|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-428 |
0e+00 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 535.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 1 MNRKREVLKGDVLVRDGAIAAVGRNLEAPGgqAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWL-DRIWKL 79
Cdd:PRK07228 13 MNAKREIVDGDVLIEDDRIAAVGDRLDLED--YDDHIDATGKVVIPGLIQGHIHLCQTLFRGIADDLELLDWLkDRIWPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 80 EAAHDERSMYCSAMVGCCELLRSGTTCVLDMGSVHHTDEVFRALLESGIRAIGGKAMMDSGDAVPAGLRESTRESLEESL 159
Cdd:PRK07228 91 EAAHDAESMYYSALLGIGELIESGTTTIVDMESVHHTDSAFEAAGESGIRAVLGKVMMDYGDDVPEGLQEDTEASLAESV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 160 RLHSQWHGAGEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNSVGLAAGN 239
Cdd:PRK07228 171 RLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEEETGMRNIHYLDEVGLTGED 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 240 VVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLLQSYL 319
Cdd:PRK07228 251 LILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGAPCNNTLDPFTEMRQAALIQKVD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 320 NRDD--FPwASLFLEAATIRGAEALGKSQEIGSIEPGKRADIITVDLSSPHTLCGEDCEPSSRLVFSARGSDVQTVVVNG 397
Cdd:PRK07228 331 RLGPtaMP-ARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDLDGLHATPSHGVDVLSHLVYAAHGSDVETTMVDG 409
|
410 420 430
....*....|....*....|....*....|.
gi 2108213175 398 RVLLEEGRLVFTDEERLLAKSSEELAKLLAR 428
Cdd:PRK07228 410 KIVMEDGELTTIDADAVRREANRSIKRLLKR 440
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
1-407 |
3.45e-163 |
|
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: 465.52 E-value: 3.45e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 1 MNRKREVLKGDVLVRDGAIAAVGRNLEAPGGQAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWL-DRIWKL 79
Cdd:cd01298 11 TDPRRVLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDLPLMEWLkDLIWPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 80 EAAHDERSMYCSAMVGCCELLRSGTTCVLDMGsVHHTDEVFRALLESGIRAIGGKAMMDSGDAVPaglrESTRESLEESL 159
Cdd:cd01298 91 ERLLTEEDVYLGALLALAEMIRSGTTTFADMY-FFYPDAVAEAAEELGIRAVLGRGIMDLGTEDV----EETEEALAEAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 160 RLHSQWHGAGEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNSVGLAAGN 239
Cdd:cd01298 166 RLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEKYGKRPVEYLEELGLLGPD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 240 VVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLLQ--S 317
Cdd:cd01298 246 VVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGAASNNNLDMFEEMRLAALLQklA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 318 YLNRDDFPwASLFLEAATIRGAEALGkSQEIGSIEPGKRADIITVDLSSPHTLCGEDcePSSRLVFSARGSDVQTVVVNG 397
Cdd:cd01298 326 HGDPTALP-AEEALEMATIGGAKALG-LDEIGSLEVGKKADLILIDLDGPHLLPVHD--PISHLVYSANGGDVDTVIVNG 401
|
410
....*....|
gi 2108213175 398 RVLLEEGRLV 407
Cdd:cd01298 402 RVVMEDGELL 411
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
1-403 |
1.69e-160 |
|
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: 458.52 E-value: 1.69e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 1 MNRKREVLK-GDVLVRDGAIAAVGRNLEAPGG-QAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWL-DRIW 77
Cdd:COG0402 12 MDPAGGVLEdGAVLVEDGRIAAVGPGAELPARyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLADDLPLLDWLeEYIW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 78 KLEAAHDERSMYCSAMVGCCELLRSGTTCVLDMGSVHH--TDEVFRALLESGIRAIGGKAMMDSGdaVPAGLRESTRESL 155
Cdd:COG0402 92 PLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHPesADALAEAAAEAGIRAVLGRGLMDRG--FPDGLREDADEGL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 156 EESLRLHSQWHGAGEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNSVGL 235
Cdd:COG0402 170 ADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYGKRPVEYLDELGL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 236 AAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLL 315
Cdd:COG0402 250 LGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLAALL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 316 Q--SYLNRDDFPWASLFlEAATIRGAEALGKSQEIGSIEPGKRADIITVDLSSPHTLCGEDcePSSRLVFSARGSDVQTV 393
Cdd:COG0402 330 QrlRGGDPTALSAREAL-EMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHLAPLHD--PLSALVYAADGRDVRTV 406
|
410
....*....|
gi 2108213175 394 VVNGRVLLEE 403
Cdd:COG0402 407 WVAGRVVVRD 416
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
6-428 |
7.74e-119 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 353.29 E-value: 7.74e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 6 EVLKGDVLVRDGAIAAVGrnlEAPGGQAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWL-DRIWKLEAAHD 84
Cdd:PRK06038 18 DLKKGSVVIEDGTITEVS---ESTPGDADTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLnDHIWPAEAKLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 85 ERSMYCSAMVGCCELLRSGTTCVLDMgsVHHTDEVFRALLESGIRAIGGKAMMDSGDavpaglRESTRESLEESLRLHSQ 164
Cdd:PRK06038 95 AEDVYAGSLLACLEMIKSGTTSFADM--YFYMDEVAKAVEESGLRAALSYGMIDLGD------DEKGEAELKEGKRFVKE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 165 WHGAGEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNSVGLAAGNVVLAH 244
Cdd:PRK06038 167 WHGAADGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQYGMCSVNYLDDIGFLGPDVLAAH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 245 CVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLLQ--SYLNRD 322
Cdd:PRK06038 247 CVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDGCASNNNLDMFEEMKTAALLHkvNTMDPT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 323 DFPwASLFLEAATIRGAEALGKsqEIGSIEPGKRADIITVDLSSPHTLCGEDcePSSRLVFSARGSDVQTVVVNGRVLLE 402
Cdd:PRK06038 327 ALP-ARQVLEMATVNGAKALGI--NTGMLKEGYLADIIIVDMNKPHLTPVRD--VPSHLVYSASGSDVDTTIVDGRILME 401
|
410 420
....*....|....*....|....*.
gi 2108213175 403 EGRLVFTDEERLLAKSSEELAKLLAR 428
Cdd:PRK06038 402 DYKVLCMDEQDVMEDAKKAAEELVSR 427
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
6-425 |
1.16e-100 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 306.34 E-value: 1.16e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 6 EVLKGDVLVRDGAIAAVGRNLEAPggqAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWL-DRIWKLEAAHD 84
Cdd:PRK08393 17 KVIRADVLIEGNKIVEVKRNINKP---ADTVIDASGSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLqNYIWPRERKLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 85 ERSMYCSAMVGCCELLRSGTTCVLDMgsVHHTDEVFRALLESGIRAIGGKAMMDSGDavpaglRESTRESLEESLRLHSQ 164
Cdd:PRK08393 94 RKDIYWGAYLGLLEMIKSGTTTFVDM--YFHMEEVAKATLEVGLRGYLSYGMVDLGD------EEKREKEIKETEKLMEF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 165 WHGAGEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNSVGLAAGNVVLAH 244
Cdd:PRK08393 166 IEKLNSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYGKSPVVLLDEIGFLNEDVIAAH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 245 CVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLLQSYLNRD-D 323
Cdd:PRK08393 246 GVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDMLREMKLAALLHKVHNLDpT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 324 FPWASLFLEAATIRGAEALGKSQeiGSIEPGKRADIITVDLSSPHTLCGEDcePSSRLVFSARGSDVQTVVVNGRVLLEE 403
Cdd:PRK08393 326 IADAETVFRMATQNGAKALGLKA--GVIKEGYLADIAVIDFNRPHLRPINN--PISHLVYSANGNDVETTIVDGKIVMLD 401
|
410 420
....*....|....*....|..
gi 2108213175 404 GRLVFTDEERLLAKSSEELAKL 425
Cdd:PRK08393 402 GEVLTLDEEKILDKFLKVIEKL 423
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
12-428 |
1.99e-99 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 303.76 E-value: 1.99e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 12 VLVRDGAIAAVGRNLEAPGG-QAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWL-DRIWKLEAAH-DERSM 88
Cdd:PRK09045 31 VAIRDGRIVAILPRAEARARyAAAETVELPDHVLIPGLINAHTHAAMSLLRGLADDLPLMTWLqDHIWPAEGAWvSEEFV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 89 YCSAMVGCCELLRSGTTCVLDMgsVHHTDEVFRALLESGIRAIGGKAMMDsgdaVPAGLRESTRESLEESLRLHSQWHGa 168
Cdd:PRK09045 111 RDGTLLAIAEMLRGGTTCFNDM--YFFPEAAAEAAHQAGMRAQIGMPVLD----FPTAWASDADEYLAKGLELHDQWRH- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 169 gEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNSVGLAAGNVVLAHCVHL 248
Cdd:PRK09045 184 -HPLISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIADSLKQHGQRPLARLARLGLLGPRLIAVHMTQL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 249 ELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLLQ--SYLNRDDFPw 326
Cdd:PRK09045 263 TDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDGAASNNDLDLFGEMRTAALLAkaVAGDATALP- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 327 ASLFLEAATIRGAEALGKSQEIGSIEPGKRADIITVDLSSPHTlcgEDC-EPSSRLVFSARGSDVQTVVVNGRVLLEEGR 405
Cdd:PRK09045 342 AHTALRMATLNGARALGLDDEIGSLEPGKQADLVAVDLSGLET---QPVyDPVSQLVYAAGREQVSHVWVAGKQLLDDRE 418
|
410 420
....*....|....*....|...
