|
Name |
Accession |
Description |
Interval |
E-value |
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
22-396 |
1.52e-172 |
|
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: 486.53 E-value: 1.52e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 22 DDGAMLTDGAVLLWVGNRAELPDLPVAQRVDLQGRVVTPGLVDCHSHAVFGGDRAREFEMRLNGASYAEIAAGGGGIAST 101
Cdd:TIGR01224 2 EDAVILIHGGKIVWIGQLAALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGILST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 102 VNATRQASESQLLESARQRIRELCRDGVTALEIKSGYGLDLANERKMLRAIRRLGDILPLTVRSTCLAAHAVPVEYQERA 181
Cdd:TIGR01224 82 VRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQGRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 182 DAWIDYICERLLPELHQEGLVDAVDAFCEHLAFSPSQVERVFQKARELGLPVKLHAEQLTLQHGAALAARYHALSADHLE 261
Cdd:TIGR01224 162 DDYVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 262 YLCEEDIAAMARHGTVAVLLPGAYYFLREkQLPPLDLLRQYRVPIALASDLNPGTSPVLSLRLMMNMACTLFRMTPEEAL 341
Cdd:TIGR01224 242 HASDAGIKALAEAGTVAVLLPGTTFYLRE-TYPPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1766864103 342 AGVTLNGAKALGLDTVCGSLEAGKEASFVAWDIAYPAELSYWLGGSLSKQVIYQG 396
Cdd:TIGR01224 321 HAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNG 375
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
28-396 |
1.68e-167 |
|
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: 473.67 E-value: 1.68e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 28 TDGAVLlWVGNRAELPDL--PVAQRVDLQGRVVTPGLVDCHSHAVFGGDRAREFEMRLNGASYAEIAAGGGGIASTVNAT 105
Cdd:cd01296 4 RDGRIA-AVGPAASLPAPgpAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVRAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 106 RQASESQLLESARQRIRELCRDGVTALEIKSGYGLDLANERKMLRAIRRLGDILPLTVRSTCLAAHAVPVEYQERaDAWI 185
Cdd:cd01296 83 RAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGR-EEYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 186 DYICERLLPELHQEGLVDAVDAFCEHLAFSPSQVERVFQKARELGLPVKLHAEQLTLQHGAALAARYHALSADHLEYLCE 265
Cdd:cd01296 162 DLVIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHTSD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 266 EDIAAMARHGTVAVLLPGAYYFLREKQlPPLDLLRQYRVPIALASDLNPGTSPVLSLRLMMNMACTLFRMTPEEALAGVT 345
Cdd:cd01296 242 EGIAALAEAGTVAVLLPGTAFSLRETY-PPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTAAT 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1766864103 346 LNGAKALGLDTVCGSLEAGKEASFVAWDIAYPAELSYWLGGSLSKQVIYQG 396
Cdd:cd01296 321 INAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-400 |
2.38e-87 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 269.91 E-value: 2.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 3 TLWHHCRIATMAAGHyqLLDDGAMLTDGAVLLWVGNRAELPDLPVAQRVDLQGRVVTPGLVDCHSHAVFGGDRAREFEMr 82
Cdd:COG1228 10 LLITNATLVDGTGGG--VIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 83 lngasyaeiaagGGGIASTVnatrqasesQLLESARQRIRELCRDGVTALEIKSGYGLDL-----ANERKMLRAIRRLGD 157
Cdd:COG1228 87 ------------GGGITPTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPLGLrdaiiAGESKLLPGPRVLAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 158 ILPLTVrstCLAAHA-VPVEyqeradawidyiCERLLPELHQEGlVDAVDAFCEH--LAFSPSQVERVFQKARELGLPVK 234
Cdd:COG1228 146 GPALSL---TGGAHArGPEE------------ARAALRELLAEG-ADYIKVFAEGgaPDFSLEELRAILEAAHALGLPVA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 235 LHAEQLtlqHGAALAARYHALSADHLEYLCEEDIAAMARHGTVaVLLPGAYYFL-----------------REKQLPPLD 297
Cdd:COG1228 210 AHAHQA---DDIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLallegaaapvaakarkvREAALANAR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 298 LLRQYRVPIALASDLNPGTSPVLSLRLMMNMACtLFRMTPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWDIAYP 377
Cdd:COG1228 286 RLHDAGVPVALGTDAGVGVPPGRSLHRELALAV-EAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPL 364
|
410 420
....*....|....*....|...
gi 1766864103 378 AELSYWlggSLSKQVIYQGKEVY 400
Cdd:COG1228 365 EDIAYL---EDVRAVMKDGRVVD 384
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-378 |
1.22e-36 |
|
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: 138.04 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 3 TLWHHCRIATMAAGHyQLLDDGAMLTDGAVLLWVGNRAELPD-LPVAQRVDLQGRVVTPGLVDCHSHAVFGGDRAR---- 77
Cdd:COG0402 2 LLIRGAWVLTMDPAG-GVLEDGAVLVEDGRIAAVGPGAELPArYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLaddl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 78 EFEMRLNGASYAeiaaggggiastvnATRQASESQLLESARQRIRELCRDGVT-ALEIksgYGLDLANERKMLRAIRRLG 156
Cdd:COG0402 81 PLLDWLEEYIWP--------------LEARLDPEDVYAGALLALAEMLRSGTTtVADF---YYVHPESADALAEAAAEAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 157 dilpltVRSTC---LAAHAVPVEYQERADAWIDYiCERLLPELH--QEGLVDAVDAFCEHLAFSPSQVERVFQKARELGL 231
Cdd:COG0402 144 ------IRAVLgrgLMDRGFPDGLREDADEGLAD-SERLIERWHgaADGRIRVALAPHAPYTVSPELLRAAAALARELGL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 232 PVKLH-AEQ---------LTLQHGAALAARYHALSAD----HLEYLCEEDIAAMARHGTVAVLLPGAYYFLReKQLPPLD 297
Cdd:COG0402 217 PLHTHlAETrdevewvleLYGKRPVEYLDELGLLGPRtllaHCVHLTDEEIALLAETGASVAHCPTSNLKLG-SGIAPVP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 298 LLRQYRVPIALASDlNPGTSPVLSLRLMMNMACTLFR--------MTPEEALAGVTLNGAKALGLDTVCGSLEAGKEASF 369
Cdd:COG0402 296 RLLAAGVRVGLGTD-GAASNNSLDMFEEMRLAALLQRlrggdptaLSAREALEMATLGGARALGLDDEIGSLEPGKRADL 374
|
....*....
