|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
3-465 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 821.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 3 RTVIHGGLVVTASDEIHADVLIEGGRIAALAAHgtdaatswSADRRIDATGMYVLPGGVDAHTHMEMPFGGTYAADTFET 82
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN--------LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 83 GTRAAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSDVNESSLKEMDRLVAEGVTSFKLFMAYPG 162
Cdd:PRK08323 74 GTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEEGITSFKLFMAYKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 163 VFYSDDGRILRAMQRASGNGGLVMMHAENGIAIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAGAPLYV 242
Cdd:PRK08323 154 ALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 243 VHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEP-GFEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVSTDH 321
Cdd:PRK08323 234 VHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPdWFEGAKYVMSPPLRDKEHQDALWRGLQDGDLQVVATDH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 322 CPFCFSGQKEMGRGDFSKIPNGMPGVEHRMDLLH-QAVVDGHLSRRRWVEIACASPARMFGLYPKKGTIAPGADADVVIY 400
Cdd:PRK08323 314 CPFCFEQKKQLGRGDFTKIPNGTPGVEDRMPLLFsEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIW 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664099816 401 DPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVGHAGHGTYLPRGTCQYL 465
Cdd:PRK08323 394 DPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQAV 458
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
4-454 |
0e+00 |
|
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: 643.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVVTASDEIHADVLIEGGRIAALAAHGTDAATSwsadRRIDATGMYVLPGGVDAHTHMEMPFGGTYAADTFETG 83
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGV----EVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 84 TRAAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSDVNESSLKEMDRLVAEGVTSFKLFMAYPGV 163
Cdd:cd01314 77 TRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVKKGISSFKVFMAYKGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 164 FYSDDGRILRAMQRASGNGGLVMMHAENGIAIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAGAPLYVV 243
Cdd:cd01314 157 LMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 244 HVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEPGFEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVSTDHCP 323
Cdd:cd01314 237 HVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWKDWFEGAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGSDHCP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 324 FCFsGQKEMGRGDFSKIPNGMPGVEHRMDLLHQAVVD-GHLSRRRWVEIACASPARMFGLYPKKGTIAPGADADVVIYDP 402
Cdd:cd01314 317 FNF-AQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAkGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDP 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 664099816 403 GAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVGHAGHG 454
Cdd:cd01314 396 NAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
6-459 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 582.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 6 IHGGLVVTASDEIHADVLIEGGRIAALaahGTDAATSwSADRRIDATGMYVLPGGVDAHTHMEMPFGGTYAADTFETGTR 85
Cdd:TIGR02033 3 IKGGTVVNADDVFQADVLIEGGKIVAV---GDNLIPP-DAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 86 AAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSDVNESSLKEMDR-LVAEGVTSFKLFMAYPGVF 164
Cdd:TIGR02033 79 AAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPeVKEEGINSFKVFMAYKNLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 165 YSDDGRILRAMQRASGNGGLVMMHAENGIAIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAGAPLYVVH 244
Cdd:TIGR02033 159 MVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 245 VSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEPGFEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVSTDHCPF 324
Cdd:TIGR02033 239 VSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKPGFEGAKYVCSPPLREPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 325 CFSGQKEMGRGDFSKIPNGMPGVEHRMDLLH-QAVVDGHLSRRRWVEIACASPARMFGLYPKKGTIAPGADADVVIYDPG 403
Cdd:TIGR02033 319 NFAQKKAIGKDDFTKIPNGGPGVEERMSLLFdEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 664099816 404 AEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVGHAGHGTYLPR 459
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
4-461 |
0e+00 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 519.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVVTASDEIHADVLIEGGRIAALAaHGTDAATswsadRRIDATGMYVLPGGVDAHTHMEMPFG-GTYAADTFET 82
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALG-EGLGPGA-----REIDATGRLVLPGGVDSHCHIDQPSGdGIMMADDFYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 83 GTRAAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSDVNESSLK-EMDRLVAEGVTSFKLFMAYP 161
Cdd:PRK13404 80 GTVSAAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVLTeELPALIAQGYTSFKVFMTYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 162 GVFYSDDGrILRAMQRASGNGGLVMMHAENGIAIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAGAPLY 241
Cdd:PRK13404 160 DLKLDDRQ-ILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPIL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 242 VVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEPGFEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVSTDH 321
Cdd:PRK13404 239 IVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDRPGMEGAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 322 CPFCFSGQK-EMGRGD---FSKIPNGMPGVEHRMDLLHQA-VVDGHLSRRRWVEIACASPARMFGLYPKKGTIAPGADAD 396
Cdd:PRK13404 319 APFRFDDTDgKLAAGAnpsFKAIANGIPGIETRLPLLFSEgVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADAD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664099816 397 VVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVGHAGHGTYLPRGT 461
Cdd:PRK13404 399 IAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-459 |
0e+00 |
|
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: 515.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 5 VIHGGLVVTASDEIHADVLIEGGRIAALAahgtDAATSWSADRRIDATGMYVLPGGVDAHTHMEMPfGGTYAaDTFETGT 84
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIG----PDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP-GLEHK-EDIETGT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 85 RAAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSDVNESSLKEMDRLVAEGVTSFKLFMAYP-GV 163
Cdd:COG0044 75 RAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALAEAGAVAFKVFMGSDdGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 164 FYSDDGRILRAMQRASGNGGLVMMHAENGIAIDVLVeqaLAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAGAPLYVV 243
Cdd:COG0044 155 PVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGV---MNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 244 HVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEpgfEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVSTDHCP 323
Cdd:COG0044 232 HVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLER---YGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 324 FCFSgQKemgRGDFSKIPNGMPGVEHRMDLLHQAVV-DGHLSRRRWVEIACASPARMFGLyPKKGTIAPGADADVVIYDP 402
Cdd:COG0044 309 HTLE-EK---ELPFAEAPNGIPGLETALPLLLTELVhKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDP 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 664099816 403 GAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVGhAGHGTYLPR 459
Cdd:COG0044 384 DAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVG-EPRGRFLRR 439
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-465 |
6.00e-142 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 415.40 E-value: 6.00e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 2 SRTVIHGGLVVTASDEIHADVLIEGGRIAALAAH---GTDAatswsadRRIDATGMYVLPGGVDAHTHMEMPFGGTYAAD 78
Cdd:PLN02942 5 TKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNlkvPDDV-------RVIDATGKFVMPGGIDPHTHLAMPFMGTETID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 79 TFETGTRAAAWGGTTTIVDFAIQSMGrSLREGLDTWHAKADGRCaVDYGFHMILSDVNESSLKEMDRLVAE-GVTSFKLF 157
Cdd:PLN02942 78 DFFSGQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAEKSC-MDYGFHMAITKWDDTVSRDMETLVKEkGINSFKFF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 158 MAYPGVFYSDDGRILRAMQRASGNGGLVMMHAENGIAIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAG 237
Cdd:PLN02942 156 MAYKGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 238 APLYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEPGFE-GAKYVCSTPLRPREHQEVLWRGLRNNELQV 316
Cdd:PLN02942 236 TPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTiASKYVMSPPIRPAGHGKALQAALSSGILQL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 317 VSTDHCPFCfSGQKEMGRGDFSKIPNGMPGVEHRMDLLHQAVVD-GHLSRRRWVEIACASPARMFGLYPKKGTIAPGADA 395
Cdd:PLN02942 316 VGTDHCPFN-STQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVEsGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 396 DVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVGHAGHGTYLPRGTCQYL 465
Cdd:PLN02942 395 DIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFSYL 464
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-457 |
1.49e-107 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 326.17 E-value: 1.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVVTASDEIHADVLIEGGRIAALAAHGTDAatswSADRRIDATGMYVLPGGVDAHTHMEMPfGGTYAaDTFETG 83