gi 2108213175 406 LVFTDEERLLAKSSEELAKLLAR 428
Cdd:PRK09045 419 LTTLDEAELLARARQWREKIAAK 441
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
5-428 |
6.83e-84 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 264.02 E-value: 6.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 5 REVLKGDVLVRDGAIAAVGRNLEAPGGQAErVINAEGCCVLPGFVQTHVHLCQTLFRGV--VEDVGLGKWLDRIWKLEAA 82
Cdd:PRK08203 19 REIADGGLVVEGGRIVEVGPGGALPQPADE-VFDARGHVVTPGLVNTHHHFYQTLTRALpaAQDAELFPWLTTLYPVWAR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 83 HDERSMYCSAMVGCCELLRSGTTCVLD------MGSVHHTDEVFRALLESGIRAIGGKAMMDSGDAV----PAGLRESTR 152
Cdd:PRK08203 98 LTPEMVRVATQTALAELLLSGCTTSSDhhylfpNGLRDALDDQIEAAREIGMRFHATRGSMSLGESDgglpPDSVVEDED 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 153 ESLEESLRLHSQWHGAGEG---RIgyALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAY 229
Cdd:PRK08203 178 AILADSQRLIDRYHDPGPGamlRI--ALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERFGMRPVDY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 230 LNSVGLAAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEM 309
Cdd:PRK08203 256 LEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNLIGEA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 310 RLASLLQSYLNRDDFPWASLFLEAATIRGAEALGKsQEIGSIEPGKRADIITVDLSSPHTLCGEDcePSSRLVFSArGSD 389
Cdd:PRK08203 336 RQALLLQRLRYGPDAMTAREALEWATLGGARVLGR-DDIGSLAPGKLADLALFDLDELRFAGAHD--PVAALVLCG-PPR 411
|
410 420 430
....*....|....*....|....*....|....*....
gi 2108213175 390 VQTVVVNGRVLLEEGRLVFTDEERLLAKSSEELAKLLAR 428
Cdd:PRK08203 412 ADRVMVGGRWVVRDGQLTTLDLAALIARHRAAARRLAAG 450
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
16-371 |
9.96e-75 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 239.87 E-value: 9.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 16 DGAIAAVGRNLEAPGGQ---------AERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWLDR-IWKLEAAHDE 85
Cdd:cd01303 26 DGLIVVVDGNIIAAGAAetlkraakpGARVIDSPNQFILPGFIDTHIHAPQYANIGSGLGEPLLDWLETyTFPEEAKFAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 86 RSmYCSAMVG--CCELLRSGTTCVLDMGSVH--HTDEVFRALLESGIRAIGGKAMMDsgDAVPAGLRESTRESLEESLRL 161
Cdd:cd01303 106 PA-YAREVYGrfLDELLRNGTTTACYFATIHpeSTEALFEEAAKRGQRAIAGKVCMD--RNAPEYYRDTAESSYRDTKRL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 162 HSQWHGAGeGRIGYALAPRFMESCSEELLrrvsENAGEL-----DLLVHSHSSETRDEVAACKaqrGLTPPA--YL---N 231
Cdd:cd01303 183 IERWHGKS-GRVKPAITPRFAPSCSEELL----AALGKLakehpDLHIQTHISENLDEIAWVK---ELFPGArdYLdvyD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 232 SVGLAAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAAcNNNLDMLLEMRL 311
Cdd:cd01303 255 KYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGG-GTSFSMLDTLRQ 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108213175 312 A---SLLQSYLNRDDFPWA---SLFLeaATIRGAEALGKSQEIGSIEPGKRADIITVDLSSPHTLC 371
Cdd:cd01303 334 AykvSRLLGYELGGHAKLSpaeAFYL--ATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLA 397
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
2-411 |
1.98e-73 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 235.93 E-value: 1.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 2 NRKREVLKGDVLVRDGAIAAVGRNLEApggqAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWLDRIWKLEA 81
Cdd:PRK06380 14 NEKREILQGNVYIEGNKIVYVGDVNEE----ADYIIDATGKVVMPGLINTHAHVGMTASKGLFDDVDLEEFLMKTFKYDS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 82 AHDERSMYCSAMVGCCELLRSGTTCVLDMgsVHHTDEVFRALLESGIRAIGGKAMMDSGDAVPAGlreSTRESLEESLRL 161
Cdd:PRK06380 90 KRTREGIYNSAKLGMYEMINSGITAFVDL--YYSEDIIAKAAEELGIRAFLSWAVLDEEITTQKG---DPLNNAENFIRE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 162 HSqwhgaGEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNSVGLAAGNVV 241
Cdd:PRK06380 165 HR-----NEELVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEVYDHVKRTGERPVEHLEKIGFLNSKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 242 LAHCVHLELDDLRILSETGTKVSHCPSSNLKLSS-GIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLLQSYLN 320
Cdd:PRK06380 240 AAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALSVKNER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 321 RDdfpwASL-----FLEAATIRGAEALgkSQEIGSIEPGKRADIITVDLSSPHTLCGEDCEPSSRLVFSARGSDVQTVVV 395
Cdd:PRK06380 320 WD----ASIikaqeILDFATINAAKAL--ELNAGSIEVGKLADLVILDARAPNMIPTRKNNIVSNIVYSLNPLNVDHVIV 393
|
410
....*....|....*.
gi 2108213175 396 NGRVLLEEGRLVFTDE 411
Cdd:PRK06380 394 NGKILKENGRLNGFNP 409
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
11-428 |
2.97e-72 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 234.19 E-value: 2.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 11 DVLVRDGAIAAVGRNLEAPGgqaERVINAEGCCVLPGFVQTHVHLCQTLFRGVVE--DVGLGKWLDRI-WKLEAAHDERS 87
Cdd:PRK12393 27 DIRIRDGRIAAIGALTPLPG---ERVIDATDCVVYPGWVNTHHHLFQSLLKGVPAgiNQSLTAWLAAVpYRFRARFDEDL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 88 MYCSAMVGCCELLRSGTTCVLDMGSVHH-------TDEVFRALLESGIRAI--GGKAMMDSGD--AVPAGLREstrESLE 156
Cdd:PRK12393 104 FRLAARIGLVELLRSGCTTVADHHYLYHpgmpfdtGDILFDEAEALGMRFVlcRGGATQTRGDhpGLPTALRP---ETLD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 157 ESL----RLHSQWHGAGEG---RIgyALAPR-FMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPA 228
Cdd:PRK12393 181 QMLadveRLVSRYHDASPDslrRV--VVAPTtPTFSLPPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYGMTPVQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 229 YLNSVGLAAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLE 308
Cdd:PRK12393 259 FVAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADMLSE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 309 MRLASLLQSYLNRDDFPWASLFLEAATIRGAEALGkSQEIGSIEPGKRADIITVDLSSPHTLCGEDcePSSRLVFSARGS 388
Cdd:PRK12393 339 AHAAWLLHRAEGGADATTVEDVVHWGTAGGARVLG-LDAIGTLAVGQAADLAIYDLDDPRFFGLHD--PAIAPVACGGPA 415
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2108213175 389 DVQTVVVNGRVLLEEGRLVFTDEERLLAKSSEELAKLLAR 428
Cdd:PRK12393 416 PVKALLVNGRPVVENGAIPGLDLAELRHDARAAVRRLLQR 455
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
1-419 |
5.26e-71 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 230.33 E-value: 5.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 1 MNRKREVLK-GDVLVRDGAIAAVGRNLEAPGGQAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWLD-RIWK 78
Cdd:PRK15493 13 MNEQNEVIEnGYIIVENDQIIDVNSGEFASDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLEtRIWP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 79 LEAAHDERSMYCSAMVGCCELLRSGTTCVLDMGSVHHTDE--VFRALLESGIRAIGGKAMMDSGDavpaglRESTRESLE 156
Cdd:PRK15493 93 LESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQdaIMETVSRSGMRAAVSRTLFSFGT------KEDEKKAIE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 157 ESLRLHSQWHGAgEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNSVGLA 236
Cdd:PRK15493 167 EAEKYVKRYYNE-SGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 237 AGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLLQ 316
Cdd:PRK15493 246 KRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 317 SYLNRD--DFPwASLFLEAATIRGAEALGKSQeIGSIEPGKRADIITVDLSS-PHTLCGEdcEPSSRLVFSARGSDVQTV 393
Cdd:PRK15493 326 KGIHQDatALP-VETALTLATKGAAEVIGMKQ-TGSLEVGKCADFITIDPSNkPHLQPAD--EVLSHLVYAASGKDISDV 401
|
410 420
....*....|....*....|....*.
