|
Name |
Accession |
Description |
Interval |
E-value |
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
2-492 |
5.27e-108 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 331.38 E-value: 5.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 2 LLLHNARILDLtDGSTGKPTDVLLSD-RVLALGPEAQQQAH-SARVRSIDLGGRLLMPGLWDEHVHVGQWALASRRFLVS 79
Cdd:COG1574 10 LLLTNGRIYTM-DPAQPVAEAVAVRDgRIVAVGSDAEVRALaGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 80 QTASCETVLEEVATHVKRSeGSDEPILqGFGFRPSLWGSN--PNARQLDAVTGDRAVILVSADLHSSWCNTAAMRKLGIE 157
Cdd:COG1574 89 GARSLDELLARLRAAAAEL-PPGEWIL-GRGWDESLWPEGrfPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALELAGIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 158 GDR------------------FLREQTSFDVQTQLSQVNPHVLDGWVGSCSTAAARLGITGIRDMEFS-TDVETWLQREA 218
Cdd:COG1574 167 ADTpdpeggeierdadgeptgVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLGpDDLAAYRELAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 219 DGRCPLRVEVSVY--PERLDEAIAQGLATGQapvtdkpGPSRVAMGPLKVIVDGSMSTRTAWCMDSYPAGagPDGAGIDS 296
Cdd:COG1574 247 AGELPLRVVLYLGadDEDLEELLALGLRTGY-------GDDRLRVGGVKLFADGSLGSRTAALLEPYADD--PGNRGLLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 297 VTPEDLVDLINRAKTGNLQCAAHAIGDRAAKEVLNAFE----VTGISGS---IEHAQVLTDADVRRFAALGVRASVQPLH 369
Cdd:COG1574 318 LDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEaaraANGRRDRrhrIEHAQLVDPDDLARFAELGVIASMQPTH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 370 LVDDRDATDVMW-SDRADRCFRFADMVRAGTELALGSDAPVSPVDPWGAIRVAVERTGDRRPSWHPEQALTLSQAITA-- 446
Cdd:COG1574 398 ATSDGDWAEDRLgPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGRGLGPEERLTVEEALRAyt 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 488471957 447 --SAR-----HVT-QVVTGGPGDVIAVAHNPFDLSGDALAGLTSDLTVVGGEVT 492
Cdd:COG1574 478 igAAYaafeeDEKgSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVV 531
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
27-444 |
1.85e-92 |
|
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: 289.59 E-value: 1.85e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 27 DRVLALGPEAQQQAHSAR-VRSIDLGGRLLMPGLWDEHVHVGQWALASRRFLVSQTASCETVLEEVATHVKRSEgsDEPI 105
Cdd:cd01300 7 GRIVAVGSDAEAKALKGPaTEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAP--PGEW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 106 LQGFGFRPSLWGSN--PNARQLDAVTGDRAVILVSADLHSSWCNTAAMRKLGIEGDR------------------FLREQ 165
Cdd:cd01300 85 ILGFGWDESLLGEGryPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITRDTpdppggeivrdadgeptgVLVEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 166 TSFDVQTQLSQVNPHVLDGWVGSCSTAAARLGITGIRDMEFST--DVETWLQREADGRCPLRVEVSVYPERLDEAIAQGL 243
Cdd:cd01300 165 AAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAadDIEAYRRLAAAGELTLRVRVALYVSPLAEDLLEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 244 ATGQAPVTDKpgpsRVAMGPLKVIVDGSMSTRTAWCMDSYpaGAGPDGAGIDSVTPEDLVDLINRAKTGNLQCAAHAIGD 323
Cdd:cd01300 245 GARKNGAGDD----RLRLGGVKLFADGSLGSRTAALSEPY--LDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 324 RAAKEVLNAFE-------VTGISGSIEHAQVLTDADVRRFAALGVRASVQPLHLVDDRDA--TDVMWSDRADRCFRFADM 394
Cdd:cd01300 319 RAVDTVLDALEaalkdnpRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAaeDRRLGEERAKRSYPFRSL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 488471957 395 VRAGTELALGSDAPVSPVDPWGAIRVAVERTGDR-RPSWHPEQALTLSQAI 444
Cdd:cd01300 399 LDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGgGVLGNPEERLSLEEAL 449
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
48-493 |
