|
Name |
Accession |
Description |
Interval |
E-value |
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
21-396 |
2.61e-179 |
|
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: 503.87 E-value: 2.61e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 21 IEDAAIVTEGHLIHWIGKQQQLPADTYSETVDLNGAWVTPGFIDCHTHSVFGGNRSVEFEKRLQGVSYAEIAASGGGIAS 100
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQLAALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGILS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 101 TVRATREASEEQLLNSALKRIRCMQQDGVTTIEIKSGYGLNYENERKMLRVIRQIGEKLPMTVKSTCLAAHALPPEYKDQ 180
Cdd:TIGR01224 81 TVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 181 SDAYIEHICTEMLPKLHAEGLVDAVDAFCEHLAFSPAQVERVFKTAQSLGLPVKLHAEQLSSLGGSSLAARYHALSADHL 260
Cdd:TIGR01224 161 PDDYVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 261 EYMTEDDVKAMAESGTVAVLLPGAFYLLREtQYPPIESLIKHGVRIALSSDLNPGTSPALSLRLMLNMGSTLFRLTPEQA 340
Cdd:TIGR01224 241 EHASDAGIKALAEAGTVAVLLPGTTFYLRE-TYPPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446660444 341 LAGITIHAAQALGLEQTHGSLEQGKVADFVAWDIEHPSEIVYWLGGDLPKRVVQHG 396
Cdd:TIGR01224 320 LHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNG 375
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
26-396 |
5.80e-179 |
|
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: 502.56 E-value: 5.80e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 26 IVTEGHLIHWIGKQQQLPADTYS--ETVDLNGAWVTPGFIDCHTHSVFGGNRSVEFEKRLQGVSYAEIAASGGGIASTVR 103
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPAaaEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 104 ATREASEEQLLNSALKRIRCMQQDGVTTIEIKSGYGLNYENERKMLRVIRQIGEKLPMTVKSTCLAAHALPPEYKDQsDA 183
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGR-EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 184 YIEHICTEMLPKLHAEGLVDAVDAFCEHLAFSPAQVERVFKTAQSLGLPVKLHAEQLSSLGGSSLAARYHALSADHLEYM 263
Cdd:cd01296 160 YIDLVIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 264 TEDDVKAMAESGTVAVLLPGAFYLLRETqYPPIESLIKHGVRIALSSDLNPGTSPALSLRLMLNMGSTLFRLTPEQALAG 343
Cdd:cd01296 240 SDEGIAALAEAGTVAVLLPGTAFSLRET-YPPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446660444 344 ITIHAAQALGLEQTHGSLEQGKVADFVAWDIEHPSEIVYWLGGDLPKRVVQHG 396
Cdd:cd01296 319 ATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-399 |
4.84e-95 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 289.55 E-value: 4.84e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 4 LWQNCHIATMQNGQYsyIEDAAIVTEGHLIHWIGKQQQLPADTYSETVDLNGAWVTPGFIDCHTHSVFGGNRSVEFEKrl 83
Cdd:COG1228 11 LITNATLVDGTGGGV--IENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 84 qgvsyaeiaasGGGIASTVratreaseeQLLNSALKRIRCMQQDGVTTIEIKSGYGLNY-----ENERKMLRVIRQIGEK 158
Cdd:COG1228 87 -----------GGGITPTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPLGLrdaiiAGESKLLPGPRVLAAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 159 LPMTVkstCLAAHAL-PPEykdqsdayiehiCTEMLPKLHAEGlVDAVDAFCEH--LAFSPAQVERVFKTAQSLGLPVKL 235
Cdd:COG1228 147 PALSL---TGGAHARgPEE------------ARAALRELLAEG-ADYIKVFAEGgaPDFSLEELRAILEAAHALGLPVAA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 236 HAEQLSslgGSSLAARYHALSADHLEYMTEDDVKAMAESGTVaVLLPGAFYLL-----------------RETQYPPIES 298
Cdd:COG1228 211 HAHQAD---DIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLallegaaapvaakarkvREAALANARR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 299 LIKHGVRIALSSDLNPGTSPALSLRLMLNMGsTLFRLTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVAWDIEHPS 378
Cdd:COG1228 287 LHDAGVPVALGTDAGVGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLE 365
|
410 420
....*....|....*....|.
gi 446660444 379 EIVYWlggDLPKRVVQHGQEV 399
Cdd:COG1228 366 DIAYL---EDVRAVMKDGRVV 383
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-378 |
6.47e-38 |
|
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: 141.50 E-value: 6.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 2 KKLWQNCHIATMqNGQYSYIEDAAIVTEGHLIHWIGKQQQLPAD-TYSETVDLNGAWVTPGFIDCHTHSVFGGNRSV--- 77
Cdd:COG0402 1 DLLIRGAWVLTM-DPAGGVLEDGAVLVEDGRIAAVGPGAELPARyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLadd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 78 -EFEKRLQGVSYaeiaasgggiastvRATREASEEQLLNSALKRIRCMQQDGVTTI-EIksgYGLNYENERKMLRVIRQI 155
Cdd:COG0402 80 lPLLDWLEEYIW--------------PLEARLDPEDVYAGALLALAEMLRSGTTTVaDF---YYVHPESADALAEAAAEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 156 GekLPMTVkSTCLAAHALPPEYKDQSDAYIEHiCTEMLPKLH--AEGLVDAVDAFCEHLAFSPAQVERVFKTAQSLGLPV 233
Cdd:COG0402 143 G--IRAVL-GRGLMDRGFPDGLREDADEGLAD-SERLIERWHgaADGRIRVALAPHAPYTVSPELLRAAAALARELGLPL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 234 KLH-AEQLS------SLGGSSLAARYH---ALSAD----HLEYMTEDDVKAMAESGTVAVLLPGAFYLLRETqYPPIESL 299
Cdd:COG0402 219 HTHlAETRDevewvlELYGKRPVEYLDelgLLGPRtllaHCVHLTDEEIALLAETGASVAHCPTSNLKLGSG-IAPVPRL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 300 IKHGVRIALSSDlNPGTSPALSLRLMLNMGSTLFR--------LTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVA 371
Cdd:COG0402 298 LAAGVRVGLGTD-GAASNNSLDMFEEMRLAALLQRlrggdptaLSAREALEMATLGGARALGLDDEIGSLEPGKRADLVV 376
|
....*..