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANT----EAEEVIDAGGLVVMPGLIDTHVHINEP-GRTEW-EGFETG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 84 TRAAAWGGTTTIVDFAIQSMGRSL-REGLDTWHAKADGRCAVDYGFHMILSDVNessLKEMDRLVAEGVTSFKLFMAYPG 162
Cdd:cd01315 76 TKAAAAGGITTIIDMPLNSIPPTTtVENLEAKLEAAQGKLHVDVGFWGGLVPGN---LDQLRPLDEAGVVGFKCFLCPSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 163 V--FYS-DDGRILRAMQRASGNGGLVMMHAENGIAIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAGAP 239
Cdd:cd01315 153 VdeFPAvDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 240 LYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEPGFEgakYVCSTPLRPREHQEVLWRGLRNNELQVVST 319
Cdd:cd01315 233 LHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTE---FKCAPPIRDAANQEQLWEALENGDIDMVVS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 320 DHCPfCFSGQKEMGRGDFSKIPNGMPGVEHRMDLLH-QAVVDGHLSRRRWVEIACASPARMFGLYPKKGTIAPGADADVV 398
Cdd:cd01315 310 DHSP-CTPELKLLGKGDFFKAWGGISGLQLGLPVMLtEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFV 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 664099816 399 IYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVGHAgHGTYL 457
Cdd:cd01315 389 VWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP-LGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
55-434 |
9.43e-102 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 307.40 E-value: 9.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 55 YVLPGGVDAHTHMEMPFGGTYAaDTFETGTRAAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSD 134
Cdd:cd01302 2 LVLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 135 VNEssLKEMDRLVAEGVTSFKLFMAY--PGVFYSDDGRILRAMQRASGNGGLVMMHAEngiaidvlveqalaegrtdpry 212
Cdd:cd01302 81 GDV--TDELKKLFDAGINSLKVFMNYyfGELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 213 hgdvrkvaleaeathRAVQLARVAGAPLYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAepgFEGAKYVC 292
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLR---LNGAWGKV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 293 STPLRPREHQEVLWRGLRNNELQVVSTDHCPFCFSgQKEMGrGDFSKIPNGMPGVEHRMDLLHQAVVDGHLSRRRWVEIA 372
Cdd:cd01302 199 NPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKE-EKESG-KDIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEIL 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664099816 373 CASPARMFGLYPKKgTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTV 434
Cdd:cd01302 277 SENPARIFGLYPKG-TIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
5-445 |
1.41e-85 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 269.65 E-value: 1.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 5 VIHGGLVVTASDEIHADVLIEGGRIAALAAhgtdaATSWSADRRIDATGMYVLPGGVDAHTHMEMPfgGTYAADTFETGT 84
Cdd:PRK06189 6 IIRGGKVVTPEGVYRADIGIKNGKIAEIAP-----EISSPAREIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 85 RAAAWGGTTTIVDFAIQSMGRSL-REGLDTWHAKADGRCAVDYGFHMILSDVNessLKEMDRLVAEGVTSFKLFMAYPGV 163
Cdd:PRK06189 79 AALAAGGCTTYFDMPLNSIPPTVtREALDAKAELARQKSAVDFALWGGLVPGN---LEHLRELAEAGVIGFKAFMSNSGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 164 --F-YSDDGRILRAMQRASGNGGLVMMHAENGIAIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAGAPL 240
Cdd:PRK06189 156 deFrSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 241 YVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEpgfEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVSTD 320
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFER---IGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 321 HCPfCFSGQKEmgRGDFSKIPNGMPGVEHRMD-LLHQAVVDGHLSRRRWVEIACASPARMFGLyPKKGTIAPGADADVVI 399
Cdd:PRK06189 313 HSP-CPPELKE--GDDFFLVWGGISGGQSTLLvMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADADFVL 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 664099816 400 YDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDR 445
Cdd:PRK06189 389 VDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDG 434
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
4-458 |
2.45e-71 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 232.82 E-value: 2.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVVTASDEIHADVLIEGGRIAALAAHGTDAAtswsadRRIDATGMYVLPGGVDAHTHMEMPfGGTYAaDTFETG 83
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAK------EVMDASGLVVSPGMVDAHTHISEP-GRSHW-EGYETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 84 TRAAAWGGTTTIVDFAIQSMGRSL-REGLDTWHAKADGRCAVDYGFHMILSDVNESSLKEMDRLvaeGVTSFKLFMAYPG 162
Cdd:PRK08044 77 TRAAAKGGITTMIEMPLNQLPATVdRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEV---GVVGFKCFVATCG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 163 -------VFYSDDGRILRAMQRASGNGGLVMMHAENGIAIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLARV 235
Cdd:PRK08044 154 drgidndFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 236 AGAPLYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEPGfEGAKyvCSTPLRPREHQEVLWRGLRNNELQ 315
Cdd:PRK08044 234 AGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIG-TLAK--CSPPIRDLENQKGMWEKLFNGEID 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 316 VVSTDHCPfCfsgQKEMGRGDFSKIPNGMPGVEHRMDLL-HQAVVDGHLSRRRWVEIACASPARMFGLyPKKGTIAPGAD 394
Cdd:PRK08044 311 CLVSDHSP-C---PPEMKAGNIMEAWGGIAGLQNCMDVMfDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKD 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664099816 395 ADVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVGHAGHGTYLP 458
Cdd:PRK08044 386 ADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFIL 449
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-462 |
1.76e-70 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 230.31 E-value: 1.76e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 1 MSRTVIHGGLVVTASDEIHADVLIEGGRIAALAahgtDAATSWSADRRIDATGMYVLPGGVDAHTHMEMPfGGTYAaDTF 80
Cdd:PRK02382 1 MRDALLKDGRVYYNNSLQPRDVRIDGGKITAVG----KDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP-GYTHK-ETW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 81 ETGTRAAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSDvnesSLKEMDRLVAEGVTSF-KLFMA 159
Cdd:PRK02382 75 YTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTG----NWDPLESLWERGVFALgEIFMA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 160 -YPGVFYSDDGRILRAMQRASGNGGLVMMHAENGIAIDVLVEqaLAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAGA 238
Cdd:PRK02382 151 dSTGGMGIDEELFEEALAEAARLGVLATVHAEDEDLFDELAK--LLKGDADADAWSAYRPAAAEAAAVERALEVASETGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 239 PLYVVHVSADEAVDEIAAARhkglpVFGETCPQYLFLSTDNLAEPGFEGAKyvcSTPLRPREHQEVLWRGLRNNELQVVS 318
Cdd:PRK02382 229 RIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKM---NPPLRSEKRREALWERLNDGTIDVVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 319 TDHCPFcfsgQKEMGRGDFSKIPNGMPGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGLyPKKGTIAPGADADVV 398
Cdd:PRK02382 301 SDHAPH----TREEKDADIWDAPSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLV 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664099816 399 IYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTvLSRGVPVIEDRAYVGHAGHGTYLPRGTC 462
Cdd:PRK02382 376 LVDPDAAREIRGDDLHSKAGWTPFEGMEGVFPELT-MVRGTVVWDGDDINAKRGRGEFLRGRGY 438
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
17-444 |
4.36e-59 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 199.59 E-value: 4.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 17 EIHADVLIEGGRIAALAAHGTDAAtswsaDRRIDATGMYVLPGGVDAHTHMEMPfGGTYAaDTFETGTRAAAWGGTTTIV 96
Cdd:TIGR00857 3 ETEVDILVEGGRIKKIGKLRIPPD-----AEVIDAKGLLVLPGFIDLHVHLRDP-GEEYK-EDIESGSKAAAHGGFTTVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 97 DFA--------IQSMGRSLREGldtwhaKADGRcaVDYGFHMILSDVNEssLKEMDRLvaegvtSFKLFMAYPGVFYSDD 168
Cdd:TIGR00857 76 DMPntkppidtPETLEWKLQRL------KKVSL--VDVHLYGGVTQGNQ--GKELTEA------YELKEAGAVGRMFTDD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 169 G-RIL------RAMQRASGNGGLVMMHAENgiaIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLARVAGAPLY 241
Cdd:TIGR00857 140 GsEVQdilsmrRALEYAAIAGVPIALHAED---PDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 242 VVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEpgfEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVSTDH 321
Cdd:TIGR00857 217 ICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVAR---LDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDH 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 322 CPFcfsgQKEMGRGDFSKIPNGMPGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGLyPKKGTIAPGADADVVIYD 401
Cdd:TIGR00857 294 APH----TLEEKTKEFAAAPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFD 368
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 664099816 402 PGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIED 444
Cdd:TIGR00857 369 LKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
53-438 |
1.13e-58 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 196.79 E-value: 1.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 53 GMYVLPGGVDAHTHMEMPfGGTYAADtFETGTRAAAWGGTTTIVD-----FAIQSMgRSLREGLdtwhAKADGRCAVDYG 127
Cdd:cd01318 1 GLLILPGVIDIHVHFREP-GLTYKED-FVSGSRAAAAGGVTTVMDmpntkPPTTTA-EALYEKL----RLAAAKSVVDYG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 128 FHMILSDVNEssLKEMDRLvaeGVTSFKLFMA----YPGVFYSDDGRILRAMQRasgnggLVMMHAENgiaiDVLVEQAL 203
