|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
1-453 |
0e+00 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 761.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 1 MSAIFAERALLPEGWARNVRFEISADGVLAGIRPDANADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWT 80
Cdd:PRK09229 2 MTTLFAERALLPDGWARNVRLTVDADGRIAAVEPGAAPAGAERLAGPVLPGMPNLHSHAFQRAMAGLTEVRGPPQDSFWS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 81 WRELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLYS 160
Cdd:PRK09229 82 WRELMYRFALRLTPDQLEAIARQLYVEMLEAGYTSVGEFHYLHHDPDGTPYADPAEMALRIVAAARAAGIGLTLLPVLYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 161 HAGFGGQPASEGQRRFINGSEAYLELLQRLRAPLEA-AGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAEQQKE 239
Cdd:PRK09229 162 HSGFGGQPPNPGQRRFINDPDGFLRLLEALRRALAAlPGARLGLAPHSLRAVTPDQLAAVLALAAPDGPVHIHIAEQTKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 240 VDDCLAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGS 319
Cdd:PRK09229 242 VDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 320 DSHVSLSVVEELRWLEYGQRLRDRKRNRLYRDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLAS 399
Cdd:PRK09229 322 DSHVSIDLVEELRLLEYGQRLRDRRRNVLAAAAQPSVGRRLFDAALAGGAQALGRAIGGLAVGARADLVVLDLDHPALAG 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 558688754 400 AEGDALLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAGEERSARAFVQVLGELLD 453
Cdd:PRK09229 402 REGDALLDRWVFAGGDAAVRDVWVAGRWVVRDGRHRLREAIAAAFRAALAALLA 455
|
|
| hutF |
TIGR02022 |
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to ... |
1-452 |
0e+00 |
|
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to glutamate in four step, the last being removal of formamide. This model describes an alternate fourth step, formiminoglutamate hydrolase, which leads to N-formyl-L-glutamate. This product may be acted on by formylglutamate amidohydrolase (TIGR02017) and bypass glutamate as a product during its degradation. Alternatively, removal of formate (by EC 3.5.1.68) would yield glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273931 [Multi-domain] Cd Length: 454 Bit Score: 669.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 1 MSAIFAERALLPEGWARNVRFEIsADGVLAGIRPDA-NADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFW 79
Cdd:TIGR02022 1 MHVYWAERALLPDGWAEGVRIAV-ADGRILAIETGVpAAPGDERLSGPLLPGLANLHSHAFQRAMAGLAEVAGSGGDSFW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 80 TWRELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLY 159
Cdd:TIGR02022 80 TWRELMYRFADRLTPEQLQAIARQLYVEMLEAGFTRVGEFHYLHHAPDGTPYADPAEMAERIAAAAADAGIGLTLLPVFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 160 SHAGFGGQPASEGQRRFINGSEAYLELLQRLRAPLEA-AGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAEQQK 238
Cdd:TIGR02022 160 AHSGFGGAAPNPGQRRFIHDPERFARLVEVLRRTLAAqPGAVLGLAPHSLRAVTPEQLAAVLQASDRQAPVHIHVAEQQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 239 EVDDCLAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIG 318
Cdd:TIGR02022 240 EVDDCLAWSGRRPVEWLLDHGPVDARWCLVHATHLTDEETKLLAKSGAVAGLCPTTEANLGDGIFPAVDFAAAGGRFGIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 319 SDSHVSLSVVEELRWLEYGQRLRDRKRNRLYRDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLA 398
Cdd:TIGR02022 320 SDSHVLIDVAEELRQLEYGQRLRDRARNVLAAGPGPSVGRALYDAALLGGAQALGRATGGLRAGARADFLTLDGDHPRLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 558688754 399 SAEGDALLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAGEERSARAFVQVLGELL 452
Cdd:TIGR02022 400 GALGDSLLDRWLFAGGKAAVRDVWVGGRWVVRDGRHALREEIGRAFAKVLRALL 453
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
9-426 |
0e+00 |
|
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: 631.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 9 ALLPEGWARNVRFEISADGVLAGIRPDANADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRELMYRM 88
Cdd:cd01313 1 ALLPEGWERNVRIEVDADGRIAAVNPDTATEAVALLGGALLPGMPNLHSHAFQRAMAGLTEYRGSAADSFWTWRELMYRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 89 VARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLYSHAGFGGQP 168
Cdd:cd01313 81 AARLTPEQIEAIARQLYIEMLLAGITAVGEFHYVHHDPDGTPYADPAELAQRVIAAASDAGIGITLLPVLYARAGFGGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 169 ASEGQRRFINGSEAYLELLQR-LRAPLEAAGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAEQQKEVDDCLAWS 247
Cdd:cd01313 161 PNPGQRRFINGYEDFLGLLEKaLRAVKEHAAARIGVAPHSLRAVPAEQLAALAALASEKAPVHIHLAEQPKEVDDCLAAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 248 GRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVSLSV 327
Cdd:cd01313 241 GRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSDSNARIDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 328 VEELRWLEYGQRLRDRKRNRLYrDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASAEGDALLN 407
Cdd:cd01313 321 LEELRQLEYSQRLRDRARNVLA-TAGGSSARALLDAALAGGAQALGLATGALEAGARADLLSLDLDHPSLAGALPDTLLD 399
|
410
....*....|....*....