gi 446660444 372 WDIEHPS 378
Cdd:COG0402 377 LDLDAPH 383
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
25-370 |
3.63e-25 |
|
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: 106.62 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 25 AIVTEGHLIHWIGKQQQLPA--DTYSETVDLNGAWVTPGFIDCHTHSVFGG--NRSVEFEK------------------- 81
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKAlkGPATEVIDLKGKTVLPGFIDSHSHLLLGGlsLLWLDLSGvtskeealariredaaaap 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 82 -----RLQGVSYAEI------------AASGG------------GIAST------------------------------- 101
Cdd:cd01300 81 pgewiLGFGWDESLLgegryptraeldAVSPDrpvlllrrdghsAWVNSaalrlagitrdtpdppggeivrdadgeptgv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 102 ---------VRATREASEEQLLNSALKRIRCMQQDGVTTIeikSGYGLNYENERKMLRVIRQIGE-KLPMTVkstCLAAH 171
Cdd:cd01300 161 lveaaaalvLEAVPPPTPEERRAALRAAARELASLGVTTV---HDAGGGAADDIEAYRRLAAAGElTLRVRV---ALYVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 172 ALPPEYKDQSDAYIEHICTEMLP----KLHAEGLVDA-----------VDAFCEHLAFSPAQVERVFKTAQSLGLPVKLH 236
Cdd:cd01300 235 PLAEDLLEELGARKNGAGDDRLRlggvKLFADGSLGSrtaalsepyldSPGTGGLLLISPEELEELVRAADEAGLQVAIH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 237 A-------------EQLSSLGGssLAARYHALsaDHLEYMTEDDVKAMAESGTVAVLLPG-AFYLL-----------RET 291
Cdd:cd01300 315 AigdravdtvldalEAALKDNP--RADHRHRI--EHAQLVSPDDIPRFAKLGVIASVQPNhLYSDGdaaedrrlgeeRAK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 292 QYPPIESLIKHGVRIALSSDLNPGT-SPALSLRLMLN--------MGSTLFRLTPEQALAGITIHAAQALGLEQTHGSLE 362
Cdd:cd01300 391 RSYPFRSLLDAGVPVALGSDAPVAPpDPLLGIWAAVTrktpgggvLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLE 470
|
....*...
gi 446660444 363 QGKVADFV 370
Cdd:cd01300 471 PGKLADFV 478
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
57-399 |
5.34e-23 |
|
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: 98.73 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 57 WVTPGFIDCHTHSVFGGNRSVEfekrlqgvsyaeiaasgggiastvratreASEEQLLNSALKRIRCMQQDGVTTIeIKS 136
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIP-----------------------------VPPEFAYEALRLGITTMLKSGTTTV-LDM 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 137 GYGLNYENERkMLRVIRQIGEKLPMTVKSTCLAahalpPEYKD-QSDAYIEHICTEM-LPKLHAEGLVDAVDAFCEHLAF 214
Cdd:pfam01979 51 GATTSTGIEA-LLEAAEELPLGLRFLGPGCSLD-----TDGELeGRKALREKLKAGAeFIKGMADGVVFVGLAPHGAPTF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 215 SPAQVERVFKTAQSLGLPVKLHAeqLSSLGG---SSLAARYHALSADHLEYMTE----DDVKAMAESG-----TVAVLLP 282
Cdd:pfam01979 125 SDDELKAALEEAKKYGLPVAIHA--LETKGEvedAIAAFGGGIEHGTHLEVAESggllDIIKLILAHGvhlspTEANLLA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 283 GAFYLLR-----------ETQYPPIESLIKHGVRIALSSD-LNPGTSPALSLRLMLNMGSTL---FRLTPEQALAGITIH 347
Cdd:pfam01979 203 EHLKGAGvahcpfsnsklRSGRIALRKALEDGVKVGLGTDgAGSGNSLNMLEELRLALELQFdpeGGLSPLEALRMATIN 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446660444 348 AAQALGLEQTHGSLEQGKVADFVAWDIEHPSEIVYWLGGDLPKRVVQHGQEV 399
Cdd:pfam01979 283 PAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-373 |
1.87e-22 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 99.10 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 4 LWQNCHIATMqNGQYSYIEdaAIVTEGHLIHWIGKQQQLPA--DTYSETVDLNGAWVTPGFIDCHTHSVFGGNRSVEFek 81
Cdd:COG1574 11 LLTNGRIYTM-DPAQPVAE--AVAVRDGRIVAVGSDAEVRAlaGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 82 RLQGV-SYAEIAA---------------SGGG-----IASTVRATR----EASEEQ------------LLNS-ALKRIrc 123
Cdd:COG1574 86 DLSGArSLDELLArlraaaaelppgewiLGRGwdeslWPEGRFPTRadldAVSPDRpvvltrvdghaaWVNSaALELA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 124 mqqdGVT--TIEIKSGYGLNYEN--------ERKMLRVIRQIGEKLPMTVKS--------------TCLAAHALPPeykD 179
Cdd:COG1574 164 ----GITadTPDPEGGEIERDADgeptgvlrEAAMDLVRAAIPPPTPEELRAalraalrelaslgiTSVHDAGLGP---D 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 180 QSDAYIE---------------HICTEMLPKLHAEGL----------VDAVDAFCE----------------------HL 212
Cdd:COG1574 237 DLAAYRElaaagelplrvvlylGADDEDLEELLALGLrtgygddrlrVGGVKLFADgslgsrtaallepyaddpgnrgLL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 213 AFSPAQVERVFKTAQSLGLPVKLHA-------------EQLssLGGSSLAARYHALSadHLEYMTEDDVKAMAESGTVAV 279
Cdd:COG1574 317 LLDPEELRELVRAADAAGLQVAVHAigdaavdevldayEAA--RAANGRRDRRHRIE--HAQLVDPDDLARFAELGVIAS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 280 LLP------GAFYLLR------ETQYPpIESLIKHGVRIALSSDlnpgtSPALSLRLMLNM----------GSTLF---R 334
Cdd:COG1574 393 MQPthatsdGDWAEDRlgperaARAYP-FRSLLDAGAPLAFGSD-----APVEPLDPLLGIyaavtrrtpsGRGLGpeeR 466
|
490 500 510
....*....|....*....|....*....|....*....
gi 446660444 335 LTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:COG1574 467 LTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLD 505
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
62-351 |
8.47e-19 |
|
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: 85.46 E-value: 8.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 62 FIDCHTHSVFGGNRSVEFEKRLQGVSYAEIAAsgggiasTVRATREASEEQLLNsalkrircmqqdGVTTIEIKSGYGLN 141
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELSPED-------LYEDTLRALEALLAG------------GVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 142 YENERKMLRVIRQIGEKLPMTVkstcLAAHALPPEYKDQSDAYIEHIcTEMLPKLHAEGlVDAVDAF--CEHLAFSPAQV 219
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRV----VLGLGIPGVPAAVDEDAEALL-LELLRRGLELG-AVGLKLAgpYTATGLSDESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 220 ERVFKTAQSLGLPVKLHAEQLSSLGGSSLAARY-----HALSADHLEYMTEDDVKAMAESG-TVAVLLPGAFYLLR-ETQ 292
Cdd:cd01292 136 RRVLEEARKLGLPVVIHAGELPDPTRALEDLVAllrlgGRVVIGHVSHLDPELLELLKEAGvSLEVCPLSNYLLGRdGEG 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 293 YPPIESLIKHGVRIALSSDLNPGTSPALSLRLMLNMG-STLFRLTPEQALAGITIHAAQA 351
Cdd:cd01292 216 AEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLkVLRLGLSLEEALRLATINPARA 275
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
6-387 |
3.33e-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: 85.72 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 6 QNCHIATMqnGQYSYIEDAAIVTEGHLIHWIGKQQQLPADTYSETVDLNGAWVTPGFIDCHTHSVFGGNRS----VEFEK 81
Cdd:cd01298 4 RNGTIVTT--DPRRVLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGladdLPLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 82 RLQGVsyaeiaasgggiasTVRATREASEEQLLNSALKRIRCMQQDGVTTIeIKSGYglnYENERKMlRVIRQIGeklpm 161
Cdd:cd01298 82 WLKDL--------------IWPLERLLTEEDVYLGALLALAEMIRSGTTTF-ADMYF---FYPDAVA-EAAEELG----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 162 tvkstcLAAHA------LPPEYKDQSDAYIEHiCTEMLPKLH--AEGLVDAvdAFCEHLAF--SPAQVERVFKTAQSLGL 231
Cdd:cd01298 138 ------IRAVLgrgimdLGTEDVEETEEALAE-AERLIREWHgaADGRIRV--ALAPHAPYtcSDELLREVAELAREYGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 232 PVKLHA----------------------EQLSSLGGSSLAAryhalsadHLEYMTEDDVKAMAESGTVAVLLPGA-FYLL 288
Cdd:cd01298 209 PLHIHLaetedeveeslekygkrpveylEELGLLGPDVVLA--------HCVWLTDEEIELLAETGTGVAHNPASnMKLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 289 RETqyPPIESLIKHGVRIALSSDlnpGTSPALSLRLM--LNMGSTLFR--------LTPEQALAGITIHAAQALGLEQTh 358
Cdd:cd01298 281 SGI--APVPEMLEAGVNVGLGTD---GAASNNNLDMFeeMRLAALLQKlahgdptaLPAEEALEMATIGGAKALGLDEI- 354
|
410 420 430
....*....|....*....|....*....|....*...