Cdd:cd01318 74 LYFGVTGSED--LEELDKA---PPAGYKIFMGdstgDLLDDEETLERIFAEGSV------LVTFHAED----EDRLRENR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 204 AEgRTDPRYHGDVRKVALEAEATHRAVQLARVAGAPLYVVHVSADEAVDEIAAARHKglpVFGETCPQYLFLSTDNLAEp 283
Cdd:cd01318 139 KE-LKGESAHPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDR- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 284 gfEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVSTDHCPFCFSgQKEMGrgdFSKIPNGMPGVEHRMDLLHQAVVDGHL 363
Cdd:cd01318 214 --LGTLGKVNPPLRSREDRKALLQALADGRIDVIASDHAPHTLE-EKRKG---YPAAPSGIPGVETALPLMLTLVNKGIL 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664099816 364 SRRRWVEIACASPARMFGLyPKKGTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRG 438
Cdd:cd01318 288 SLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-434 |
1.36e-58 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 198.75 E-value: 1.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 1 MSRTVIHGGLVVTASDE-IHADVLIEGGRIAALAAHGTDAATswsaDRRIDATGMYVLPGGVDAHTHMEMPfGGTYAADT 79
Cdd:PRK07575 2 MMSLLIRNARILLPSGElLLGDVLVEDGKIVAIAPEISATAV----DTVIDAEGLTLLPGVIDPQVHFREP-GLEHKEDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 80 FeTGTRAAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSDVNESSLKEmdrlvAEGVTSFKLFM- 158
Cdd:PRK07575 77 F-TASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLT-----ANPTCGIKIFMg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 159 AYPGVFYSDD----GRILRAMQRasgnggLVMMHAENGIAIdvLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLAR 234
Cdd:PRK07575 151 SSHGPLLVDEeaalERIFAEGTR------LIAVHAEDQARI--RARRAEFAGISDPADHSQIQDEEAALLATRLALKLSK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 235 VAGAPLYVVHVSADEAVDEIAaaRHKGLPVFGETCPQYLFLSTDNLAEPGfEGAKYvcSTPLRPREHQEVLWRGLRNNEL 314
Cdd:PRK07575 223 KYQRRLHILHLSTAIEAELLR--QDKPSWVTAEVTPQHLLLNTDAYERIG-TLAQM--NPPLRSPEDNEALWQALRDGVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 315 QVVSTDHCPFCFSgqkEMGRGdFSKIPNGMPGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGLyPKKGTIAPGAD 394
Cdd:PRK07575 298 DFIATDHAPHTLE---EKAQP-YPNSPSGMPGVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYD 372
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 664099816 395 ADVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTG-QVRTV 434
Cdd:PRK07575 373 ADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGwPVTTI 413
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
2-444 |
1.02e-57 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 196.18 E-value: 1.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 2 SRTVIHGGLVVTASDE-IHADVLIEGGRIAALAAHGTDAAtswsaDRRIDATGMYVLPGGVDAHTHMEMPfGGTYAaDTF 80
Cdd:PRK09357 1 MMILIKNGRVIDPKGLdEVADVLIDDGKIAAIGENIEAEG-----AEVIDATGLVVAPGLVDLHVHLREP-GQEDK-ETI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 81 ETGTRAAAWGGTTTIVDFA-----IQSmgrslREGLDTWHAKADGRCAVD---YGfhMILSDVNESSLKEMDRLVAEGVT 152
Cdd:PRK09357 74 ETGSRAAAAGGFTTVVAMPntkpvIDT-----PEVVEYVLDRAKEAGLVDvlpVG--AITKGLAGEELTEFGALKEAGVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 153 SFklfmaypgvfySDDG------RILR-AMQRASGNGGLVMMHAENgiaiDVLVEQALA-EGRTDPRYHgdVRKVALEAE 224
Cdd:PRK09357 147 AF-----------SDDGipvqdaRLMRrALEYAKALDLLIAQHCED----PSLTEGGVMnEGEVSARLG--LPGIPAVAE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 225 ATH--RAVQLARVAGAPLYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEpgfEGAKYVCSTPLRPREHQ 302
Cdd:PRK09357 210 EVMiaRDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLT---YDPNYKVNPPLRTEEDR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 303 EVLWRGLRNNELQVVSTDHCPFcfsgQKEMGRGDFSKIPNGMPGVEHRMDLLHQAVVD-GHLSRRRWVEIACASPARMFG 381
Cdd:PRK09357 287 EALIEGLKDGTIDAIATDHAPH----AREEKECEFEAAPFGITGLETALSLLYTTLVKtGLLDLEQLLEKMTINPARILG 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664099816 382 LypKKGTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIED 444
Cdd:PRK09357 363 L--PAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
4-451 |
2.60e-56 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 193.21 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVVTASDEIHADVLIEGGRIAALAAHGTDaatswSADRRIDATGMYVLPGGVDAHTHMEMPfgGTYAADTFETG 83
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGA-----SAGEVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 84 TRAAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSDVNESSLKEMDRLvaEGVTSFKLFM-AYPG 162
Cdd:PRK09060 80 SRAAVLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELERL--PGCAGIKVFMgSSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 163 VFYSDD----GRILRAMQRAsgngglVMMHAENgiaidvlvEQALAEGRT-----DPRYHGDVRKVALEAEATHRAVQLA 233
Cdd:PRK09060 158 DLLVEDdeglRRILRNGRRR------AAFHSED--------EYRLRERKGlrvegDPSSHPVWRDEEAALLATRRLVRLA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 234 RVAGAPLYVVHVSADEAVDEIAAarHKGLPVFgETCPQYLFLStdnlAEPGFE--GAKYVCSTPLRPREHQEVLWRGLRN 311
Cdd:PRK09060 224 RETGRRIHVLHVSTAEEIDFLAD--HKDVATV-EVTPHHLTLA----APECYErlGTLAQMNPPIRDARHRDGLWRGVRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 312 NELQVVSTDHCPFcfsgQKEMGRGDFSKIPNGMPGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGLyPKKGTIAP 391
Cdd:PRK09060 297 GVVDVLGSDHAPH----TLEEKAKPYPASPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAV 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664099816 392 GADADVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTG-QVRTVLsRGVPVIEDRAYVGHA 451
Cdd:PRK09060 372 GYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGwPVGTIV-RGQRVMWDGELVGPP 431
|
|
| PLN02795 |
PLN02795 |
allantoinase |
4-438 |
7.30e-54 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 188.06 E-value: 7.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVVTASDEIHADVLIEGGRIAALAaHGTDAATSWSADRRIDATGMYVLPGGVDAHTHMEMPfgGTYAADTFETG 83
Cdd:PLN02795 46 FVLYSKRVVTPAGVIPGAVEVEGGRIVSVT-KEEEAPKSQKKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 84 TRAAAWGGTTTIVDFAIQSMGRSL-REGLDTWHAKADGRCAVDYGFHMILSDVNESSLKEMDRLVAEGVTSFKLFMA--- 159
Cdd:PLN02795 123 TKAAAAGGITTLVDMPLNSFPSTTsVETLELKIEAAKGKLYVDVGFWGGLVPENAHNASVLEELLDAGALGLKSFMCpsg 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 160 ---YPGVFYSDdgrILRAMQRASGNGGLVMMHAEngIAIDVLVEQALAEGRTDPRYHGDVRKVALEAEATHRAVQLA--- 233
Cdd:PLN02795 203 indFPMTTATH---IKAALPVLAKYGRPLLVHAE--VVSPVESDSRLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAkdt 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 234 ----RVAGAPLYVVHVS-ADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEpgfeGA-KYVCSTPLRPREHQEVLWR 307
Cdd:PLN02795 278 rpggVAEGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPD----GDtRYKCAPPIRDAANRELLWK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 308 GLRNNELQVVSTDHCPfCFSGQKEMGRGDFSKIPNGMPGVE------------HRMDLLHQAvvdghlsrRRWVEiacaS 375
Cdd:PLN02795 354 ALLDGDIDMLSSDHSP-SPPDLKLLEEGNFLRAWGGISSLQfvlpatwtagraYGLTLEQLA--------RWWSE----R 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664099816 376 PARMFGLyPKKGTIAPGADADVVIYDPGAEQTI--SAETHHMAVDYSAYEGRRVTGQVRTVLSRG 438
Cdd:PLN02795 421 PAKLAGL-DSKGAIAPGKDADIVVWDPEAEFVLdeSYPIYHKHKSLSPYLGTKLSGKVIATFVRG 484
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
45-431 |
1.55e-53 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 183.59 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 45 ADRRIDATGMYVLPGGVDAHTHMEMPfGGTYAaDTFETGTRAAAWGGTTTIV-----DFAIQSMgrSLREGLDTWHAKAD 119
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP-GFEYK-ETLESGAKAAAAGGFTTVVcmpntNPVIDNP--AVVELLKNRAKDVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 120 GRCAVDYGfhMILSDVNESSLKEMDRLVAEGVTSFklfmaypgvfySDDGR-------ILRAMQRASGNGGLVMMHAEN- 191
Cdd:cd01317 77 IVRVLPIG--ALTKGLKGEELTEIGELLEAGAVGF-----------SDDGKpiqdaelLRRALEYAAMLDLPIIVHPEDp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 192 GIAIDVLV-EQALAEgrtdprYHG--DVRKVAlEAEATHRAVQLARVAGAPLYVVHVSADEAVDEIAAARHKGLPVFGET 268
Cdd:cd01317 144 SLAGGGVMnEGKVAS------RLGlpGIPPEA-ETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 269 CPQYLFLSTDNLAepGFEGAKYVcSTPLRPREHQEVLWRGLRNNELQVVSTDHCPFcfsgQKEMGRGDFSKIPNGMPGVE 348
Cdd:cd01317 217 TPHHLLLDDEALE--SYDTNAKV-NPPLRSEEDREALIEALKDGTIDAIASDHAPH----TDEEKDLPFAEAPPGIIGLE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 349 HRMDLLHQAVVD-GHLSRRRWVEIACASPARMFGLYPkkGTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYEGRRV 427
Cdd:cd01317 290 TALPLLWTLLVKgGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKL 367
|
....
gi 664099816 428 TGQV 431
Cdd:cd01317 368 KGRV 371
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-450 |
1.39e-47 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 169.67 E-value: 1.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 1 MSRTVIHGGLVVTASDEIHADVLIEGGRIAALAAHGTDAatswSADRRIDATGMYVLPGGVDAHTHMEMPfGGTYAADtF 80
Cdd:PRK09236 1 MKRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAK----SADTVIDAAGRYLLPGMIDDQVHFREP-GLTHKGD-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 81 ETGTRAAAWGGTTTIVDfaiqsMGRSL-----REGLDTWHAKADGRCAVDYGFHMILSDVNESSLKEMDRLVAEGVtsfK 155
Cdd:PRK09236 75 ASESRAAVAGGITSFME-----MPNTNpptttLEALEAKYQIAAQRSLANYSFYFGATNDNLDEIKRLDPKRVCGV---K 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 156 LFM-AYPGVFYSDDGRILRAMQRASGNggLVMMHAENGIAIDVLVEQALAE-GRT-DPRYHGDVRKValEA--EATHRAV 230