gi 558688754 408 RWLFAGGDRQVRDVMVAGR 426
Cdd:cd01313 400 AWVFAAGDREVRDVVVGGR 418
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
14-431 |
2.78e-106 |
|
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: 321.39 E-value: 2.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 14 GWARNVRFEIsADGVLAGIRPDANA----DGAERL---GGAVLPGMPNLHSHAFQRAMAGLAEvagnpNDSFWTWR-ELM 85
Cdd:COG0402 17 GVLEDGAVLV-EDGRIAAVGPGAELparyPAAEVIdagGKLVLPGLVNTHTHLPQTLLRGLAD-----DLPLLDWLeEYI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 86 YRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHdldgrsyadpaELSLRISRAASAAGIGLTLLPVLYSHagfg 165
Cdd:COG0402 91 WPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHP-----------ESADALAEAAAEAGIRAVLGRGLMDR---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 166 GQPASEGQRRfingsEAYLELLQRLRAPLEAAGHSL---GLCFHSLRAVTPQQIATVLA-AGHDDLPVHIHIAEQQKEVD 241
Cdd:COG0402 156 GFPDGLREDA-----DEGLADSERLIERWHGAADGRirvALAPHAPYTVSPELLRAAAAlARELGLPLHTHLAETRDEVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 242 DCLAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSD- 320
Cdd:COG0402 231 WVLELYGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDg 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 321 --SHVSLSVVEELRWLEYGQRLRDRKRNR-----------------LYRDDQpmigrtlydaalaggaqalgqpIGSLAV 381
Cdd:COG0402 311 aaSNNSLDMFEEMRLAALLQRLRGGDPTAlsarealematlggaraLGLDDE----------------------IGSLEP 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 558688754 382 GRRADLLVLDGNDPYLASAegDALLNRWLFAGGDRQVRDVMVAGRWVVRD 431
Cdd:COG0402 369 GKRADLVVLDLDAPHLAPL--HDPLSALVYAADGRDVRTVWVAGRVVVRD 416
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
48-428 |
1.14e-20 |
|
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: 92.56 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 48 VLPGMPNLHSHAFQRAMAGlaevagnpndsfwtwrelmyrmvARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDLD 127
Cdd:pfam01979 2 VLPGLIDAHVHLEMGLLRG-----------------------IPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 128 grsyadpaelsLRISRAASAAGIGLTLLpvlyshaGFGGQPASEGQRRfiNGSEAYLELLQRLRAPLEAAGHSL--GLCF 205
Cdd:pfam01979 59 -----------EALLEAAEELPLGLRFL-------GPGCSLDTDGELE--GRKALREKLKAGAEFIKGMADGVVfvGLAP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 206 HSLRAVTPQQIATVLAAGHD-DLPVHIHIAEQQKEVDDCLAWSGRR-----PLQWLYENVAVDQ-RWCLVHATHADPAEV 278
Cdd:pfam01979 119 HGAPTFSDDELKAALEEAKKyGLPVAIHALETKGEVEDAIAAFGGGiehgtHLEVAESGGLLDIiKLILAHGVHLSPTEA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 279 AAMARSGAVAGLCL--STEANLGDGIFPATDFLAQGGRLGIGSDSHVS---LSVVEELRWLeYGQRLRDRKRNRLYRDDQ 353
Cdd:pfam01979 199 NLLAEHLKGAGVAHcpFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSgnsLNMLEELRLA-LELQFDPEGGLSPLEALR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 354 PM-------IGRTLYdaalaggaqalgqpIGSLAVGRRADLLVLDGNdpylasaegdaLLNRWLFAGGDRQVRDVMVAGR 426
Cdd:pfam01979 278 MAtinpakaLGLDDK--------------VGSIEVGKDADLVVVDLD-----------PLAAFFGLKPDGNVKKVIVKGK 332
|
..
gi 558688754 427 WV 428
Cdd:pfam01979 333 IV 334
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
1-453 |
0e+00 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 761.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 1 MSAIFAERALLPEGWARNVRFEISADGVLAGIRPDANADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWT 80
Cdd:PRK09229 2 MTTLFAERALLPDGWARNVRLTVDADGRIAAVEPGAAPAGAERLAGPVLPGMPNLHSHAFQRAMAGLTEVRGPPQDSFWS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 81 WRELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLYS 160
Cdd:PRK09229 82 WRELMYRFALRLTPDQLEAIARQLYVEMLEAGYTSVGEFHYLHHDPDGTPYADPAEMALRIVAAARAAGIGLTLLPVLYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 161 HAGFGGQPASEGQRRFINGSEAYLELLQRLRAPLEA-AGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAEQQKE 239
Cdd:PRK09229 162 HSGFGGQPPNPGQRRFINDPDGFLRLLEALRRALAAlPGARLGLAPHSLRAVTPDQLAAVLALAAPDGPVHIHIAEQTKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 240 VDDCLAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGS 319
Cdd:PRK09229 242 VDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 320 DSHVSLSVVEELRWLEYGQRLRDRKRNRLYRDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLAS 399
Cdd:PRK09229 322 DSHVSIDLVEELRLLEYGQRLRDRRRNVLAAAAQPSVGRRLFDAALAGGAQALGRAIGGLAVGARADLVVLDLDHPALAG 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 558688754 400 AEGDALLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAGEERSARAFVQVLGELLD 453
Cdd:PRK09229 402 REGDALLDRWVFAGGDAAVRDVWVAGRWVVRDGRHRLREAIAAAFRAALAALLA 455
|
|
| hutF |
TIGR02022 |
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to ... |
1-452 |
0e+00 |
|
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to glutamate in four step, the last being removal of formamide. This model describes an alternate fourth step, formiminoglutamate hydrolase, which leads to N-formyl-L-glutamate. This product may be acted on by formylglutamate amidohydrolase (TIGR02017) and bypass glutamate as a product during its degradation. Alternatively, removal of formate (by EC 3.5.1.68) would yield glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273931 [Multi-domain] Cd Length: 454 Bit Score: 669.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 1 MSAIFAERALLPEGWARNVRFEIsADGVLAGIRPDA-NADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFW 79
Cdd:TIGR02022 1 MHVYWAERALLPDGWAEGVRIAV-ADGRILAIETGVpAAPGDERLSGPLLPGLANLHSHAFQRAMAGLAEVAGSGGDSFW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 80 TWRELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLY 159
Cdd:TIGR02022 80 TWRELMYRFADRLTPEQLQAIARQLYVEMLEAGFTRVGEFHYLHHAPDGTPYADPAEMAERIAAAAADAGIGLTLLPVFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 160 SHAGFGGQPASEGQRRFINGSEAYLELLQRLRAPLEA-AGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAEQQK 238
Cdd:TIGR02022 160 AHSGFGGAAPNPGQRRFIHDPERFARLVEVLRRTLAAqPGAVLGLAPHSLRAVTPEQLAAVLQASDRQAPVHIHVAEQQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 239 EVDDCLAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIG 318
Cdd:TIGR02022 240 EVDDCLAWSGRRPVEWLLDHGPVDARWCLVHATHLTDEETKLLAKSGAVAGLCPTTEANLGDGIFPAVDFAAAGGRFGIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 319 SDSHVSLSVVEELRWLEYGQRLRDRKRNRLYRDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLA 398
Cdd:TIGR02022 320 SDSHVLIDVAEELRQLEYGQRLRDRARNVLAAGPGPSVGRALYDAALLGGAQALGRATGGLRAGARADFLTLDGDHPRLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 558688754 399 SAEGDALLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAGEERSARAFVQVLGELL 452
Cdd:TIGR02022 400 GALGDSLLDRWLFAGGKAAVRDVWVGGRWVVRDGRHALREEIGRAFAKVLRALL 453
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
9-426 |
0e+00 |
|
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: 631.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 9 ALLPEGWARNVRFEISADGVLAGIRPDANADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRELMYRM 88
Cdd:cd01313 1 ALLPEGWERNVRIEVDADGRIAAVNPDTATEAVALLGGALLPGMPNLHSHAFQRAMAGLTEYRGSAADSFWTWRELMYRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 89 VARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLYSHAGFGGQP 168
Cdd:cd01313 81 AARLTPEQIEAIARQLYIEMLLAGITAVGEFHYVHHDPDGTPYADPAELAQRVIAAASDAGIGITLLPVLYARAGFGGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 169 ASEGQRRFINGSEAYLELLQR-LRAPLEAAGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAEQQKEVDDCLAWS 247
Cdd:cd01313 161 PNPGQRRFINGYEDFLGLLEKaLRAVKEHAAARIGVAPHSLRAVPAEQLAALAALASEKAPVHIHLAEQPKEVDDCLAAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 248 GRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVSLSV 327
Cdd:cd01313 241 GRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSDSNARIDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 328 VEELRWLEYGQRLRDRKRNRLYrDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASAEGDALLN 407
Cdd:cd01313 321 LEELRQLEYSQRLRDRARNVLA-TAGGSSARALLDAALAGGAQALGLATGALEAGARADLLSLDLDHPSLAGALPDTLLD 399
|
410
....*....|....*....
