSADLLVLNANP 408
Cdd:cd01309 268 KKGGVAFAISSDH--PVLNI----RNLNLEAAKAvkyGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDP 341
|
..
gi 1469299500 409 LD 410
Cdd:cd01309 342 LE 343
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
13-407 |
3.87e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 58.19 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 13 ALAHATIVTGDKagtILRNMTIVVgADGRIEQVAPSIETSIPAeyhyLDGTGKIVMPGLINAHTH-----LFSQGkplnp 87
Cdd:COG1820 1 AITNARIFTGDG---VLEDGALLI-EDGRIAAIGPGAEPDAEV----IDLGGGYLAPGFIDLHVHggggvDFMDG----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 88 klaTPKG-QRMVATFAhsplgkpymaatvKHNATTLLESGVTTirtlgdvgyEVVTLRDQIDA-----GQILGPRILAS- 160
Cdd:COG1820 68 ---TPEAlRTIARAHA-------------RHGTTSFLPTTITA---------PPEDLLRALAAiaeaiEQGGGAGILGIh 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 161 --GPLMAiPEGHGA-PLIALTSGTPEEartaVAQNLKAGVNAIKIaatggVTDAQEIGEAgspqmsveqMRAIcDEAHQY 237
Cdd:COG1820 123 leGPFLS-PEKKGAhPPEYIRPPDPEE----LDRLLEAAGGLIKL-----VTLAPELPGA---------LEFI-RYLVEA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 238 GVIVGA-H-AQSPEGVRRSLLAGVDTIEH----------------GSVLDD-----ELIGMFRH-NPNALR------GYS 287
Cdd:COG1820 183 GVVVSLgHtDATYEQARAAFEAGATHVTHlfnamsplhhrepgvvGAALDDddvyaELIADGIHvHPAAVRlalrakGPD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 288 ALIP----TLSAGLPL---TLLGQDVTgitdiqlensknVVGGMvsgARQAHeaglmiGV--GTDTGMtfvpqyatWREL 358
Cdd:COG1820 263 RLILvtdaMAAAGLPDgeyELGGLEVT------------VKDGV---ARLAD------GTlaGSTLTM--------DDAV 313
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1469299500 359 ELLVAYAGFSPAEALHAATAVNASILGADAETGSLEVGKSADLLVLNAN 407
Cdd:COG1820 314 RNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
17-428 |
9.33e-09 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 57.17 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 17 ATIVTGDKAGTILRNMTIVVgADGRIEQVAPSIETSIPAEyHYLDGTGKIVMPGLINAHTHLF---------SQGKPLNP 87
Cdd:PRK08203 9 LAIVTMDAARREIADGGLVV-EGGRIVEVGPGGALPQPAD-EVFDARGHVVTPGLVNTHHHFYqtltralpaAQDAELFP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 88 KLATpkgqrMVATFAHspLGKPYMAATVKHNATTLLESGVTTI--------RTLGDVgyevvtLRDQIDAGQILGPRILA 159
Cdd:PRK08203 87 WLTT-----LYPVWAR--LTPEMVRVATQTALAELLLSGCTTSsdhhylfpNGLRDA------LDDQIEAAREIGMRFHA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 160 SGPLMAIPEGHGaplialtsGTPEEartAVAQNLkagvNAIkIAATGGVTDAQEIGEAG----------SPqMSV--EQM 227
Cdd:PRK08203 154 TRGSMSLGESDG--------GLPPD---SVVEDE----DAI-LADSQRLIDRYHDPGPGamlrialapcSP-FSVsrELM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 228 RAICDEAHQYGVIVGAH-AQSPEGVRRSL----LAGVDTIE------------HGSVLDDELIGMF-------RHNP--N 281
Cdd:PRK08203 217 RESAALARRLGVRLHTHlAETLDEEAFCLerfgMRPVDYLEdlgwlgpdvwlaHCVHLDDAEIARLartgtgvAHCPcsN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 282 ALRGySALIPT---LSAGLPLTlLGQDVTgitdiqlenSKNVVGGMVSGARQAheaglmigvgtdtgmtfvpqyatwrel 358