gi 2108213175 394 VVNGRVLLEEGRLVFTDEERLLAKSS 419
Cdd:PRK15493 402 IINGKRVVWNGECKTLDEERIIFEAS 427
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
10-384 |
4.79e-68 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 221.36 E-value: 4.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 10 GDVLVRDGAIAAVG--RNLEAPGGQAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVeDVGLGKWLDR-IWKLEA----- 81
Cdd:TIGR02967 7 GLLVVENGRIVAVGdyAELKETLPAGVEIDDYRGHLIMPGFIDTHIHYPQTEMIASY-GEQLLEWLEKyTFPTEArfadp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 82 AHDERSmycsAMVGCCELLRSGTTCVLDMGSVHHT--DEVFRALLESGIRAIGGKAMMDSGdaVPAGLRESTRESLEESL 159
Cdd:TIGR02967 86 DHAEEV----AEFFLDELLRNGTTTALVFATVHPEsvDALFEAALKRGMRMIAGKVLMDRN--APDYLRDTAESSYDESK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 160 RLHSQWHGagEGRIGYALAPRFMESCSEELLRRVSENAGE-LDLLVHSHSSETRDEVAACKAqrgLTP--PAYLN---SV 233
Cdd:TIGR02967 160 ALIERWHG--KGRLLYAVTPRFAPTSSPEQLAAAGELAKEyPDVYVQTHLSENKDEIAWVKE---LFPeaKDYLDvydHY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 234 GLAAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAAcNNNLDMLLEMRLA- 312
Cdd:TIGR02967 235 GLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGG-GTSFSMLQTLREAy 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108213175 313 ---SLLQSYLNrddfPWASLFLeaATIRGAEALGKSQEIGSIEPGKRADIITVDLSSPhtlcgedcePSSRLVFS 384
Cdd:TIGR02967 314 kvsQLQGARLS----PFEAFYL--ATLGGARALDLDDRIGNFEPGKEADFVVLDPAAT---------PLLALRFE 373
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
10-366 |
4.16e-67 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 220.06 E-value: 4.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 10 GDVLVRDGAIAAVG--RNLEAPGGQAERVINAEGCCVLPGFVQTHVHLCQTlfrgvveDV------GLGKWLDR-IWKLE 80
Cdd:PRK09228 32 GLLLVEDGRIVAAGpyAELRAQLPADAEVTDYRGKLILPGFIDTHIHYPQT-------DMiasygeQLLDWLNTyTFPEE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 81 AAHDERSmYCSAMVG--CCELLRSGTTCVLDMGSVH--HTDEVFRALLESGIRAIGGKAMMDSGdaVPAGLRESTRESLE 156
Cdd:PRK09228 105 RRFADPA-YAREVAEffLDELLRNGTTTALVFGTVHpqSVDALFEAAEARNMRMIAGKVLMDRN--APDGLRDTAESGYD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 157 ESLRLHSQWHGagEGRIGYALAPRFMESCSEELLRRvsenAGEL-----DLLVHSHSSETRDEVAACKAqrgLTPPA--Y 229
Cdd:PRK09228 182 DSKALIERWHG--KGRLLYAITPRFAPTSTPEQLEA----AGALarehpDVWIQTHLSENLDEIAWVKE---LFPEArdY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 230 LnSV----GLAAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCD-GAAcnNNLD 304
Cdd:PRK09228 253 L-DVyeryGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDvGGG--TSFS 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108213175 305 MLLEMRLASLLQSYLNRDDFPWASLFLeaATIRGAEALGKSQEIGSIEPGKRADIITVDLSS 366
Cdd:PRK09228 330 MLQTMNEAYKVQQLQGYRLSPFQAFYL--ATLGGARALGLDDRIGNLAPGKEADFVVLDPAA 389
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
8-410 |
1.05e-65 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 216.02 E-value: 1.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 8 LKGDVLVRDGAIAAVGRNLEAPGGQAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWL-DRIWKLEAAHDER 86
Cdd:PRK06687 20 LDGILAVKDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHEWLnDYIWPAESEFTPD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 87 SMYCSAMVGCCELLRSGTTCVLDMGSVHHTD--EVFRALLESGIRAIGGKAMMDSGDAVPAGLRESTRESLEESLRLHSQ 164
Cdd:PRK06687 100 MTTNAVKEALTEMLQSGTTTFNDMYNPNGVDiqQIYQVVKTSKMRCYFSPTLFSSETETTAETISRTRSIIDEILKYKNP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 165 whgagegRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNSVGLAAGNVVLAH 244
Cdd:PRK06687 180 -------NFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYGKRPLAFLEELGYLDHPSVFAH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 245 CVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLLQSYLNRDdf 324
Cdd:PRK06687 253 GVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVASNNNLDMFEEGRTAALLQKMKSGD-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 325 pwASLF-----LEAATIRGAEALGKSQEIGSIEPGKRADIITVDLSSP-HTLCGEDCepSSRLVFSARGSDVQTVVVNGR 398
Cdd:PRK06687 331 --ASQFpietaLKVLTIEGAKALGMENQIGSLEVGKQADFLVIQPQGKiHLQPQENM--LSHLVYAVKSSDVDDVYIAGE 406
|
410
....*....|..
gi 2108213175 399 VLLEEGRLVFTD 410
Cdd:PRK06687 407 QVVKQGQVLTVE 418
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
44-400 |
7.46e-65 |
|
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: 211.21 E-value: 7.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 44 VLPGFVQTHVHLCQTLFRGVVEDVGLGKWldriwkleaahdersmycSAMVGCCELLRSGTTCVLDMGSVHHTDevFRAL 123
Cdd:pfam01979 2 VLPGLIDAHVHLEMGLLRGIPVPPEFAYE------------------ALRLGITTMLKSGTTTVLDMGATTSTG--IEAL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 124 LES------GIRAIGGKAMMDSgDAVPAGLRESTRESLEESlrlhSQWHGAGEGRIGYALAPRFMESCSEELLRRVSENA 197
Cdd:pfam01979 62 LEAaeelplGLRFLGPGCSLDT-DGELEGRKALREKLKAGA----EFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 198 GELDLLVHSHSSETRDEVAACKAQRG-----LTPPAYLNSVGLAAG-NVVLAHCVHLELDDLRILSET--GTKVSHCPSS 269
Cdd:pfam01979 137 KKYGLPVAIHALETKGEVEDAIAAFGggiehGTHLEVAESGGLLDIiKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 270 NLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLASLLQSylNRDDFPWASLFLEAATIRGAEALGKSQEIG 349
Cdd:pfam01979 217 NSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQF--DPEGGLSPLEALRMATINPAKALGLDDKVG 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2108213175 350 SIEPGKRADIITVDLssphtlcgedcEPSSRLVFSARGSDVQTVVVNGRVL 400
Cdd:pfam01979 295 SIEVGKDADLVVVDL-----------DPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
9-428 |
1.64e-59 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 200.61 E-value: 1.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 9 KGDVLVRDGAIAAVGRNLEAPGgqAErVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWLDRIWKLEAAHDERS- 87
Cdd:PRK08204 23 RGDILIEGDRIAAVAPSIEAPD--AE-VVDARGMIVMPGLVDTHRHTWQSVLRGIGADWTLQTYFREIHGNLGPMFRPEd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 88 MYCSAMVGCCELLRSGTTCVLD----MGSVHHTDEVFRALLESGIRAIGGKAmmdSGDAVPAGLRESTRESLEESLRLHS 163
Cdd:PRK08204 100 VYIANLLGALEALDAGVTTLLDwshiNNSPEHADAAIRGLAEAGIRAVFAHG---SPGPSPYWPFDSVPHPREDIRRVKK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 164 QWHGAGEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETrdevAACKAQRGLTppaYLNSVGLAAGNVVLA 243
Cdd:PRK08204 177 RYFSSDDGLLTLGLAIRGPEFSSWEVARADFRLARELGLPISMHQGFG----PWGATPRGVE---QLHDAGLLGPDLNLV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 244 HCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNlDMLLEMRLAslLQSYLNRDD 323
Cdd:PRK08204 250 HGNDLSDDELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGG-DMFTQMRFA--LQAERARDN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 324 ----------FPWASL----FLEAATIRGAEALGKSQEIGSIEPGKRADIITVDLSSPHTLCGEDcePSSRLVFSARGSD 389
Cdd:PRK08204 327 avhlreggmpPPRLTLtarqVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATDLNLAPVHD--PVGAVVQSAHPGN 404
|
410 420 430
....*....|....*....|....*....|....*....