gi 558688754 408 RWLFAGGDRQVRDVMVAGR 426
Cdd:cd01313 400 AWVFAAGDREVRDVVVGGR 418
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
14-431 |
2.78e-106 |
|
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: 321.39 E-value: 2.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 14 GWARNVRFEIsADGVLAGIRPDANA----DGAERL---GGAVLPGMPNLHSHAFQRAMAGLAEvagnpNDSFWTWR-ELM 85
Cdd:COG0402 17 GVLEDGAVLV-EDGRIAAVGPGAELparyPAAEVIdagGKLVLPGLVNTHTHLPQTLLRGLAD-----DLPLLDWLeEYI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 86 YRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHdldgrsyadpaELSLRISRAASAAGIGLTLLPVLYSHagfg 165
Cdd:COG0402 91 WPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHP-----------ESADALAEAAAEAGIRAVLGRGLMDR---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 166 GQPASEGQRRfingsEAYLELLQRLRAPLEAAGHSL---GLCFHSLRAVTPQQIATVLA-AGHDDLPVHIHIAEQQKEVD 241
Cdd:COG0402 156 GFPDGLREDA-----DEGLADSERLIERWHGAADGRirvALAPHAPYTVSPELLRAAAAlARELGLPLHTHLAETRDEVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 242 DCLAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSD- 320
Cdd:COG0402 231 WVLELYGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDg 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 321 --SHVSLSVVEELRWLEYGQRLRDRKRNR-----------------LYRDDQpmigrtlydaalaggaqalgqpIGSLAV 381
Cdd:COG0402 311 aaSNNSLDMFEEMRLAALLQRLRGGDPTAlsarealematlggaraLGLDDE----------------------IGSLEP 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 558688754 382 GRRADLLVLDGNDPYLASAegDALLNRWLFAGGDRQVRDVMVAGRWVVRD 431
Cdd:COG0402 369 GKRADLVVLDLDAPHLAPL--HDPLSALVYAADGRDVRTVWVAGRVVVRD 416
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
22-434 |
1.13e-42 |
|
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: 155.44 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 22 EISADGVLAGIRPDANADGAERLggaVLPGMPNLHSHAFQRAMAGLAEvagnpNDSFWTW-RELMYRMVARLSPEQIEVI 100
Cdd:cd01298 31 AVGPALPLPAYPADEVIDAKGKV---VMPGLVNTHTHLAMTLLRGLAD-----DLPLMEWlKDLIWPLERLLTEEDVYLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 101 ARQLYIEMLKAGYTAVAEFHYVHHDldgrsyadpaelslRISRAASAAGIgltllpvlYSHAGFGG--QPASEGQRRfin 178
Cdd:cd01298 103 ALLALAEMIRSGTTTFADMYFFYPD--------------AVAEAAEELGI--------RAVLGRGImdLGTEDVEET--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 179 gsEAYLELLQRLRAPLEAAGHSL---GLCFHSLRAVTPQQIATVLA-AGHDDLPVHIHIAEQQKEVDDCLAWSGRRPLQW 254
Cdd:cd01298 158 --EEALAEAERLIREWHGAADGRirvALAPHAPYTCSDELLREVAElAREYGVPLHIHLAETEDEVEESLEKYGKRPVEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 255 LYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVS---LSVVEEL 331
Cdd:cd01298 236 LEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGAASnnnLDMFEEM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 332 RWLEYGQRLRdrkrnrlYRDDQPMIGRTLYDAALAGGAQALGQP-IGSLAVGRRADLLVLDGNDPYLASAEGDALLnrWL 410
Cdd:cd01298 316 RLAALLQKLA-------HGDPTALPAEEALEMATIGGAKALGLDeIGSLEVGKKADLILIDLDGPHLLPVHDPISH--LV 386
|
410 420
....*....|....*....|....
gi 558688754 411 FAGGDRQVRDVMVAGRWVVRDGRH 434
Cdd:cd01298 387 YSANGGDVDTVIVNGRVVMEDGEL 410
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
28-436 |
1.42e-22 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 99.54 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 28 VLAGirPDANADGAERLGGA---VLPGMPNLHSHAFQRAMAGLAEVAgnpNDSFWTWRELMYRMVARLSPEQIEVIARQL 104
Cdd:PRK08203 36 VGPG--GALPQPADEVFDARghvVTPGLVNTHHHFYQTLTRALPAAQ---DAELFPWLTTLYPVWARLTPEMVRVATQTA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 105 YIEMLKAGYTAVAEFHYVhhdldgrsYADPAELSLRISRAAsAAGIGLTLLPVLYSH---AGFGGQPAsegqRRFINGSE 181
Cdd:PRK08203 111 LAELLLSGCTTSSDHHYL--------FPNGLRDALDDQIEA-AREIGMRFHATRGSMslgESDGGLPP----DSVVEDED 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 182 AYLELLQRL-RAPLEAAGHS-----LGLCfhSLRAVTPQ--QIATVLAAGHDdLPVHIHIAEQQKEVDDCLAWSGRRPLQ 253
Cdd:PRK08203 178 AILADSQRLiDRYHDPGPGAmlriaLAPC--SPFSVSRElmRESAALARRLG-VRLHTHLAETLDEEAFCLERFGMRPVD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 254 WLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSD---SHVSLSVVEE 330
Cdd:PRK08203 255 YLEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgsaSNDGSNLIGE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 331 LRWLEYGQRLRDRKRNR----------------LYRDDqpmigrtlydaalaggaqalgqpIGSLAVGRRADLLVLDGND 394
Cdd:PRK08203 335 ARQALLLQRLRYGPDAMtarealewatlggarvLGRDD-----------------------IGSLAPGKLADLALFDLDE 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 558688754 395 PYLASAeGDALLNrwLFAGGDRQVRDVMVAGRWVVRDGRHAG 436
Cdd:PRK08203 392 LRFAGA-HDPVAA--LVLCGPPRADRVMVGGRWVVRDGQLTT 430
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
45-433 |
7.11e-22 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 97.38 E-value: 7.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 45 GGAVLPGMPNLHSHAfqrAMAGLAEVAGNPNDSFWTwRELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFhYVHH 124
Cdd:PRK06687 53 GAWIMPGLVNCHTHS---AMTGLRGIRDDSNLHEWL-NDYIWPAESEFTPDMTTNAVKEALTEMLQSGTTTFNDM-YNPN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 125 DLDGRsyadpaelslRISRAASAAGIGLTLLPVLYShagfggqpaSEgqrrfingSEAYLELLQRLRAPLE--------- 195
Cdd:PRK06687 128 GVDIQ----------QIYQVVKTSKMRCYFSPTLFS---------SE--------TETTAETISRTRSIIDeilkyknpn 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 196 ----AAGHSLGLCFHSLRAvtpqqiATVLAAGHDDLPVHIHIAEQQKEVDDCLAWSGRRPLQWLYENVAVDQRWCLVHAT 271
Cdd:PRK06687 181 fkvmVAPHSPYSCSRDLLE------ASLEMAKELNIPLHVHVAETKEESGIILKRYGKRPLAFLEELGYLDHPSVFAHGV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 272 HADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVS---LSVVEELRWLEYGQRLRDRKRNRl 348
Cdd:PRK06687 255 ELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVASnnnLDMFEEGRTAALLQKMKSGDASQ- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 349 YRDDQPMIGRTLydaaLAGGAQALGQPIGSLAVGRRADLLVLDGNDP-YLASAEGdaLLNRWLFAGGDRQVRDVMVAGRW 427
Cdd:PRK06687 334 FPIETALKVLTI----EGAKALGMENQIGSLEVGKQADFLVIQPQGKiHLQPQEN--MLSHLVYAVKSSDVDDVYIAGEQ 407
|
....*.