Cdd:PRK09236 147 VFMgASTGNMLVDNPETLERIFRDAPT--LIATHCEDTPTIKANLAKYKEKyGDDiPAEMHPLIRSA--EAcyKSSSLAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 231 QLARVAGAPLYVVHVS-ADE----AVDEIAAARhkglpVFGETCPQYLFLSTDNLAEpgfEGAKYVCSTPLRPREHQEVL 305
Cdd:PRK09236 223 SLAKKHGTRLHVLHIStAKElslfENGPLAEKR-----ITAEVCVHHLWFDDSDYAR---LGNLIKCNPAIKTASDREAL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 306 WRGLRNNELQVVSTDHCPFCFSgQKEmgrGDFSKIPNGMPGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGLyPK 385
Cdd:PRK09236 295 RQALADDRIDVIATDHAPHTWE-EKQ---GPYFQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDI-KE 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664099816 386 KGTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVGH 450
Cdd:PRK09236 370 RGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLVES 434
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
18-449 |
3.72e-38 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 142.99 E-value: 3.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 18 IHADVLIEGGRIAALAAHgtdaatSWSADRRIDATGMYVLPGGVDAHTHMEmPFGGTYAaDTFETGTRAAAWGGTTTIVD 97
Cdd:PRK04250 13 VEGGIGIENGRISKISLR------DLKGKEVIKVKGGIILPGLIDVHVHLR-DFEESYK-ETIESGTKAALHGGITLVFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 98 F------AIQSMGRSLREGLdtwhakADGRCAVDYGFHMILsdvnESSLKEMDRLVAEgvtSFKLFM-AYPGVFYSDDGR 170
Cdd:PRK04250 85 MpntkppIMDEKTYEKRMRI------AEKKSYADYALNFLI----AGNCEKAEEIKAD---FYKIFMgASTGGIFSENFE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 171 IlrAMQRASGnggLVMMHAENGIAIDVLVEqalaegrtdpryhgdvRKVALEAEATHRAVQLARVAGAPLYVVHVSADEA 250
Cdd:PRK04250 152 V--DYACAPG---IVSVHAEDPELIREFPE----------------RPPEAEVVAIERALEAGKKLKKPLHICHISTKDG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 251 VDEIaaaRHKGLP-VFGETCPQYLFLSTDNlaepgFEGAKYV-CSTPLRPREHQEVLWRGLRNneLQVVSTDHCPFCFSg 328
Cdd:PRK04250 211 LKLI---LKSNLPwVSFEVTPHHLFLTRKD-----YERNPLLkVYPPLRSEEDRKALWENFSK--IPIIASDHAPHTLE- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 329 QKEMGRGdfskipnGMPGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGLypKKGTIAPGADADVVIYDPGAEQTI 408
Cdd:PRK04250 280 DKEAGAA-------GIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGI--KNYGIEEGNYANFAVFDMKKEWTI 350
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 664099816 409 SAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDRAYVG 449
Cdd:PRK04250 351 KAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIG 391
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
57-454 |
7.66e-28 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 113.31 E-value: 7.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 57 LPGGVDAHTHMEMPfGGTYAADtFETGTRAAAWGGTTTIvdfaiQSMGRSLREGLDTWH-------AKADGRCavDYGFH 129
Cdd:cd01316 5 LPGLIDVHVHLREP-GATHKED-FASGTKAALAGGFTMV-----RAMPNTNPSIVDVASlklvqslAQAKARC--DYAFS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 130 MILSDVNESSLKEMdrlvaegvtsfklfmaypgvfysddgrilramqrASGNGGLVMMHAE---NGIAIDVLVEQALAEg 206
Cdd:cd01316 76 IGATSTNAATVGEL----------------------------------ASEAVGLKFYLNEtfsTLILDKITAWASHFN- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 207 rTDPryhgDVRKVALEAEATHRA--VQLARVAGAPLYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEPG 284
Cdd:cd01316 121 -AWP----STKPIVTHAKSQTLAavLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 285 FEGAKYVCStplrpREHQEVLWRGLrnNELQVVSTDHCPFCFSGQKEmgrgdfSKIPNGMPGVEHRMDLLHQAVVDGHLS 364
Cdd:cd01316 196 YEVRPFLPT-----REDQEALWENL--DYIDCFATDHAPHTLAEKTG------NKPPPGFPGVETSLPLLLTAVHEGRLT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 365 RRRWVEIACASPARMFGLYPKKGTiapgadadVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIED 444
Cdd:cd01316 263 IEDIVDRLHTNPKRIFNLPPQSDT--------YVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFID 334
|
410
....*....|
gi 664099816 445 RAYVGHAGHG 454
Cdd:cd01316 335 GEIVAPPGFG 344
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
6-445 |
4.74e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 106.68 E-value: 4.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 6 IHGGLVV--TASDEIHADVLIEGGRIAALAAhgtdAATSWSADRRIDATGMYVLPGGVDAHTHMEMPfGGTYAAdTFETG 83
Cdd:PRK07627 5 IKGGRLIdpAAGTDRQADLYVAAGKIAAIGQ----APAGFNADKTIDASGLIVCPGLVDLSARLREP-GYEYKA-TLESE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 84 TRAAAWGGTTTIV-----DFAIQSMGrsLREGLdTWHAKADGRCAVdYGFHMILSDVNESSLKEMDRLVAEGVTSFklfm 158
Cdd:PRK07627 79 MAAAVAGGVTSLVcppdtDPVLDEPG--LVEML-KFRARNLNQAHV-YPLGALTVGLKGEVLTEMVELTEAGCVGF---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 159 AYPGVFYSDDGRILRAMQRASGNGGLVMMH------AENGIAidvlveqalAEGRTDPRYHGDVRKVALEAEATHRAVQL 232
Cdd:PRK07627 151 SQANVPVVDTQVLLRALQYASTFGFTVWLRpldaflGRGGVA---------ASGAVASRLGLSGVPVAAETIALHTIFEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 233 ARVAGAPLYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLaepGFEGAKYVCSTPLRPREHQEVLWRGLRNN 312
Cdd:PRK07627 222 MRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDI---GYFDSQFRLDPPLRSQRDREAIRAALADG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 313 ELQVVSTDHCPFcfsgqkemgrGD------FSKIPNGMPGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGLypKK 386
Cdd:PRK07627 299 TIDAICSDHTPV----------DDdekllpFAEATPGATGLELLLPLTLKWADEAKVPLARALARITSAPARVLGL--PA 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 664099816 387 GTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIEDR 445
Cdd:PRK07627 367 GRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAFERR 425
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
56-460 |
9.67e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 105.71 E-value: 9.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 56 VLPGGVDAHTHMEMPfGGTYAADtFETGTRAAAWGGTTTIVDFA--------IQSMGRSLRegldtwhaKADGRCAVDYG 127
Cdd:PRK01211 44 ILPAATDIHVHFRTP-GETEKED-FSTGTLSAIFGGTTFIMDMPnnnipikdYNAFSDKLG--------RVAPKAYVDFS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 128 FHMILSDVNESSLKEMDrlvaegvTSFKLFMA----------------------YPGVFYSDDGRILRAMQRASGNgglv 185
Cdd:PRK01211 114 LYSMETGNNALILDERS-------IGLKVYMGgttntngtdieggeikkineanIPVFFHAELSECLRKHQFESKN---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 186 mmhaengiaidvlveqalaegrtdPRYHGDVRKVALEAEAthraVQLARVAGAPLYVV-HVSADEAVDEIAAarhkglpv 264
Cdd:PRK01211 183 ------------------------LRDHDLARPIECEIKA----VKYVKNLDLKTKIIaHVSSIDVIGRFLR-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 265 fgETCPQYLFLSTD-NLAEPGfegakyVCSTPLRPREHQEVLWRGLRNNELQVVSTDHCPfcfsgQKEMGRGDFSKIPNG 343
Cdd:PRK01211 227 --EVTPHHLLLNDDmPLGSYG------KVNPPLRDRWTQERLLEEYISGRFDILSSDHAP-----HTEEDKQEFEYAKSG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 344 MPGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGLypKKGTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYE 423
Cdd:PRK01211 294 IIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFN 371
|
410 420 430
....*....|....*....|....*....|....*..
gi 664099816 424 GRRVTGQvRTVLSRGVPVIEDRAYVGHAgHGTYLPRG 460
Cdd:PRK01211 372 GFDAIFP-SHVIMRGEVVIDNYELISER-TGKFVPKG 406
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-450 |
2.75e-20 |
|
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: 92.75 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVV--TASDEIHADVLIEGGRIAALAAhgtdaATSWSADRRIDATGMYVLPGGVDAHTHmempfggtYAADTFE 81
Cdd:cd01297 2 LVIRNGTVVdgTGAPPFTADVGIRDGRIAAIGP-----ILSTSAREVIDAAGLVVAPGFIDVHTH--------YDGQVFW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 82 TGT-RAAAWGGTTTIV------------------DFAIQSMGRSLREGLD-TWHAKAD-------GRCAVDYGFH----- 129
Cdd:cd01297 69 DPDlRPSSRQGVTTVVlgncgvspapanpddlarLIMLMEGLVALGEGLPwGWATFAEyldaleaRPPAVNVAALvghaa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 130 -----MILSDV--NESSLKEMDRLVAEGVTS----FKLFMAYPGVFYSDDGRIL---RAMQRAsgnGGLVMMHaengiai 195
Cdd:cd01297 149 lrravMGLDAReaTEEELAKMRELLREALEAgalgISTGLAYAPRLYAGTAELValaRVAARY---GGVYQTH------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 196 dvlveqalaegrtdPRYHGDVRkvaleAEATHRAVQLARVAGAPLYVVHVSA---------DEAVDEIAAARHKGLPVFG 266
Cdd:cd01297 219 --------------VRYEGDSI-----LEALDELLRLGRETGRPVHISHLKSagapnwgkiDRLLALIEAARAEGLQVTA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 267 ETCPqYLFLSTDNLAEpgfegakyvcstplrprehqevlwrgLRNNELQVVSTDHCPFCFSGQKEMgrGDFSKIpngmpg 346
Cdd:cd01297 280 DVYP-YGAGSEDDVRR--------------------------IMAHPVVMGGSDGGALGKPHPRSY--GDFTRV------ 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 347 vehrmdLLHQAVVDGHLSRRRWVEIACASPARMFGLYpKKGTIAPGADADVVIYDPgaeQTISAETHHMAVDysayegRR 426
Cdd:cd01297 325 ------LGHYVRERKLLSLEEAVRKMTGLPARVFGLA-DRGRIAPGYRADIVVFDP---DTLADRATFTRPN------QP 388
|
490 500
....*....|....*....|....
gi 664099816 427 VTGqVRTVLSRGVPVIEDRAYVGH 450
Cdd:cd01297 389 AEG-IEAVLVNGVPVVRDGAFTGA 411
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
1-431 |
3.31e-17 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 83.50 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 1 MSRTVIHGGLV---VTASDEIhADVLIEGGRIAALAAHGTDAAtswSADRRIDATGMYVLPGGVDAHTHMEMPfgGTYAA 77
Cdd:PRK07369 1 MSNELLQQVRVldpVSNTDRI-ADVLIEDGKIQAIEPHIDPIP---PDTQIIDASGLILGPGLVDLYSHSGEP--GFEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 78 DTFETGTRAAAWGGTTTI---------VDFAiqsmgrslrEGLDTWHAKADGRCAVDYGFHMILS-DVNESSLKEMDRLV 147