Cdd:PRK08203 297 MRLA-SGIAPVrelRAAGVPVG-LGVDGS---------ASNDGSNLIGEARQA--------------------------- 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469299500 359 eLLVAYAGFSPA-----EALHAATAVNASILGADaETGSLEVGKSADLLVLNanpLDDLRA--LEHP--ALVIAAGHPV 428
Cdd:PRK08203 339 -LLLQRLRYGPDamtarEALEWATLGGARVLGRD-DIGSLAPGKLADLALFD---LDELRFagAHDPvaALVLCGPPRA 412
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
33-409 |
9.58e-09 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 56.97 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 33 TIVVGADGRIEQVAPSIETSipaeyHYLDGTGKIVmPGLINAHTHL-------FSQGKPLNPKLATPKGQRMVAtFAHSP 105
Cdd:PRK07213 20 GNLVIEDGIIKGFTNEVHEG-----NVIDAKGLVI-PPLINAHTHIgdssikdIGIGKSLDELVKPPNGLKHKF-LNSCS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 106 LGKpyMAATVKHNATTLLESGVTTIRTLGDVGYEVVTLRDQIDAGQILGPRILasgplmaipeghGAPlialTSGTPEEA 185
Cdd:PRK07213 93 DKE--LVEGMKEGLYDMYNNGIKAFCDFREGGIKGINLLKKASSDLPIKPIIL------------GRP----TEADENEL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 186 RTAVAQNLKAgvnaikiaatggvtdAQEIGEAGSPQMSVEQMRAICDEAHQYGVIVGAH-AQSPEGVRRSLL-------- 256
Cdd:PRK07213 155 KKEIREILKN---------------SDGIGLSGANEYSDEELKFICKECKREKKIFSIHaAEHKGSVEYSLEkygmteie 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 257 ----AGV--DTIEHGSVLDDELIGMFRHNPNALrgysALIP----TLSAGLPltllgqdvtgitDIqlensknvvggmvs 326
Cdd:PRK07213 220 rlinLGFkpDFIVHATHPSNDDLELLKENNIPV----VVCPranaSFNVGLP------------PL-------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 327 gaRQAHEAGLMIGVGTDTGMTFVPqyATWRELELLVAYAGFSPAEALHAATAVNASILGADaETGSLEVGKSADLLVLNA 406
Cdd:PRK07213 270 --NEMLEKGILLGIGTDNFMANSP--SIFREMEFIYKLYHIEPKEILKMATINGAKILGLI-NVGLIEEGFKADFTFIKP 344
|
...
gi 1469299500 407 NPL 409
Cdd:PRK07213 345 TNI 347
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
61-428 |
2.00e-08 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 56.39 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 61 DGTGKIVMPGLINAHTHLFSQGK-----PLNPKLATPKGQRMVATFAH-----------------------------SPL 106
Cdd:pfam07969 4 DAKGRLVLPGFVDPHTHLDGGGLnlrelRLPDVLPNAVVKGQAGRTPKgrwlvgegwdeaqfaetrfpyaladldevAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 107 GKPYMAATVKHNA---TTLLESGVTTIRTLGDVGYEVVTLRDQIDAGQILGPRILASGPLMAIPE-------------GH 170
Cdd:pfam07969 84 GPVLLRALHTHAAvanSAALDLAGITKATEDPPGGEIARDANGEGLTGLLREGAYALPPLLAREAeaaavaaalaalpGF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 171 G-----------------APLIALTSGTPEEARTAVAQNL-------KAGVNAIKIAA-------TGGVTDAQ-EIGEAG 218
Cdd:pfam07969 164 GitsvdggggnvhslddyEPLRELTAAEKLKELLDAPERLglphsiyELRIGAMKLFAdgvlgsrTAALTEPYfDAPGTG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 219 SPQMSVEQMRAICDEAHQYGVIVGAHAQSPEGVRRSLLA-----------GVDTIEHGSVLDDeligmfrHNPNALRGYS 287