gi 446660444 359 GSLEQGKVADFVAWDIEHP---------SEIVYWLGGD 387
Cdd:cd01298 355 GSLEVGKKADLILIDLDGPhllpvhdpiSHLVYSANGG 392
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
49-400 |
1.47e-17 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 84.12 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 49 ETVDLNGAWVTPGFIDCHTHSVFGG--------------NRSVEFEKRLQ------GVSYAEIAASGGGIASTVRATREA 108
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGlnlrelrlpdvlpnAVVKGQAGRTPkgrwlvGEGWDEAQFAETRFPYALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 109 SEEQLLN-------SALKRIRCMQqdgvttieiKSGYGLNYENERkMLRVIRQIGEKLPMTV------------------ 163
Cdd:pfam07969 81 APDGPVLlralhthAAVANSAALD---------LAGITKATEDPP-GGEIARDANGEGLTGLlregayalppllareaea 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 164 KSTCLAAHALP----------PEYKDQSDAYIEH-------ICTEMLPKLHAEGL--------VDAVDAF---------- 208
Cdd:pfam07969 151 AAVAAALAALPgfgitsvdggGGNVHSLDDYEPLreltaaeKLKELLDAPERLGLphsiyelrIGAMKLFadgvlgsrta 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 209 -----------CEHLAFSPAQVERVFKTAQSLGLPVKLHAEQLSSLGGSSLAARYHAL--------SADH---LEYMTED 266
Cdd:pfam07969 231 altepyfdapgTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEklgnqgrvRIEHaqgVVPYTYS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 267 DVKAMAESGTVA----VLLPGAFYLLRET-------QYPPIESLIKHGVRIALSSDLNPGT-SPALSLR--LML--NMGS 330
Cdd:pfam07969 311 QIERVAALGGAAgvqpVFDPLWGDWLQDRlgaerarGLTPVKELLNAGVKVALGSDAPVGPfDPWPRIGaaVMRqtAGGG 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446660444 331 TLF----RLTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVAWDIE----HPSEIVYwlggDLPKRVVQHGQEVI 400
Cdd:pfam07969 391 EVLgpdeELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDpltvDPPAIAD----IRVRLTVVDGRVVY 464
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
49-373 |
1.48e-17 |
|
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: 83.11 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 49 ETVDLNGAWVTPGFIDCHTHsvFGGNRSVEFEKRLQGVSYAeiaasgggiasTVRATREAseeqllnsalkriRCMQQDG 128
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHTH--LGSDPGDLPLDLALPVEYR-----------TIRATRQA-------------RAALRAG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 129 VTTIeiKSGYGLNYENERKMlrvirqIGEKLP----MTVKSTCLAAHA-LPPEYKDQSDAYIEHICT------------- 190
Cdd:cd01299 56 FTTV--RDAGGADYGLLRDA------IDAGLIpgprVFASGRALSQTGgHGDPRGLSGLFPAGGLAAvvdgveevraavr 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 191 EMLP------KLHAEGLVDAVDAFCEHLAFSPAQVERVFKTAQSLGLPVKLHAEqlsSLGGSSLAARYHALSADHLEYMT 264
Cdd:cd01299 128 EQLRrgadqiKIMATGGVLSPGDPPPDTQFSEEELRAIVDEAHKAGLYVAAHAY---GAEAIRRAIRAGVDTIEHGFLID 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 265 EDDVKAMAESGTVAV---LLPGAFYLLRETQYPPIESLIKH-----------------GVRIALSSDL----NPGTSPAL 320
Cdd:cd01299 205 DETIELMKEKGIFLVptlATYEALAAEGAAPGLPADSAEKValvleagrdalrrahkaGVKIAFGTDAgfpvPPHGWNAR 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446660444 321 SLRLMLNMGstlfrLTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:cd01299 285 ELELLVKAG-----GTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
3-371 |
1.75e-17 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 83.52 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 3 KLWQNCHIATMQNGQYSYIeDAAIVTEGHLIHWIGKQQQLPADTYSETVDLNGAWVTPGFIDCHTHSVFGGNRSVEFEKR 82
Cdd:PRK06687 2 KVFQHVNIVTCDQDFHVYL-DGILAVKDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 83 LQG--VSYAEIAASGGGIASTVRATREASEEQLLNsalkrircmqqdGVTTieIKSGYGLNYENERKMLRVIRQIGEKL- 159
Cdd:PRK06687 81 LHEwlNDYIWPAESEFTPDMTTNAVKEALTEMLQS------------GTTT--FNDMYNPNGVDIQQIYQVVKTSKMRCy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 160 --PMTVKSTCLAAHalppEYKDQSDAYIEHICTEMLPKLHAeglvdavdAFCEHLAFSPAQ--VERVFKTAQSLGLPVKL 235
Cdd:PRK06687 147 fsPTLFSSETETTA----ETISRTRSIIDEILKYKNPNFKV--------MVAPHSPYSCSRdlLEASLEMAKELNIPLHV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 236 HAEQ--------LSSLGGSSLA-------ARYHALSADHLEyMTEDDVKAMAESgTVAVLLPGAFYLLRETQYPPIESLI 300
Cdd:PRK06687 215 HVAEtkeesgiiLKRYGKRPLAfleelgyLDHPSVFAHGVE-LNEREIERLASS-QVAIAHNPISNLKLASGIAPIIQLQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 301 KHGVRIALSSD----------LNPGTSPALsLRLMLNMGSTLFrlTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFV 370
Cdd:PRK06687 293 KAGVAVGIATDsvasnnnldmFEEGRTAAL-LQKMKSGDASQF--PIETALKVLTIEGAKALGMENQIGSLEVGKQADFL 369
|
.