Cdd:PRK07369 75 ETLASLAAAAAAGGFTRVailpdtfppLDNP---------ATLARLQQQAQQIPPVQLHFWGALTlGGQGKQLTELAELA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 148 AEGVTSFklfmaypgvfySDDGRI--LRAMQRAsgnggLVMMHAENG-IAIdVLVEQALA------EGRTDPRYHGDVRK 218
Cdd:PRK07369 146 AAGVVGF-----------TDGQPLenLALLRRL-----LEYLKPLGKpVAL-WPCDRSLAgngvmrEGLLALRLGLPGDP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 219 VALEAEATHRAVQLARVAGAPLYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLA--------EPgfegaky 290
Cdd:PRK07369 209 ASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEALAsydpnlrlDP------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 291 vcstPLRPREHQEVLWRGLRNNELQVVSTDHCPFCFSgQKEMGrgdFSKIPNGMPGVEHRMDLL-HQAVVDGHLSR-RRW 368
Cdd:PRK07369 282 ----PLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYE-EKTVA---FAEAPPGAIGLELALPLLwQNLVETGELSAlQLW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664099816 369 VEIACAsPARMFGLYPKkgTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYEGRRVTGQV 431
Cdd:PRK07369 354 QALSTN-PARCLGQEPP--SLAPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
55-419 |
1.91e-16 |
|
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: 80.24 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 55 YVLPGGVDAHTHMEMPFG------GTYAADTFETGTRAAAWGGTTTIVDFAIqsmgrsLREGLDTWHAKADGRCAVDYGF 128
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLrgipvpPEFAYEALRLGITTMLKSGTTTVLDMGA------TTSTGIEALLEAAEELPLGLRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 129 H----MILSDVNESSLKEMDRLVAEGVTSFKL---------FMAYPGVFYSDDGrILRAMQRASGNGGLVMMHAENGIAI 195
Cdd:pfam01979 75 LgpgcSLDTDGELEGRKALREKLKAGAEFIKGmadgvvfvgLAPHGAPTFSDDE-LKAALEEAKKYGLPVAIHALETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 196 DVLVEQALAEGRTDPrYHGDVrkvaLEAEATHRAVQLARVAGaplyvVHVSADEAVDEIAAARHKGLPvfgeTCPqylfl 275
Cdd:pfam01979 154 VEDAIAAFGGGIEHG-THLEV----AESGGLLDIIKLILAHG-----VHLSPTEANLLAEHLKGAGVA----HCP----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 276 stdnlaepgfegakyvcSTPLRPREHQEVLWRGLRNNELQVVSTDHCPfcfsgqkeMGRgdfskIPNGMPGVEHRMdlLH 355
Cdd:pfam01979 215 -----------------FSNSKLRSGRIALRKALEDGVKVGLGTDGAG--------SGN-----SLNMLEELRLAL--EL 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664099816 356 QAVVDGHLSRRRWVEIACASPARMFGLYPKKGTIAPGADADVVIYDPGAEQTISAETHHMAVDY 419
Cdd:pfam01979 263 QFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKK 326
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
16-443 |
4.74e-16 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 80.08 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 16 DEIhADVLIEGGRIAALAAHGTDAATSWSADRrIDATGMYVLPGGVDAHTHMEMPfgGTYAADTFETGTRAAAWGGTTTI 95
Cdd:PRK09059 20 DEI-GTVLIEDGVIVAAGKGAGNQGAPEGAEI-VDCAGKAVAPGLVDARVFVGEP--GAEHRETIASASRAAAAGGVTSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 96 VdfaiqSMGrslreglDTwHAKADGRCAVDYgfhmILSDVNESSLKEM-------DRLVAEGVTSFKLFMAYPGVFYSD- 167
Cdd:PRK09059 96 I-----MMP-------DT-DPVIDDVALVEF----VKRTARDTAIVNIhpaaaitKGLAGEEMTEFGLLRAAGAVAFTDg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 168 -----DGRILR-AMQRASGNGGLVMMHAENGiaiDVLVEQALAEGRTDPRYhgDVRKVALEAEAT--HRAVQLARVAGAP 239
Cdd:PRK09059 159 rrsvaNTQVMRrALTYARDFDAVIVHETRDP---DLGGNGVMNEGLFASWL--GLSGIPREAEVIplERDLRLAALTRGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 240 LYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLSTDNLAEpgfEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVST 319
Cdd:PRK09059 234 YHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGE---YRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 320 DHCPfcfsGQKEMGRGDFSKIPNGMPGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGLypKKGTIAPGADADVVI 399
Cdd:PRK09059 311 SHDP----QDVDTKRLPFSEAAAGAIGLETLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGL--PAGTLKPGAPADIIV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 664099816 400 YDPGAEQTISAETHHMAVDYSAYEGRRVTGQVRTVLSRGVPVIE 443
Cdd:PRK09059 385 IDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-401 |
2.27e-15 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 77.69 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 1 MSRTVIHGGLVVT-ASDEI--HADVLIEGGRIAALAAHgtDAATSWSADRRIDATGMYVLPGGVDAHTHM---------- 67
Cdd:COG1228 7 AGTLLITNATLVDgTGGGVieNGTVLVEDGKIAAVGPA--ADLAVPAGAEVIDATGKTVLPGLIDAHTHLglgggravef 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 68 EMPFGGTYAADTFETGTRAAAW---GGTTTIVD--FAIQSMGRSLREG----LDTWHAKADGRC-AVDYGFHMIlsdVNE 137
Cdd:COG1228 85 EAGGGITPTVDLVNPADKRLRRalaAGVTTVRDlpGGPLGLRDAIIAGesklLPGPRVLAAGPAlSLTGGAHAR---GPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 138 SSLKEMDRLVAEGVTSFKLFMAYPGVFYSDDgRILRAMQRASGNGGLVMMHAENGIAIDVLVEqalaegrtdpryhgdvr 217
Cdd:COG1228 162 EARAALRELLAEGADYIKVFAEGGAPDFSLE-ELRAILEAAHALGLPVAAHAHQADDIRLAVE----------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 218 kvaleaeathravqlarvAGAPLyVVHVSA--DEAVDEIAAARhkglPVFgetcpqylFLSTDNLAEPGFEGAKYVCSTP 295
Cdd:COG1228 224 ------------------AGVDS-IEHGTYldDEVADLLAEAG----TVV--------LVPTLSLFLALLEGAAAPVAAK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 296 LRP-REHQEVLWRGLRNNELQVV-STDHcpfcfsgqkemgrgdfskiPNGMPgveHRMDLLHQAV--VDGHLSRRRWVEI 371
Cdd:COG1228 273 ARKvREAALANARRLHDAGVPVAlGTDA-------------------GVGVP---PGRSLHRELAlaVEAGLTPEEALRA 330
|
410 420 430
....*....|....*....|....*....|
gi 664099816 372 ACASPARMFGLYPKKGTIAPGADADVVIYD 401
Cdd:COG1228 331 ATINAAKALGLDDDVGSLEPGKLADLVLLD 360
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-444 |
7.31e-15 |
|
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: 76.02 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 3 RTVIHGGLVVTASDEI----HADVLIEGGRIAALAAhGTDAATSWSADRRIDATGMYVLPGGVDAHTHMEMpfggtyaad 78
Cdd:COG0402 1 DLLIRGAWVLTMDPAGgvleDGAVLVEDGRIAAVGP-GAELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 79 tfeTGTRAAAWGGtttivdfaiqsmgrSLREGLDTWHAKADGRcavdygfhMILSDVNESSLKEMDRLVAEGVTSfklFM 158
Cdd:COG0402 71 ---TLLRGLADDL--------------PLLDWLEEYIWPLEAR--------LDPEDVYAGALLALAEMLRSGTTT---VA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 159 AYPGVFYSDDGRILRAMQRA--SGNGGLVMM--HAENGIAIDvlVEQALAEGRTD-PRYHGDVR---KVAL--------E 222
Cdd:COG0402 123 DFYYVHPESADALAEAAAEAgiRAVLGRGLMdrGFPDGLRED--ADEGLADSERLiERWHGAADgriRVALaphapytvS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 223 AEATHRAVQLARVAGAPLyVVHVSadEAVDEIAAARHKglpvFGETCPQYlflstdnLAEPGFEGAKYVC--STPLRPRE 300
Cdd:COG0402 201 PELLRAAAALARELGLPL-HTHLA--ETRDEVEWVLEL----YGKRPVEY-------LDELGLLGPRTLLahCVHLTDEE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 301 hqevlWRGLRNNELQVVstdHCPFC--FSGqkeMGRGDFSK-----IPNGM----PGVEHRMDLL--------HQAVVDG 361
Cdd:COG0402 267 -----IALLAETGASVA---HCPTSnlKLG---SGIAPVPRllaagVRVGLgtdgAASNNSLDMFeemrlaalLQRLRGG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 362 H---LSRRRWVEIACASPARMFGLYPKKGTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYEgrrvtGQVRTVLSRG 438
Cdd:COG0402 336 DptaLSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHLAPLHDPLSALVYAADG-----RDVRTVWVAG 410
|
....*.
gi 664099816 439 VPVIED 444
Cdd:COG0402 411 RVVVRD 416
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
1-460 |
2.42e-14 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 75.21 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 1 MSRTVIHGGLVV--TASDEIHADVLIEGGRIAALAAHGTDAATswsadRRIDATGMYVLPGGVDAHTHmempfggtYAAD 78
Cdd:COG3653 1 MFDLLIRGGTVVdgTGAPPFRADVAIKGGRIVAVGDLAAAEAA-----RVIDATGLVVAPGFIDIHTH--------YDLQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 79 TFETGTRAAA-WGGTTTIV----------------DFAIQSMGR--SLREGLD-TWH-------AKADGRCAVDYGFHMI 131
Cdd:COG3653 68 LLWDPRLEPSlRQGVTTVVmgncgvsfapvrpedrDRLIDLMEGveGIPEGLDwDWEsfgeyldALERRGLGVNVASLVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 132 LSDV------------NESSLKEMDRLVAEGV--------TSfklfMAYPGVFYSDDGRILRAMQRASGNGGLVMMHaen 191
Cdd:COG3653 148 HGTLrayvmglddrppTPEELARMRALLREAMeagalglsTG----LIYVPGTYASTDELVALAKVVAEYGGVYQSH--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 192 giaidvlveqalaegrtdPRYHGDVRKVALEAeathrAVQLARVAGAPLYVVHVSA---------DEAVDEIAAARHKGL 262
Cdd:COG3653 221 ------------------MRDEGDGLLEAVDE-----LIRIGREAGVPVHISHLKAagkpnwgkaDEVLALIEAARAEGL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 263 PVFGETCPqYLFLSTD-------------------NLAEP----------------------GFEGAKYVCSTPLRP--- 298
Cdd:COG3653 278 DVTADVYP-YPAGSTGlgallppwaaagglderlaRLRDPatrariraeieeglpdnllgrgGWDNILISDSPPNEPlvg 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 299 -----------REHQEVLWRGLRNNELQVVSTDHCpFCFSGQKEMGRGDFSKI-----PNGMPgveH-RM-----DLLHQ 356
Cdd:COG3653 357 kslaeiaaergVDPADAALDLLLEEDGRVLIVYFI-MSEEDVRELLRHPWVMIgsdggLGGKA---HpRAygtfpRVLGH 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 357 AVVD-GHLSRRRWVEIACASPARMFGLyPKKGTIAPGADADVVIYDPgaeQTISaethhmavDYSAYE--GRRVTGqVRT 433
Cdd:COG3653 433 YVRErGVLSLEEAVRKLTSLPADRLGL-KDRGLLRPGYRADLVVFDP---ATLA--------DRATFDlpAQRADG-IRA 499
|
570 580
....*....|....*....|....*..
gi 664099816 434 VLSRGVPVIEDRAYVGhAGHGTYLPRG 460
Cdd:COG3653 500 VIVNGVVVVEDGKPTG-ARPGRVLRGG 525
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
5-97 |
1.13e-13 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 72.12 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 5 VIHGGLVVTASDEIHA--DVLIEGGRIAALAAHGTDAAtswsADRRIDATGMYVLPGGVDAHTHM--EMPFGGTYAAD-T 79
Cdd:COG3964 3 LIKGGRVIDPANGIDGvmDIAIKDGKIAAVAKDIDAAE----AKKVIDASGLYVTPGLIDLHTHVfpGGTDYGVDPDGvG 78
|
90
....*....|....*...