Cdd:pfam07969 244 WPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAfeavaeklgnqGRVRIEHAQGVVP-------YTYSQIERVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 288 AL--IPTLSAGLPLTLLGQDVTGITDIQLENSkNVVGGMVSgarqaheAGLMIGVGTDTGMT-FVPQYA--------TWR 356
Cdd:pfam07969 317 ALggAAGVQPVFDPLWGDWLQDRLGAERARGL-TPVKELLN-------AGVKVALGSDAPVGpFDPWPRigaavmrqTAG 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469299500 357 ELELLVAYAGFSPAEALHAATAVNASILGADAETGSLEVGKSADLLVLNANPLD---DLRALEHPALVIAAGHPV 428
Cdd:pfam07969 389 GGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTvdpPAIADIRVRLTVVDGRVV 463
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
35-428 |
2.01e-08 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 56.10 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 35 VVGADGRIEQVAPSIEtsIPAEYHYLDGTGKIVMPGLINAHTHL---FSQGKPLNPKLaTPKGQRMVATFAhspLGKPYM 111
Cdd:cd01293 17 IAIEDGRIAAIGPALA--VPPDAEEVDAKGRLVLPAFVDPHIHLdktFTGGRWPNNSG-GTLLEAIIAWEE---RKLLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 112 AATVKHNATTLLE----SGVTTIRTLGDV-------GYEVV-----TLRDQIDAgQILgprilasgplmAIPEgHGaplI 175
Cdd:cd01293 91 AEDVKERAERALElaiaHGTTAIRTHVDVdpaaglkALEALlelreEWADLIDL-QIV-----------AFPQ-HG---L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 176 ALTSGTPEEARTAvaqnLKAGvnaikiAATGGVTDAQEIGEAGspqmsVEQMRAICDEAHQYGVIVGAH---AQSPEGV- 251
Cdd:cd01293 155 LSTPGGEELMREA----LKMG------ADVVGGIPPAEIDEDG-----EESLDTLFELAQEHGLDIDLHldeTDDPGSRt 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 252 ---------RRSLLAGVdTIEHGSVLDDeligmfrHNPNALRgysALIPTL-SAGLPLTLLGQdvTGITDIQLENSKNVV 321
Cdd:cd01293 220 leelaeeaeRRGMQGRV-TCSHATALGS-------LPEAEVS---RLADLLaEAGISVVSLPP--INLYLQGREDTTPKR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 322 GGMVSgARQAHEAGLMIGVGTDTGM-TFVP-----------------QYATWRELELLVAYAGFSPAEALhaatavnasi 383
Cdd:cd01293 287 RGVTP-VKELRAAGVNVALGSDNVRdPWYPfgsgdmlevanlaahiaQLGTPEDLALALDLITGNAARAL---------- 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1469299500 384 lgaDAETGSLEVGKSADLLVLNA-NPLDDLRALEHPALVIAAGHPV 428
Cdd:cd01293 356 ---GLEDYGIKVGCPADLVLLDAeDVAEAVARQPPRRVVIRKGRVV 398
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
14-249 |
4.43e-08 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 55.10 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 14 LAHATIVTGDKagtiLRNMTIVVgADGRIEQVAPSIETSIPAEYhyLDGTGKIVMPGLINAHTHLfsqGKPlnpklatpk 93
Cdd:COG0044 2 IKNGRVVDPGG----LERADVLI-EDGRIAAIGPDLAAPEAAEV--IDATGLLVLPGLIDLHVHL---REP--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 94 GQRMVATFAHSplgkpyMAATVKhnattlleSGVTTI----RTLGdvgyeVVTLRDQIDAgqilgprilasgpLMAIPEG 169
Cdd:COG0044 63 GLEHKEDIETG------TRAAAA--------GGVTTVvdmpNTNP-----VTDTPEALEF-------------KLARAEE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 170 HG----APLIALTSGTPEEArTAVAQNLKAGVNAIKIAATggvtdaqeiGEAGSPQMSVEQMRAICDEAHQYGVIVGAHA 245
Cdd:COG0044 111 KAlvdvGPHGALTKGLGENL-AELGALAEAGAVAFKVFMG---------SDDGNPVLDDGLLRRALEYAAEFGALVAVHA 180
|
....