gi 1766864103 370 VAWDIAYPA 378
Cdd:COG0402 375 VVLDLDAPH 383
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
3-373 |
1.48e-24 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 105.27 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 3 TLWHHCRIATMAAGHyqlLDDGAMLTDGAVLLWVGNRAELPDL--PVAQRVDLQGRVVTPGLVDCHSHAVFGGDRAREfe 80
Cdd:COG1574 10 LLLTNGRIYTMDPAQ---PVAEAVAVRDGRIVAVGSDAEVRALagPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLG-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 81 MRLNGA-SYAEIAA----------------GGG----------------------------------------------G 97
Cdd:COG1574 85 VDLSGArSLDELLArlraaaaelppgewilGRGwdeslwpegrfptradldavspdrpvvltrvdghaawvnsaalelaG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 98 I-ASTVN----------------------------ATRQASESQLLESARQRIRELCRDGVTALeiksgygLDLANERKM 148
Cdd:COG1574 165 ItADTPDpeggeierdadgeptgvlreaamdlvraAIPPPTPEELRAALRAALRELASLGITSV-------HDAGLGPDD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 149 LRAIRRLGDILPLTVRsTCLAAHAVPVEYQERADawidyicERLLPELHQEGL-VDAVDAFCE----------------- 210
Cdd:COG1574 238 LAAYRELAAAGELPLR-VVLYLGADDEDLEELLA-------LGLRTGYGDDRLrVGGVKLFADgslgsrtaallepyadd 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 211 -----HLAFSPSQVERVFQKARELGLPVKLHA-------------EQLTLQHGAAlaARYHALSadHLEYLCEEDIAAMA 272
Cdd:COG1574 310 pgnrgLLLLDPEELRELVRAADAAGLQVAVHAigdaavdevldayEAARAANGRR--DRRHRIE--HAQLVDPDDLARFA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 273 RHGTVAVLLPG-AYYF--LREKQLPPLDLLRQYR--------VPIALASDlnpgtSPVLSLRLMMNMACTLFR------- 334
Cdd:COG1574 386 ELGVIASMQPThATSDgdWAEDRLGPERAARAYPfrslldagAPLAFGSD-----APVEPLDPLLGIYAAVTRrtpsgrg 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1766864103 335 ------MTPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWD 373
Cdd:COG1574 461 lgpeerLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLD 505
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
25-370 |
3.06e-22 |
|
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: 98.15 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 25 AMLTDGAVLLWVGNRAELPDL--PVAQRVDLQGRVVTPGLVDCHSHAVFGG------------------DRAREFE---- 80
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKALkgPATEVIDLKGKTVLPGFIDSHSHLLLGGlsllwldlsgvtskeealARIREDAaaap 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 81 ---------------------------------------------------MRLNGASYAEIAAGGGGI----------- 98
Cdd:cd01300 81 pgewilgfgwdesllgegryptraeldavspdrpvlllrrdghsawvnsaaLRLAGITRDTPDPPGGEIvrdadgeptgv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 99 ------ASTVNATRQASESQLLESARQRIRELCRDGVTALeikSGYGLDLANERKMLRAIRRLGDiLPLTVRstclaahA 172
Cdd:cd01300 161 lveaaaALVLEAVPPPTPEERRAALRAAARELASLGVTTV---HDAGGGAADDIEAYRRLAAAGE-LTLRVR-------V 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 173 VPVEYQERADAWIDYiCERLLPELHQEGLVDAVDAF----------------------CEHLAFSPSQVERVFQKARELG 230
Cdd:cd01300 230 ALYVSPLAEDLLEEL-GARKNGAGDDRLRLGGVKLFadgslgsrtaalsepyldspgtGGLLLISPEELEELVRAADEAG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 231 LPVKLHA------EQlTL----QHGAALAARYHALSADHLEYLCEEDIAAMARHGTVAVLLPG----AYYFLREKQLPPL 296
Cdd:cd01300 309 LQVAIHAigdravDT-VLdaleAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNhlysDGDAAEDRRLGEE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 297 DLLRQYR--------VPIALASDLNPGT-SPVLSLRLMMN--------MACTLFRMTPEEALAGVTLNGAKALGLDTVCG 359
Cdd:cd01300 388 RAKRSYPfrslldagVPVALGSDAPVAPpDPLLGIWAAVTrktpgggvLGNPEERLSLEEALRAYTIGAAYAIGEEDEKG 467
|
490
....*....|.