gi 558688754 428 VVRDGR 433
Cdd:PRK06687 408 VVKQGQ 413
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
48-428 |
1.14e-20 |
|
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: 92.56 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 48 VLPGMPNLHSHAFQRAMAGlaevagnpndsfwtwrelmyrmvARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDLD 127
Cdd:pfam01979 2 VLPGLIDAHVHLEMGLLRG-----------------------IPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 128 grsyadpaelsLRISRAASAAGIGLTLLpvlyshaGFGGQPASEGQRRfiNGSEAYLELLQRLRAPLEAAGHSL--GLCF 205
Cdd:pfam01979 59 -----------EALLEAAEELPLGLRFL-------GPGCSLDTDGELE--GRKALREKLKAGAEFIKGMADGVVfvGLAP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 206 HSLRAVTPQQIATVLAAGHD-DLPVHIHIAEQQKEVDDCLAWSGRR-----PLQWLYENVAVDQ-RWCLVHATHADPAEV 278
Cdd:pfam01979 119 HGAPTFSDDELKAALEEAKKyGLPVAIHALETKGEVEDAIAAFGGGiehgtHLEVAESGGLLDIiKLILAHGVHLSPTEA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 279 AAMARSGAVAGLCL--STEANLGDGIFPATDFLAQGGRLGIGSDSHVS---LSVVEELRWLeYGQRLRDRKRNRLYRDDQ 353
Cdd:pfam01979 199 NLLAEHLKGAGVAHcpFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSgnsLNMLEELRLA-LELQFDPEGGLSPLEALR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 354 PM-------IGRTLYdaalaggaqalgqpIGSLAVGRRADLLVLDGNdpylasaegdaLLNRWLFAGGDRQVRDVMVAGR 426
Cdd:pfam01979 278 MAtinpakaLGLDDK--------------VGSIEVGKDADLVVVDLD-----------PLAAFFGLKPDGNVKKVIVKGK 332
|
..
gi 558688754 427 WV 428
Cdd:pfam01979 333 IV 334
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
26-453 |
6.56e-18 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 85.50 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 26 DGVLAGIRPDANADGAERL---GGAVLPGMPNLHSHAFQRAMAGlaeVAGNPNDSFWTW-RELMYRMVARLSPEQIEVIA 101
Cdd:PRK12393 32 DGRIAAIGALTPLPGERVIdatDCVVYPGWVNTHHHLFQSLLKG---VPAGINQSLTAWlAAVPYRFRARFDEDLFRLAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 102 RQLYIEMLKAGYTAVAEFHYVHHDlDGRsyADPAELslrISRAASAAGIGLTL-----LPVLYSHAGF--GGQPASegqr 174
Cdd:PRK12393 109 RIGLVELLRSGCTTVADHHYLYHP-GMP--FDTGDI---LFDEAEALGMRFVLcrggaTQTRGDHPGLptALRPET---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 175 rfingSEAYLELLQRLRAPLEAAGHSlglcfhSLRAV-----------TPQQIATVLAAGHD-DLPVHIHIAEQQKEVDD 242
Cdd:PRK12393 179 -----LDQMLADVERLVSRYHDASPD------SLRRVvvapttptfslPPELLREVARAARGmGLRLHSHLSETVDYVDF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 243 CLAWSGRRPLQ------WLYENVavdqrWcLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLG 316
Cdd:PRK12393 248 CREKYGMTPVQfvaehdWLGPDV-----W-FAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 317 IGSD---SHVSLSVVEELR--WLeygqrlrdrkrnrLYR----DDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADL 387
Cdd:PRK12393 322 LGVDgaaSNESADMLSEAHaaWL-------------LHRaeggADATTVEDVVHWGTAGGARVLGLDAIGTLAVGQAADL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 558688754 388 LVLDGNDPYLA----SAEGDALlnrwlfAGGDRQVRDVMVAGRWVVRDGRHAG--EERSARAFVQVLGELLD 453
Cdd:PRK12393 389 AIYDLDDPRFFglhdPAIAPVA------CGGPAPVKALLVNGRPVVENGAIPGldLAELRHDARAAVRRLLQ 454
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
45-439 |
9.86e-16 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 78.95 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 45 GGAVLPGMPNLHSHAFQRAMAGLAEvagnpNDSFWTWREL-MYRMVARLSPEqIEVIARQL-YIEMLKAGYTAVAE-FHY 121
Cdd:PRK15493 54 GKWVLPGLVNTHTHVVMSLLRGIGD-----DMLLQPWLETrIWPLESQFTPE-LAVASTELgLLEMVKSGTTSFSDmFNP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 122 VHHDLDGrsyadpaeLSLRISRAASAAGIGLTLLpvlyshaGFGGQpasEGQRRFINGSEAYLELLQRLRAPLEA--AGH 199
Cdd:PRK15493 128 IGVDQDA--------IMETVSRSGMRAAVSRTLF-------SFGTK---EDEKKAIEEAEKYVKRYYNESGMLTTmvAPH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 200 SLGLCFHSLRavtpQQIATVlaAGHDDLPVHIHIAEQQKEVDDCLAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVA 279
Cdd:PRK15493 190 SPYTCSTELL----EECARI--AVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDNERA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 280 AMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVS---LSVVEELRWLEYGQRlrdrkrnRLYRDDQPM- 355
Cdd:PRK15493 264 FLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASnnnLDMFEEMRIATLLQK-------GIHQDATALp 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 356 IGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLD-GNDPYLASAegDALLNRWLFAGGDRQVRDVMVAGRWVVRDG-- 432
Cdd:PRK15493 337 VETALTLATKGAAEVIGMKQTGSLEVGKCADFITIDpSNKPHLQPA--DEVLSHLVYAASGKDISDVIINGKRVVWNGec 414
|
....*..