gi 446660444 371 A 371
Cdd:PRK06687 370 V 370
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
36-400 |
1.20e-16 |
|
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: 80.75 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 36 IGKQQQLPADtySETVDLNGAWVTPGFIDCHTH--SVFGGNRSvefekrlqgvSYAEIAASGGGIASTVRATREASEEQL 113
Cdd:cd01293 27 IGPALAVPPD--AEEVDAKGRLVLPAFVDPHIHldKTFTGGRW----------PNNSGGTLLEAIIAWEERKLLLTAEDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 114 LNSALKRIRCMQQDGVTTI----EIKSGYGLNYenerkmLRVIRQIGEKLpmtvKSTC-LAAHALPPEykdqsdayiEHI 188
Cdd:cd01293 95 KERAERALELAIAHGTTAIrthvDVDPAAGLKA------LEALLELREEW----ADLIdLQIVAFPQH---------GLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 189 CTEmlpklHAEGLV-DAVDA---------FCEHLAFSPAQVERVFKTAQSLGLPVKLHAEQLSSLGGSSLA--ARY---- 252
Cdd:cd01293 156 STP-----GGEELMrEALKMgadvvggipPAEIDEDGEESLDTLFELAQEHGLDIDLHLDETDDPGSRTLEelAEEaerr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 253 ---------HALSadhLEYMTEDDVKA----MAESG-TVAVLLPGAFYLL-RETQYP------PIESLIKHGVRIALSSD 311
Cdd:cd01293 231 gmqgrvtcsHATA---LGSLPEAEVSRladlLAEAGiSVVSLPPINLYLQgREDTTPkrrgvtPVKELRAAGVNVALGSD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 312 --LNP----GTSPALSLrlmLNMGSTLFRLTPEQ----ALAGITIHAAQALGLEQthGSLEQGKVADFVAWDIEHPSEIV 381
Cdd:cd01293 308 nvRDPwypfGSGDMLEV---ANLAAHIAQLGTPEdlalALDLITGNAARALGLED--YGIKVGCPADLVLLDAEDVAEAV 382
|
410
....*....|....*....
gi 446660444 382 YwlgGDLPKRVVQHGQEVI 400
Cdd:cd01293 383 A---RQPPRRVVIRKGRVV 398
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
36-373 |
5.46e-15 |
|
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: 75.43 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 36 IGKQQQLPADTysETVDLNGAWVTPGFIDCHTHsvfggnrsvefekrlqgvsyaeIAASGGGiasTVRATREASEE---- 111
Cdd:cd01309 7 VGAEITTPADA--EVIDAKGKHVTPGLIDAHSH----------------------LGLDEEG---GVRETSDANEEtdpv 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 112 ----------QLLNSALKRIRcmqQDGVTTIEIKSGYGL----------NYENERKMLRVIRQIGEKL------------ 159
Cdd:cd01309 60 tphvraidgiNPDDEAFKRAR---AGGVTTVQVLPGSANliggqgvvikTDGGTIEDMFIKAPAGLKMalgenpkrvygg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 160 PMTVKSTCLAAHALPPEYKDQSDAYIEhictEMLPKLHAEGLVDAVDAFCEHLAfspaqveRVFKTAqslgLPVKLHAEQ 239
Cdd:cd01309 137 KGKEPATRMGVAALLRDAFIKAQEYGR----KYDLGKNAKKDPPERDLKLEALL-------PVLKGE----IPVRIHAHR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 240 LSSLggssLAARYHA------LSADHL--EYMTeddVKAMAESGTVAVL-----LPGAFYLLRETQYPPIESLIKHGVRI 306
Cdd:cd01309 202 ADDI----LTAIRIAkefgikITIEHGaeGYKL---ADELAKHGIPVIYgptltLPKKVEEVNDAIDTNAYLLKKGGVAF 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446660444 307 ALSSDlnpgtSPALSLR-LMLNMG-STLFRLTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:cd01309 275 AISSD-----HPVLNIRnLNLEAAkAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
215-373 |
2.53e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 74.27 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 215 SPAQVERVFKTAQSLGLPVKLHAEQLSSLGGSSLAARYHA---LSAD----HLEYMTEDDVKAMAESGTVAVLLPGAfyl 287
Cdd:PRK08204 199 SWEVARADFRLARELGLPISMHQGFGPWGATPRGVEQLHDaglLGPDlnlvHGNDLSDDELKLLADSGGSFSVTPEI--- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 288 lrETQ----YPPIESLIKHGVRIALSSDLNPGTSPAL--SLRLMLNM-----GSTLFR----------LTPEQALAGITI 346
Cdd:PRK08204 276 --EMMmghgYPVTGRLLAHGVRPSLGVDVVTSTGGDMftQMRFALQAerardNAVHLReggmppprltLTARQVLEWATI 353
|
170 180
....*....|....*....|....*..
gi 446660444 347 HAAQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:PRK08204 354 EGARALGLEDRIGSLTPGKQADLVLID 380
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
18-373 |
2.06e-12 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 68.05 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 18 YSYIEDAAIVTEGHLIHWIGK----QQQLPADTysETVDLNGAWVTPGFIDCHTH----SVFGG----------NRSVEF 79
Cdd:TIGR02967 1 LEYFEDGLLVVENGRIVAVGDyaelKETLPAGV--EIDDYRGHLIMPGFIDTHIHypqtEMIASygeqllewleKYTFPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 80 EKRLQGVSYAEIAAsgggiastvratreaseEQLLNSALKrircmqqDGVTT------IEIKSGYGLNYENERKMLRVIr 153
Cdd:TIGR02967 79 EARFADPDHAEEVA-----------------EFFLDELLR-------NGTTTalvfatVHPESVDALFEAALKRGMRMI- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 154 qIGEklpmtvksTCLAAHAlPPEYKD-------QSDAYIEHI-----------------CT----EMLPKLHAEglvdAV 205
Cdd:TIGR02967 134 -AGK--------VLMDRNA-PDYLRDtaessydESKALIERWhgkgrllyavtprfaptSSpeqlAAAGELAKE----YP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 206 DAFCE-HLAFSPAQVERV---FKTAQSLgLPVKLHAEQLsslggsslaaRYHALSAdHLEYMTEDDVKAMAESGTVAVLL 281
Cdd:TIGR02967 200 DVYVQtHLSENKDEIAWVkelFPEAKDY-LDVYDHYGLL----------GRRSVFA-HCIHLSDEECQRLAETGAAIAHC 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 282 PGA-FYL------LRETQyppiesliKHGVRIALSSDLNPGTSPALsLRLM------LNMGSTlfRLTPEQALAGITIHA 348
Cdd:TIGR02967 268 PTSnLFLgsglfnLKKAL--------EHGVRVGLGTDVGGGTSFSM-LQTLreaykvSQLQGA--RLSPFEAFYLATLGG 336
|
410 420
....*....|....*....|....*
gi 446660444 349 AQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:TIGR02967 337 ARALDLDDRIGNFEPGKEADFVVLD 361
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
33-399 |
3.60e-12 |
|
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: 67.09 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 33 IHWIGKQQQLPAdTYSETV--DLNGAWVTPGFIDCHTHSVFGGNrsvefekrLQGVSYAEIAA-SGGGIASTVRATREAS 109
Cdd:cd01312 3 ILEVGDYEKLEK-RYPGAKheFFPNGVLLPGLINAHTHLEFSAN--------VAQFTYGRFRAwLLSVINSRDELLKQPW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 110 EEQLLNSalkrIRCMQQDGVTTIEIKSGYGL---------------------NYENERKMLRVIRQIGEKL--------- 159
Cdd:cd01312 74 EEAIRQG----IRQMLESGTTSIGAISSDGSllpalassglrgvffnevigsNPSAIDFKGETFLERFKRSksfesqlfi 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 160 -------PMTVKSTclAAHALPPEYKDQSDAYIEHIcteMLPKLHAEGLVDAVDAFCEHLA-FSPAQVERVFKTAQSLgl 231
Cdd:cd01312 150 paisphaPYSVHPE--LAQDLIDLAKKLNLPLSTHF---LESKEEREWLEESKGWFKHFWEsFLKLPKPKKLATAIDF-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 232 pvklhAEQLSSLGGsslaaryhALSADHLEYMTEDDVKAMAESGTVAVLLPGAFYLLrETQYPPIESLIKHGVRIALSSD 311
Cdd:cd01312 223 -----LDMLGGLGT--------RVSFVHCVYANLEEAEILASRGASIALCPRSNRLL-NGGKLDVSELKKAGIPVSLGTD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 312 lnpGTSPALSLRLMLNMgSTLFRLTPEQ--------ALAGITIHAAQALGLEQthGSLEQGKVADFVAWDIEHPSEivyw 383
Cdd:cd01312 289 ---GLSSNISLSLLDEL-RALLDLHPEEdllelaseLLLMATLGGARALGLNN--GEIEAGKRADFAVFELPGPGI---- 358
|
410
....*....|....*.