gi 1766864103 360 SLEAGKEASFV 370
Cdd:cd01300 468 SLEPGKLADFV 478
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
36-400 |
9.19e-19 |
|
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: 86.98 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 36 VGNRAELPdlPVAQRVDLQGRVVTPGLVDCHSHA-------VFGGDRAREF----------------------EMRLNGA 86
Cdd:cd01309 7 VGAEITTP--ADAEVIDAKGKHVTPGLIDAHSHLgldeeggVRETSDANEEtdpvtphvraidginpddeafkRARAGGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 87 SYAEIAAGGGGIastvnatrQASESQLLESARQRIRELCRDGVTALEIKSGYGLDLANERKMLRAIRRLGDILPLtvRST 166
Cdd:cd01309 85 TTVQVLPGSANL--------IGGQGVVIKTDGGTIEDMFIKAPAGLKMALGENPKRVYGGKGKEPATRMGVAALL--RDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 167 CLAAHavpvEYQERADAWIDYICERLLPELHQEGLVDAVD----AFCEhlAFSPSQVERVFQKARELGLPvklhaeqLTL 242
Cdd:cd01309 155 FIKAQ----EYGRKYDLGKNAKKDPPERDLKLEALLPVLKgeipVRIH--AHRADDILTAIRIAKEFGIK-------ITI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 243 QHGAAlaaryhalsadhlEYLCEEDIAamaRHGTVAVLLP--GAYYFLREKQLP---PLDLLRQYRVPIALASDlnpgtS 317
Cdd:cd01309 222 EHGAE-------------GYKLADELA---KHGIPVIYGPtlTLPKKVEEVNDAidtNAYLLKKGGVAFAISSD-----H 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 318 PVLSLRLMMNMACTLFR--MTPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWDiAYPAELsywlgGSLSKQVIYQ 395
Cdd:cd01309 281 PVLNIRNLNLEAAKAVKygLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWN-GDPLEP-----TSKPEQVYID 354
|
....*
gi 1766864103 396 GKEVY 400
Cdd:cd01309 355 GRLVY 359
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
57-399 |
2.63e-18 |
|
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: 85.25 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 57 VVTPGLVDCHSHavfggdrarefemrlngasyaeiaaggggIASTVNATRQASESQLLESARQRIRELCRDGVTALeIKS 136
Cdd:pfam01979 1 IVLPGLIDAHVH-----------------------------LEMGLLRGIPVPPEFAYEALRLGITTMLKSGTTTV-LDM 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 137 GYGLDLANERkMLRAIRRLGDILPLTVRSTCLAA---HAVPVEYQERADAWIDYICERLlpelhqEGLVDAVDAFCEHLA 213
Cdd:pfam01979 51 GATTSTGIEA-LLEAAEELPLGLRFLGPGCSLDTdgeLEGRKALREKLKAGAEFIKGMA------DGVVFVGLAPHGAPT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 214 FSPSQVERVFQKARELGLPVKLHA-EQLTLQHGAALAARYHALSADHLEYLCE----EDIAAMARHGT------------ 276
Cdd:pfam01979 124 FSDDELKAALEEAKKYGLPVAIHAlETKGEVEDAIAAFGGGIEHGTHLEVAESggllDIIKLILAHGVhlspteanllae 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 277 ----VAVLLPGAYYFLREKQLPPLDLLRQYRVPIALASD-LNPGTSPVLsLRLMMNMACTLFR----MTPEEALAGVTLN 347
Cdd:pfam01979 204 hlkgAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDgAGSGNSLNM-LEELRLALELQFDpeggLSPLEALRMATIN 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1766864103 348 GAKALGLDTVCGSLEAGKEASFVAWDIAYPAELSYWLGGSLSKQVIYQGKEV 399
Cdd:pfam01979 283 PAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
62-351 |
4.59e-18 |
|
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: 83.54 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 62 LVDCHSHAVFGGDRAREFEMRLNGASYAeiaaggggiastvnatrqaSESQLLESARQRIRELCRDGVTALEIKSGYGLD 141
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEEL-------------------SPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 142 LANERKMLRAIRRLGDILPLTVRSTCLAAHAVPveyqERADAWIDYIcERLLPELHQEGlVDAVDAF--CEHLAFSPSQV 219
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRVVLGLGIPGVPA----AVDEDAEALL-LELLRRGLELG-AVGLKLAgpYTATGLSDESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 220 ERVFQKARELGLPVKLHAEQLTLQHGAALAARY-----HALSADHLEYLCEEDIAAMARHG-TVAVLLPGAYYFLREK-Q 292
Cdd:cd01292 136 RRVLEEARKLGLPVVIHAGELPDPTRALEDLVAllrlgGRVVIGHVSHLDPELLELLKEAGvSLEVCPLSNYLLGRDGeG 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 293 LPPLDLLRQYRVPIALASDLNPGTSPVLSLRLM-MNMACTLFRMTPEEALAGVTLNGAKA 351
Cdd:cd01292 216 AEALRRLLELGIRVTLGTDGPPHPLGTDLLALLrLLLKVLRLGLSLEEALRLATINPARA 275
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
7-373 |
8.28e-18 |
|
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: 84.56 E-value: 8.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 7 HCRIATMAAGHyqLLDDGAMLTDGAVLLWVGNRAELPDLPVAQRVDLQGRVVTPGLVDCHSHAVFGGDRarefemrlnga 86
Cdd:cd01298 5 NGTIVTTDPRR--VLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLR----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 87 syaeiaagggGIASTVNatrqasesqLLE--------SARQRIRELCRDG--VTALE-IKSG----------YGLDLAne 145
Cdd:cd01298 72 ----------GLADDLP---------LMEwlkdliwpLERLLTEEDVYLGalLALAEmIRSGtttfadmyffYPDAVA-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 146 rkmlRAIRRLGdilpltVRstCLAAHAV---PVEYQERADAWIDYiCERLLPELHQ--EGLVDAVDAFCEHLAFSPSQVE 220
Cdd:cd01298 131 ----EAAEELG------IR--AVLGRGImdlGTEDVEETEEALAE-AERLIREWHGaaDGRIRVALAPHAPYTCSDELLR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 221 RVFQKARELGLPVKLHA-----EQLTLQ--HG---AALAARYHALSAD----HLEYLCEEDIAAMARHGTVAVLLPGAYY 286
Cdd:cd01298 198 EVAELAREYGVPLHIHLaetedEVEESLekYGkrpVEYLEELGLLGPDvvlaHCVWLTDEEIELLAETGTGVAHNPASNM 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 287 FLrEKQLPPLDLLRQYRVPIALASDlnpGTSPVLSLRLM--MNMACTLFR--------MTPEEALAGVTLNGAKALGLDT 356
Cdd:cd01298 278 KL-ASGIAPVPEMLEAGVNVGLGTD---GAASNNNLDMFeeMRLAALLQKlahgdptaLPAEEALEMATIGGAKALGLDE 353
|
410
....*....|....*..