gi 2108213175 390 VQTVVVNGRVLLEEGRLVFTDEERLLAKSSEELAKLLAR 428
Cdd:PRK08204 405 VDSVMVAGRAVKRNGKLLGVDLERLRRLAAASRDRLLSR 443
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
10-428 |
1.01e-51 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 181.01 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 10 GDVLVRDGAIAAVGRNLEapgGQAERVINAEGCCVLPGFVQTHVHL-CQTLFRGVVEDVGLGKwlDRIWKLE-AAHDERS 87
Cdd:PRK06151 24 GEVVFEGDRILFVGHRFD---GEVDRVIDAGNALVGPGFIDLDALSdLDTTILGLDNGPGWAK--GRVWSRDyVEAGRRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 88 MYC------SAMVGCCELLRSGTTCVLDMGSVHH-----TDEVFRALLES----GIRAIGGKAMMDSGDAVPAGLR---- 148
Cdd:PRK06151 99 MYTpeelafQKRYAFAQLLRNGITTAMPIASLFYrqwaeTYAEFAAAAEAagrlGLRVYLGPAYRSGGSVLEADGSlevv 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 149 ---ESTRESLEESLRLHSQWHGAGEGRIGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLT 225
Cdd:PRK06151 179 fdeARGLAGLEEAIAFIKRVDGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHGTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 226 PPAYLNSVGLAAGNVVLAHCVHL---------ELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDG 296
Cdd:PRK06151 259 PLEWLADVGLLGPRLLIPHATYIsgsprlnysGGDDLALLAEHGVSIVHCPLVSARHGSALNSFDRYREAGINLALGTDT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 297 AACnnnlDMLLEMRLASLLQSYLNRD-DFPWASLFLEAATIRGAEALGKSqEIGSIEPGKRADIITVDLSSPHTlcGEDC 375
Cdd:PRK06151 339 FPP----DMVMNMRVGLILGRVVEGDlDAASAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLDGLHM--GPVF 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2108213175 376 EPSSRLVFSARGSDVQTVVVNGRVLLEEGRLVFTDEERLLAKSSEELAKLLAR 428
Cdd:PRK06151 412 DPIRTLVTGGSGRDVRAVFVDGRVVMEDGRLPGVDLAALRAQAQQQFDKLVAD 464
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
10-428 |
7.76e-50 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 174.74 E-value: 7.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 10 GDVLVRDGAIAAVGR--NLEAPGGQAErVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDV----GLGKWLDRIW-KLEAA 82
Cdd:PRK07203 22 GAIAIEGNVIVEIGTtdELKAKYPDAE-FIDAKGKLIMPGLINSHNHIYSGLARGMMANIppppDFISILKNLWwRLDRA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 83 HDERSMYCSAMVGCCELLRSGTTCVLDmgsvHHtdevfralleSGIRAIGGKAMMDSGDAVPAGLREST----------- 151
Cdd:PRK07203 101 LTLEDVYYSALICSLEAIKNGVTTVFD----HH----------ASPNYIGGSLFTIADAAKKVGLRAMLcyetsdrdgek 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 152 --RESLEESLRLhSQWHGAG-----EGRIGyALAPrFmeSCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGL 224
Cdd:PRK07203 167 elQEGVEENIRF-IKHIDEAkddmvEAMFG-LHAS-F--TLSDATLEKCREAVKETGRGYHIHVAEGIYDVSDSHKKYGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 225 TPPAYLNSVGLAAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACnnnlD 304
Cdd:PRK07203 242 DIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTDGYTS----D 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 305 MLLEMRLASLLQSYLNRD-DFPWASLFLEAATiRGAEALGK--SQEIGSIEPGKRADIITVDLSSPHTLCGEDCepSSRL 381
Cdd:PRK07203 318 MFESYKVANFKHKHAGGDpNVGWPESPAMLFE-NNNKIAERyfGAKFGILEEGAKADLIIVDYNPPTPLNEDNI--NGHI 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2108213175 382 VFSARGSDVQTVVVNGRVLLEEGRLVFTDEERLLAKSSEELAKLLAR 428
Cdd:PRK07203 395 LFGMNGGSVDTTIVNGKVVMEDRKFLNFDEESIYARARKAAAKLWKR 441
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
14-398 |
1.39e-38 |
|
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238638 [Multi-domain] Cd Length: 418 Bit Score: 144.14 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 14 VRDGAIAAVgrnleAPGGQAERVINAEGCcVLPGFVQTHVHLCQTLFRGVVEDVGLG-----KWLDRIWKLEAAHDERSM 88
Cdd:cd01313 16 DADGRIAAV-----NPDTATEAVALLGGA-LLPGMPNLHSHAFQRAMAGLTEYRGSAadsfwTWRELMYRFAARLTPEQI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 89 YCSAMVGCCELLRSGTTCVLDMGSVHHTDE-------------VFRALLESGIR-----------AIGGKAMMD------ 138
Cdd:cd01313 90 EAIARQLYIEMLLAGITAVGEFHYVHHDPDgtpyadpaelaqrVIAAASDAGIGitllpvlyaraGFGGPAPNPgqrrfi 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 139 SGDAVPAGLRESTRESLEESLRLhsqwhgagegRIGyaLAPRFMESCSEELLRRVSENAGElDLLVHSHSSETRDEVAAC 218
Cdd:cd01313 170 NGYEDFLGLLEKALRAVKEHAAA----------RIG--VAPHSLRAVPAEQLAALAALASE-KAPVHIHLAEQPKEVDDC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 219 KAQRGLTPPAYLNSVGLAAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDgaa 298
Cdd:cd01313 237 LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSD--- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 299 CNNNLDMLLEMRLASLLQSYLNR------DDFPW-ASLFLEAATIRGAEALGksQEIGSIEPGKRADIITVDLSSPHTLC 371
Cdd:cd01313 314 SNARIDLLEELRQLEYSQRLRDRarnvlaTAGGSsARALLDAALAGGAQALG--LATGALEAGARADLLSLDLDHPSLAG 391
|
410 420
....*....|....*....|....*..
gi 2108213175 372 GEDCEPSSRLVFSARGSDVQTVVVNGR 398
Cdd:cd01313 392 ALPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
17-398 |
1.56e-38 |
|
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238637 [Multi-domain] Cd Length: 381 Bit Score: 142.97 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 17 GAIAAVGRNLE----APGGQAERVinaEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWLDRIWKLEAAHDERSMYCSA 92
Cdd:cd01312 1 DKILEVGDYEKlekrYPGAKHEFF---PNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLKQPWEEAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 93 MVGCCELLRSGTTCVLDMGSvhHTDEVfRALLESGIRAIGGKAMMDSGDAVPAGLRESTRESLEESLRLHSQwhgagegR 172
Cdd:cd01312 78 RQGIRQMLESGTTSIGAISS--DGSLL-PALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQ-------L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 173 IGYALAPRFMESCSEELLRRVSENAGELDLLVHSHSSETRDE------------------VAACKAQRGLTPPAYLNSVG 234
Cdd:cd01312 148 FIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEErewleeskgwfkhfwesfLKLPKPKKLATAIDFLDMLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 235 LAAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRLasL 314
Cdd:cd01312 228 GLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRA--L 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 315 LQSYLNRDDFPWASLFLEAATIRGAEALGksQEIGSIEPGKRADIITVDLssphtlcGEDCEP-SSRLVFSARGSDVQTV 393
Cdd:cd01312 306 LDLHPEEDLLELASELLLMATLGGARALG--LNNGEIEAGKRADFAVFEL-------PGPGIKeQAPLQFILHAKEVRHL 376
|
....*
gi 2108213175 394 VVNGR 398
Cdd:cd01312 377 FISGK 381
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
10-363 |
9.36e-33 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 127.38 E-value: 9.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 10 GDVLVRDGAIAAVGRNLEAPGGQAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGkwlDRIWKLEAAHDERSMY 89