gi 1469299500 246 QSPE 249
Cdd:COG0044 181 EDPD 184
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
17-448 |
1.37e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 53.47 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 17 ATIVTGDKAGTILRNMTIVVgADGRIEQVAPSIEtsiPAEYHYLDGTGKIVMPGLINAHTHLFSQG-KPLNPKLATPKGQ 95
Cdd:PRK08204 9 GTVLTMDPAIGDLPRGDILI-EGDRIAAVAPSIE---APDAEVVDARGMIVMPGLVDTHRHTWQSVlRGIGADWTLQTYF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 96 RMVatfaHSPLGKPYMAATVkHNATTL-----LESGVTtirTLGDVGYEVVTLrDQIDAgQILGprILASGPLMAIpeGH 170
Cdd:PRK08204 85 REI----HGNLGPMFRPEDV-YIANLLgaleaLDAGVT---TLLDWSHINNSP-EHADA-AIRG--LAEAGIRAVF--AH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 171 GAPLIAltsgtPEEARTAVAQNLkAGVNAIKIA----ATGGVTDAQEI--GEAGSPQMSVEQMRAICD-----EAHQYGV 239
Cdd:PRK08204 151 GSPGPS-----PYWPFDSVPHPR-EDIRRVKKRyfssDDGLLTLGLAIrgPEFSSWEVARADFRLARElglpiSMHQGFG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 240 IVGAHAQSPEGVRRSLLAGVD-TIEHGSVLDDELIGMFrhnpnALRGYSALI-PTLSAGLPltlLGQDVTGitdiqlens 317
Cdd:PRK08204 225 PWGATPRGVEQLHDAGLLGPDlNLVHGNDLSDDELKLL-----ADSGGSFSVtPEIEMMMG---HGYPVTG--------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 318 knvvggmvsgarQAHEAGLMIGVGTD----------TGMTFVPQYAT-------WRELELLVAYAGFSPAEALHAATAVN 380
Cdd:PRK08204 288 ------------RLLAHGVRPSLGVDvvtstggdmfTQMRFALQAERardnavhLREGGMPPPRLTLTARQVLEWATIEG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 381 ASILGADAETGSLEVGKSADLLVLNANPLDDLRALE---------HPA---LVIAAGHPVWRPGPKRFADIDALLDEAYA 448
Cdd:PRK08204 356 ARALGLEDRIGSLTPGKQADLVLIDATDLNLAPVHDpvgavvqsaHPGnvdSVMVAGRAVKRNGKLLGVDLERLRRLAAA 435
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
329-413 |
5.08e-07 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 51.89 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 329 RQAHEAGLMIGVGTDTGMTFVPQ--------YATWRELE-LLVAYAGFSPAEALHAATAVNASILGADAETGSLEVGKSA 399
Cdd:cd01303 304 RKLLDAGIKVGLGTDVGGGTSFSmldtlrqaYKVSRLLGyELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEF 383
|
90
....*....|....*.
gi 1469299500 400 DLLVLN--ANPLDDLR 413
Cdd:cd01303 384 DAVVIDpsATPLLADR 399
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
329-414 |
5.21e-07 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 51.73 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 329 RQAHEAGLMIGVGTDT--GMTFVPqyatwreL-ELLVAY-------AGFSPAEALHAATAVNASILGADAETGSLEVGKS 398
Cdd:PRK09228 307 KRADAAGVRVGLGTDVggGTSFSM-------LqTMNEAYkvqqlqgYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKE 379
|
90
....*....|....*...
gi 1469299500 399 ADLLVLN--ANPLDDLRA 414
Cdd:PRK09228 380 ADFVVLDpaATPLLALRT 397
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
71-377 |
2.37e-06 |
|
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: 48.87 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 71 LINAHTHLFSqgkPLNPKLATPKGQRMVATFAHSPLgKPYMAATVKHnattLLESGVTTIRTLGDVGYEVVTLRD-QIDA 149
Cdd:cd01292 1 FIDTHVHLDG---SALRGTRLNLELKEAEELSPEDL-YEDTLRALEA----LLAGGVTTVVDMGSTPPPTTTKAAiEAVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 150 GQILGPRILASGPLMAIPEGHGAPLIALTSGTPEEARTAvaqnLKAGVNAIKIAATGGVTDAqeigeagspqmSVEQMRA 229
Cdd:cd01292 73 EAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRG----LELGAVGLKLAGPYTATGL-----------SDESLRR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 230 ICDEAHQYGVIVGAHAQSP--------EGVRRSLLAGVDTIEHGSVLDDELIGMFRhnpnaLRGYSALIptlsAGLPLTL 301
Cdd:cd01292 138 VLEEARKLGLPVVIHAGELpdptraleDLVALLRLGGRVVIGHVSHLDPELLELLK-----EAGVSLEV----CPLSNYL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469299500 302 LGQDVTGITDIQLensknvvggmvsgarqAHEAGLMIGVGTDT--GMTFVPQYATWRELeLLVAYAGFSPAEALHAAT 377
Cdd:cd01292 209 LGRDGEGAEALRR----------------LLELGIRVTLGTDGppHPLGTDLLALLRLL-LKVLRLGLSLEEALRLAT 269
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
27-78 |