3.37e-40 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 150.76 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 48 IDLGGRLLMPGLWDEHVHVGQWALASRRFLVSQTASCETVLEEVATHVKrsegsDEPILqGFGFRPSLWGSN--PNARQ- 124
Cdd:pfam07969 3 IDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAVVKGQAGRTPK-----GRWLV-GEGWDEAQFAETrfPYALAd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 125 LDAVTGDRAVILVSADLHSSWCNTAAMRKLGIEGDR-------------------FLREQTsfdvQTQLSQVNPHVLDGW 185
Cdd:pfam07969 77 LDEVAPDGPVLLRALHTHAAVANSAALDLAGITKATedppggeiardangegltgLLREGA----YALPPLLAREAEAAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 186 VGSCSTAAARLGITGIRD---MEFSTDVETWLQREADGrcplrvevSVYPERLDEAIAQGLATGQAPVTDkpgpsrvamG 262
Cdd:pfam07969 153 VAAALAALPGFGITSVDGgggNVHSLDDYEPLRELTAA--------EKLKELLDAPERLGLPHSIYELRI---------G 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 263 PLKVIVDGSMSTRTAWCMDSYpagAGPDGAGIDSVTPEDLVDLINRAKTGNLQCAAHAIGDRAAKEVLNAFEVTGI---- 338
Cdd:pfam07969 216 AMKLFADGVLGSRTAALTEPY---FDAPGTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEklgn 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 339 --SGSIEHAQVL---TDADVRRFAALGVRASVQPLHLVDDRDATDVMWSD-RADRCFRFADMVRAGTELALGSDAPVSPV 412
Cdd:pfam07969 293 qgRVRIEHAQGVvpyTYSQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAeRARGLTPVKELLNAGVKVALGSDAPVGPF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 413 DPWGAIRVAVERTGDRRPSWH-PEQALTLSQAITASARHVTQVV----------TGGPGDVIAVAHNPFDLSGDALAGLT 481
Cdd:pfam07969 373 DPWPRIGAAVMRQTAGGGEVLgPDEELSLEEALALYTSGPAKALgledrkgtlgVGKDADLVVLDDDPLTVDPPAIADIR 452
|
490
....*....|..
gi 488471957 482 SDLTVVGGEVTA 493
Cdd:pfam07969 453 VRLTVVDGRVVY 464
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-76 |
2.67e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 64.98 E-value: 2.67e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488471957 1 MLLLHNARILDLTDGSTGKPTDVLLSD-RVLALGPEAQQQAHSArVRSIDLGGRLLMPGLWDEHVHVGQWALASRRF 76
Cdd:COG1228 9 TLLITNATLVDGTGGGVIENGTVLVEDgKIAAVGPAADLAVPAG-AEVIDATGKTVLPGLIDAHTHLGLGGGRAVEF 84
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
3-68 |
4.17e-06 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 48.93 E-value: 4.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488471957 3 LLHNARILDltDGSTgKPTDVLLSD-RVLALGPEAQQqAHSARVrsIDLGGRLLMPGLWDEHVHVGQ 68
Cdd:COG0044 1 LIKNGRVVD--PGGL-ERADVLIEDgRIAAIGPDLAA-PEAAEV--IDATGLLVLPGLIDLHVHLRE 61
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-74 |
4.35e-06 |
|
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: 49.05 E-value: 4.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488471957 2 LLLHNARILDlTDGSTGKPTDVLL---SDRVLALGPEAQQQAHSARVRSIDLGGRLLMPGLWDEHVHVGQWALASR 74
Cdd:COG0402 2 LLIRGAWVLT-MDPAGGVLEDGAVlveDGRIAAVGPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGL 76
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
2-66 |
2.39e-05 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 46.31 E-value: 2.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488471957 2 LLLHNARILDLTDGsTGKPTDVLLSD-RVLALGPEAQQQAHsarVRSIDLGGRLLMPGLWDEHVHV 66
Cdd:COG3964 2 LLIKGGRVIDPANG-IDGVMDIAIKDgKIAAVAKDIDAAEA---KKVIDASGLYVTPGLIDLHTHV 63
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-66 |
3.40e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 45.96 E-value: 3.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488471957 1 MLLLHNARILDLTDGstGKPTDVLLSD-RVLALGPEAQQQAhsARVrsIDLGGRLLMPGLWDEHVHV 66
Cdd:PRK09357 2 MILIKNGRVIDPKGL--DEVADVLIDDgKIAAIGENIEAEG--AEV--IDATGLVVAPGLVDLHVHL 62
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