gi 1766864103 357 VcGSLEAGKEASFVAWD 373
Cdd:cd01298 354 I-GSLEVGKKADLILID 369
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
42-380 |
2.23e-15 |
|
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: 77.29 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 42 LPDLPVAQRVDLQGRVVTPGLVDCHSH--AVFGGDRAREFemrlngasyaeiAAGGGGIASTVNATRQASESQllESARQ 119
Cdd:cd01293 31 LAVPPDAEEVDAKGRLVLPAFVDPHIHldKTFTGGRWPNN------------SGGTLLEAIIAWEERKLLLTA--EDVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 120 RIRELCRdgvtaLEIKSGYgldlanerkmlRAIRRLGDILPlTVRSTCLAA-HAVPVEYQERADAWI------DYIC--- 189
Cdd:cd01293 97 RAERALE-----LAIAHGT-----------TAIRTHVDVDP-AAGLKALEAlLELREEWADLIDLQIvafpqhGLLStpg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 190 -ERLLPELHQEG--LVDAVDAFcEHLAFSPSQVERVFQKARELGLPVKLH------AEQLTLQHGAALAARY-------- 252
Cdd:cd01293 160 gEELMREALKMGadVVGGIPPA-EIDEDGEESLDTLFELAQEHGLDIDLHldetddPGSRTLEELAEEAERRgmqgrvtc 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 253 -HALSADHL-EYLCEEDIAAMARHGT--VAVLLPGAYYFLREKQ------LPPLDLLRQYRVPIALASD--LNP----GT 316
Cdd:cd01293 239 sHATALGSLpEAEVSRLADLLAEAGIsvVSLPPINLYLQGREDTtpkrrgVTPVKELRAAGVNVALGSDnvRDPwypfGS 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1766864103 317 SPVLSLrlmMNMACTLFRMTPEE----ALAGVTLNGAKALGLDTvcGSLEAGKEASFVAWDIAYPAEL 380
Cdd:cd01293 319 GDMLEV---ANLAAHIAQLGTPEdlalALDLITGNAARALGLED--YGIKVGCPADLVLLDAEDVAEA 381
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
51-400 |
5.33e-14 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 73.33 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 51 VDLQGRVVTPGLVDCHSHAVFGGDRAREfeMRLNGASY--------AEIAAGGGGIASTVNATRQASESQLleSARQRIR 122
Cdd:pfam07969 3 IDAKGRLVLPGFVDPHTHLDGGGLNLRE--LRLPDVLPnavvkgqaGRTPKGRWLVGEGWDEAQFAETRFP--YALADLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 123 ELCRDG-------VTALEIKSGYGLDLANERKM-----LRAIRRLGDILPLTVRSTCLAAHAVP---VEYQERA------ 181
Cdd:pfam07969 79 EVAPDGpvllralHTHAAVANSAALDLAGITKAtedppGGEIARDANGEGLTGLLREGAYALPPllaREAEAAAvaaala 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 182 ----------DAWIDYICERLLPELHQE-----GLVDAVDAFCEHLAFSPS----------------------------- 217
Cdd:pfam07969 159 alpgfgitsvDGGGGNVHSLDDYEPLREltaaeKLKELLDAPERLGLPHSIyelrigamklfadgvlgsrtaaltepyfd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 218 ------------QVERVFQKARELGLPVKLHA-EQLTLQHG-AALAARYHAL------SADHLEYLC---EEDIAAMARH 274
Cdd:pfam07969 239 apgtgwpdfedeALAELVAAARERGLDVAIHAiGDATIDTAlDAFEAVAEKLgnqgrvRIEHAQGVVpytYSQIERVAAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 275 GTVAVLLPGAYYFL-----------REKQLPPLDLLRQYRVPIALASDLNPGT----SPV---LSLRLMMNMACTLF--R 334
Cdd:pfam07969 319 GGAAGVQPVFDPLWgdwlqdrlgaeRARGLTPVKELLNAGVKVALGSDAPVGPfdpwPRIgaaVMRQTAGGGEVLGPdeE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 335 MTPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWDIAY----PAELSYwlggSLSKQVIYQGKEVY 400
Cdd:pfam07969 399 LSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPltvdPPAIAD----IRVRLTVVDGRVVY 464
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
16-378 |
9.44e-14 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 72.38 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 16 GHYQLLDDGAMLTDGAVLLWVGNRAelpDLPVAQRVDLQGRVVTPGLVDCHS-----HAVFGGDRAREFEM-RLNGASYA 89
Cdd:PRK06151 16 GDHRLLRDGEVVFEGDRILFVGHRF---DGEVDRVIDAGNALVGPGFIDLDAlsdldTTILGLDNGPGWAKgRVWSRDYV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 90 EiaaggggiastVNATRQASESQLLESARQRIRELCRDGVT-ALEIKSGYGLDLANERKMLRAIRRLGDILPLTV----- 163
Cdd:PRK06151 93 E-----------AGRREMYTPEELAFQKRYAFAQLLRNGITtAMPIASLFYRQWAETYAEFAAAAEAAGRLGLRVylgpa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 164 -RSTCLAAHA----VPVEYQERADAWID---YICERLlpELHQEGLVDAVDAFCEHLAFSPSQVERVFQKARELGLPVKL 235
Cdd:PRK06151 162 yRSGGSVLEAdgslEVVFDEARGLAGLEeaiAFIKRV--DGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 236 HAEQLTLQ-------HGAA----------LAARY---HALSA---DHLEYLCEEDIAAMARHGTVAVLLPgAYYFLREKQ 292
Cdd:PRK06151 240 HCAQGVLEvetvrrlHGTTplewladvglLGPRLlipHATYIsgsPRLNYSGGDDLALLAEHGVSIVHCP-LVSARHGSA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 293 LPPLDLLRQYRVPIALASDLNPGTspvlslrLMMNMACTLF--RMTPEEALAG--------VTLNGAKALGLDTVcGSLE 362
Cdd:PRK06151 319 LNSFDRYREAGINLALGTDTFPPD-------MVMNMRVGLIlgRVVEGDLDAAsaadlfdaATLGGARALGRDDL-GRLA 390
|
410
....*....|....*.