gi 446660444 384 lGGDLPKRVVQHGQEV 399
Cdd:cd01312 359 -KEQAPLQFILHAKEV 373
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
16-373 |
5.67e-12 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 66.75 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 16 GQYSYIEDAAIVTEGHLIHWIGK----QQQLPADTysETVDLNGAWVTPGFIDCHTH----SVFGG---------NRSVe 78
Cdd:PRK09228 24 DALRYIEDGLLLVEDGRIVAAGPyaelRAQLPADA--EVTDYRGKLILPGFIDTHIHypqtDMIASygeqlldwlNTYT- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 79 F--EKRLQGVSYA-EIAA-------SGGGIASTVRAT-REASEEQLLNSALKR-IR------CMQQ---DGVT-TIEikS 136
Cdd:PRK09228 101 FpeERRFADPAYArEVAEffldellRNGTTTALVFGTvHPQSVDALFEAAEARnMRmiagkvLMDRnapDGLRdTAE--S 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 137 GYglnyeNERKML--------RVIRQIGEKLPMTvkST---CLAAHALPPEYkdqSDAYIEhictemlpklhaeglvdav 205
Cdd:PRK09228 179 GY-----DDSKALierwhgkgRLLYAITPRFAPT--STpeqLEAAGALAREH---PDVWIQ------------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 206 dafcEHLAFSPAQVERV---FKTAQSLgLPVKLHAEQLsslGGSSLAAryHALsadHLEymtEDDVKAMAESGTVAVLLP 282
Cdd:PRK09228 230 ----THLSENLDEIAWVkelFPEARDY-LDVYERYGLL---GPRAVFA--HCI---HLE---DRERRRLAETGAAIAFCP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 283 --------GAFYLLRetqyppiesLIKHGVRIALSSDLNPGTSpalslrlmLNMGSTL-----------FRLTPEQALAG 343
Cdd:PRK09228 294 tsnlflgsGLFDLKR---------ADAAGVRVGLGTDVGGGTS--------FSMLQTMneaykvqqlqgYRLSPFQAFYL 356
|
410 420 430
....*....|....*....|....*....|
gi 446660444 344 ITIHAAQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:PRK09228 357 ATLGGARALGLDDRIGNLAPGKEADFVVLD 386
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
21-380 |
7.71e-11 |
|
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: 63.19 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 21 IEDAAIVTEGHLIHWIGKQQQLPADTysETVDLNGAWVTPGFIDCHTHSvfggnrsvefekRLQGVSYAEIAASG----- 95
Cdd:COG0044 13 LERADVLIEDGRIAAIGPDLAAPEAA--EVIDATGLLVLPGLIDLHVHL------------REPGLEHKEDIETGtraaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 96 -GGI---------------ASTVRATREASEEQL-------------LNSALKRIRCMQQDGVTTIEIKSGY--GLNYEN 144
Cdd:COG0044 79 aGGVttvvdmpntnpvtdtPEALEFKLARAEEKAlvdvgphgaltkgLGENLAELGALAEAGAVAFKVFMGSddGNPVLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 145 ERKMLRVIRQIGEkLPMTVkstclAAHAlppEykDqsdayiEHICTEML-------PKLHAEGlvdaVDAFCEHLAfspa 217
Cdd:COG0044 159 DGLLRRALEYAAE-FGALV-----AVHA---E--D------PDLIRGGVmnegktsPRLGLKG----RPAEAEEEA---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 218 qVERVFKTAQSLGlpVKLHAEQLSSLGGSSLAARYHA----LSAD----HLeYMTEDDVkamAESGTVAVLlpgafyllr 289
Cdd:COG0044 214 -VARDIALAEETG--ARLHIVHVSTAEAVELIREAKArglpVTAEvcphHL-TLTDEDL---ERYGTNFKV--------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 290 etqYPPI------ESLIKhGVR---I-ALSSDLNP----------GTSPA------LSLRLMLNMGSTLFRLTPEQALAG 343
Cdd:COG0044 278 ---NPPLrteedrEALWE-GLAdgtIdVIATDHAPhtleekelpfAEAPNgipgleTALPLLLTELVHKGRLSLERLVEL 353
|
410 420 430
....*....|....*....|....*....|....*..