Cdd:COG1228 29 GTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGG---ITPTVDLVNPADKRLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 90 csamvgccELLRSGTTCVLDM--GSVHHTDEVFRALLES--GIRAIGGKAMMDSGDAVPAGLRESTRESLEESLRLHSQW 165
Cdd:COG1228 106 --------RALAAGVTTVRDLpgGPLGLRDAIIAGESKLlpGPRVLAAGPALSLTGGAHARGPEEARAALRELLAEGADY 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 166 --HGAGEGRIGYalaprfmescSEELLRRVSENAGELDLLVHSHSSETRDEVAAckaqrgltppaylnsvgLAAGNVVLA 243
Cdd:COG1228 178 ikVFAEGGAPDF----------SLEELRAILEAAHALGLPVAAHAHQADDIRLA-----------------VEAGVDSIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 244 HCVHLELDDLRILSETGTkVSHCPSSNLKLSSGIADIGGIV------------------RAGVKISLGCDGAACNN-NLD 304
Cdd:COG1228 231 HGTYLDDEVADLLAEAGT-VVLVPTLSLFLALLEGAAAPVAakarkvreaalanarrlhDAGVPVALGTDAGVGVPpGRS 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2108213175 305 MLLEMRLASllqsylnRDDFPWASLfLEAATIRGAEALGKSQEIGSIEPGKRADIITVD 363
Cdd:COG1228 310 LHRELALAV-------EAGLTPEEA-LRAATINAAKALGLDDDVGSLEPGKLADLVLLD 360
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
11-428 |
6.22e-32 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 126.12 E-value: 6.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 11 DVLVR---DGAIAAVGRNLEAPGgqAERVinaeGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGK-----WLDRIWKLEAA 82
Cdd:PRK09229 19 NVRLTvdaDGRIAAVEPGAAPAG--AERL----AGPVLPGMPNLHSHAFQRAMAGLTEVRGPPQdsfwsWRELMYRFALR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 83 HDERSMYCSAMVGCCELLRSGTTCVLDMGSVHH-------------TDEVFRALLESGIR--------AIGGkammdSGD 141
Cdd:PRK09229 93 LTPDQLEAIARQLYVEMLEAGYTSVGEFHYLHHdpdgtpyadpaemALRIVAAARAAGIGltllpvlyAHSG-----FGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 142 AVPAGLRESTRESLEESLRLHS----QWHGAGEGRIGyaLAPRFMESCSEELLRRVSENAGElDLLVHSHSSETRDEVAA 217
Cdd:PRK09229 168 QPPNPGQRRFINDPDGFLRLLEalrrALAALPGARLG--LAPHSLRAVTPDQLAAVLALAAP-DGPVHIHIAEQTKEVDD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 218 CKAQRGLTPPAYLnsvgLAAGNV----VLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLG 293
Cdd:PRK09229 245 CLAWSGARPVEWL----LDHAPVdarwCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 294 CDGAACNNNLD--MLLEM--RLASLLQSYLNRDDFPW-ASLFLEAATIRGAEALGksQEIGSIEPGKRADIITVDLSSPH 368
Cdd:PRK09229 321 SDSHVSIDLVEelRLLEYgqRLRDRRRNVLAAAAQPSvGRRLFDAALAGGAQALG--RAIGGLAVGARADLVVLDLDHPA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 369 TLCGEDCEPSSRLVFSARGSDVQTVVVNGRVLLEEGRlvFTDEERLLAKSSEELAKLLAR 428
Cdd:PRK09229 399 LAGREGDALLDRWVFAGGDAAVRDVWVAGRWVVRDGR--HRLREAIAAAFRAALAALLAA 456
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
45-365 |
1.23e-24 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 105.05 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 45 LPGFVQTHVHL-----CQTLFRGvvedvGLGKWLDRIWK----LEAAHDERSMYCSamvgCCELLRSGTTCVLDMGSvhH 115
Cdd:PRK08418 57 LPAFINPHTHLefsanKTTLDYG-----DFIPWLGSVINhredLLEKCKGALIQQA----INEMLKSGVGTIGAISS--F 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 116 TDEVfRALLESGIR------AIGGKA-MMDSgdavpagLRESTRESLEESLRLHSQwhgagegRIGYALAPRFMESCSEE 188
Cdd:PRK08418 126 GIDL-EICAKSPLRvvffneILGSNAsAVDE-------LYQDFLARFEESKKFKSK-------KFIPAIAIHSPYSVHPI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 189 LLRRVSENAGELDLLVHSH---SSETR-------------------DEVAACKAQRGLtppAYLNSVglaagNVVLAHCV 246
Cdd:PRK08418 191 LAKKALQLAKKENLLVSTHfleSKAERewleeskgwfkkffekflkEPKPLYTPKEFL---ELFKGL-----RTLFTHCV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 247 HLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDMLLEMRlASLLqSYLNRDDFPW 326
Cdd:PRK08418 263 YASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISLSLLDELR-AALL-THANMPLLEL 340
|
330 340 350
....*....|....*....|....*....|....*....
gi 2108213175 327 ASLFLEAATIRGAEALGksQEIGSIEPGKRADIITVDLS 365
Cdd:PRK08418 341 AKILLLSATRYGAKALG--LNNGEIKEGKDADLSVFELP 377
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
48-341 |
4.07e-23 |
|
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: 98.17 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 48 FVQTHVHLCQTLFRGVvedvglgkWLDRIWKLEAAHDERSMYCSAMVGCCELLRSGTTCVLDMGSVH-------HTDEVF 120
Cdd:cd01292 1 FIDTHVHLDGSALRGT--------RLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPpptttkaAIEAVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 121 RALLES-GIRAIGGKAMMDSGDAVPAGLRESTRESLEESLRLhsqwhgageGRIGYALA-PRFMESCSEELLRRVSENAG 198
Cdd:cd01292 73 EAARASaGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLEL---------GAVGLKLAgPYTATGLSDESLRRVLEEAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 199 ELDLLVHSHSSETRDEVAACKAqrgltppayLNSVGLAAGNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIA 278
Cdd:cd01292 144 KLGLPVVIHAGELPDPTRALED---------LVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDGE 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108213175 279 DIGGIVRA---GVKISLGCDGAACNNNLDMLLEMRLASLLQSYLNRddfpwASLFLEAATIRGAEA 341
Cdd:cd01292 215 GAEALRRLlelGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLGLS-----LEEALRLATINPARA 275
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
12-367 |
1.39e-21 |
|
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: 95.40 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 12 VLVRDGAIAAVGR--NLEAPGGQAERVINAEGCCVLPGFVQTHVHLcqtLFRGvvedvglgkwlDRIwkleaahDERSMY 89
Cdd:cd01296 1 IAIRDGRIAAVGPaaSLPAPGPAAAEEIDAGGRAVTPGLVDCHTHL---VFAG-----------DRV-------DEFAAR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 90 CsAMVGCCELLRSGttcvldmGSVHHTDEVFRA-----LLESGIRAIggKAMMDSG--------------DAVPAGLRES 150
Cdd:cd01296 60 L-AGASYEEILAAG-------GGILSTVRATRAasedeLFASALRRL--ARMLRHGtttvevksgygldlETELKMLRVI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 151 TRESLEESLRLHSQWHGAGEGRIGYALAPRFMESCSEELL--------------------------RRVSENAGELDLLV 204
Cdd:cd01296 130 RRLKEEGPVDLVSTFLGAHAVPPEYKGREEYIDLVIEEVLpavaeenladfcdvfcekgafsleqsRRILEAAKEAGLPV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 205 HSHSSETrdevaackaqrgltppAYLNSVGLAA--GNVVLAHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGG 282
Cdd:cd01296 210 KIHADEL----------------SNIGGAELAAelGALSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARK 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 283 IVRAGVKISLGCD---GAACNNNldMLLEMRLASLLqsylNRDDFPWAslfLEAATIRGAEALGKSQEIGSIEPGKRADI 359
Cdd:cd01296 274 LIDAGVPVALGTDfnpGSSPTSS--MPLVMHLACRL----MRMTPEEA---LTAATINAAAALGLGETVGSLEVGKQADL 344
|
....*...