gi 1766864103 363 AGKEASFVAWDIAYPA 378
Cdd:PRK06151 391 PGAKADIVVFDLDGLH 406
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
259-373 |
7.61e-13 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 69.45 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 259 HLEYLCEEDIAAMARHGTVAVLLPGAYYFLREKqLPPLDLLRQYRVPIALASDLNPGTSpvLSLRLMMNMA---CTL--F 333
Cdd:PRK09228 270 HCIHLEDRERRRLAETGAAIAFCPTSNLFLGSG-LFDLKRADAAGVRVGLGTDVGGGTS--FSMLQTMNEAykvQQLqgY 346
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1766864103 334 RMTPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWD 373
Cdd:PRK09228 347 RLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLD 386
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
48-373 |
8.88e-12 |
|
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: 65.78 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 48 AQRVDLQGRVVTPGLVDCHSHAVFGGDRAREF------EMRLNGASYAEIA----------AGGGGIAstvnATRQASES 111
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDlalpveYRTIRATRQARAAlragfttvrdAGGADYG----LLRDAIDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 112 QLLESARQRIrelcrdGVTALEIKSGYGLDLANERKMlraiRRLGDILPLTVRSTCLAAhaVPVEYQERADA---WIDYI 188
Cdd:cd01299 77 GLIPGPRVFA------SGRALSQTGGHGDPRGLSGLF----PAGGLAAVVDGVEEVRAA--VREQLRRGADQikiMATGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 189 CERLLPELhqeglvdavdafcEHLAFSPSQVERVFQKARELGLPVKLHAEqlTLQhGAALAARYHALSADHLEYLCEEDI 268
Cdd:cd01299 145 VLSPGDPP-------------PDTQFSEEELRAIVDEAHKAGLYVAAHAY--GAE-AIRRAIRAGVDTIEHGFLIDDETI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 269 AAMARHGTVAVLLPGAYYFL----REKQLPPLDLLRQYR----------------VPIALASDL-NPGTSPVLSLRLMMN 327
Cdd:cd01299 209 ELMKEKGIFLVPTLATYEALaaegAAPGLPADSAEKVALvleagrdalrrahkagVKIAFGTDAgFPVPPHGWNARELEL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1766864103 328 MACTLfrMTPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWD 373
Cdd:cd01299 289 LVKAG--GTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
33-397 |
8.67e-11 |
|
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238637 [Multi-domain] Cd Length: 381 Bit Score: 62.85 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 33 LLWVGNRAEL----PDlPVAQRvdLQGRVVTPGLVDCHSHAVFGGDRARefemrlngASYAEIaagGGGIASTVNATRQA 108
Cdd:cd01312 3 ILEVGDYEKLekryPG-AKHEF--FPNGVLLPGLINAHTHLEFSANVAQ--------FTYGRF---RAWLLSVINSRDEL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 109 SESQLLESARQRIRELCRDGVTALEIKSGYGLDLAnerkmLRAIRRLGDILPLTVrstcLAAHavPVEYQERADAwidyI 188
Cdd:cd01312 69 LKQPWEEAIRQGIRQMLESGTTSIGAISSDGSLLP-----ALASSGLRGVFFNEV----IGSN--PSAIDFKGET----F 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 189 CERLL--PELHQEGLVDAVDAFCEHlAFSPSQVERVFQKARELGLPVKLH-----AEQLTLQHGAA-------------- 247
Cdd:cd01312 134 LERFKrsKSFESQLFIPAISPHAPY-SVHPELAQDLIDLAKKLNLPLSTHfleskEEREWLEESKGwfkhfwesflklpk 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 248 -------------LAARYHALSADHLEYLCEEDIAAMARHGTVAVLLPGAYYFLREKQLPpLDLLRQYRVPIALASDlnp 314
Cdd:cd01312 213 pkklataidfldmLGGLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLD-VSELKKAGIPVSLGTD--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 315 GTSPVLSLRLM--MNMACTLFRM-----TPEEALAGVTLNGAKALGLDTvcGSLEAGKEASFVAWDIAYP-----AELSY 382
Cdd:cd01312 289 GLSSNISLSLLdeLRALLDLHPEedlleLASELLLMATLGGARALGLNN--GEIEAGKRADFAVFELPGPgikeqAPLQF 366
|
410
....*....|....*
gi 1766864103 383 WLGGSLSKQVIYQGK 397
Cdd:cd01312 367 ILHAKEVRHLFISGK 381
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
215-373 |
1.20e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 59.63 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 215 SPSQVERVFQKARELGLPVKLHAEQLTLQHGAALAARYHA---LSAD----HLEYLCEEDIAAMARHGTVAVLLPgayyf 287
Cdd:PRK08204 199 SWEVARADFRLARELGLPISMHQGFGPWGATPRGVEQLHDaglLGPDlnlvHGNDLSDDELKLLADSGGSFSVTP----- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 288 lrEKQL------PPLDLLRQYRVPIALASDLNPGTSPvlSLRLMMNMACTLFR-------------------MTPEEALA 342
Cdd:PRK08204 274 --EIEMmmghgyPVTGRLLAHGVRPSLGVDVVTSTGG--DMFTQMRFALQAERardnavhlreggmppprltLTARQVLE 349
|
170 180 190
....*....|....*....|....*....|.