gi 446660444 344 ITIHAAQALGLEQtHGSLEQGKVADFVAWDIEHPSEI 380
Cdd:COG0044 354 LSTNPARIFGLPR-KGRIAVGADADLVLFDPDAEWTV 389
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
213-378 |
1.24e-10 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 62.94 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 213 AFSPAQVERVFKTAQSlGLPVKLH-AEQ-------LSSLGGS--SLAARYHALSAD----HLEYMTEDDVKAMAESGTVA 278
Cdd:PRK09229 212 AVTPDQLAAVLALAAP-DGPVHIHiAEQtkevddcLAWSGARpvEWLLDHAPVDARwclvHATHLTDAETARLARSGAVA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 279 VLLP--------GAFyllretqypPIESLIKHGVRIALSSDLNPGTSPALSLRLM----------------LNMGSTLFR 334
Cdd:PRK09229 291 GLCPtteanlgdGIF---------PAVDYLAAGGRFGIGSDSHVSIDLVEELRLLeygqrlrdrrrnvlaaAAQPSVGRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446660444 335 LTpEQALAGitihAAQALGleQTHGSLEQGKVADFVAWDIEHPS 378
Cdd:PRK09229 362 LF-DAALAG----GAQALG--RAIGGLAVGARADLVVLDLDHPA 398
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
215-387 |
2.02e-10 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 62.24 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 215 SPAQVERVFKTAQSLGLPVKLH--------AEQLSSLGGSSLAaRYHALS-------ADHLEYMTEDDVKAMAESGTVAV 279
Cdd:PRK09045 200 SDENLERIRTLAEQLDLPIHIHlhetaqeiADSLKQHGQRPLA-RLARLGllgprliAVHMTQLTDAEIALLAETGCSVV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 280 LLPGAFYLLrETQYPPIESLIKHGVRIALssdlnpGTSPALS---------LRL--MLNMGSTL--FRLTPEQALAGITI 346
Cdd:PRK09045 279 HCPESNLKL-ASGFCPVAKLLQAGVNVAL------GTDGAASnndldlfgeMRTaaLLAKAVAGdaTALPAHTALRMATL 351
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446660444 347 HAAQALGLEQTHGSLEQGKVADFVAWD--------IEHP-SEIVYWLGGD 387
Cdd:PRK09045 352 NGARALGLDDEIGSLEPGKQADLVAVDlsgletqpVYDPvSQLVYAAGRE 401
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
40-399 |
2.78e-10 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 61.49 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 40 QQLPADTYSETVDLNGAWVTPGFIDCHTH---SVFGG----NRS-------VEFEKRLQgvsyaeiAASGGGIAstVRAT 105
Cdd:PRK05985 31 PALAAPPGAEVEDGGGALALPGLVDGHIHldkTFWGDpwypNEPgpslrerIANERRRR-------AASGHPAA--ERAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 106 REAseEQLLNSALKRIRCMqqdgvttIEIKSGYGLnyENERKMLRVIRQIGEKLPMTVKstclaahALPpeykdQSDAYI 185
Cdd:PRK05985 102 ALA--RAAAAAGTTAMRSH-------VDVDPDAGL--RHLEAVLAARETLRGLIDIQIV-------AFP-----QSGVLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 186 EHICTEMLPKLHAEG--LVDAVDafcehlafsPA--------QVERVFKTAQSLGLPVKLHAEQLSSLGGSSL---AARY 252
Cdd:PRK05985 159 RPGTAELLDAALRAGadVVGGLD---------PAgidgdpegQLDIVFGLAERHGVGIDIHLHEPGELGAFQLeriAART 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 253 HALS---------ADHLEYMTEDDVK----AMAESGtVAVLL--PGAfyllreTQYPPIESLIKHGVRIALSSD-----L 312
Cdd:PRK05985 230 RALGmqgrvavshAFCLGDLPEREVDrlaeRLAEAG-VAIMTnaPGS------VPVPPVAALRAAGVTVFGGNDgirdtW 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 313 NP-GTSPALSLRLMLNMGSTLFR---LtpEQALAGITIHAAQALGLEQtHGsLEQGKVADFVAWDIEHPSEIVYwlggDL 388
Cdd:PRK05985 303 WPyGNGDMLERAMLIGYRSGFRTddeL--AAALDCVTHGGARALGLED-YG-LAVGARADFVLVDAETVAEAVV----AV 374
|
410
....*....|...
gi 446660444 389 PKR--VVQHGQEV 399
Cdd:PRK05985 375 PVRrlVVRGGRIV 387
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
15-377 |
1.67e-09 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 59.29 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 15 NGQYSYIEDAAIVTEGHLIHWIGKQQQLPADtysETVDLNGAWVTPGFIDCHTHS-----VFGGNRSVEFEK-RLQGVSY 88
Cdd:PRK06151 15 DGDHRLLRDGEVVFEGDRILFVGHRFDGEVD---RVIDAGNALVGPGFIDLDALSdldttILGLDNGPGWAKgRVWSRDY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 89 AEiaasgggiastvRATREA-SEEQLlnsALKRIRCMQQ---DGVTT-IEIKSGYglnyenerkmlrvIRQIGEklpmTV 163
Cdd:PRK06151 92 VE------------AGRREMyTPEEL---AFQKRYAFAQllrNGITTaMPIASLF-------------YRQWAE----TY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 164 KSTCLAAHA---------LPPEYKD-----QSDAYIEHICTEMLpKLHaeGLVDAVdAFCEHL----------AFSPAQV 219
Cdd:PRK06151 140 AEFAAAAEAagrlglrvyLGPAYRSggsvlEADGSLEVVFDEAR-GLA--GLEEAI-AFIKRVdgahnglvrgMLAPDRI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 220 E--------RVFKTAQSLGLPVKLHAEQ-------LSSLGGSS----------LAARY---HALSA---DHLEYMTEDDV 268
Cdd:PRK06151 216 EtctvdllrRTAAAARELGCPVRLHCAQgvlevetVRRLHGTTplewladvglLGPRLlipHATYIsgsPRLNYSGGDDL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 269 KAMAESGTVAVLLPGAFYlLRETQYPPIESLIKHGVRIALSSDlnpgTSPAlslRLMLNM--GSTLFRLT---PEQA-LA 342
Cdd:PRK06151 296 ALLAEHGVSIVHCPLVSA-RHGSALNSFDRYREAGINLALGTD----TFPP---DMVMNMrvGLILGRVVegdLDAAsAA 367
|
410 420 430
....*....|....*....|....*....|....*....