2-68 |
1.92e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 43.87 E-value: 1.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488471957 2 LLLHNARILDLTDGSTGkPTDVLLSD-RVLALGPEAQQQAHSARVRSIDLGGRLLMPGLWDEHVHVGQ 68
Cdd:PRK09059 5 ILLANARIIDPSRGLDE-IGTVLIEDgVIVAAGKGAGNQGAPEGAEIVDCAGKAVAPGLVDARVFVGE 71
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
2-66 |
2.87e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 43.55 E-value: 2.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488471957 2 LLLHNARILDLTDGSTgKPTDVLLSDRVLALGPEAQQQAHsarvRSIDLGGRLLMPGLWDEHVHV 66
Cdd:COG1001 7 LVIKNGRLVNVFTGEI-LEGDIAIAGGRIAGVGDYIGEAT----EVIDAAGRYLVPGFIDGHVHI 66
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
2-71 |
3.10e-04 |
|
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: 42.96 E-value: 3.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488471957 2 LLLHNARILDLTDGSTGKPTDVLLSD-RVLALGPEAQQQAHSArVRSIDLGGRLLMPGLWDEHVHVGQWAL 71
Cdd:cd01298 1 ILIRNGTIVTTDPRRVLEDGDVLVEDgRIVAVGPALPLPAYPA-DEVIDAKGKVVMPGLVNTHTHLAMTLL 70
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
2-66 |
4.65e-04 |
|
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: 42.59 E-value: 4.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488471957 2 LLLHNARILDlTDGSTgkPTDVLLSD-RVLALGPEAQQQAHsarVRSIDLGGRLLMPGLWDEHVHV 66
Cdd:cd01314 1 LIIKNGTIVT-ADGSF--KADILIEDgKIVAIGPNLEAPGG---VEVIDATGKYVLPGGIDPHTHL 60
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
2-66 |
8.69e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 41.76 E-value: 8.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488471957 2 LLLHNARILDLTDGsTGKPTDVLLSD-RVLALGPEAQqqAHSARVRsIDLGGRLLMPGLWDEHVHV 66
Cdd:PRK09237 1 LLLRGGRVIDPANG-IDGVIDIAIEDgKIAAVAGDID--GSQAKKV-IDLSGLYVSPGWIDLHVHV 62
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
2-65 |
9.96e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 41.46 E-value: 9.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488471957 2 LLLHNARILDltdgstGKPTDVLLSD-RVLALGPeaQQQAHSARVrSIDLGGRLLMPGLWDEHVH 65
Cdd:PRK05985 4 LLFRNVRPAG------GAAVDILIRDgRIAAIGP--ALAAPPGAE-VEDGGGALALPGLVDGHIH 59
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
1-68 |
1.04e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 41.33 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 1 MLLLHNARILDLT-DGSTGKPTD---------VLLSD-RVLALGPEAQ-QQAHSARVRSIDLGGRLLMPGLWDEHVHVGQ 68
Cdd:PRK09228 2 TTKAYRGRLLHFTaDPAEVDDEDalryiedglLLVEDgRIVAAGPYAElRAQLPADAEVTDYRGKLILPGFIDTHIHYPQ 81
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1-66 |
1.06e-03 |
|
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: 41.51 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488471957 1 MLLLHNARILdLTDGSTgkPTDVLLSD-RVLALGPEAQQqahSARVRSIDLGGRLLMPGLWDEHVHV 66
Cdd:cd01315 1 DLVIKNGRVV-TPDGVR--EADIAVKGgKIAAIGPDIAN---TEAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
3-65 |
1.31e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 40.85 E-value: 1.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488471957 3 LLHNARILdlTDGSTGKPTDVLLSD-RVLALGPEAQQQAhsarvRSIDLGGRLLMPGLWDEHVH 65
Cdd:COG1820 1 AITNARIF--TGDGVLEDGALLIEDgRIAAIGPGAEPDA-----EVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
2-84 |
1.92e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 40.43 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 2 LLLHNARILdLTDGSTGKpTDVLLSD-RVLALGPEAQQqahSARVRSIDLGGRLLMPGLWDEHVHVGQWALASRRFLvsQ 80
Cdd:PRK07575 5 LLIRNARIL-LPSGELLL-GDVLVEDgKIVAIAPEISA---TAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDL--F 77
|
....