gi 664099816 80 FETgtraaawgGTTTIVD 97
Cdd:COG3964 79 VRS--------GVTTVVD 88
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
53-399 |
4.66e-13 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 70.56 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 53 GMYVLPGGVDAHTHM---EMPFGGTYAadtfeTGTRAAAWGGTTTIVDFA-----IQSMGRsLREGLDTWHAKAdgrcAV 124
Cdd:PRK00369 42 GTLILPGAIDLHVHLrglKLSYKEDVA-----SGTSEAAYGGVTLVADMPntippLNTPEA-ITEKLAELEYYS----RV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 125 DYGfhmILSDVNEsSLKEMDRLvaeGVTSFKLfmaypgvfYSDDGRILRAMQRASGNGGLVMMHAEngiaidvlVEQALA 204
Cdd:PRK00369 112 DYF---VYSGVTK-DPEKVDKL---PIAGYKI--------FPEDLEREETFRVLLKSRKLKILHPE--------VPLALK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 205 EGRtdpryhGDVRKVALEAEATHRAVQLARVagaplYVVHVSADEAVdeiAAARHKGLPVfgETCPQYLFLstDNLAEPG 284
Cdd:PRK00369 169 SNR------KLRRNCWYEIAALYYVKDYQNV-----HITHASNPRTV---RLAKELGFTV--DITPHHLLV--NGEKDCL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 285 FEgakyvCSTPLRPREHQEVLWRGLrnNELQVVSTDHCPFCfSGQKEMgrgDFSKIPNGMPGVEHRMDLLHQAVVDGHLS 364
Cdd:PRK00369 231 TK-----VNPPIRDINERLWLLQAL--SEVDAIASDHAPHS-SFEKLQ---PYEVCPPGIAALSFTPPFIYTLVSKGILS 299
|
330 340 350
....*....|....*....|....*....|....*
gi 664099816 365 RRRWVEIACASPARMFGLypKKGTIAPGADADVVI 399
Cdd:PRK00369 300 IDRAVELISTNPARILGI--PYGEIKEGYRANFTV 332
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
4-448 |
1.36e-11 |
|
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: 66.07 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVVTASDE---IHADVLIEGGRIAALAAhgTDAATSWSADRRIDATGMYVLPGGVDAHTHMEMPFGGTYAAD-- 78
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGP--ALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDlp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 79 -------------------TFETGTRAA----AWGGTTTIVDfaiqsMGRSLREGLdtwhAKAdgrcAVDYGFHMILS-- 133
Cdd:cd01298 79 lmewlkdliwplerllteeDVYLGALLAlaemIRSGTTTFAD-----MYFFYPDAV----AEA----AEELGIRAVLGrg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 134 --DVNESSLKEMDRLVAEgvtSFKLFMAYPGvfySDDGRIlRAMqrasgngglVMMHAENGIAIDVLVEqalaegrtdpr 211
Cdd:cd01298 146 imDLGTEDVEETEEALAE---AERLIREWHG---AADGRI-RVA---------LAPHAPYTCSDELLRE----------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 212 yhgdvrkvaleaeathrAVQLARVAGAPLYvVHVSadEAVDEIAAARHKglpvFGETCPQYlflstdnLAEPGFEGAKYV 291
Cdd:cd01298 199 -----------------VAELAREYGVPLH-IHLA--ETEDEVEESLEK----YGKRPVEY-------LEELGLLGPDVV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 292 C--STPLRPREHQEVLWRGlrnnelqvVSTDHCPfcFSGQKeMGRGdFSKIP----NGMP---GV-------------EH 349
Cdd:cd01298 248 LahCVWLTDEEIELLAETG--------TGVAHNP--ASNMK-LASG-IAPVPemleAGVNvglGTdgaasnnnldmfeEM 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 350 RMDLLHQAVVDG---HLSRRRWVEIACASPARMFGLyPKKGTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYegrr 426
Cdd:cd01298 316 RLAALLQKLAHGdptALPAEEALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYSAN---- 390
|
490 500
....*....|....*....|..
gi 664099816 427 vTGQVRTVLSRGVPVIEDRAYV 448
Cdd:cd01298 391 -GGDVDTVIVNGRVVMEDGELL 411
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
1-444 |
1.69e-11 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 66.26 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 1 MSRTVIHGGLVV---TASDEIhADVLIEGGRIAALaahGTDAATswsADRRIDATGMYVLPGGVDAHTHmempfGGTYAA 77
Cdd:PRK09061 18 PYDLVIRNGRVVdpeTGLDAV-RDVGIKGGKIAAV---GTAAIE---GDRTIDATGLVVAPGFIDLHAH-----GQSVAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 78 DtfetgtRAAAWGGTTTIVDFAIQSMgrslreGLDTWHAKADGRC-AVDYGFH--------MILSDVNESSLKEmDRLVA 148
Cdd:PRK09061 86 Y------RMQAFDGVTTALELEAGVL------PVARWYAEQAGEGrPLNYGASvgwtpariAVLTGPQAEGTIA-DFGKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 149 EGVTSFKLFMAYPGVFysddGRILRAMQRASGNGGL---VMMHAENGIAIDVLVEQALAEGRTDPRYHGDVRKVAL---- 221
Cdd:PRK09061 153 LGDPRWQERAATPAEL----AEILELLEQGLDEGALgigIGAGYAPGTGHKEYLELARLAARAGVPTYTHVRYLSNvdpr 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 222 -EAEATHRAVQLARVAGAPLYVVHVS------ADEAVDEIAAARHKGLPVFGETCPqYLFLSTDNLA---EPGF------ 285
Cdd:PRK09061 229 sSVDAYQELIAAAAETGAHMHICHVNstslrdIDRCLALVEKAQAQGLDVTTEAYP-YGAGSTVVGAaffDPGWlermgl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 286 ------------------EGAKYVCSTPLRP----------REHQEVLWRGLRnNELQVVSTDHCPFCFSGQKemgRGDF 337
Cdd:PRK09061 308 gygslqwvetgerlltreELAKLRANDPGGLvlihfldednPRDRALLDRSVL-FPGAAIASDAMPWTWSDGT---VYEG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 338 SKIPNGMPGVEHRMDLLHQAVVDGHLSRRR----WVEI--ACAS-PARMFGLY----PKKGTIAPGADADVVIYDPgaeQ 406
Cdd:PRK09061 384 DAWPLPEDAVSHPRSAGTFARFLREYVRERkalsLLEAirKCTLmPAQILEDSvpamRRKGRLQAGADADIVVFDP---E 460
|
490 500 510
....*....|....*....|....*....|....*....
gi 664099816 407 TISaethhmavDYSAYE-GRRVTGQVRTVLSRGVPVIED 444
Cdd:PRK09061 461 TIT--------DRATFEdPNRPSEGVRHVLVNGVPVVSN 491
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-92 |
8.32e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 63.87 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 1 MSRTVIHGGLVVTASDEIH----ADVLIEGGRIAALAAHgTDAAtswsADRRIDATGMYVLPGGVDAHTHmempfggtya 76
Cdd:PRK08204 1 MKRTLIRGGTVLTMDPAIGdlprGDILIEGDRIAAVAPS-IEAP----DAEVVDARGMIVMPGLVDTHRH---------- 65
|
90
....*....|....*.
gi 664099816 77 adTFETGTRAAAWGGT 92
Cdd:PRK08204 66 --TWQSVLRGIGADWT 79
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
22-438 |
1.32e-10 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 62.80 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 22 VLIEGGRIaalaahgTDAATSWSADRRIDATGMYVLPGGVDAHTHmemPFGGTYAADTFETGTRAAAWGGTTTIV----- 96
Cdd:PRK08417 1 IRIKDGKI-------TEIGSDLKGEEILDAKGKTLLPALVDLNVS---LKNDSLSSKNLKSLENECLKGGVGSIVlypds 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 97 ----------DFaIQSMGRSLREGL-DTWHAKA-DGRcavdygfhmiLSDVneSSLKEMDrlvAEGvtsfkLFMAypgvf 164
Cdd:PRK08417 71 tpaidneialEL-INSAQRELPMQIfPSIRALDeDGK----------LSNI--ATLLKKG---AKA-----LELS----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 165 ySD-DGRILRA-MQRASGNGGLVMMHAENGIAIDVLVeqaLAEGRTD--------PRYhGDVRKVALEAEathravqLAR 234
Cdd:PRK08417 125 -SDlDANLLKViAQYAKMLDVPIFCRCEDSSFDDSGV---MNDGELSfelglpgiPSI-AETKEVAKMKE-------LAK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 235 VAGAPLYVVHVSADEAVDEIAAARHKGLPVFGETCPQYLFLStDNLAEPGFEGAKYvcSTPLRPREHQEVLWRGLRNNEL 314
Cdd:PRK08417 193 FYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILD-DSACENFNTAAKL--NPPLRSKEDRLALLEALKEGKI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 315 QVVSTDHCPFCFSgQKEMGrgdFSKIPNGMPGVEHRMDLLHQAVV-DGHLSRRRWVEIACASPARMFGLypKKGTIAPGA 393
Cdd:PRK08417 270 DFLTSLHSAKSNS-KKDLA---FDEAAFGIDSICEYFSLCYTYLVkEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGK 343
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 664099816 394 DADVVIYDPgaEQTISAEThhmavDYSAYEGRRVTGQVRTVLSRG 438
Cdd:PRK08417 344 EADLVLFDP--NESTIIDD-----NFSLYSGDELYGKIEAVIIKG 381
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-97 |
2.17e-10 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 62.18 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 5 VIHGGLVVTASDEIHA--DVLIEGGRIAALAAHGTDAAtswsADRRIDATGMYVLPGGVDAHTHMEmpFGGT---YAADT 79
Cdd:PRK09237 2 LLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQ----AKKVIDLSGLYVSPGWIDLHVHVY--PGSTpygDEPDE 75
|
90
....*....|....*...
gi 664099816 80 FetGTRAaawgGTTTIVD 97
Cdd:PRK09237 76 V--GVRS----GVTTVVD 87
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
61-329 |
4.88e-10 |
|
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: 60.04 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 61 VDAHTHMEMP----------------FGGTYAADTFETGTRAAAWGGTTTIVDFA----IQSMGRSLREGLDTWHAKADG 120
Cdd:cd01292 2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGstppPTTTKAAIEAVAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 121 RCAVDYGFH----MILSDVNESSLKEMDRLVAEGVTSFKLFMAYPGVFYSDDgRILRAMQRASGNGGLVMMHAENGIAID 196
Cdd:cd01292 82 RVVLGLGIPgvpaAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDE-SLRRVLEEARKLGLPVVIHAGELPDPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 197 VLVEQALAEGRTDPRyhgdvrkvaleaeathravqlarvagapLYVVHVSADEAVDEIAAARHkglPVFGETCPQYLFLS 276
Cdd:cd01292 161 RALEDLVALLRLGGR----------------------------VVIGHVSHLDPELLELLKEA---GVSLEVCPLSNYLL 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 664099816 277 TdnlaepgfegakyvcstplRPREHQEVLWRGLRNNELQVVSTDHCPFCFSGQ 329
Cdd:cd01292 210 G-------------------RDGEGAEALRRLLELGIRVTLGTDGPPHPLGTD 243
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-65 |
2.70e-09 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 58.65 E-value: 2.70e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664099816 1 MSRTVIHGGLVVTASDEIHADVLIEGGRIAALAAHGTDAATSwsadrrIDATGMYVLPGGVDAHT 65
Cdd:PRK15446 1 MMEMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA------IDAEGDYLLPGLVDLHT 59
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
4-96 |
7.66e-09 |
|
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: 57.20 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVVTASDEIHADVLIEGGRIAALAAHGTDAATswsaDRRIDATGMYVLPGGVDAHTHmempfGG------TYAA 77
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA----DEIIDLKGQYLVPGFIDIHIH-----GGggadfmDGTA 71
|
90
....*....|....*....
gi 664099816 78 DTFETGTRAAAWGGTTTIV 96
Cdd:cd00854 72 EALKTIAEALAKHGTTSFL 90
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-96 |
1.49e-08 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 57.03 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 4 TVIHGGLVV-TASDEIH-ADVLIEGGRIAALAAHGTDAAtswsadRRIDATGMYVLPGGVDAHTHME--M--PFGgtYAa 77
Cdd:COG1001 7 LVIKNGRLVnVFTGEILeGDIAIAGGRIAGVGDYIGEAT------EVIDAAGRYLVPGFIDGHVHIEssMvtPAE--FA- 77
|
90
....*....|....*....