gi 446660444 343 GI----TIHAAQALGLEQThGSLEQGKVADFVAWDIEHP 377
Cdd:PRK06151 368 DLfdaaTLGGARALGRDDL-GRLAPGAKADIVVFDLDGL 405
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
259-373 |
1.76e-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: 59.21 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 259 HLEYMTEDDVKAMAESGTVAVLLP--------GAFyllretqypPIESLIKHGVRIALSSDLNPGTSPALsLRLM----- 325
Cdd:cd01303 267 HCVHLSEEEFNLLKERGASVAHCPtsnlflgsGLF---------DVRKLLDAGIKVGLGTDVGGGTSFSM-LDTLrqayk 336
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446660444 326 ----LNMGST-LFRLTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:cd01303 337 vsrlLGYELGgHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVID 389
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
29-378 |
1.75e-08 |
|
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: 55.92 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 29 EGHLIHWI--GKQQQLPADTYSETVDLNGAWVTPGFIDCHTHSvfggnrsveFEKRLQGVsyAEIAASGGGIAST----- 101
Cdd:cd01313 9 RNVRIEVDadGRIAAVNPDTATEAVALLGGALLPGMPNLHSHA---------FQRAMAGL--TEYRGSAADSFWTwrelm 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 102 VRATREASEEQLLNSALKRIRCMQQDGVTTI-EIK----SGYGLNYENERKM-LRVIRQIGEK-LPMTVKSTCL------ 168
Cdd:cd01313 78 YRFAARLTPEQIEAIARQLYIEMLLAGITAVgEFHyvhhDPDGTPYADPAELaQRVIAAASDAgIGITLLPVLYaragfg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 169 --AAHALPPEYKDQSDAYIEHICTEM-LPKLHAeglvDAVDAFCEH--LAFSPAQVERVFKTAQSLGlPVKLH-AEQ--- 239
Cdd:cd01313 158 gpAPNPGQRRFINGYEDFLGLLEKALrAVKEHA----AARIGVAPHslRAVPAEQLAALAALASEKA-PVHIHlAEQpke 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 240 ----LSSLGG---SSLAARYHA---LSADHLEYMTEDDVKAMAESGTVAVLLP-GAFYLLRETqyPPIESLIKHGVRIAL 308
Cdd:cd01313 233 vddcLAAHGRrpvELLLDHGHLdarWCLVHATHLTDNETLLLGRSGAVVGLCPtTEANLGDGI--FPAAALLAAGGRIGI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 309 SSDLNPGTSPALSLRLM----------LNMGSTLFRLTPEQALAGITIHAAQALGLeqTHGSLEQGKVADFVAWDIEHPS 378
Cdd:cd01313 311 GSDSNARIDLLEELRQLeysqrlrdraRNVLATAGGSSARALLDAALAGGAQALGL--ATGALEAGARADLLSLDLDHPS 388
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
1-401 |
3.15e-08 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 55.45 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 1 MKKLWQNCHIATMqNGQYSYIEDAAIVTEGHLIHWIGKQQQLPADTYSETVDLNGAWVTPGFIDCHTHSVFGGNRSVE-- 78
Cdd:PRK15493 1 MKTTYVNATIVTM-NEQNEVIENGYIIVENDQIIDVNSGEFASDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 79 ------FEKRL-----QGVSYAEIAASGGGIASTVRA--------------TREASEEQLLNSALKRI--RCM-----QQ 126
Cdd:PRK15493 80 mllqpwLETRIwplesQFTPELAVASTELGLLEMVKSgttsfsdmfnpigvDQDAIMETVSRSGMRAAvsRTLfsfgtKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 127 DGVTTIEIKSGYGLNYENERKMLrvirqigeklpmtvkSTCLAAHAlppeykdqsdayiEHIC-TEMLPKLhAEGLVDAV 205
Cdd:PRK15493 160 DEKKAIEEAEKYVKRYYNESGML---------------TTMVAPHS-------------PYTCsTELLEEC-ARIAVENQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 206 DAFCEHLAFSPAQVERVfkTAQSLGLPVKlHAEQLSSLGGSSLAARYHALSADHLEYMTEDDVKAMAESGTVAVLLPGAf 285
Cdd:PRK15493 211 TMVHIHLSETEREVRDI--EAQYGKRPVE-YAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGI- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 286 yllretqyPPIESLIKHGVRIALSSDlNPGTSPALSLRLMLNMGSTLFR--------LTPEQALAGITIHAAQALGLEQT 357
Cdd:PRK15493 287 --------ANVKAMLEAGIKVGIATD-SVASNNNLDMFEEMRIATLLQKgihqdataLPVETALTLATKGAAEVIGMKQT 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446660444 358 hGSLEQGKVADFVAWDI----------EHPSEIVYWLGGDLPKRVVQHGQEVIF 401
Cdd:PRK15493 358 -GSLEVGKCADFITIDPsnkphlqpadEVLSHLVYAASGKDISDVIINGKRVVW 410
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
6-68 |
3.77e-08 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 54.86 E-value: 3.77e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446660444 6 QNCHIATMqNGQYSYIEDAAIVTEGHLIHWIGKQQQLPAdTYSETVDLNGAWVTPGFIDCHTH 68
Cdd:PRK08203 7 NPLAIVTM-DAARREIADGGLVVEGGRIVEVGPGGALPQ-PADEVFDARGHVVTPGLVNTHHH 67
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
21-68 |
2.97e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 52.02 E-value: 2.97e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446660444 21 IEDAAIVTEGHLIHWIGKQQQLPAdtysETVDLNGAWVTPGFIDCHTH 68
Cdd:COG1820 14 LEDGALLIEDGRIAAIGPGAEPDA----EVIDLGGGYLAPGFIDLHVH 57
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
1-108 |
5.89e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 47.91 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 1 MKKLWQNCHIATmqngQYSYIEDAAIVTEGHLIHWIGKQQQLPadTYSETVDLNGAWVTPGFIDCHTHSVFG---GNRSV 77
Cdd:TIGR00221 3 ESYLLKDIAIVT----GNEVIDNGAVGINDGKISTVSTEAELE--PEIKEIDLPGNVLTPGFIDIHIHGCGGvdtNDASF 76
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446660444 78 EFEKRLQG-------VSY--AEIAASGGGIASTVRATREA 108
Cdd:TIGR00221 77 ETLEIMSErlpksgcTSFlpTLITQPDENIKQAVKNMREY 116
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
335-373 |
7.27e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.79 E-value: 7.27e-06
10 20 30
....*....|....*....|....*....|....*....
gi 446660444 335 LTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:COG1820 322 LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLD 360
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
33-69 |
9.42e-06 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 47.48 E-value: 9.42e-06
10 20 30
....*....|....*....|....*....|....*..
gi 446660444 33 IHWIGKqqqLPADTYSETVDLNGAWVTPGFIDCHTHS 69
Cdd:COG3653 31 IVAVGD---LAAAEAARVIDATGLVVAPGFIDIHTHY 64
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
19-96 |
1.49e-05 |
|
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: 46.83 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 19 SYIEDAAIvtEGHLIHWIGkqQQLPADTYSETVDLNGAWVTPGFIDCHTH--SVFGGNRSVE-FEkrlqgvSYAEIAASG 95
Cdd:cd01314 14 SFKADILI--EDGKIVAIG--PNLEAPGGVEVIDATGKYVLPGGIDPHTHleLPFMGTVTADdFE------SGTRAAAAG 83
|
.
gi 446660444 96 G 96
Cdd:cd01314 84 G 84
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
7-64 |
2.12e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 46.12 E-value: 2.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446660444 7 NCHIATmqngQYSYIEDAAIVTEGHLIHWIGKQQQLPADTysETVDLNGAWVTPGFID 64
Cdd:PRK11170 6 NGRIYT----GHEVLDDHAVVIADGLIEAVCPVAELPPGI--EQRDLNGAILSPGFID 57
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
321-373 |
3.90e-05 |
|
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: 45.26 E-value: 3.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446660444 321 SLRLMLNMGStlfrLTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:cd00854 314 AVRNMVKWGG----CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD 362
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
21-122 |
3.93e-05 |
|
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: 45.26 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 21 IEDAAIVTEGHLIHWIGKQQqlPADTYSETVDLNGAWVTPGFIDCHTHSVFGGNRSVEFEKRLQGVSYAeIAASG--GGI 98
Cdd:cd00854 14 LEDGAVLVEDGKIVAIGPED--ELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAEALKTIAEA-LAKHGttSFL 90
|
90 100
....*....|....*....|....