gi 558688754 433 RHAGEER 439
Cdd:PRK15493 415 KTLDEER 421
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
26-433 |
2.23e-14 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 74.56 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 26 DGVLAGIRPDANAD----GAERL---GGAVLPGMPNLHSHAFQRAMAGLAEvagnpnD-SFWTW-RELMYRMVARLSPEQ 96
Cdd:PRK09045 35 DGRIVAILPRAEARaryaAAETVelpDHVLIPGLINAHTHAAMSLLRGLAD------DlPLMTWlQDHIWPAEGAWVSEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 97 IEVIARQLYI-EMLKAGYTAVAEfHYVHHDLdgrsyadpaelslrISRAASAAG----IGLTLL--PVLYSHagfggqpa 169
Cdd:PRK09045 109 FVRDGTLLAIaEMLRGGTTCFND-MYFFPEA--------------AAEAAHQAGmraqIGMPVLdfPTAWAS-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 170 segqrrfinGSEAYL----ELLQRLRapleaaGHSL-GLCF--HSLRAV---TPQQIATVlaAGHDDLPVHIHIAEQQKE 239
Cdd:PRK09045 166 ---------DADEYLakglELHDQWR------HHPLiSTAFapHAPYTVsdeNLERIRTL--AEQLDLPIHIHLHETAQE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 240 VDDCLAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGS 319
Cdd:PRK09045 229 IADSLKQHGQRPLARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 320 DSHVS---LSVVEELRW--------------LEYGQRLRDRKRN---RLYRDDQpmigrtlydaalaggaqalgqpIGSL 379
Cdd:PRK09045 309 DGAASnndLDLFGEMRTaallakavagdataLPAHTALRMATLNgarALGLDDE----------------------IGSL 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 558688754 380 AVGRRADLLVLDGNDPYLASAEGdaLLNRWLFAGGDRQVRDVMVAGRWVVRDGR 433
Cdd:PRK09045 367 EPGKQADLVAVDLSGLETQPVYD--PVSQLVYAAGREQVSHVWVAGKQLLDDRE 418
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
45-433 |
5.87e-14 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 73.43 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 45 GGAVLPGMPNLHSH---AFQRamaGLAEVAGNPNDSFWTWRELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVaefhY 121
Cdd:PRK07203 54 GKLIMPGLINSHNHiysGLAR---GMMANIPPPPDFISILKNLWWRLDRALTLEDVYYSALICSLEAIKNGVTTV----F 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 122 VHHdldgrsyADPAEL--SL-RISRAASAAGI-GLTLLPVLYSHagfGGQPASEG---QRRFINGSEA----YLELLQRL 190
Cdd:PRK07203 127 DHH-------ASPNYIggSLfTIADAAKKVGLrAMLCYETSDRD---GEKELQEGveeNIRFIKHIDEakddMVEAMFGL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 191 RAPLEAAGHSLGLCFHSLRAVtpqqiatvlaaghdDLPVHIHIAEQQKEVDDCLAWSGRRPLQWLYENVAVDQRWCLVHA 270
Cdd:PRK07203 197 HASFTLSDATLEKCREAVKET--------------GRGYHIHVAEGIYDVSDSHKKYGKDIVERLADFGLLGEKTLAAHC 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 271 THADPAEVAAMARSGAVagLCLSTEANLGD--GIFPATDFLAQGGRLGIGSDSHVSlSVVEELR---------------- 332
Cdd:PRK07203 263 IYLSDEEIDLLKETDTF--VVHNPESNMGNavGYNPVLEMIKNGILLGLGTDGYTS-DMFESYKvanfkhkhaggdpnvg 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 333 WLEYGQRLRDRKRNrlyrddqpMIGRTLydaalaggaqalGQPIGSLAVGRRADLLVLDGNDPylASAEGDALLNRWLFA 412
Cdd:PRK07203 340 WPESPAMLFENNNK--------IAERYF------------GAKFGILEEGAKADLIIVDYNPP--TPLNEDNINGHILFG 397
|
410 420
....*....|....*....|.
gi 558688754 413 GGDRQVRDVMVAGRWVVRDGR 433
Cdd:PRK07203 398 MNGGSVDTTIVNGKVVMEDRK 418
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
26-436 |
1.25e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 69.26 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 26 DGVLAGIRPDANADGAERL---GGAVLPGMPNLHSHAFQRAMAGLAevagnPNDSFWTW-RELMYRMVARLSPEQIEVIA 101
Cdd:PRK08204 30 GDRIAAVAPSIEAPDAEVVdarGMIVMPGLVDTHRHTWQSVLRGIG-----ADWTLQTYfREIHGNLGPMFRPEDVYIAN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 102 RQLYIEMLKAGYTAVAEFHyvhHDLDGRSYADPAELSLRIS--RAASAAGIGLTLLPVLYSHAGFGGQPASEGQRRFING 179
Cdd:PRK08204 105 LLGALEALDAGVTTLLDWS---HINNSPEHADAAIRGLAEAgiRAVFAHGSPGPSPYWPFDSVPHPREDIRRVKKRYFSS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 180 SEAYLELLQRLRAP----LEAAGHSLGLcfhslravtpqqiatvlaAGHDDLPVHIHIAEQqkevddclAWSGR-RPLQW 254
Cdd:PRK08204 182 DDGLLTLGLAIRGPefssWEVARADFRL------------------ARELGLPISMHQGFG--------PWGATpRGVEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 255 LYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGiFPATD-FLAQGGRLGIGSDSHVSLS--VVEEL 331
Cdd:PRK08204 236 LHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHG-YPVTGrLLAHGVRPSLGVDVVTSTGgdMFTQM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 332 RWLEYGQRLRDrkrNRLYRDDQPMIGRTL---------YDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASAeG 402
Cdd:PRK08204 315 RFALQAERARD---NAVHLREGGMPPPRLtltarqvleWATIEGARALGLEDRIGSLTPGKQADLVLIDATDLNLAPV-H 390
|
410 420 430
....*....|....*....|....*....|....