2.43e-06 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 49.52 E-value: 2.43e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469299500 27 TILRNMTIV---------VGA-DGRIEQVAPSIEtsIPAEYHYLDGTGKIVMPGLINAHTHL 78
Cdd:cd01314 1 LIIKNGTIVtadgsfkadILIeDGKIVAIGPNLE--APGGVEVIDATGKYVLPGGIDPHTHL 60
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
29-425 |
2.77e-06 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 49.31 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 29 LRNMTIVVgADGRIEQVAPSIETSIPAEYHYLDGTGKIVMPGLINAHTHLFSQGKPLNPKLATPKGQRMVATFAHSP--- 105
Cdd:cd01308 15 LGKKDILI-AGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVTLSDLTTAGVTtvv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 106 --LGKPYMAATVKH---NATTLLESGVTTIRTLGdvGYEVV--TLRDQIDAGQILGPRILASGPLMAIPEGHGAPLIALT 178
Cdd:cd01308 94 gcLGTDGISRSMEDllaKARALEEEGITCFVYTG--SYEVPtrTITGSIRKDLLLIDKVIGVGEIAISDHRSSQPTVEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 179 SGTPEEARTAVAQNLKAGVNAIKIAATggvtdaqeiGEAGSPQMSVEQMRAIcdEAHQYgvivgahaqSPEGVRRS---L 255
Cdd:cd01308 172 ARIAAEARVGGLLGGKAGIVHIHLGDG---------KRALSPIFELIEETEI--PITQF---------LPTHINRTaplF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 256 LAGVDTIEHGSVLD-DELIGMFRHNPNALRGYSALIPTLSAGLPLtllgQDVTGITDIQlensknvvGGMVSGARQAHEA 334
Cdd:cd01308 232 EQGVEFAKMGGTIDlTSSIDPQFRKEGEVRPSEALKRLLEQGVPL----ERITFSSDGN--------GSLPKFDENGNLV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 335 GLMIGvGTDTgmtfvpqyaTWRELELLVAYAGFSPAEALHAATAVNASILGADAEtGSLEVGKSADLLVLNanplDDLRa 414
Cdd:cd01308 300 GLGVG-SVDT---------LLREVREAVKCGDIPLEVALRVITSNVARILKLRKK-GEIQPGFDADLVILD----KDLD- 363
|
410
....*....|.
gi 1469299500 415 LEHpalVIAAG 425
Cdd:cd01308 364 INS---VIAKG 371
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
17-80 |
2.83e-06 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 49.55 E-value: 2.83e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469299500 17 ATIVTGDKAGTILRNMTIVVgADGRIEQVAPSIEtsIPAEY---HYLDGTGKIVMPGLINAHTHLFS 80
Cdd:PRK07203 7 GTAITRDPAKPVIEDGAIAI-EGNVIVEIGTTDE--LKAKYpdaEFIDAKGKLIMPGLINSHNHIYS 70
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
23-85 |
3.04e-06 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 49.01 E-value: 3.04e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469299500 23 DKAGTILRNMTIVVgADGRIEQVAPSIETSipAEYHYLDGTGKIVMPGLINAHTHLFSQGKPL 85
Cdd:COG3964 11 DPANGIDGVMDIAI-KDGKIAAVAKDIDAA--EAKKVIDASGLYVTPGLIDLHTHVFPGGTDY 70
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
13-417 |
4.11e-06 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 48.85 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 13 ALAHATIVTGDKAGTILRNMTIVVgADGRIEQVAPSIETSIPAEYHYLDGTGKIVMPGLINAHTHlfsqgkplnPKLATP 92
Cdd:PRK06687 3 VFQHVNIVTCDQDFHVYLDGILAV-KDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTH---------SAMTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 93 KGQRMVATF----------AHSPLGKPYMAATVKHNATTLLESGVTTIRTLGDV-GYEVvtlrDQI-DAGQILGPRILAS 160
Cdd:PRK06687 73 RGIRDDSNLhewlndyiwpAESEFTPDMTTNAVKEALTEMLQSGTTTFNDMYNPnGVDI----QQIyQVVKTSKMRCYFS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 161 GPLMAIPEGHGAPLIALTSGTPEEARTAVAQNLKagvnaIKIAATGGVTDAQEIGEAG---SPQMSVEQMRAICDEAHQY 237
Cdd:PRK06687 149 PTLFSSETETTAETISRTRSIIDEILKYKNPNFK-----VMVAPHSPYSCSRDLLEASlemAKELNIPLHVHVAETKEES 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 238 GVIVGAHAQSPegvrRSLLAGVDTIEHGSVlddeligmFRH----NPNALRGYSAlIPTLSAGLPLT--LLGQDVTGITD 311
Cdd:PRK06687 224 GIILKRYGKRP----LAFLEELGYLDHPSV--------FAHgvelNEREIERLAS-SQVAIAHNPISnlKLASGIAPIIQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 312 IQlensknvvggmvsgarqahEAGLMIGVGTDT--GMTFVPQYATWRELELLVAY-----AGFSPAEALHAATAVNASIL 384
Cdd:PRK06687 291 LQ-------------------KAGVAVGIATDSvaSNNNLDMFEEGRTAALLQKMksgdaSQFPIETALKVLTIEGAKAL 351
|
410 420 430
....*....|....*....|....*....|...