gi 446660444 99 ASTVRATREAseeqlLNSALKRIR 122
Cdd:cd00854 91 PTTVTAPPEE-----IAKALAAIA 109
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
259-401 |
1.39e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 43.83 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 259 HLEYMTEDDVKAMAESGTVAVLLPGAFYLLrETQYPPIESLIKHGVRIALSSD-------LNPGT--SPALSLRLMLNMG 329
Cdd:PRK07228 255 HCVWLDEEEREILAETGTHVTHCPSSNLKL-ASGIAPVPDLLERGINVALGADgapcnntLDPFTemRQAALIQKVDRLG 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446660444 330 STlfRLTPEQALAGITIHAAQALGLEQTHGSLEQGKVADFVAWDIEH----PSEivywlGGDLPKRVV--QHGQEVIF 401
Cdd:PRK07228 334 PT--AMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDLDGlhatPSH-----GVDVLSHLVyaAHGSDVET 404
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
21-69 |
1.87e-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: 43.44 E-value: 1.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446660444 21 IEDAAIVTeghlihwIGKQQQLPADtysETVDLNGAWVTPGFIDCHTHS 69
Cdd:cd01297 24 IRDGRIAA-------IGPILSTSAR---EVIDAAGLVVAPGFIDVHTHY 62
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
42-73 |
2.16e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 42.92 E-value: 2.16e-04
10 20 30
....*....|....*....|....*....|..
gi 446660444 42 LPADTYSETVDLNGAWVTPGFIDCHTHSVFGG 73
Cdd:PRK09237 35 IDGSQAKKVIDLSGLYVSPGWIDLHVHVYPGS 66
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
6-68 |
2.51e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 43.17 E-value: 2.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446660444 6 QNCHIATMQNGQysyIEDAAIVTEGHLIHWIGKQQQlPAdtySETVDLNGAWVTPGFIDCHTH 68
Cdd:COG1001 10 KNGRLVNVFTGE---ILEGDIAIAGGRIAGVGDYIG-EA---TEVIDAAGRYLVPGFIDGHVH 65
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
325-376 |
3.24e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 42.53 E-value: 3.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446660444 325 MLNMGSTLfrltpEQALAGITIHAAQALGLEQThGSLEQGKVADFVAWDIEH 376
Cdd:PRK09237 291 FLALGMPL-----EEVIAAVTKNAADALRLPEL-GRLQVGSDADLTLFTLKD 336
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
42-71 |
5.02e-04 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 42.08 E-value: 5.02e-04
10 20 30
....*....|....*....|....*....|
gi 446660444 42 LPADTYSETVDLNGAWVTPGFIDCHTHsVF 71
Cdd:COG3964 36 IDAAEAKKVIDASGLYVTPGLIDLHTH-VF 64
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
20-68 |
6.67e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 41.46 E-value: 6.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446660444 20 YIEDAAIVTEGHLIHWIGKQQQLPAdTY--SETVDLNGAWVTPGFIDCHTH 68
Cdd:PRK07203 18 VIEDGAIAIEGNVIVEIGTTDELKA-KYpdAEFIDAKGKLIMPGLINSHNH 67
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
295-384 |
1.02e-03 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 41.11 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 295 PIESLIKHGVRIALSSDlnpGTSPALSLRLMLNMGSTLFRLTPE-------QALAGITIHAAQALGLEQthGSLEQGKVA 367
Cdd:PRK08418 295 DLEKAKKAGINYSIATD---GLSSNISLSLLDELRAALLTHANMpllelakILLLSATRYGAKALGLNN--GEIKEGKDA 369
|
90 100
....*....|....*....|.
gi 446660444 368 DFVAWD----IEHPSEIVYWL 384
Cdd:PRK08418 370 DLSVFElpeeCTKKEQLPLQF 390
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-68 |
1.40e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 40.56 E-value: 1.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446660444 1 MKKLWQNCHIATMQNGqysyIEDAAIVTEGHLIHWIGKQQQLPADtysETVDLNGAWVTPGFIDCHTH 68
Cdd:PRK09357 1 MMILIKNGRVIDPKGL----DEVADVLIDDGKIAAIGENIEAEGA---EVIDATGLVVAPGLVDLHVH 61
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
20-138 |
1.74e-03 |
|
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: 40.07 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 20 YIEDAAIVTEGHLIHWIGKQQQLPADTYSETVDLNGAWVTPGFIDCHTHsVFGGNRSVEFEKRLQGVSYAEIAAsgGGIA 99
Cdd:cd01308 14 YLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVH-IIGGGGEGGPSTRTPEVTLSDLTT--AGVT 90
|
90 100 110
....*....|....*....|....*....|....*....
gi 446660444 100 STVRATREASEEQLLNSALKRIRCMQQDGVTTIEIKSGY 138
Cdd:cd01308 91 TVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSY 129
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
58-349 |
4.46e-03 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 38.54 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 58 VTPGFIDCHTH---SVF---GGNRSVEfekrlqgvsyaEIAASGGGIAStvRATREASEEQLLNSALKRIRCMQQDGVtt 131
Cdd:cd01305 2 LIPALVNAHTHlgdSAIkevGDGLPLD-----------DLVAPPDGLKH--RLLAQADDRELAEAMRKVLRDMRETGI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 132 ieiksGYGLNY-ENERKMLRVIRQIGEKLPmTVKSTCLAAhalpPEYKDQSDAYIEHictemlpklhaeglvdavdafCE 210
Cdd:cd01305 67 -----GAFADFrEGGVEGIELLRRALGKLP-VPFEVILGR----PTEPDDPEILLEV---------------------AD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446660444 211 HLAFSPA---QVERVFKTAQSLGLPVKLHA-EQLSSLGGSSLAAryhALSAD-----HLEYMTEDDVKAMAESGTVAVLL 281
Cdd:cd01305 116 GLGLSSAndvDLEDILELLRRRGKLFAIHAsETRESVGMTDIER---ALDLEpdllvHGTHLTDEDLELVRENGVPVVLC 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446660444 282 P---GAFYLLRetqyPPIESLIKHGVRIALSSD---LNPgTSPALSLRLMLNMGSTLFRLTPEQALAGITIHAA 349
Cdd:cd01305 193 PrsnLYFGVGI----PPVAELLKLGIKVLLGTDnvmVNE-PDMWAEMEFLAKYSRLQGYLSPLEILRMATVNAA 261
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
341-373 |
5.71e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 38.92 E-value: 5.71e-03
10 20 30
....*....|....*....|....*....|...
gi 446660444 341 LAGITIHAAQALGLEQTHGSLEQGKVADFVAWD 373
Cdd:PRK13308 406 IAKYTINPAITFGIDDHIGSLEPGKLADIVLWR 438
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
13-72 |
6.22e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 38.63 E-value: 6.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446660444 13 MQNGQYSYIED-----AAIVTEGHLIHWIGKQQQLPADTyseTVDLNGAWVTPGFIDCHTHSVFG 72
Cdd:PRK08393 5 IKNGYVIYGENlkvirADVLIEGNKIVEVKRNINKPADT---VIDASGSVVSPGFINAHTHSPMV 66
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
37-97 |
6.31e-03 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 38.61 E-value: 6.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446660444 37 GKQQQLPADTYSETVDLNGAWVTPGFIDCHTH--SVFGGNRSVE-FEkrlqgvsYAEIAASGGG 97
Cdd:PRK08323 26 GKIAAIGANLGDEVIDATGKYVMPGGIDPHTHmeMPFGGTVSSDdFE-------TGTRAAACGG 82
|
|
| |