gi 558688754 403 DAlLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAG 436
Cdd:PRK08204 391 DP-VGAVVQSAHPGNVDSVMVAGRAVKRNGKLLG 423
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
18-436 |
4.91e-12 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 67.22 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 18 NVRFEISADGVLAGIRPDAN--ADGAerlGGAVLPGMPNLHSHAFQRAMAGLAEvagnpNDSFWTWRELMYRMVARLSPE 95
Cdd:PRK06380 23 NVYIEGNKIVYVGDVNEEADyiIDAT---GKVVMPGLINTHAHVGMTASKGLFD-----DVDLEEFLMKTFKYDSKRTRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 96 QIEVIARQLYIEMLKAGYTAVAEFHYvHHDLdgrsyadpaelslrISRAASAAGIgltllpvlyshagfggqpasegqRR 175
Cdd:PRK06380 95 GIYNSAKLGMYEMINSGITAFVDLYY-SEDI--------------IAKAAEELGI-----------------------RA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 176 FINGSEAYLELLQRLRAPLEAAGHSLGlCFHSLRAVTPQ--------------QIATVLAAGHDDLpVHIHIAEQQKEVD 241
Cdd:PRK06380 137 FLSWAVLDEEITTQKGDPLNNAENFIR-EHRNEELVTPSigvqgiyvandetyLKAKEIAEKYDTI-MHMHLSETRKEVY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 242 DCLAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDG-IFPATDFLAQGGRLGIGSD 320
Cdd:PRK06380 215 DHVKRTGERPVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGgSPPIPEMLDNGINVTIGTD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 321 SHVSLSVVEELRWLEYGQRLRDRKRnrlyRDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASA 400
Cdd:PRK06380 295 SNGSNNSLDMFEAMKFSALSVKNER----WDASIIKAQEILDFATINAAKALELNAGSIEVGKLADLVILDARAPNMIPT 370
|
410 420 430
....*....|....*....|....*....|....*.
gi 558688754 401 EGDALLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAG 436
Cdd:PRK06380 371 RKNNIVSNIVYSLNPLNVDHVIVNGKILKENGRLNG 406
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
220-425 |
4.44e-11 |
|
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: 64.61 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 220 LAAGHDDLPVHIHIAEQQKEVddclAW-----SGRRPLQWLYENVA-VDQRWCLVHATHADPAEVAAMARSGAVAGLCLS 293
Cdd:cd01303 216 LAKEHPDLHIQTHISENLDEI----AWvkelfPGARDYLDVYDKYGlLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPT 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 294 TEANLGDGIFPATDFLAQGGRLGIGSDSH--VSLSVVEELRW-LEYGQRLRDRKRNR-------------------LYRD 351
Cdd:cd01303 292 SNLFLGSGLFDVRKLLDAGIKVGLGTDVGggTSFSMLDTLRQaYKVSRLLGYELGGHaklspaeafylatlggaeaLGLD 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 352 DQpmigrtlydaalaggaqalgqpIGSLAVGRRADLLVLDGNDPYLA------SAEGDALLNRWLFAGGDRQVRDVMVAG 425
Cdd:cd01303 372 DK----------------------IGNFEVGKEFDAVVIDPSATPLLadrmfrVESLEEALFKFLYLGDDRNIREVYVAG 429
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
45-451 |
5.38e-11 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 64.05 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 45 GGAVLPGMPNLHSHAFQRAMAGLAEvagnpNDSFWTW-RELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFhYVH 123
Cdd:PRK08393 49 GSVVSPGFINAHTHSPMVLLRGLAD-----DVPLMEWlQNYIWPRERKLKRKDIYWGAYLGLLEMIKSGTTTFVDM-YFH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 124 HDldgrsyadpaelslRISRAASAAGigltllpvLYSHAGFG----GQPasEGQRRFINGSEAYLELLQRLRAPLEA--- 196
Cdd:PRK08393 123 ME--------------EVAKATLEVG--------LRGYLSYGmvdlGDE--EKREKEIKETEKLMEFIEKLNSPRVHfvf 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 197 AGHSLGLC-FHSLRAVTPqqiatvLAAGHDDLpVHIHIAEQQKEVDDCLAWSGRRPLQWLYENVAVDQRWCLVHATHADP 275
Cdd:PRK08393 179 GPHAPYTCsLALLKWVRE------KAREWNKL-ITIHLSETMDEIKQIREKYGKSPVVLLDEIGFLNEDVIAAHGVWLSS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 276 AEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSD---SHVSLSVVEELRWLEYGQRLRDRkrnrlyrdd 352
Cdd:PRK08393 252 RDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDgaaSNNNLDMLREMKLAALLHKVHNL--------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 353 QPMI--GRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASAegDALLNRWLFAGGDRQVRDVMVAGRWVVR 430
Cdd:PRK08393 323 DPTIadAETVFRMATQNGAKALGLKAGVIKEGYLADIAVIDFNRPHLRPI--NNPISHLVYSANGNDVETTIVDGKIVML 400
|
410 420
....*....|....*....|...