gi 664099816 78 dtfetgtRAAAWGGTTTIV 96
Cdd:COG1001 78 -------RAVLPHGTTTVI 89
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
2-174 |
1.87e-08 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 56.55 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 2 SRTVIHGGLVVT--ASDEI-HADVLIEGGRIAALAahgtDAATSWSADRRIDATGMYVLPGGVDAHTHMEMPFGGTYAAD 78
Cdd:PRK07228 1 MTILIKNAGIVTmnAKREIvDGDVLIEDDRIAAVG----DRLDLEDYDDHIDATGKVVIPGLIQGHIHLCQTLFRGIADD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 79 T------------FETG-----TRAAAW--------GGTTTIVDF--------AIQSMGRSLREGLdtwhakaDGRCAVD 125
Cdd:PRK07228 77 LelldwlkdriwpLEAAhdaesMYYSALlgigelieSGTTTIVDMesvhhtdsAFEAAGESGIRAV-------LGKVMMD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 664099816 126 YGfhmilSDVNESSLKEMDRLVAEgvtSFKLFMAYPGvfySDDGRILRA 174
Cdd:PRK07228 150 YG-----DDVPEGLQEDTEASLAE---SVRLLEKWHG---ADNGRIRYA 187
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
22-401 |
1.96e-08 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 56.11 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 22 VLIEGGRIAALAAHGTDAATSWSADRRIDATGMYVLPGGVDAHTHmeMPFGGtYAADTFE---TGTR----AAAWGGttt 94
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTH--LVFAG-DRVDEFAarlAGASyeeiLAAGGG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 95 ivdfaIQSMGRSLREGlDTWHAKAdgrcavdygfhmilsdvneSSLKEMDRLVAEGVTSFKLFMAYpGVFYSDDGRILRA 174
Cdd:cd01296 75 -----ILSTVRATRAA-SEDELFA-------------------SALRRLARMLRHGTTTVEVKSGY-GLDLETELKMLRV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 175 MQRASGNGGL------VMMHA------ENGIAIDVLVEQALAEGRTDPRYHG-DV--RKVALEAEATHRAVQLARVAGAP 239
Cdd:cd01296 129 IRRLKEEGPVdlvstfLGAHAvppeykGREEYIDLVIEEVLPAVAEENLADFcDVfcEKGAFSLEQSRRILEAAKEAGLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 240 lyvVHVSADEaVDEIAAArhkglpvfgETCPQYLFLSTDNLAEPGFEGAK-----------------YVCSTPLRPREhq 302
Cdd:cd01296 209 ---VKIHADE-LSNIGGA---------ELAAELGALSADHLEHTSDEGIAalaeagtvavllpgtafSLRETYPPARK-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 303 evlwrgLRNNELQV-VSTDHCPfcfsgqkemGRGDFSKIPNGMpgvehrmdllHQAVVDGHLSRRRWVEIACASPARMFG 381
Cdd:cd01296 274 ------LIDAGVPVaLGTDFNP---------GSSPTSSMPLVM----------HLACRLMRMTPEEALTAATINAAAALG 328
|
410 420
....*....|....*....|
gi 664099816 382 LYPKKGTIAPGADADVVIYD 401
Cdd:cd01296 329 LGETVGSLEVGKQADLVILD 348
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
21-97 |
8.50e-08 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 53.87 E-value: 8.50e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664099816 21 DVLIEGGRIAALAAHGTDAAtswsADRRIDATGMYVLPGGVDAHTHM--EMPFGGTYAadtfetgTRAAAWGGTTTIVD 97
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPA----ATQIVDAGGCYVSPGWIDLHVHVyqGGTRYGDRP-------DMIGVKSGVTTVVD 68
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
21-402 |
1.33e-07 |
|
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: 53.55 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 21 DVLIEGGRIAALA----AHGTDAATSwsadrrIDATGMYVLPGGVDAHTHMEMPFG-GTYAADTFETGTRAAAWGGTTTI 95
Cdd:cd01308 19 DILIAGGKILAIEdqlnLPGYENVTV------VDLHGKILVPGFIDQHVHIIGGGGeGGPSTRTPEVTLSDLTTAGVTTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 96 VD-FAIQSMGRSLREGLdtwhAKADGrcavdygfhmilsdvnesslkemdrLVAEGVTSFklfmAYPGVFYSDDGRILRA 174
Cdd:cd01308 93 VGcLGTDGISRSMEDLL----AKARA-------------------------LEEEGITCF----VYTGSYEVPTRTITGS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 175 MQRasgngGLVMMHAENGIAidvlvEQALAEGRTD-PRYHgdvrkvaleaEATHRAVQlARVAG-----APLYVVHVSAD 248
Cdd:cd01308 140 IRK-----DLLLIDKVIGVG-----EIAISDHRSSqPTVE----------ELARIAAE-ARVGGllggkAGIVHIHLGDG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 249 EavdeiaaarhKGL-PVFG--ETC--PQYLFLST-----DNLAEPGFEGAK--------------YVCSTPLRPrehQEV 304
Cdd:cd01308 199 K----------RALsPIFEliEETeiPITQFLPThinrtAPLFEQGVEFAKmggtidltssidpqFRKEGEVRP---SEA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 305 LWRGLRNNelqvVSTDHCPFCFSGQKEMGRGDFSKIPNGM--PGVEHRMDLLHQAVVDGHLSRRRWVEIACASPARMFGL 382
Cdd:cd01308 266 LKRLLEQG----VPLERITFSSDGNGSLPKFDENGNLVGLgvGSVDTLLREVREAVKCGDIPLEVALRVITSNVARILKL 341
|
410 420
....*....|....*....|
gi 664099816 383 YpKKGTIAPGADADVVIYDP 402
Cdd:cd01308 342 R-KKGEIQPGFDADLVILDK 360
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
1-129 |
1.89e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 53.22 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 1 MSRTVIHGGLVVTA-SDEI-HADVLIEGGRIAALAAhgtdaATSWSADRRIDATGMYVLPGGVDAHTHMEMPFGGTYAAD 78
Cdd:PRK06038 1 MADIIIKNAYVLTMdAGDLkKGSVVIEDGTITEVSE-----STPGDADTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 79 ------------------TFE---TGTRAAAW----GGTTTIVDFAI----------------------------QSMGR 105
Cdd:PRK06038 76 lplaewlndhiwpaeaklTAEdvyAGSLLACLemikSGTTSFADMYFymdevakaveesglraalsygmidlgddEKGEA 155
|
170 180
....*....|....*....|....*..
gi 664099816 106 SLREGLD---TWHAKADGRCAVDYGFH 129
Cdd:PRK06038 156 ELKEGKRfvkEWHGAADGRIKVMYGPH 182
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
5-96 |
2.03e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 52.79 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 5 VIHGGLVVTASDEIH-ADVLIEGGRIAALAAHGTDAATswsadrRIDATGMYVLPGGVDAHTH-------MEmpfgGTya 76
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPGAEPDAE------VIDLGGGYLAPGFIDLHVHggggvdfMD----GT-- 68
|
90 100
....*....|....*....|
gi 664099816 77 ADTFETGTRAAAWGGTTTIV 96
Cdd:COG1820 69 PEALRTIARAHARHGTTSFL 88
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
1-69 |
3.12e-07 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 52.49 E-value: 3.12e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664099816 1 MSRTVIHGGLVVTASDE--IHADVLIEGGRIAALaahGTDA-ATSW--SADRRIDATGMYVLPGGVDAHTHMEM 69
Cdd:COG1574 7 AADLLLTNGRIYTMDPAqpVAEAVAVRDGRIVAV---GSDAeVRALagPATEVIDLGGKTVLPGFIDAHVHLLG 77
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
2-66 |
3.67e-07 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 52.50 E-value: 3.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664099816 2 SRTVIHGGLVVTASDEIH---ADVLIEGGRIAalaahgtDAATSWSADRRIDATGMYVLPGGVDAHTH 66
Cdd:COG1229 1 MELIIKNGRVYDPANGIDgevMDIAIKDGKIV-------EEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
1-67 |
1.59e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 50.24 E-value: 1.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 664099816 1 MSRTVIHGGLVVT--ASDEIHAD--VLIEGGRIAALAAHGTDAATswsADRRIDATGMYVLPGGVDAHTHM 67
Cdd:PRK08203 1 TTLWIKNPLAIVTmdAARREIADggLVVEGGRIVEVGPGGALPQP---ADEVFDARGHVVTPGLVNTHHHF 68
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
6-401 |
1.94e-06 |
|
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: 49.94 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 6 IHGGLVVTASDEIhADVLIEGGRIAALAAHGTDAAtswsADRRIDATGMYVLPGGVDAHTHMempfggtyaaDTFETGTR 85
Cdd:cd01293 2 LRNARLADGGTAL-VDIAIEDGRIAAIGPALAVPP----DAEEVDAKGRLVLPAFVDPHIHL----------DKTFTGGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 86 AAAWGGTTTIVDFAIQSMGRSLREGLDTW-HAKADGRCAVDYGFHMILSDVN------ESSLKEM--------DRLVAEG 150
Cdd:cd01293 67 WPNNSGGTLLEAIIAWEERKLLLTAEDVKeRAERALELAIAHGTTAIRTHVDvdpaagLKALEALlelreewaDLIDLQI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 151 VtsfklfmAYP--GVFYSDDGRILraMQRASGNGGLVM---MHAENGIAIDVLVEQ--ALAEGR-------TDPRYHGDV 216
Cdd:cd01293 147 V-------AFPqhGLLSTPGGEEL--MREALKMGADVVggiPPAEIDEDGEESLDTlfELAQEHgldidlhLDETDDPGS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 217 RKVALEAEATHRAVQLARVAGAPLYVVHVSADEAVDEIAAA-RHKGLPVFgeTCPQylflstdnlaepgfegakyvCSTP 295
Cdd:cd01293 218 RTLEELAEEAERRGMQGRVTCSHATALGSLPEAEVSRLADLlAEAGISVV--SLPP--------------------INLY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 296 LRPREHQEVLWRGL-RNNELQ------VVSTDHC--PFCfsgqkEMGRGDfskipngMpgvehrMDLLHQAVVDGHLsrR 366
Cdd:cd01293 276 LQGREDTTPKRRGVtPVKELRaagvnvALGSDNVrdPWY-----PFGSGD-------M------LEVANLAAHIAQL--G 335
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 664099816 367 RWVEIACA------SPARMFGLypKKGTIAPGADADVVIYD 401
Cdd:cd01293 336 TPEDLALAldlitgNAARALGL--EDYGIKVGCPADLVLLD 374
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
5-97 |
2.10e-06 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 49.76 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 5 VIHGGLV--VTASDEIHADVLIEGGRIAALAAHGtdaatSWSADRRIDATGMYVLPGGVDAHTHmeMPFGGTyaadtfET 82
Cdd:PRK12394 6 LITNGHIidPARNINEINNLRIINDIIVDADKYP-----VASETRIIHADGCIVTPGLIDYHAH--VFYDGT------EG 72
|
90
....*....|....*...