gi 1469299500 385 GADAETGSLEVGKSADLLVLNANPLDDLRALEH 417
Cdd:PRK06687 352 GMENQIGSLEVGKQADFLVIQPQGKIHLQPQEN 384
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
126-403 |
4.94e-06 |
|
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: 48.84 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 126 GVTTIRTLGDVGYEVVTLRDQIDAGQILGPRILASGPLMAIPEGHGAPLIALTSGTPEEartavaqnlKAGVNAIKIAAt 205
Cdd:cd01300 196 GVTTVHDAGGGAADDIEAYRRLAAAGELTLRVRVALYVSPLAEDLLEELGARKNGAGDD---------RLRLGGVKLFA- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 206 GGVTDAQ----------EIGEAGSPQMSVEQMRAICDEAHQYGVIVGAHAQSPEGVRRSL-----------LAGV-DTIE 263
Cdd:cd01300 266 DGSLGSRtaalsepyldSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGDRAVDTVLdaleaalkdnpRADHrHRIE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 264 HGSVLDDELIGMFRhnpnALRGYSALIPT--LSAG--LPLTLLGQDVTGITDiqlensknvvggmvsGARQAHEAGLMIG 339
Cdd:cd01300 346 HAQLVSPDDIPRFA----KLGVIASVQPNhlYSDGdaAEDRRLGEERAKRSY---------------PFRSLLDAGVPVA 406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469299500 340 VGTDTGMTFV-PQYA--------TWRELELLVAYAGFSPAEALHAATAVNASILGADAETGSLEVGKSADLLV 403
Cdd:cd01300 407 LGSDAPVAPPdPLLGiwaavtrkTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
17-78 |
5.75e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 48.21 E-value: 5.75e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469299500 17 ATIVTGDKAGtiLRNMTIVVgADGRIEQVAPSIETSIPAeyhYLDGTGKIVMPGLINAHTHL 78
Cdd:PRK06038 9 AYVLTMDAGD--LKKGSVVI-EDGTITEVSESTPGDADT---VIDAKGSVVMPGLVNTHTHA 64
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
13-405 |
6.81e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 47.96 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 13 ALAHATIVTGDKagtiLRNMTIVVgADGRIEQVAPSIEtsIPAEYHYLDGTGKIVMPGLINAHTH-----LFSQGkplnp 87
Cdd:cd00854 2 IIKNARILTPGG----LEDGAVLV-EDGKIVAIGPEDE--LEEADEIIDLKGQYLVPGFIDIHIHggggaDFMDG----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 88 klaTPKGQRMVAtfahsplgkpymAATVKHNATTLLESGVTTirTLGDVGYEVVTLRDQIDAGQilGPRIL---ASGPLM 164
Cdd:cd00854 70 ---TAEALKTIA------------EALAKHGTTSFLPTTVTA--PPEEIAKALAAIAEAIAEGQ--GAEILgihLEGPFI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 165 AiPEGHGA-PLIALTSGTPEEartaVAQNLKAGVNAIKIaatggVTDAQEIGEAGspqmsveqmrAICDEAHQYGVIVGA 243
Cdd:cd00854 131 S-PEKKGAhPPEYLRAPDPEE----LKKWLEAAGGLIKL-----VTLAPELDGAL----------ELIRYLVERGIIVSI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 244 -H-AQSPEGVRRSLLAGVDTIEH----------------GSVLDD-----ELIGMFRH-NPNALR------GYSALI--- 290
Cdd:cd00854 191 gHsDATYEQAVAAFEAGATHVTHlfnamsplhhrepgvvGAALSDddvyaELIADGIHvHPAAVRlayrakGADKIVlvt 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 291 -PTLSAGLP---LTLLGQDVTgitdiqlensknVVGGmvsGARQAHE--AG----LMIGVGTdtgmtfvpqyatwrelel 360
Cdd:cd00854 271 dAMAAAGLPdgeYELGGQTVT------------VKDG---VARLADGtlAGstltMDQAVRN------------------ 317
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1469299500 361 LVAYAGFSPAEALHAATAVNASILGADAETGSLEVGKSADLLVLN 405
Cdd:cd00854 318 MVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD 362
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
14-77 |
4.20e-05 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 45.67 E-value: 4.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 14 LAHAT-IVTGDKAGTILRNMTIVVgADGRIEQVAPSIEtsipAEYHY-----LDGTGKIVMPGLINAHTH 77
Cdd:PRK09045 10 LIEARwIVPVEPAGVVLEDHAVAI-RDGRIVAILPRAE----ARARYaaaetVELPDHVLIPGLINAHTH 74
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
27-78 |