gi 1766864103 343 GVTLNGAKALGLDTVCGSLEAGKEASFVAWD 373
Cdd:PRK08204 350 WATIEGARALGLEDRIGSLTPGKQADLVLID 380
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
259-373 |
4.80e-09 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 57.67 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 259 HLEYLCEEDIAAMARHGTVAVLLPGAYYFLrEKQLPPLDLLRQYRVPIALASDLNPGTSPvlSLRLMMNMACTLFRM--- 335
Cdd:cd01303 267 HCVHLSEEEFNLLKERGASVAHCPTSNLFL-GSGLFDVRKLLDAGIKVGLGTDVGGGTSF--SMLDTLRQAYKVSRLlgy 343
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1766864103 336 --------TPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWD 373
Cdd:cd01303 344 elgghaklSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVID 389
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
215-375 |
6.84e-09 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 57.23 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 215 SPSQVERVFQKARELGLPVKLH--------AEQLTlQHGAALAARYHALS-------ADHLEYLCEEDIAAMARHGTVAV 279
Cdd:PRK09045 200 SDENLERIRTLAEQLDLPIHIHlhetaqeiADSLK-QHGQRPLARLARLGllgprliAVHMTQLTDAEIALLAETGCSVV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 280 LLPgayyflrEKQLP------PLDLLRQYRVPIALASDlnpGTSPVLSLRLM--MNMACTLFR--------MTPEEALAG 343
Cdd:PRK09045 279 HCP-------ESNLKlasgfcPVAKLLQAGVNVALGTD---GAASNNDLDLFgeMRTAALLAKavagdataLPAHTALRM 348
|
170 180 190
....*....|....*....|....*....|..
gi 1766864103 344 VTLNGAKALGLDTVCGSLEAGKEASFVAWDIA 375
Cdd:PRK09045 349 ATLNGARALGLDDEIGSLEPGKQADLVAVDLS 380
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
23-399 |
3.82e-08 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 55.01 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 23 DGAMLTDGAVLLWVGNRAELPDLPVAQRVDLQGRVVTPGLVDCHSHAVFGGDRAREFEMRLNG--ASYAEIAAGGGGIAS 100
Cdd:PRK06687 21 DGILAVKDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHEwlNDYIWPAESEFTPDM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 101 TVNATRQAsesqllesarqrIRELCRDGVTAL-EIKSGYGLDLaneRKMLRAIRRLGdiLPLTVRSTCLAAHA-VPVEYQ 178
Cdd:PRK06687 101 TTNAVKEA------------LTEMLQSGTTTFnDMYNPNGVDI---QQIYQVVKTSK--MRCYFSPTLFSSETeTTAETI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 179 ERADAWIDYICERLLPELHQeglvdavdAFCEHLAFSPSQ--VERVFQKARELGLPVKLHAEQLTLQHGAALAaRYHALS 256
Cdd:PRK06687 164 SRTRSIIDEILKYKNPNFKV--------MVAPHSPYSCSRdlLEASLEMAKELNIPLHVHVAETKEESGIILK-RYGKRP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 257 ADHLEYLCEEDIAAMARHGTvavllpgayyflrekQLPPLDLLRQYRVPIALASD------LNPGTSPVLSLRLM----- 325
Cdd:PRK06687 235 LAFLEELGYLDHPSVFAHGV---------------ELNEREIERLASSQVAIAHNpisnlkLASGIAPIIQLQKAgvavg 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 326 -----------MNM------ACTLFRM--------TPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWDIA----- 375
Cdd:PRK06687 300 iatdsvasnnnLDMfeegrtAALLQKMksgdasqfPIETALKVLTIEGAKALGMENQIGSLEVGKQADFLVIQPQgkihl 379
|
410 420
....*....|....*....|....*....
gi 1766864103 376 YPAE-----LSYWLGGSLSKQVIYQGKEV 399
Cdd:PRK06687 380 QPQEnmlshLVYAVKSSDVDDVYIAGEQV 408
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
3-68 |
4.35e-07 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 51.78 E-value: 4.35e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1766864103 3 TLW--HHCRIATMAAGHYQLlDDGAMLTDGAVLLWVGNRAELPDlPVAQRVDLQGRVVTPGLVDCHSH 68
Cdd:PRK08203 2 TLWikNPLAIVTMDAARREI-ADGGLVVEGGRIVEVGPGGALPQ-PADEVFDARGHVVTPGLVNTHHH 67
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
40-373 |
2.78e-06 |
|
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: 49.32 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 40 AELPDLPVAQRVDLQGRVVTPGLVDCHSHavfggdrarefeMRLNGASYAE------IAAGGGGIASTV---NATRQASE 110
Cdd:COG0044 30 PDLAAPEAAEVIDATGLLVLPGLIDLHVH------------LREPGLEHKEdietgtRAAAAGGVTTVVdmpNTNPVTDT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 111 SQLLESARQRIRELC-------------------------RDGVTALEIKSGY--GLDLANERKMLRAIRRLGDiLPLTV 163
Cdd:COG0044 98 PEALEFKLARAEEKAlvdvgphgaltkglgenlaelgalaEAGAVAFKVFMGSddGNPVLDDGLLRRALEYAAE-FGALV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 164 rstclAAHAvpveyQEradawiDYICERLLPElhqEGLVDA------VDAFCEHLAfspsqVERVFQKARELGlpVKLHA 237
Cdd:COG0044 177 -----AVHA-----ED------PDLIRGGVMN---EGKTSPrlglkgRPAEAEEEA-----VARDIALAEETG--ARLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 238 EQLTLQHGAALAARYHA----LSAD----HLeYLCEEDIaamARHGTVAVLlpgayyflrekqLPPL------DLLRQY- 302
Cdd:COG0044 231 VHVSTAEAVELIREAKArglpVTAEvcphHL-TLTDEDL---ERYGTNFKV------------NPPLrteedrEALWEGl 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 303 --------------------RVPIALASdlnPGTSPV-LSLRLMMNMACTLFRMTPEEALAGVTLNGAKALGLDTvCGSL 361
Cdd:COG0044 295 adgtidviatdhaphtleekELPFAEAP---NGIPGLeTALPLLLTELVHKGRLSLERLVELLSTNPARIFGLPR-KGRI 370
|
410
....*....|..