gi 2108213175 360 ITVDLSSP 367
Cdd:cd01296 345 VILDAPSY 352
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
6-360 |
2.90e-21 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 94.72 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 6 EVLKGDVLVRDGAIAavGRNLEAPGGQaerVINAEGCcVLPGFVQTHVHLCQTlfrgVVEDVGLGKWLDRIWK------- 78
Cdd:PRK07213 16 EPKKGNLVIEDGIIK--GFTNEVHEGN---VIDAKGL-VIPPLINAHTHIGDS----SIKDIGIGKSLDELVKppnglkh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 79 --LEAAHDERSMYcsAMV-GCCELLRSGTTCVLDmgsvhhtdevFRallESGIRAIG--GKAMMD----------SGDAV 143
Cdd:PRK07213 86 kfLNSCSDKELVE--GMKeGLYDMYNNGIKAFCD----------FR---EGGIKGINllKKASSDlpikpiilgrPTEAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 144 PAGLRESTRESLEES--LRLHsqwhGAGEgrigyalaprfMESCSEELLRRVSENAGELDLLvhsHSSETRDEVAACKAQ 221
Cdd:PRK07213 151 ENELKKEIREILKNSdgIGLS----GANE-----------YSDEELKFICKECKREKKIFSI---HAAEHKGSVEYSLEK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 222 RGLTPPAYLNSVGLAAGNVVlaHCVHLELDDLRILSETGTKVSHCPSSNLKLSSGIADIGGIVRAGVKISLGCDGAACNN 301
Cdd:PRK07213 213 YGMTEIERLINLGFKPDFIV--HATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTDNFMANS 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2108213175 302 NlDMLLEMRLaSLLQSYLNRDDfpwaslFLEAATIRGAEALGkSQEIGSIEPGKRADII 360
Cdd:PRK07213 291 P-SIFREMEF-IYKLYHIEPKE------ILKMATINGAKILG-LINVGLIEEGFKADFT 340
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
11-400 |
7.22e-17 |
|
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: 81.91 E-value: 7.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 11 DVLVRDGAIAAVGRNLEAPGGQAErvINAEGCCVLPGFVQTHVHLCQTLFRGVVEDVGLGKWLDRIW---KLEAAHDERS 87
Cdd:cd01293 16 DIAIEDGRIAAIGPALAVPPDAEE--VDAKGRLVLPAFVDPHIHLDKTFTGGRWPNNSGGTLLEAIIaweERKLLLTAED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 88 MYCSAMVGCCELLRSGTTCV---LDMGSVhHTDEVFRALLE-----SGIRAIGGKAMMDSGdavpAGLRESTRESLEESL 159
Cdd:cd01293 94 VKERAERALELAIAHGTTAIrthVDVDPA-AGLKALEALLElreewADLIDLQIVAFPQHG----LLSTPGGEELMREAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 160 RLhsqwhgaGEGRIGyALAPRFMESCSEELLRRVSENAGE----LDLLVH---SHSSETRDEVAACKAQRGLTppaylns 232
Cdd:cd01293 169 KM-------GADVVG-GIPPAEIDEDGEESLDTLFELAQEhgldIDLHLDetdDPGSRTLEELAEEAERRGMQ------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 233 vglaaGNVVLAHCVHL------ELDDL-RILSETGTKVSHCPSSNLKLSS---------GIADIGGIVRAGVKISLGCDG 296
Cdd:cd01293 234 -----GRVTCSHATALgslpeaEVSRLaDLLAEAGISVVSLPPINLYLQGredttpkrrGVTPVKELRAAGVNVALGSDN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 297 aaCNN------NLDMLLEMRLASLLqSYLNRDDFPWASLFLeaATIRGAEALGKSQeiGSIEPGKRADIITVDLSSPhtl 370
Cdd:cd01293 309 --VRDpwypfgSGDMLEVANLAAHI-AQLGTPEDLALALDL--ITGNAARALGLED--YGIKVGCPADLVLLDAEDV--- 378
|
410 420 430
....*....|....*....|....*....|
gi 2108213175 371 cgedcepsSRLVfsARGSDVQTVVVNGRVL 400
Cdd:cd01293 379 --------AEAV--ARQPPRRVVIRKGRVV 398
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
44-341 |
7.56e-15 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 73.97 E-value: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 44 VLPGFVQTHVHLCQTLFRgvveDVGLGKWLDRIWK---------LEAAHDErsmycsamvGCCELLRSGTTCVLDMGSVH 114
Cdd:cd01305 2 LIPALVNAHTHLGDSAIK----EVGDGLPLDDLVAppdglkhrlLAQADDR---------ELAEAMRKVLRDMRETGIGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 115 HTDevFRallESGIRAI----GGKAMMDSGDAVPAGlRESTRESLEESLRLHSqwhgagegriGYALAPRF---MESCSE 187
Cdd:cd01305 69 FAD--FR---EGGVEGIellrRALGKLPVPFEVILG-RPTEPDDPEILLEVAD----------GLGLSSANdvdLEDILE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 188 ELLRRvsenagelDLLVHSHSSETRDEVAACKAQRGLtppaylnsvglAAGNVVLAHCVHLELDDLRILSETGTKVSHCP 267
Cdd:cd01305 133 LLRRR--------GKLFAIHASETRESVGMTDIERAL-----------DLEPDLLVHGTHLTDEDLELVRENGVPVVLCP 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108213175 268 SSNLKLSSGIADIGGIVRAGVKISLGCDGAACnNNLDMLLEMRLASLLQSYLNRDDfpwASLFLEAATIRGAEA 341
Cdd:cd01305 194 RSNLYFGVGIPPVAELLKLGIKVLLGTDNVMV-NEPDMWAEMEFLAKYSRLQGYLS---PLEILRMATVNAAEF 263
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
9-407 |
5.68e-13 |
|
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: 70.12 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 9 KGDVLVRDGAIAAVGRNLEAPggQAERVINAEGCCVLPGFVQTHVHLcqtlfrgvvedvglgkwldRIWKLEAAHDERSM 88
Cdd:COG0044 15 RADVLIEDGRIAAIGPDLAAP--EAAEVIDATGLLVLPGLIDLHVHL-------------------REPGLEHKEDIETG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 89 YCSAMVGccellrsGTTCVLDM------------------------------------GSVHHTDEvFRALLESGIRAIg 132
Cdd:COG0044 74 TRAAAAG-------GVTTVVDMpntnpvtdtpealefklaraeekalvdvgphgaltkGLGENLAE-LGALAEAGAVAF- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 133 gKAMMDSGDAVP----AGLRESTRESLEESLRL--HSQ------WHGAGEGRIGYALAPRFMESCSEEL-LRRVSENAGE 199
Cdd:COG0044 145 -KVFMGSDDGNPvlddGLLRRALEYAAEFGALVavHAEdpdlirGGVMNEGKTSPRLGLKGRPAEAEEEaVARDIALAEE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 200 LDLLVH-SHSSeTRDEVAACKA--QRGLtppaylnsvglaagNV---VLAHcvHLELDDLRILSE-TGTKVShcP----- 267
Cdd:COG0044 224 TGARLHiVHVS-TAEAVELIREakARGL--------------PVtaeVCPH--HLTLTDEDLERYgTNFKVN--Pplrte 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 268 SSNLKLSSGIADigGIVRAgvkisLGCDGAACNN---NLDML--------LEMRLASLLQSYLNRDDFPWAsLFLEAATI 336
Cdd:COG0044 285 EDREALWEGLAD--GTIDV-----IATDHAPHTLeekELPFAeapngipgLETALPLLLTELVHKGRLSLE-RLVELLST 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108213175 337 RGAEALGKSQEiGSIEPGKRADIITVDLSSPHTLCGEDCEpsSRLVFSA------RGSdVQTVVVNGRVLLEEGRLV 407
Cdd:COG0044 357 NPARIFGLPRK-GRIAVGADADLVLFDPDAEWTVTAEDLH--SKSKNTPfegrelTGR-VVATIVRGRVVYEDGEVV 429
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
35-363 |
1.25e-11 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 65.39 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 35 RVINAEGCCVLPGFVQTHVHLCQTLFRGVvedvGLGKWLDRIWKLEAAHDERSMycsamvgccelLRSGTTCVLDMGSVH 114
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHTHLGSDPGDLP----LDLALPVEYRTIRATRQARAA-----------LRAGFTTVRDAGGAD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 115 HTDEvfRALLESGIraIGGKAMMDSGDA--VPAGlrestresleeslrlhsqwHGAGEGRIGYALAPRFMESCS--EELL 190
Cdd:cd01299 67 YGLL--RDAIDAGL--IPGPRVFASGRAlsQTGG-------------------HGDPRGLSGLFPAGGLAAVVDgvEEVR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 191 RRVSENAGE-LDLL-------VHS------HSSETRDEVAACKA---QRGL-------TPPAYLNSVglAAGNVVLAHCV 246
Cdd:cd01299 124 AAVREQLRRgADQIkimatggVLSpgdpppDTQFSEEELRAIVDeahKAGLyvaahayGAEAIRRAI--RAGVDTIEHGF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 247 HLELDDLRILSETGTKVSHCPS---------------------SNLKLSSGIADIGGIVRAGVKISLGCDGAACNNNLDM 305
Cdd:cd01299 202 LIDDETIELMKEKGIFLVPTLAtyealaaegaapglpadsaekVALVLEAGRDALRRAHKAGVKIAFGTDAGFPVPPHGW 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2108213175 306 LL-EMRLASllqsylnrDDFPWASLFLEAATIRGAEALGKSQEIGSIEPGKRADIITVD 363
Cdd:cd01299 282 NArELELLV--------KAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
9-140 |
1.69e-11 |
|
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: 65.70 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 9 KGDVLVRDGAIAAVGRNLEAPGGqaERVINAEGCCVLPGFVQTHVHLcQTLFRGVVedvglgkwldriwkleAAHDERSM 88
Cdd:cd01314 16 KADILIEDGKIVAIGPNLEAPGG--VEVIDATGKYVLPGGIDPHTHL-ELPFMGTV----------------TADDFESG 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2108213175 89 YCSAMVGccellrsGTTCVLDMGSVHHTDEVFRAlLESGIRAIGGKAMMDSG 140
Cdd:cd01314 77 TRAAAAG-------GTTTIIDFAIPNKGQSLLEA-VEKWRGKADGKSVIDYG 120
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
7-229 |
1.59e-10 |
|
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: 62.79 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 7 VLKGDVLVRDGAIAAVGRNLEAPGgqAERVINAEGCCVLPGFVQTHVHLcQTLFRGVVedvglgkwldriwkleAAHDER 86
Cdd:TIGR02033 14 VFQADVLIEGGKIVAVGDNLIPPD--AVEVIDATGKYVLPGGIDVHTHL-EMPFGGTT----------------TADDFF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 87 SMYCSAMVGccellrsGTTCVLDMG------SVHHTDEVFRALLEsgiraigGKAMMDSG------DAVPAGLRESTRES 154
Cdd:TIGR02033 75 TGTKAAAAG-------GTTTIIDFVvpekgsSLTEALETWHEKAE-------GKSVIDYGfhmditHWNDSVLEEHIPEV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108213175 155 LEEslrlhsqwhgaGEGRIGYALAPRFMESCSEELLRRVSENAGELD--LLVHSHSSETRDEVAACKAQRGLTPPAY 229
Cdd:TIGR02033 141 KEE-----------GINSFKVFMAYKNLLMVDDEELFEILKRLKELGalLQVHAENGDIIAELQARMLAQGITGPEY 206
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
9-54 |
1.18e-09 |
|
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: 60.00 E-value: 1.18e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2108213175 9 KGDVLVRDGAIAAVGRNLEAPGgqaERVINAEGCCVLPGFVQTHVH 54
Cdd:cd01297 19 TADVGIRDGRIAAIGPILSTSA---REVIDAAGLVVAPGFIDVHTH 61
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
11-112 |
2.24e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 58.71 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 11 DVLVRDGAIAAVGRNLEAPggQAERVINAEGCCVLPGFVQTHVHLcqtlfrgvvedvglgkwldrIWKLEAAHDERSMYC 90
Cdd:PRK09237 20 DIAIEDGKIAAVAGDIDGS--QAKKVIDLSGLYVSPGWIDLHVHV--------------------YPGSTPYGDEPDEVG 77
|
90 100
....*....|....*....|..