gi 558688754 431 DGR--HAGEERSARAFVQVLGEL 451
Cdd:PRK08393 401 DGEvlTLDEEKILDKFLKVIEKL 423
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
26-434 |
6.73e-11 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 63.87 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 26 DGVLAGIRPDANADGAERL----GGAVLPGMPNLHSHAFQRAMAGLAEvagnpNDSFWTW-RELMYRMVARLSPEQIEVI 100
Cdd:PRK07228 28 DDRIAAVGDRLDLEDYDDHidatGKVVIPGLIQGHIHLCQTLFRGIAD-----DLELLDWlKDRIWPLEAAHDAESMYYS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 101 ARQLYIEMLKAGYTAVAEFHYVHHdldgrsyADPAelslriSRAASAAGIGLTLLPVLYSHAGFGGQPASEGQRRFINGS 180
Cdd:PRK07228 103 ALLGIGELIESGTTTIVDMESVHH-------TDSA------FEAAGESGIRAVLGKVMMDYGDDVPEGLQEDTEASLAES 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 181 EAYLEllqrlraplEAAGHSLGlcfhSLR-AVTPQQIATV----------LAAGHDdLPVHIHIAEQQKEVDDCLAWSGR 249
Cdd:PRK07228 170 VRLLE---------KWHGADNG----RIRyAFTPRFAVSCteellrgvrdLADEYG-VRIHTHASENRGEIETVEEETGM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 250 RPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDS---HVSLS 326
Cdd:PRK07228 236 RNIHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGapcNNTLD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 327 VVEELRWLEYGQrlrdrKRNRLyrDDQPMIGRTLYDAALAGGAQAL--GQPIGSLAVGRRADLLVLDGNDPYLASAEGDA 404
Cdd:PRK07228 316 PFTEMRQAALIQ-----KVDRL--GPTAMPARTVFEMATLGGAKAAgfEDEIGSLEEGKKADLAILDLDGLHATPSHGVD 388
|
410 420 430
....*....|....*....|....*....|
gi 558688754 405 LLNRWLFAGGDRQVRDVMVAGRWVVRDGRH 434
Cdd:PRK07228 389 VLSHLVYAAHGSDVETTMVDGKIVMEDGEL 418
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
45-426 |
1.59e-10 |
|
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: 62.47 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 45 GGAVLPGMPNLHSHafqramaglAEVAGNPN----DSFWTWRELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFh 120
Cdd:cd01312 26 NGVLLPGLINAHTH---------LEFSANVAqftyGRFRAWLLSVINSRDELLKQPWEEAIRQGIRQMLESGTTSIGAI- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 121 yVHHDLDGRSYADPaelSLRIsraasaagigltllpVLYSHAgFGGQPASEGQRrfingSEAYLELLQRlRAPLEAAGHS 200
Cdd:cd01312 96 -SSDGSLLPALASS---GLRG---------------VFFNEV-IGSNPSAIDFK-----GETFLERFKR-SKSFESQLFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 201 LGLCFHSLRAVTPQQIATVL-AAGHDDLPVHIHIAEQQKEVD---DCLAWSGRR---------------PLQWLYENVAV 261
Cdd:cd01312 150 PAISPHAPYSVHPELAQDLIdLAKKLNLPLSTHFLESKEEREwleESKGWFKHFwesflklpkpkklatAIDFLDMLGGL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 262 DQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSD---SHVSLSVVEELRWL--EY 336
Cdd:cd01312 230 GTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDglsSNISLSLLDELRALldLH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 337 GQRLRDRKRNRLYRddqpmiGRTLYDAALAGGAqalgqpIGSLAVGRRADLLVLDGNDPylaSAEGDALLNRWLFAGgdr 416
Cdd:cd01312 310 PEEDLLELASELLL------MATLGGARALGLN------NGEIEAGKRADFAVFELPGP---GIKEQAPLQFILHAK--- 371
|
410
....*....|
gi 558688754 417 QVRDVMVAGR 426
Cdd:cd01312 372 EVRHLFISGK 381
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
212-432 |
1.16e-09 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 60.20 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 212 TPQQIATV--LAAGHDDLPVHIHIAEQQKEVddclAWSGRrplqwLYEN----VAVDQRWCLV-------HATHADPAEV 278
Cdd:PRK09228 209 TPEQLEAAgaLAREHPDVWIQTHLSENLDEI----AWVKE-----LFPEardyLDVYERYGLLgpravfaHCIHLEDRER 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 279 AAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDshV----SLSVVEELRWLEYGQRLRDRKRN-------- 346
Cdd:PRK09228 280 RRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTD--VgggtSFSMLQTMNEAYKVQQLQGYRLSpfqafyla 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 347 ------RLYRDDQpmigrtlydaalaggaqalgqpIGSLAVGRRADLLVLDGN-DPYLA-SAEGDALLNRWLFA----GG 414
Cdd:PRK09228 358 tlggarALGLDDR----------------------IGNLAPGKEADFVVLDPAaTPLLAlRTARAESLEELLFAlmtlGD 415
|
250
....*....|....*...
gi 558688754 415 DRQVRDVMVAGRWVVRDG 432
Cdd:PRK09228 416 DRAVAETYVAGRPVYRRL 433
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
54-340 |
1.32e-08 |
|
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: 55.80 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 54 NLHSHAFQRAMAGlaevagnpndsfwTWRELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDldgrsYAD 133
Cdd:cd01292 3 DTHVHLDGSALRG-------------TRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP-----TTT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 134 PAELSLRISRAASAAGIGLTLLPVLYSHAGFGGQPASEGQRRFINGSEAYLellqrlrapleAAGHSLGLCFHSLRAVTP 213
Cdd:cd01292 65 KAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELG-----------AVGLKLAGPYTATGLSDE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 214 QQIATVLAAGHDDLPVHIHIAEQQKEVddclawsgrRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLS 293
Cdd:cd01292 134 SLRRVLEEARKLGLPVVIHAGELPDPT---------RALEDLVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPL 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 558688754 294 TEANLGDGIFPATDF---LAQGGRLGIGSDSHVSLSVV---EELRWLEYGQRL 340
Cdd:cd01292 205 SNYLLGRDGEGAEALrrlLELGIRVTLGTDGPPHPLGTdllALLRLLLKVLRL 257
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
216-446 |
8.01e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 54.28 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 216 IATVLAAGHDDLPVHIHIAEQQKEVDDCLAWSGRRPLQWLYENVAVDQRWCLVHATHAD---------PAEVAAMARSGA 286
Cdd:PRK06151 224 RRTAAAARELGCPVRLHCAQGVLEVETVRRLHGTTPLEWLADVGLLGPRLLIPHATYISgsprlnysgGDDLALLAEHGV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 287 VAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVSlSVVEELRWLEYGQRLRDRKRNRLYRDDqpmigrtLYDAALA 366
Cdd:PRK06151 304 SIVHCPLVSARHGSALNSFDRYREAGINLALGTDTFPP-DMVMNMRVGLILGRVVEGDLDAASAAD-------LFDAATL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 367 GGAQALGQP-IGSLAVGRRADLLVLDGNDPYLASAEgDALlnRWLFAGGD-RQVRDVMVAGRWVVRDGRHAG-EERSARA 443
Cdd:PRK06151 376 GGARALGRDdLGRLAPGAKADIVVFDLDGLHMGPVF-DPI--RTLVTGGSgRDVRAVFVDGRVVMEDGRLPGvDLAALRA 452
|
...
gi 558688754 444 FVQ 446
Cdd:PRK06151 453 QAQ 455
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
45-433 |
6.35e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 51.29 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 45 GGAVLPGMPNLHSHA---FQRAMAGLAEVAGNPNDSFWTWRelmyrmvARLSPEQIEVIARQLYIEMLKAGYTAVAEFhY 121
Cdd:PRK06038 50 GSVVMPGLVNTHTHAamtLFRGYADDLPLAEWLNDHIWPAE-------AKLTAEDVYAGSLLACLEMIKSGTTSFADM-Y 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 122 VHHDldgrsyadpaelslRISRAASAAGIGLTLlpvlySHAGF-------GGQPASEGqRRFINGSEAYLEllQRLRAPL 194
Cdd:PRK06038 122 FYMD--------------EVAKAVEESGLRAAL-----SYGMIdlgddekGEAELKEG-KRFVKEWHGAAD--GRIKVMY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 195 eaAGHSLGLCFHSLRAVTPQQiatvlaAGHDDLPVHIHIAEQQKEVDDCLAWSGRRPLQWLYENVAVDQRWCLVHATHAD 274
Cdd:PRK06038 180 --GPHAPYTCSEEFLSKVKKL------ANKDGVGIHIHVLETEAELNQMKEQYGMCSVNYLDDIGFLGPDVLAAHCVWLS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 275 PAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSD---SHVSLSVVEELRWLEYGQrlrdrKRNRLyrD 351
Cdd:PRK06038 252 DGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDgcaSNNNLDMFEEMKTAALLH-----KVNTM--D 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 352 DQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASAEGdaLLNRWLFAGGDRQVRDVMVAGRWVVRD 431
Cdd:PRK06038 325 PTALPARQVLEMATVNGAKALGINTGMLKEGYLADIIIVDMNKPHLTPVRD--VPSHLVYSASGSDVDTTIVDGRILMED 402
|
..