gi 1766864103 362 EAGKEASFVAWD 373
Cdd:COG0044 371 AVGADADLVLFD 382
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
46-377 |
3.60e-06 |
|
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: 48.61 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 46 PVAQRVDLQGRVVTPGLVDCHSHAvfggdrareFEMRLNGasyaeIAAGGGGIASTVNATRQA--------SESQLLESA 117
Cdd:cd01313 28 TATEAVALLGGALLPGMPNLHSHA---------FQRAMAG-----LTEYRGSAADSFWTWRELmyrfaarlTPEQIEAIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 118 RQRIRELCRDGVTA------LEIKSGyGLDLANERKM-LRAIRRLGDI-LPLTVRSTCLA----AHAVPVEYQER----- 180
Cdd:cd01313 94 RQLYIEMLLAGITAvgefhyVHHDPD-GTPYADPAELaQRVIAAASDAgIGITLLPVLYAragfGGPAPNPGQRRfingy 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 181 ADAWiDYICERLLPELHQEGLVDAVdAFCEHLAFSPSQVERVFQKARELGlPVKLH-AEQ-----------------LTL 242
Cdd:cd01313 173 EDFL-GLLEKALRAVKEHAAARIGV-APHSLRAVPAEQLAALAALASEKA-PVHIHlAEQpkevddclaahgrrpveLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 243 QHGAaLAARYHALSADHLEylcEEDIAAMARHGTVAVLLPGAYYFLREKQLPPLDLLRQyRVPIALASDLNPGTSPVLSL 322
Cdd:cd01313 250 DHGH-LDARWCLVHATHLT---DNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAA-GGRIGIGSDSNARIDLLEEL 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1766864103 323 RLM----------MNMACTLFRMTPEEALAGVTLNGAKALGLDTvcGSLEAGKEASFVAWDIAYP 377
Cdd:cd01313 325 RQLeysqrlrdraRNVLATAGGSSARALLDAALAGGAQALGLAT--GALEAGARADLLSLDLDHP 387
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
26-138 |
4.43e-06 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 48.54 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 26 MLTDGAVLLWVGNRAELPDLPVAQRVDLQGRVVTPGLVDCHSHAVFGGDRA----REFEMRLNGASYAeiaagggGIAST 101
Cdd:cd01308 20 ILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGgpstRTPEVTLSDLTTA-------GVTTV 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 1766864103 102 VNATRQASESQLLESARQRIRELCRDGVTALEIKSGY 138
Cdd:cd01308 93 VGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSY 129
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
336-373 |
5.94e-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: 5.94e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1766864103 336 TPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWD 373
Cdd:cd00854 325 PLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD 362
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
295-370 |
6.80e-06 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 48.04 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 295 PLDLLRQYRVPIALASDlnpGTSPVLSLRLMMNMACTLFRMTPEEALA-------GVTLNGAKALGLDtvCGSLEAGKEA 367
Cdd:PRK08418 295 DLEKAKKAGINYSIATD---GLSSNISLSLLDELRAALLTHANMPLLElakilllSATRYGAKALGLN--NGEIKEGKDA 369
|
...
gi 1766864103 368 SFV 370
Cdd:PRK08418 370 DLS 372
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
322-373 |
7.77e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.40 E-value: 7.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1766864103 322 LRLMMNMActlfRMTPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFVAWD 373
Cdd:COG1820 313 VRNLVEWT----GLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLD 360
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
23-370 |
9.86e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 47.30 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 23 DGAMLTDGAVLLWVGNRAELPDLPvaQRVDLQGRVVTPGLVDCHSHAV---FGG--------DRAREFEMRLNGASYAEi 91
Cdd:PRK07228 21 DGDVLIEDDRIAAVGDRLDLEDYD--DHIDATGKVVIPGLIQGHIHLCqtlFRGiaddlellDWLKDRIWPLEAAHDAE- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 92 aaggggiastvnatrqasesQLLESARQRIRELCRDGVTALeiksgygLDLANERKMLRAIRRLGDILPLTVRSTCL--A 169
Cdd:PRK07228 98 --------------------SMYYSALLGIGELIESGTTTI-------VDMESVHHTDSAFEAAGESGIRAVLGKVMmdY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 170 AHAVPVEYQERADAWIDYiCERLLPELHQEGLVDAVDAFCEHLAFSPSQ--VERVFQKARELGLPVKLHA-----EQLTL 242
Cdd:PRK07228 151 GDDVPEGLQEDTEASLAE-SVRLLEKWHGADNGRIRYAFTPRFAVSCTEelLRGVRDLADEYGVRIHTHAsenrgEIETV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 243 Q-----------HGAALAARYHALSadHLEYLCEEDIAAMARHGTVAVLLPGAYYFLREKQLPPLDLLRQyRVPIALASD 311
Cdd:PRK07228 230 EeetgmrnihylDEVGLTGEDLILA--HCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLER-GINVALGAD 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1766864103 312 -------LNPGTSpvlslrlmMNMACTLFR--------MTPEEALAGVTLNGAKALGLDTVCGSLEAGKEASFV 370
Cdd:PRK07228 307 gapcnntLDPFTE--------MRQAALIQKvdrlgptaMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLA 372
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
21-68 |
1.23e-05 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 47.24 E-value: 1.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1766864103 21 LDDGAMLTDGAVLLWVGNRAELPDL-PVAQRVDLQGRVVTPGLVDCHSH 68
Cdd:PRK07203 19 IEDGAIAIEGNVIVEIGTTDELKAKyPDAEFIDAKGKLIMPGLINSHNH 67
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
190-351 |
2.54e-05 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 45.94 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 190 ERLLPELHQEGLVdAVDAFCEHLAFSPSQVERVFQKARELGLPVKLHA-EQLTLQHgaalaaRYHALSADHLEYL----- 263
Cdd:PRK09358 156 EALAARYRDDGVV-GFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAgEAGGPES------IWEALDELGAERIghgvr 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 264 CEEDIAAMARhgtvavllpgayyfLREKQLP--------------------PLDLLRQYRVPIALASDlNP---GTspvl 320
Cdd:PRK09358 229 AIEDPALMAR--------------LADRRIPlevcptsnvqtgavpslaehPLKTLLDAGVRVTINTD-DPlvfGT---- 289
|
170 180 190
....*....|....*....|....*....|.