gi 2108213175 91 samvgccelLRSGTTCVLDMGS 112
Cdd:PRK09237 78 ---------VRSGVTTVVDAGS 90
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
9-55 |
7.27e-09 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 57.49 E-value: 7.27e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2108213175 9 KGDVLVRDGAIAAVGRNleapggQAERVINAEGCCVLPGFVQTHVHL 55
Cdd:PRK08323 18 KADVLIEDGKIAAIGAN------LGDEVIDATGKYVMPGGIDPHTHM 58
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
9-55 |
2.44e-08 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 55.59 E-value: 2.44e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2108213175 9 KGDVLVRDGAIAAVGRNLEAPGgqaERVINAEGCCVLPGFVQTHVHL 55
Cdd:PRK09357 19 VADVLIDDGKIAAIGENIEAEG---AEVIDATGLVVAPGLVDLHVHL 62
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
12-55 |
6.89e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 54.42 E-value: 6.89e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2108213175 12 VLVRDGAIAAVGRNLEAPG--GQAERVINAEGCCVLPGFVQTHVHL 55
Cdd:COG1574 30 VAVRDGRIVAVGSDAEVRAlaGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
6-159 |
1.60e-07 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 53.16 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 6 EVLKGDVLVRDGAIAAVGRNLeapgGQAERVINAEGCCVLPGFVQTHVHLCQTLFRGVVedvglgkwldriwkleAAHDE 85
Cdd:PRK13404 18 DTFQADIGIRGGRIAALGEGL----GPGAREIDATGRLVLPGGVDSHCHIDQPSGDGIM----------------MADDF 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108213175 86 RSMYCSAMVGccellrsGTTCVLDMGSVHHTDEVFRALLESGIRAiGGKAMMDSgdAVPAGLRESTRESLEESL 159
Cdd:PRK13404 78 YTGTVSAAFG-------GTTTVIPFAAQHRGQSLREAVEDYHRRA-AGKAVIDY--AFHLIVADPTEEVLTEEL 141
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
11-88 |
1.68e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 53.01 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 11 DVLVRDGAIAAVGRNLEAPGGQAerVINAEGCCVLPGFVQTHVHLCQTLF--RGVVEDVGlGKWLDRI-----WKLEAAH 83
Cdd:PRK05985 18 DILIRDGRIAAIGPALAAPPGAE--VEDGGGALALPGLVDGHIHLDKTFWgdPWYPNEPG-PSLRERIanerrRRAASGH 94
|
....*..
gi 2108213175 84 D--ERSM 88
Cdd:PRK05985 95 PaaERAL 101
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
6-55 |
2.59e-07 |
|
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: 52.68 E-value: 2.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2108213175 6 EVLKGDVLVRDGAIAAVGRNLEAPggQAERVINAEGCCVLPGFVQTHVHL 55
Cdd:cd01315 14 GVREADIAVKGGKIAAIGPDIANT--EAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
6-110 |
2.94e-07 |
|
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: 52.44 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 6 EVLKGDVLVRDGAIAAVGRnLEAPGGqaERVINAEGCCVLPGFVQTHVHLcqtlfrgvvedvglgkwldRIWKLEAAHDE 85
Cdd:TIGR00857 2 KETEVDILVEGGRIKKIGK-LRIPPD--AEVIDAKGLLVLPGFIDLHVHL-------------------RDPGEEYKEDI 59
|
90 100
....*....|....*....|....*
gi 2108213175 86 RSMYCSAMVGccellrsGTTCVLDM 110
Cdd:TIGR00857 60 ESGSKAAAHG-------GFTTVADM 77
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
5-54 |
3.38e-07 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 52.41 E-value: 3.38e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2108213175 5 REVLKGDVLVRDGAIAAVGrnlEAPGgQAERVINAEGCCVLPGFVQTHVH 54
Cdd:COG1001 20 GEILEGDIAIAGGRIAGVG---DYIG-EATEVIDAAGRYLVPGFIDGHVH 65
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
11-55 |
4.75e-07 |
|
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: 51.93 E-value: 4.75e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2108213175 11 DVLVRDGAIAAVGRN--LEAPGGQAERVINAEGCCVLPGFVQTHVHL 55
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeAKALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
11-54 |
7.21e-07 |
|
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: 50.79 E-value: 7.21e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2108213175 11 DVLVRDGAIAAVGRNLEAPGgqAERVINAEGCCVLPGFVQTHVH 54
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPA--ATQIVDAGGCYVSPGWIDLHVH 42
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
5-61 |
1.18e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 50.44 E-value: 1.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2108213175 5 REVLKGDVLVRDGAIAAVGRNLEAPGgqAERVINAEGCCVLPGFVQTHVHlcqtlFR 61
Cdd:PRK07575 17 GELLLGDVLVEDGKIVAIAPEISATA--VDTVIDAEGLTLLPGVIDPQVH-----FR 66
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
16-363 |
1.51e-06 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 50.00 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 16 DGAIAAVGRNLEAPGGQaeRVINAEGCCVLPGFVQTHVHLcqtlfrGVVEDVGLG----------------KWLDRIWKL 79
Cdd:cd01309 1 DGKIVAVGAEITTPADA--EVIDAKGKHVTPGLIDAHSHL------GLDEEGGVRetsdaneetdpvtphvRAIDGINPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 80 -EAAHDERS---MYCSAMVGCCELLrSGTTCVLDMGSVHHTDEVFRAllESGIRAIGG---KAMMDSGDAVPA---GLRE 149
Cdd:cd01309 73 dEAFKRARAggvTTVQVLPGSANLI-GGQGVVIKTDGGTIEDMFIKA--PAGLKMALGenpKRVYGGKGKEPAtrmGVAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 150 STRESLEESLRLHSQWHgAGEGRIGYALAPRFMESCSEELLRrvsenaGELDLLVHSHSSetrDEVAAC---KAQRGLtp 226
Cdd:cd01309 150 LLRDAFIKAQEYGRKYD-LGKNAKKDPPERDLKLEALLPVLK------GEIPVRIHAHRA---DDILTAiriAKEFGI-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 227 paylnsvglaagNVVLAHCvhleLDDLRI---LSETGTKVSHCPSSNLK-----LSSGIADIGGIVRAG-VKISLGCDGA 297
Cdd:cd01309 218 ------------KITIEHG----AEGYKLadeLAKHGIPVIYGPTLTLPkkveeVNDAIDTNAYLLKKGgVAFAISSDHP 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108213175 298 ACN-NNLdmLLEMRLASllqsylnRDDFPWASLfLEAATIRGAEALGKSQEIGSIEPGKRADIITVD 363
Cdd:cd01309 282 VLNiRNL--NLEAAKAV-------KYGLSYEEA-LKAITINPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
7-61 |
1.83e-06 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 49.87 E-value: 1.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2108213175 7 VLKGDVLVRDGAIAAVGRNLEAPGgqAERVINAEGCCVLPGFVQTHVHlcqtlFR 61
Cdd:PRK09236 17 IFEGDVLIENGRIAKIASSISAKS--ADTVIDAAGRYLLPGMIDDQVH-----FR 64
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
6-61 |
2.66e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 49.27 E-value: 2.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2108213175 6 EVLKGDVLVRDGAIAAVGRNLEapGGQAERVINAEGCCVLPGFVQTHVHlcqtlFR 61
Cdd:PRK02382 16 SLQPRDVRIDGGKITAVGKDLD--GSSSEEVIDARGMLLLPGGIDVHVH-----FR 64
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
10-54 |
3.47e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 49.31 E-value: 3.47e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2108213175 10 GDVLVRDGAIAAVGRNLeapgGQAERVINAEGCCVLPGFVQTHVH 54
Cdd:PRK09061 39 RDVGIKGGKIAAVGTAA----IEGDRTIDATGLVVAPGFIDLHAH 79
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
9-56 |
5.78e-06 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 48.15 E-value: 5.78e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2108213175 9 KGDVLVRDGAIAAVGRNLEAPGGQAERVINAEGCCVLPGFVQTHVHLC 56
Cdd:cd01308 17 KKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHII 64
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
79-400 |
7.60e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.91 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 79 LEAAHDERSMYCSAMVgccELLRSGTTCVLDMGSVHHTDEVFRALLESgirAIGGKAMMDSGDAVPAGLRESTRESLEES 158
Cdd:pfam07969 143 LLAREAEAAAVAAALA---ALPGFGITSVDGGGGNVHSLDDYEPLREL---TAAEKLKELLDAPERLGLPHSIYELRIGA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 159 LRLHSQwhGAGEGRIGYALAPRFME------SCSEELLRRVSENAGELDLLVHSHSSETRDEVAACKAQRGLTPPAYLNs 232
Cdd:pfam07969 217 MKLFAD--GVLGSRTAALTEPYFDApgtgwpDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGNQ- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 233 vglaaGNVVLAHC---VHLELDDLRILSETGTKVSHCPSSNLKLS------------SGIADIGGIVRAGVKISLGCDGA 297
Cdd:pfam07969 294 -----GRVRIEHAqgvVPYTYSQIERVAALGGAAGVQPVFDPLWGdwlqdrlgaeraRGLTPVKELLNAGVKVALGSDAP 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 298 ACNnnLDMLLEMRLASLLQSYLNRDDFPWASL--FLEAA---TIRGAEALGKSQEIGSIEPGKRADIITVDLSsphtlcG 372
Cdd:pfam07969 369 VGP--FDPWPRIGAAVMRQTAGGGEVLGPDEElsLEEALalyTSGPAKALGLEDRKGTLGVGKDADLVVLDDD------P 440
|
330 340
....*....|....*....|....*...