gi 664099816 83 GTRAAAW---GGTTTIVD 97
Cdd:PRK12394 73 GVRPDMYmppNGVTTVVD 90
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
5-69 |
3.00e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 49.41 E-value: 3.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664099816 5 VIHGGLVVTASDE--IHADVLIEGGRIAALAAHGTDaatswSADRRIDATGMYVLPGGVDAHTHMEM 69
Cdd:PRK08393 4 LIKNGYVIYGENLkvIRADVLIEGNKIVEVKRNINK-----PADTVIDASGSVVSPGFINAHTHSPM 65
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
11-400 |
3.69e-06 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 49.21 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 11 VVTASDEIHADVLIEGGRIAALAAHGTDAATSwsadRRIDATGMYVLPGGVDAHTHMempfggtyaaDTFETGTRAAAWG 90
Cdd:PRK07583 32 GDTLEGLVLVDIEIADGKIAAILPAGGAPDEL----PAVDLKGRMVWPCFVDMHTHL----------DKGHIWPRSPNPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 91 GTttiVDFAIQSMGRSlREGldtwHAKADG---------RCAVDYGFHMI---------LSDVNESSLKEM-----DRLV 147
Cdd:PRK07583 98 GT---FPGALDAVTAD-REA----HWSAEDlyrrmefglRCAYAHGTSAIrthldsfapQAAISWEVFAELreawaGRIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 148 AEGVTSFklfmayPGVFYSDD-GRILRAMQRASGN--GGLVMMHAENGIAIDVLVEQALAEG-----RTDPRYHGDVRKV 219
Cdd:PRK07583 170 LQAVSLV------PLDAYLTDaGERLADLVAEAGGllGGVTYMNPDLDAQLDRLFRLARERGldldlHVDETGDPASRTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 220 ALEAEATHR---------------AVQ--------LARVAGAPLYVVhvsadeavdeiaaarhkGLPvfgeTCPQYLfls 276
Cdd:PRK07583 244 KAVAEAALRngfegkvtcghccslAVQpeeqaqatIALVAEAGIAIV-----------------SLP----MCNLYL--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 277 TDNlaEPGfegakyvcSTPlrprehqevLWRG------LRNNELQV-VSTDHC--PFcfsgqkeMGRGDfskipngmpgv 347
Cdd:PRK07583 300 QDR--QPG--------RTP---------RWRGvtlvheLKAAGIPVaVASDNCrdPF-------YAYGD----------- 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 664099816 348 eHRM-DLLHQAVVDGHL--SRRRWVEIACASPARMFGLyPKKGTIAPGADADVVIY 400
Cdd:PRK07583 343 -HDMlEVFREAVRILHLdhPYDDWPAAVTTTPADIMGL-PDLGRIAVGAPADLVLF 396
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
49-427 |
6.15e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 48.30 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 49 IDATGMYVLPGGVDAHTHMEMPF--------------------------------GGTYAADTFETGTRAAAWGGTT--- 93
Cdd:pfam07969 3 IDAKGRLVLPGFVDPHTHLDGGGlnlrelrlpdvlpnavvkgqagrtpkgrwlvgEGWDEAQFAETRFPYALADLDEvap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 94 ----------TIVDFAIQSMGRSLREGLDTWHAK-------ADGRCAV----DYGFHMILSDVNESSLKEMDRLVAE--- 149
Cdd:pfam07969 83 dgpvllralhTHAAVANSAALDLAGITKATEDPPggeiardANGEGLTgllrEGAYALPPLLAREAEAAAVAAALAAlpg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 150 -GVTSfkLFMAYPGVFYSDDGRILRAMQRASGNGGLVMMHAENGI----------AIDVLVEQALAEGR---TDPRYHGD 215
Cdd:pfam07969 163 fGITS--VDGGGGNVHSLDDYEPLRELTAAEKLKELLDAPERLGLphsiyelrigAMKLFADGVLGSRTaalTEPYFDAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 216 VRKVALEAEAT-HRAVQLARVAGAPLYVvHVSADEAVD----EIAAARHK---GLPVFGETCpQYLFLSTDNLAEP---- 283
Cdd:pfam07969 241 GTGWPDFEDEAlAELVAAARERGLDVAI-HAIGDATIDtaldAFEAVAEKlgnQGRVRIEHA-QGVVPYTYSQIERvaal 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 284 ----------GFEGAKYVCSTPLRPREHQEVLWRGLRNNELQVVSTDHCPFCfsgqkemgrgdfskIPNGMPGVEH---- 349
Cdd:pfam07969 319 ggaagvqpvfDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVG--------------PFDPWPRIGAavmr 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664099816 350 -RMDLLHQAVVDGHLSRRRWVEIACASPARMFGLYPKKGTIAPGADADVVIYDPGAEQTISAETHHMAVDYSAYEGRRV 427
Cdd:pfam07969 385 qTAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDGRVV 463
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
6-444 |
1.26e-05 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 47.41 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 6 IHGGLVVTASDEIHA---DVLIEGGRIaalaahgTDAATSWSADRRIDATGMYVLPGGVDAHTHM--------------- 67
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDGKI-------VESSSGAKPAKVIDASGKVVMAGGVDMHSHIaggkvnvgrilrped 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 68 ----EMPFGGTYAA-------DTFETGTRAAAWGGTTTIVDFAIQSMGRSLREGLDTWHAKADGRCAVDYGFHMILSDVN 136
Cdd:cd01304 74 hrrdPVPKGALRRAgvgfsvpSTLATGYRYAEMGYTTAFEAAMPPLNARHTHEEMADTPILDKGAYPLLGNNWFVLEYLR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 137 ESSLKEMDRLVAEGVTSFKLF---MAYPG----------VFYSDD---------GRILRAMQRASGNGGL---VMMHAEN 191
Cdd:cd01304 154 DGDMEKLAAYVAWTLKASKGYgikVVNPGgteawgwgqnVLSLDDpvpyfditpREILKGLAEANEELGLphsIHVHCNN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 192 -GIA--IDVLVEQ-ALAEG-RTDPR---YHgdvrkvaleaeATHraVQLARVAGAPLYVVHVSADEAVDEIAAARH---- 259
Cdd:cd01304 234 lGVPgnYETTLETmKAAEGvKPDPRrqvLH-----------LTH--VQFHSYGGTSWRDFESGAERIADYVNANDHvtid 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 260 KGLPVFGETCPqylfLSTDNLAE---PGFEGAKYVCS----------TPLRPREHQEV---LWR-GLR-----NNELQVV 317
Cdd:cd01304 301 VGQVIFGETTT----MTGDGPMQfdlHGLTGLKWVNCdieletgsgvVPFIYSPKNPVnalQWAiGLElflliDDPWKVI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 318 -STDH---CPFC-------FSGQKEMGRGDFSKIPngmPGVEHRMDLlhqAVVDGHLSrrrWVEIAC---ASPARMFGLy 383
Cdd:cd01304 377 lTTDHpngGPFTrypriiaWLMSKKFRAEEIATLH---KWAQDRSAL---PGIDREYS---LYEIAImtrAGPAKLLGL- 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664099816 384 PKKGTIAPGADADVVIYDPGAEQtisaethhmaVDYSAYEGR-RVTGQVRTVLSRGVPVIED 444
Cdd:cd01304 447 SDKGHLGVGADADIAIYDDDPDQ----------VDPSDYEKVeKAFSRAAYVLKDGEIVVKD 498
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
348-411 |
1.63e-05 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 47.11 E-value: 1.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664099816 348 EHRMDLLHQAVVD----GHLSRR-RWVEIAC---ASPARMFGLyPKKGTIAPGADADVVIYDPGAEQTISAE 411
Cdd:COG1229 406 DEMLAKLHPWAAArstlASIDREySLYEIAImtrAGPAKALGL-ADRGHLGVGADADIAIYDINPDDKDYED 476
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
16-96 |
2.60e-05 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 46.75 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664099816 16 DEIHADVLIEGGRIAALAAHGTDAAtswsADRRIDATGMYVLPGGVDAHTHMEmpfGGTYAADTFETGTRAAawgGTTTI 95
Cdd:PRK10027 46 GEISGPIVIKGRYIAGVGAEYADAP----ALQRIDARGATAVPGFIDAHLHIE---SSMMTPVTFETATLPR---GLTTV 115
|
.
gi 664099816 96 V 96
Cdd:PRK10027 116 I 116
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
20-73 |
2.97e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 46.08 E-value: 2.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 664099816 20 ADVLIEGGRIAALAAHGTDAAtswsADRRIDATGMYVLPGGVDAHTHMEMPFGG 73
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPP----GAEVEDGGGALALPGLVDGHIHLDKTFWG 66
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
351-402 |
1.42e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 43.93 E-value: 1.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 664099816 351 MDLLHQAVVDGHLSRRRWVEIACASPARMFGLYPKKGTIAPGADADVVIYDP 402
Cdd:COG1820 310 DDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDD 361
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
20-68 |
1.51e-04 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 43.85 E-value: 1.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 664099816 20 ADVLIEGGRIAALAAhGTDAatswSADRRIDATGMYVLPGGVDAHTHME 68
Cdd:PRK07572 18 IDIGIAGGRIAAVEP-GLQA----EAAEEIDAAGRLVSPPFVDPHFHMD 61
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
17-69 |
1.67e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 43.75 E-value: 1.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 664099816 17 EIHAdVLIEGGRIAALAAHgTDAATSWSADRRIDATGMYVLPGGVDAHTHMEM 69
Cdd:PRK09045 27 EDHA-VAIRDGRIVAILPR-AEARARYAAAETVELPDHVLIPGLINAHTHAAM 77
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
21-69 |
2.68e-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: 43.45 E-value: 2.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 664099816 21 DVLIEGGRIAALaahGTDA---ATSWSADRRIDATGMYVLPGGVDAHTHMEM 69
Cdd:cd01300 1 AVAVRDGRIVAV---GSDAeakALKGPATEVIDLKGKTVLPGFIDSHSHLLL 49
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-69 |
1.20e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 41.02 E-value: 1.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664099816 1 MSrTVIHGGLVVTASDE---IHADVLIEGGRIAALaahGTDAAtswSADRRIDATGMYVLPGGVDAHTHMEM 69
Cdd:PRK06380 1 MS-ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYV---GDVNE---EADYIIDATGKVVMPGLINTHAHVGM 65
|
|
| |