8.26e-05 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 44.78 E-value: 8.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469299500 27 TILRNMTIV---------VG-ADGRIEQVAPSIETSIpaeyhyLDGTGKIVMPGLINAHTHL 78
Cdd:PRK08323 3 TLIKNGTVVtaddtykadVLiEDGKIAAIGANLGDEV------IDATGKYVMPGGIDPHTHM 58
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
370-425 |
1.32e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 44.13 E-value: 1.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469299500 370 AEALHAATAVNASILGADAETGSLEVGKSADLLVLnanpldDLRALE-----HPA--LVIAAG 425
Cdd:PRK09045 343 HTALRMATLNGARALGLDDEIGSLEPGKQADLVAV------DLSGLEtqpvyDPVsqLVYAAG 399
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
39-78 |
1.33e-04 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 44.06 E-value: 1.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1469299500 39 DGRIEQVAPSIEtsIPAEYHYLDGTGKIVMPGLINAHTHL 78
Cdd:PLN02942 29 DGIIVAVAPNLK--VPDDVRVIDATGKFVMPGGIDPHTHL 66
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
38-85 |
1.56e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 43.69 E-value: 1.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1469299500 38 ADGRIEQVAPSIETSIPAEYhyLDGTGKIVMPGLINAHTHLFSQGKPL 85
Cdd:PRK09237 24 EDGKIAAVAGDIDGSQAKKV--IDLSGLYVSPGWIDLHVHVYPGSTPY 69
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
27-432 |
2.70e-04 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 43.05 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 27 TILRNMTIVVGA------------DGRIEQVAPSIETSIPAEyhyLDGTGKIVMPGLINAHTHlfSQGKPLNPklatpkg 94
Cdd:cd01297 2 LVIRNGTVVDGTgappftadvgirDGRIAAIGPILSTSAREV---IDAAGLVVAPGFIDVHTH--YDGQVFWD------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 95 qrmvatfahsplgkPYMAATVKHNATT--LLESGVTTI----RTLGDVGYEVVTLRDQIDAGQILGP------RILASGP 162
Cdd:cd01297 70 --------------PDLRPSSRQGVTTvvLGNCGVSPApanpDDLARLIMLMEGLVALGEGLPWGWAtfaeylDALEARP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 163 LM---AIPEGHGApLIALTSG------TPEE-ARTA--VAQNLKAGvnAIKIAATGGVTDAQeigeagspQMSVEQMRAI 230
Cdd:cd01297 136 PAvnvAALVGHAA-LRRAVMGldareaTEEElAKMRelLREALEAG--ALGISTGLAYAPRL--------YAGTAELVAL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 231 CDEAHQYGVIVGAHaqspegvrrsllagVDTiEHGSVLD--DELIGMFRHnpnalrgysaliptlsAGLPLTL-----LG 303
Cdd:cd01297 205 ARVAARYGGVYQTH--------------VRY-EGDSILEalDELLRLGRE----------------TGRPVHIshlksAG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 304 QDVTGITDIQLE--NSKNVVGGMVS------GARQAHEAGLMI-----GVGTDTGMTFVPQYATW-----------RELE 359
Cdd:cd01297 254 APNWGKIDRLLAliEAARAEGLQVTadvypyGAGSEDDVRRIMahpvvMGGSDGGALGKPHPRSYgdftrvlghyvRERK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 360 LLvayagfSPAEALHAATAVNASILGaDAETGSLEVGKSADLLVLNANPLDDLRALEHPA-------LVIAAGHPVWRPG 432
Cdd:cd01297 334 LL------SLEEAVRKMTGLPARVFG-LADRGRIAPGYRADIVVFDPDTLADRATFTRPNqpaegieAVLVNGVPVVRDG 406
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
17-78 |
3.45e-04 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 42.66 E-value: 3.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469299500 17 ATIVTGDKagtiLRNMTIVVgADGRIEQVAPSIETsiPAEYHYLDGTGKIVMPGLINAHTHL 78
Cdd:cd01315 7 GRVVTPDG----VREADIAV-KGGKIAAIGPDIAN--TEAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
333-425 |
8.25e-04 |
|
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: 41.67 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469299500 333 EAGLMIGVGTDTGMTF-VPQYATWRELEL---------LVAYAGFSPAEALHAATAVNASILGADaeTGSLEVGKSADLL 402
Cdd:cd01313 303 AAGGRIGIGSDSNARIdLLEELRQLEYSQrlrdrarnvLATAGGSSARALLDAALAGGAQALGLA--TGALEAGARADLL 380
|
90 100
....*....|....*....|....*....