gi 2108213175 373 EDCEPSSRLVFSARGsdvqtVVVNGRVL 400
Cdd:pfam07969 441 LTVDPPAIADIRVRL-----TVVDGRVV 463
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
3-55 |
2.39e-05 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 46.23 E-value: 2.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2108213175 3 RKREVLKGDVLVRDGAIAAVGRNLEAPGGQaerVINAEGCCVLPGFVQTHVHL 55
Cdd:PRK06189 14 TPEGVYRADIGIKNGKIAEIAPEISSPARE---IIDADGLYVFPGMIDVHVHF 63
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
11-55 |
2.56e-05 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 46.37 E-value: 2.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2108213175 11 DVLVRDGAIAAVGRNLEAPGGQaeRVINAEGCCVLPGFVQTHVHL 55
Cdd:PLN02942 24 DVYVEDGIIVAVAPNLKVPDDV--RVIDATGKFVMPGGIDPHTHL 66
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
9-55 |
3.85e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 45.68 E-value: 3.85e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2108213175 9 KGDVLVRDGAIAAVGrnlEAPGGQAERVINAEGCCVLPGFVQTHVHL 55
Cdd:PRK09060 22 RADIGIRDGRIAAIG---DLSGASAGEVIDCRGLHVLPGVIDSQVHF 65
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
5-54 |
4.22e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 45.26 E-value: 4.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2108213175 5 REVLKGDVLVRDGAIAAVGRNLEAPGGqaERVINAEGCCVLPGFVQTHVH 54
Cdd:cd00854 12 GGLEDGAVLVEDGKIVAIGPEDELEEA--DEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
11-55 |
5.15e-05 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 45.23 E-value: 5.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2108213175 11 DVLVRDGAIAAVGRNLeapgGQAERVINAEGCCVLPGFVQTHVHL 55
Cdd:PRK08044 22 DIAVKGGKIAAIGQDL----GDAKEVMDASGLVVSPGMVDAHTHI 62
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
10-54 |
7.17e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 44.70 E-value: 7.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2108213175 10 GDVLVRDGAIAAVGRNLEApggqAERVINAEGCCVLPGFVQTHVH 54
Cdd:COG1820 17 GALLIEDGRIAAIGPGAEP----DAEVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
8-56 |
8.36e-05 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 44.37 E-value: 8.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108213175 8 LKGDVLVRDGAIAAVGRNL-----------------EAPGGQAERVINAEGCCVLPGFVQTHVHLC 56
Cdd:PRK12394 1 MKNDILITNGHIIDPARNIneinnlriindiivdadKYPVASETRIIHADGCIVTPGLIDYHAHVF 66
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
333-409 |
1.03e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 44.32 E-value: 1.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108213175 333 AATIRGAEALGKSQeIGSIEPGKRADIITV-DLssphtlcgEDCEpssrlvfsargsdVQTVVVNGRVLLEEGRLVFT 409
Cdd:COG1001 292 MATLNAAEHFGLKD-LGAIAPGRRADIVLLdDL--------EDFK-------------VEKVYADGKLVAEDGKLLVD 347
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
6-55 |
3.47e-04 |
|
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 42.84 E-value: 3.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2108213175 6 EVLKGDVLVRDGAIAAVGRNleapggQAERVINAEGCCVLPGFVQTHVHL 55
Cdd:TIGR01178 16 EIIPGDIAIANGHIAGVGKY------NGVKVIDALGEYAVPGFIDAHIHI 59
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
6-52 |
4.13e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 42.47 E-value: 4.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2108213175 6 EVLKGDVLVRDGAIAAVGRNLEAPGGQaervINAEGCCVLPGFVQTH 52
Cdd:PRK15446 16 EVVDGSLLIEDGRIAAIDPGASALPGA----IDAEGDYLLPGLVDLH 58
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
11-49 |
5.76e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 41.97 E-value: 5.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2108213175 11 DVLVRDGAIAAVGRnleAPGG-QAERVINAEGCCVLPGFV 49
Cdd:PRK07627 22 DLYVAAGKIAAIGQ---APAGfNADKTIDASGLIVCPGLV 58
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
331-360 |
5.84e-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: 41.91 E-value: 5.84e-04
10 20 30
....*....|....*....|....*....|
gi 2108213175 331 LEAATIRGAEALGKSQEIGSIEPGKRADII 360
Cdd:cd01300 449 LRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
331-363 |
6.26e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 41.62 E-value: 6.26e-04
10 20 30
....*....|....*....|....*....|...
gi 2108213175 331 LEAATIRGAEALGKSQEIGSIEPGKRADIITVD 363
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLD 360
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
7-55 |
7.81e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 41.70 E-value: 7.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2108213175 7 VLKGDVLVRDGAIAAVGR--------NLEAPGGQAERVINAEGCCVLPGFVQTHVHL 55
Cdd:PRK13207 82 IVKADIGIKDGRIVAIGKagnpdiqdGVDIIIGPGTEVIAGEGLIVTAGGIDTHIHF 138
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
265-366 |
5.76e-03 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 38.91 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108213175 265 HCPSSNLKlssgiADIggivrAGVKISLGCDGaacnnnldmlLEMRLaSLLQSYLNRDDFPWASLFLEAATIRGAEALGk 344
Cdd:PRK08417 276 HSAKSNSK-----KDL-----AFDEAAFGIDS----------ICEYF-SLCYTYLVKEGIITWSELSRFTSYNPAQFLG- 333
|
90 100
....*....|....*....|..
gi 2108213175 345 sQEIGSIEPGKRADIITVDLSS 366
Cdd:PRK08417 334 -LNSGEIEVGKEADLVLFDPNE 354
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
335-360 |
6.22e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 39.00 E-value: 6.22e-03
10 20
....*....|....*....|....*.
gi 2108213175 335 TIRGAEALGKSQEIGSIEPGKRADII 360
Cdd:PRK13207 409 TINPAIAHGISHEVGSVEVGKLADLV 434
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
6-55 |
6.30e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 38.66 E-value: 6.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2108213175 6 EVLKGDVLVRDGAIAAVGrnLEAPGGQAERVINAEGCCVLPGFVQTHVHL 55
Cdd:PRK10027 46 GEISGPIVIKGRYIAGVG--AEYADAPALQRIDARGATAVPGFIDAHLHI 93
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
9-54 |
7.94e-03 |
|
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: 38.55 E-value: 7.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2108213175 9 KGDVLVRDGAIAAvgrnlEAPGGQAERVINAEGCCVLPGFVQTHVH 54
Cdd:cd01304 17 KMDIFIRDGKIVE-----SSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| |