gi 558688754 432 GR 433
Cdd:PRK06038 403 YK 404
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
26-431 |
1.22e-06 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 50.34 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 26 DGVLAGIRPDANA---DGAERL---GGAVLPGMPNLHSHAFqraMAGLAEVAGNPNDSFWTWRELMYRMVARLSpeqiev 99
Cdd:COG1228 35 DGKIAAVGPAADLavpAGAEVIdatGKTVLPGLIDAHTHLG---LGGGRAVEFEAGGGITPTVDLVNPADKRLR------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 100 iarqlyiEMLKAGYTAVaefhyvhHDLDGrsyaDPAELSLRISRAASAAGIGLTLLPVLYSHAGFGGQPAsegqrrfinG 179
Cdd:COG1228 106 -------RALAAGVTTV-------RDLPG----GPLGLRDAIIAGESKLLPGPRVLAAGPALSLTGGAHA---------R 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 180 SEAylELLQRLRAPLEAAGHSL-GLCFHSLRAVTPQQIATVLAAGHD-DLPVHIHiAEQQKEVDDCLAwSGrrplqwlye 257
Cdd:COG1228 159 GPE--EARAALRELLAEGADYIkVFAEGGAPDFSLEELRAILEAAHAlGLPVAAH-AHQADDIRLAVE-AG--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 258 nvaVDqrwCLVHATHADPAEVAAMARSGAVA---GLCLSTEANLGDGIF--------------PATDFLAQGGRLGIGSD 320
Cdd:COG1228 226 ---VD---SIEHGTYLDDEVADLLAEAGTVVlvpTLSLFLALLEGAAAPvaakarkvreaalaNARRLHDAGVPVALGTD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 321 SHVS----LSVVEELRWL-EYG---------------QRLRdrkrnrlyRDDQpmigrtlydaalaggaqalgqpIGSLA 380
Cdd:COG1228 300 AGVGvppgRSLHRELALAvEAGltpeealraatinaaKALG--------LDDD----------------------VGSLE 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 558688754 381 VGRRADLLVLDGNDP-YLASAegdallnrwlfaggdRQVRDVMVAGRWVVRD 431
Cdd:COG1228 350 PGKLADLVLLDGDPLeDIAYL---------------EDVRAVMKDGRVVDRS 386
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
83-428 |
9.84e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 47.87 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 83 ELMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVAEFHYVHHDLDG-RSYADPAELSLRISRAASAAGIGLTLLPVLYSH 161
Cdd:COG1574 195 DLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLGPDDLAAyRELAAAGELPLRVVLYLGADDEDLEELLALGLR 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 162 AGFGGQPASEGQRR-FINGSeaylelLQ----RLRAPLEAAGHSLGLCFHslravTPQQIATVLAAGHD-DLPVHIH--- 232
Cdd:COG1574 275 TGYGDDRLRVGGVKlFADGS------LGsrtaALLEPYADDPGNRGLLLL-----DPEELRELVRAADAaGLQVAVHaig 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 233 ----------IAEQQKEVddclawsGRRplqwlyenvavDQRWCLVHATHADPAEVAAMARSGAVA--------GLCLST 294
Cdd:COG1574 344 daavdevldaYEAARAAN-------GRR-----------DRRHRIEHAQLVDPDDLARFAELGVIAsmqpthatSDGDWA 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 295 EANLGD----GIFPATDFLAQGGRLGIGSDSHVSLsvVEELRWLEYGQRLRDRKrNRLYRDDQPM----------IG--R 358
Cdd:COG1574 406 EDRLGPeraaRAYPFRSLLDAGAPLAFGSDAPVEP--LDPLLGIYAAVTRRTPS-GRGLGPEERLtveealraytIGaaY 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 359 TLYDAALaggaqalgqpIGSLAVGRRADLLVLDGnDPYLASAEgdALLnrwlfaggDRQVRDVMVAGRWV 428
Cdd:COG1574 483 AAFEEDE----------KGSLEPGKLADFVVLDR-DPLTVPPE--EIK--------DIKVLLTVVGGRVV 531
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
84-324 |
1.87e-04 |
|
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: 43.84 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 84 LMYRMVARLSPEQIEVIARQLYIEMLKAGYTAVaefhyvhHDLDGRSYADPAELslrisRAASAAG---IGLTLLPVLYS 160
Cdd:cd01300 168 LVLEAVPPPTPEERRAALRAAARELASLGVTTV-------HDAGGGAADDIEAY-----RRLAAAGeltLRVRVALYVSP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 161 HA-----GFGGQPASEGQRR--------FINGSeaylelLQ----RLRAPLEAAGHSLGLCFHSlravtPQQIA-TVLAA 222
Cdd:cd01300 236 LAedlleELGARKNGAGDDRlrlggvklFADGS------LGsrtaALSEPYLDSPGTGGLLLIS-----PEELEeLVRAA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 223 GHDDLPVHIHI----AeqqkeVDDCLAWsgrrplqwlYENVA-----VDQRWCLVHATHADPAEVAAMARsgavAGLCLS 293
Cdd:cd01300 305 DEAGLQVAIHAigdrA-----VDTVLDA---------LEAALkdnprADHRHRIEHAQLVSPDDIPRFAK----LGVIAS 366
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 558688754 294 TEAN-------------LG----DGIFPATDFLAQGGRLGIGSDSHVS 324
Cdd:cd01300 367 VQPNhlysdgdaaedrrLGeeraKRSYPFRSLLDAGVPVALGSDAPVA 414
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
209-321 |
1.14e-03 |
|
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: 41.09 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558688754 209 RAVTPQQIATVLAAGHD-DLPVHIHIaeqqkevdDCLAWSGRRPLQWLYENVAVDqrwclvHATHADPAEVAAMARSGAV 287
Cdd:cd01296 188 GAFSLEQSRRILEAAKEaGLPVKIHA--------DELSNIGGAELAAELGALSAD------HLEHTSDEGIAALAEAGTV 253
|
90 100 110
....*....|....*....|....*....|....
gi 558688754 288 AGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDS 321
Cdd:cd01296 254 AVLLPGTAFSLRETYPPARKLIDAGVPVALGTDF 287
|
|
| |