gi 1766864103 321 SLRLMMNMACTLFRMTPEEaLAGVTLNGAKA 351
Cdd:PRK09358 290 TLTEEYEALAEAFGLSDED-LAQLARNALEA 319
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
23-402 |
7.37e-05 |
|
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: 44.74 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 23 DGAMLTDGAVLLWVGNRAELPDLPVaqrVDLQGRVVTPGLVDCHSHavfggdrAREFemrlnGASYAE------IAAGGG 96
Cdd:TIGR00857 5 EVDILVEGGRIKKIGKLRIPPDAEV---IDAKGLLVLPGFIDLHVH-------LRDP-----GEEYKEdiesgsKAAAHG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 97 GIaSTV----NATRQASESQLLESARQRIRE--LCRDGVTALEIKSGYGLDLAN--ERKMLRAI--------RRLGDILP 160
Cdd:TIGR00857 70 GF-TTVadmpNTKPPIDTPETLEWKLQRLKKvsLVDVHLYGGVTQGNQGKELTEayELKEAGAVgrmftddgSEVQDILS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 161 LTVRSTCLAAHAVPVEYQERADAWIDYICERLLPELHQEGLVdAVDAFCEHLAfspsqVERVFQKARELGLPVklHAEQL 240
Cdd:TIGR00857 149 MRRALEYAAIAGVPIALHAEDPDLIYGGVMHEGPSAAQLGLP-ARPPEAEEVA-----VARLLELAKHAGCPV--HICHI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 241 TLQHGAALA----ARYHALSAD----HLeYLCEEDIaamARHGTVAVLLPGayyfLREKQ--LPPLDLLRQYRVPIaLAS 310
Cdd:TIGR00857 221 STKESLELIvkakSQGIKITAEvtphHL-LLSEEDV---ARLDGNGKVNPP----LREKEdrLALIEGLKDGIIDI-IAT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 311 DLNPGT------------SPVLSLRLMMNMACTLF---RMTPEEALAGVTLNGAKALGLDTVcGSLEAGKEASFVAWDI- 374
Cdd:TIGR00857 292 DHAPHTleektkefaaapPGIPGLETALPLLLQLLvkgLISLKDLIRMLSINPARIFGLPDK-GTLEEGNPADITVFDLk 370
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1766864103 375 ---AYPAELSY-------WLGGSLSKQVIY---QGKEVYCD 402
Cdd:TIGR00857 371 kewTINAETFYskakntpFEGMSLKGKPIAtilRGKVVYED 411
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
46-401 |
2.67e-04 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 42.77 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 46 PVAQRVDLQGRVVTPGLVDCHSHavFGGDRAREFEMRLNGAsyAEIAAGGG---------GIASTVNATRQASESQLLE- 115
Cdd:PRK06189 40 PAREIIDADGLYVFPGMIDVHVH--FNEPGRTHWEGFATGS--AALAAGGCttyfdmplnSIPPTVTREALDAKAELARq 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 116 -SA-------------RQRIRELCRDGVTALE-IKSGYGLD---LANERKML---RAIRRLGDILPLTVRSTCLAAHAVP 174
Cdd:PRK06189 116 kSAvdfalwgglvpgnLEHLRELAEAGVIGFKaFMSNSGTDefrSSDDLTLYegmKEIAALGKILALHAESDALTRHLTT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 175 VEYQERADAWIDYICERllPElhqeglVDAVDAfcehlafspsqVERVFQKARELGLPvkLHAEQLTLQHGAALAARYHA 254
Cdd:PRK06189 196 QARQQGKTDVRDYLESR--PV------VAELEA-----------VQRALLYAQETGCP--LHFVHISSGKAVALIAEAKK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 255 LSAD-HLE----YLC--EEDiaaMARHGTVAVLLPGayyfLREKQLPPL--DLLRQYRVPIaLASDLNP----------- 314
Cdd:PRK06189 255 RGVDvSVEtcphYLLftEED---FERIGAVAKCAPP----LRSRSQKEElwRGLLAGEIDM-ISSDHSPcppelkegddf 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 315 -----GTSPVLSLRLMMNMACTLFRMTPEEALAGVT-LNGAKALGLdTVCGSLEAGKEASFVAWDIAYPAELSYWLGGSL 388
Cdd:PRK06189 327 flvwgGISGGQSTLLVMLTEGYIERGIPLETIARLLaTNPAKRFGL-PQKGRLEVGADADFVLVDLDETYTLTKEDLFYR 405
|
410
....*....|...
gi 1766864103 389 SKQVIYQGKEVYC 401
Cdd:PRK06189 406 HKQSPYEGRTFPG 418
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
6-74 |
1.97e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 40.08 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1766864103 6 HHCRIATmaagHYQLLDDGAMLTDGAVLLWVGNRAELPdlpvAQRVDLQGRVVTPGLVDCHSHAVFGGD 74
Cdd:COG1820 3 TNARIFT----GDGVLEDGALLIEDGRIAAIGPGAEPD----AEVIDLGGGYLAPGFIDLHVHGGGGVD 63
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
41-69 |
2.19e-03 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 40.16 E-value: 2.19e-03
10 20
....*....|....*....|....*....
gi 1766864103 41 ELPDLPVAQRVDLQGRVVTPGLVDCHSHA 69
Cdd:COG3653 36 DLAAAEAARVIDATGLVVAPGFIDIHTHY 64
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
48-75 |
3.79e-03 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 38.99 E-value: 3.79e-03
10 20
....*....|....*....|....*...
gi 1766864103 48 AQRVDLQGRVVTPGLVDCHSHAVFGGDR 75
Cdd:COG3964 42 KKVIDASGLYVTPGLIDLHTHVFPGGTD 69
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
40-124 |
5.32e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 38.64 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766864103 40 AELPDLPVAQRVDLQGRVVTPGLVDCHSHavfggdrarefeMRLNGASYAE-I-------AAGG-GGIASTVNATRQASE 110
Cdd:PRK09357 33 GENIEAEGAEVIDATGLVVAPGLVDLHVH------------LREPGQEDKEtIetgsraaAAGGfTTVVAMPNTKPVIDT 100
|
90
....*....|....
gi 1766864103 111 SQLLESARQRIREL 124
Cdd:PRK09357 101 PEVVEYVLDRAKEA 114
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| |