gi 488471957 81 TASC 84
Cdd:PRK07575 78 TASR 81
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
2-66 |
2.04e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 40.58 E-value: 2.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488471957 2 LLLHNARILDLTDGSTgKPTDVLLS-DRVLALGPEAQQQAhsaRVRSIDLGGRLLMPGLWDEHVHV 66
Cdd:PRK10027 32 YIIDNVSILDLINGGE-ISGPIVIKgRYIAGVGAEYADAP---ALQRIDARGATAVPGFIDAHLHI 93
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
258-471 |
3.10e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 39.58 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 258 RVAMGP--LKVIVDGSMSTRTawcmdsypagagpDGAGIDSVTPEDLVDLINRAKTGNLQCAAHAIGDRAAKEVLNAfev 335
Cdd:cd01299 129 QLRRGAdqIKIMATGGVLSPG-------------DPPPDTQFSEEELRAIVDEAHKAGLYVAAHAYGAEAIRRAIRA--- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 336 tGISgSIEHAQVLTDADVRRFAALGVrASVQPLHLVDD-----------RDATDVMWSDRADRCFRFADMVRAGTELALG 404
Cdd:cd01299 193 -GVD-TIEHGFLIDDETIELMKEKGI-FLVPTLATYEAlaaegaapglpADSAEKVALVLEAGRDALRRAHKAGVKIAFG 269
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488471957 405 SDApVSPVDPWGAI----RVAVERTGDrrpswhPEQALTLSQAITASARHVT----QVVTGGPGDVIAVAHNPFD 471
Cdd:cd01299 270 TDA-GFPVPPHGWNarelELLVKAGGT------PAEALRAATANAAELLGLSdelgVIEAGKLADLLVVDGDPLE 337
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
188-491 |
4.63e-03 |
|
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: 39.02 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 188 SCSTAAARLGITGIRDMEFSTDVETWLQREADGRCP--LRVEVSVYPERLDEAIAQGLATGQAPvtdKPGPsRVAMGPLK 265
Cdd:pfam01979 34 LGITTMLKSGTTTVLDMGATTSTGIEALLEAAEELPlgLRFLGPGCSLDTDGELEGRKALREKL---KAGA-EFIKGMAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 266 VIVDGSMSTRTAWcmdsypagagpdgagidSVTPEDLVDLINRAKTGNLQCAAHAIGDRAAKE-VLNAFEVTGISGSI-E 343
Cdd:pfam01979 110 GVVFVGLAPHGAP-----------------TFSDDELKAALEEAKKYGLPVAIHALETKGEVEdAIAAFGGGIEHGTHlE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 344 HAQVLTDADVRRFA-ALGVRASVQPLHLVdDRDATDVMWSDRADR-------CFRFADMVRAGTELALGSDAPVS--PVD 413
Cdd:pfam01979 173 VAESGGLLDIIKLIlAHGVHLSPTEANLL-AEHLKGAGVAHCPFSnsklrsgRIALRKALEDGVKVGLGTDGAGSgnSLN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 414 PWGAIRVAVERTGDRRPSWHPEQALTLSQAITASA----RHVTQVVTGGPGDVIAVAHNP-FDLSGDALAGlTSDLTVVG 488
Cdd:pfam01979 252 MLEELRLALELQFDPEGGLSPLEALRMATINPAKAlgldDKVGSIEVGKDADLVVVDLDPlAAFFGLKPDG-NVKKVIVK 330
|
...
gi 488471957 489 GEV 491
Cdd:pfam01979 331 GKI 333
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
231-443 |
8.02e-03 |
|
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: 38.08 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 231 YPERLDEAIAQGLATGQAPVTDKPGPSRVAMGPLKVIVDGSMSTRTAWCMDSYPAGA---GPDGAGIDS-VTPEDLVDLI 306
Cdd:cd01292 60 PPTTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAvglKLAGPYTATgLSDESLRRVL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471957 307 NRAKTGNLQCAAHA----IGDRAAKEVLNAFEVtGISGSIEHAQVLTDADVRRFAALGVRASVQPLHLVDDRdatdvmwS 382
Cdd:cd01292 140 EEARKLGLPVVIHAgelpDPTRALEDLVALLRL-GGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLG-------R 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488471957 383 DRADRcFRFADMVRAGTELALGSDAPVSP--VDPWGAIRVAVERTGDRRPSWHPEQALTLSQA 443
Cdd:cd01292 212 DGEGA-EALRRLLELGIRVTLGTDGPPHPlgTDLLALLRLLLKVLRLGLSLEEALRLATINPA 273
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
2-68 |
8.15e-03 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 38.53 E-value: 8.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488471957 2 LLLHNARILDLTDGSTGkptDVLLSD-RVLALGpeaqqQAHSARVRSIDLGGRLLMPGLWDEHVHVGQ 68
Cdd:PRK13404 6 LVIRGGTVVTATDTFQA---DIGIRGgRIAALG-----EGLGPGAREIDATGRLVLPGGVDSHCHIDQ 65
|
|
| |