gi 1469299500 403 VLN------ANPLDDLRAlehPALVIAAG 425
Cdd:cd01313 381 SLDldhpslAGALPDTLL---DAWVFAAG 406
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
17-78 |
1.40e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 40.75 E-value: 1.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469299500 17 ATIVTGDkAGTILRNMTIVVgADGRIEQVAPSIetsIPAEY-HYLDGTGKIVMPGLINAHTHL 78
Cdd:PRK07228 8 AGIVTMN-AKREIVDGDVLI-EDDRIAAVGDRL---DLEDYdDHIDATGKVVIPGLIQGHIHL 65
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
13-78 |
1.55e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 40.64 E-value: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469299500 13 ALAHATIVTGDKAGTILR-NMTIvvgaDGRIEQVAPSIEtsiPAEYHYLDGTGKIVMPGLINAHTHL 78
Cdd:PRK06380 4 LIKNAWIVTQNEKREILQgNVYI----EGNKIVYVGDVN---EEADYIIDATGKVVMPGLINTHAHV 63
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
39-78 |
1.98e-03 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 40.45 E-value: 1.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1469299500 39 DGRIEQVAPSIETsiPAEYHYLDGTGKIVMPGLINAHTHL 78
Cdd:TIGR02033 23 GGKIVAVGDNLIP--PDAVEVIDATGKYVLPGGIDVHTHL 60
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
38-78 |
2.71e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 39.92 E-value: 2.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1469299500 38 ADGRIEQVAPSIETsiPAEYHYLDGTGKIVMPGLINAHTHL 78
Cdd:PRK05985 22 RDGRIAAIGPALAA--PPGAEVEDGGGALALPGLVDGHIHL 60
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
39-78 |
3.25e-03 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 39.68 E-value: 3.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1469299500 39 DGRIEQVAPSIETsiPAEyHYLDGTGKIVMPGLINAHTHL 78
Cdd:PRK06189 27 NGKIAEIAPEISS--PAR-EIIDADGLYVFPGMIDVHVHF 63
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
19-80 |
3.87e-03 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 39.57 E-value: 3.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469299500 19 IVTGDKAGTILRNMTIVVgaDGRIEQVAP--SIETSIP-AEYHYLDGTgkIVMPGLINAHTHL-FS 80
Cdd:PRK08418 9 IFTCDENFEILEDGAVVF--DDKILEIGDyeNLKKKYPnAKIQFFKNS--VLLPAFINPHTHLeFS 70
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-85 |
5.50e-03 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 38.85 E-value: 5.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1469299500 34 IVVGADGRIEQVAPSIETSIPAEYhyLDGTGKIVMPGLINAHTHLFSQGKPL 85
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQI--VDAGGCYVSPGWIDLHVHVYQGGTRY 50
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
39-78 |
5.64e-03 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 38.96 E-value: 5.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1469299500 39 DGRIEQVAPSIetsIPAEYHYLDGTGKIVMPGLINAHTHL 78
Cdd:TIGR00857 12 GGRIKKIGKLR---IPPDAEVIDAKGLLVLPGFIDLHVHL 48
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
27-78 |
8.70e-03 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 38.53 E-value: 8.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469299500 27 TILRNMTIVVGAD----------GRIEQVApsieTSIPAEYHYLDGTGKIVMPGLINAHTHL 78
Cdd:PRK13404 6 LVIRGGTVVTATDtfqadigirgGRIAALG----EGLGPGAREIDATGRLVLPGGVDSHCHI 63
|
|
| |
