|
Name |
Accession |
Description |
Interval |
E-value |
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
82-598 |
2.47e-171 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 496.32 E-value: 2.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 82 AMGDVVALAAGFLMPFAFAPFGFYGLTIVALALLFQVLLVASAGRGFWRGWIFGLAMFGTGVFWIHESF-RFAAVSLPLA 160
Cdd:PRK00302 6 WLRLLLALLAGALGTLAFAPFDLWPLALLSLAGLLWLLLGASPKQAALIGFLWGFGYFGSGLSWIYVSIhTFGGMPAWLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 161 LLLTGGLIGILAIYPALFGFFAALWSRRFampsgsaptpasgrllsiSLGALLVFPAGWTLLEWMRGWFLTGFPWLQVGY 240
Cdd:PRK00302 86 PLLVLLLAAYLALYPALFAALWRRLWPKS------------------GLRRALALPALWVLTEWLRGWLLTGFPWLALGY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 241 AH-GDSPLAGLAPLLGVYGVGWAVALSAGLLLVAFRlvmenrnlATKARIIGLSSLLALGGGIWGGSSWLdqgAWSTPTG 319
Cdd:PRK00302 148 SQiPDGPLAQLAPIFGVYGLSFLVVLVNALLALALI--------KRRWRLALLALLLLLLAALGYGLRRL---QWTTPAP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 320 A-PIGVALIQGNIPQDEKWLPALRQPTLERYLSLTRREAGR-DLVVWPETALPGSYHHFTD-FIAILRREARFHHMNILF 396
Cdd:PRK00302 217 EpALKVALVQGNIPQSLKWDPAGLEATLQKYLDLSRPALGPaDLIIWPETAIPFLLEDLPQaFLKALDDLAREKGSALIT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 397 GVP--TLEGKSQRHFNSIAAITDMGEVLFYHKKHLVPFGEYLPMAGILRGILDFLKIPMSDFSAGPAGQLPFSVAGQSIG 474
Cdd:PRK00302 297 GAPraENKQGRYDYYNSIYVLGPYGILNRYDKHHLVPFGEYVPLESLLRPLAPFFNLPMGDFSRGPYVQPPLLAKGLKLA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 475 ASVCYEASFGENIIASL-SRATLLVNVSNEAWFGDSRGPHQNLQMARMRALESERYLLRATNTGISAIIDPQGRIVGRAP 553
Cdd:PRK00302 377 PLICYEIIFPEEVRANVrQGADLLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDPLGRIIAQLP 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1584356770 554 QFQLSVLTGTVTGMRGVTPYARYGNWIIVSGALLVLMIGIVIGAF 598
Cdd:PRK00302 457 QFTEGVLDGTVPPTTGLTPYARWGDWPLLLLALLLLLLALLLALR 501
|
|
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
101-595 |
6.92e-170 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 491.67 E-value: 6.92e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 101 PFGFYGLTIVALALLFQVLL-VASAGRGFWRGWIFGLAMFGTGVFWIHESF-RFAAVSLPLALLLTGGLIGILAIYPALF 178
Cdd:COG0815 1 PFGLWPLAFVALAPLLLLLRgARSPRRAFLLGWLFGLGFFLAGLYWLYVSLhVFGGLPAWLAPLAVLLLAAYLALFFALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 179 GFFAALWSRRFampsgsaptpasgrllsiSLGALLVFPAGWTLLEWMRGWFLTGFPWLQVGYAHGD-SPLAGLAPLLGVY 257
Cdd:COG0815 81 AALARRLRRRG------------------GLLRPLAFAALWVLLEWLRGWLFTGFPWLRLGYSQADfSPLAQLAPLGGVY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 258 GVGWAVALSAGLLLVAFRlvmenrnlATKARIIGLSSLLALGGGIWGgsswLDQGAWSTPTGAPIGVALIQGNIPQDEKW 337
Cdd:COG0815 143 GLSFLVVLVNALLALALL--------RRRRRLAALALALALLLAALR----LSPVPWTEPAGEPLRVALVQGNIPQDLKW 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 338 LPALRQPTLERYLSLTRREAGR--DLVVWPETALPGSYHHFTDFIAILRREARFHHMNILFGVPTLEGKSQRHFNSIAAI 415
Cdd:COG0815 211 DPEQRREILDRYLDLTRELADDgpDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRYYNSALLL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 416 TDMGEVL-FYHKKHLVPFGEYLPMAGILRGILDFLKIPMSDFSAGPaGQLPFSVAGQSIGASVCYEASFGENIIASL-SR 493
Cdd:COG0815 291 DPDGGILgRYDKHHLVPFGEYVPLRDLLRPLIPFLDLPLGDFSPGT-GPPVLDLGGVRVGPLICYESIFPELVRDAVrAG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 494 ATLLVNVSNEAWFGDSRGPHQNLQMARMRALESERYLLRATNTGISAIIDPQGRIVGRAPQFQLSVLTGTVTGMRGVTPY 573
Cdd:COG0815 370 ADLLVNITNDAWFGDSIGPYQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPY 449
|
490 500
....*....|....*....|..
gi 1584356770 574 ARYGNWIIVSGALLVLMIGIVI 595
Cdd:COG0815 450 ARWGDWPALLLLLLALLLALLL 471
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
324-587 |
3.56e-108 |
|
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.
Pssm-ID: 143595 Cd Length: 270 Bit Score: 326.09 E-value: 3.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 324 VALIQGNIPQDEKWLPALRQPTLERYLSLTRREAGR--DLVVWPETALPGSYHHFTDFIAILRREARFHHMNILFGVPTL 401
Cdd:cd07571 3 VALVQGNIPQDEKWDPEQRQATLDRYLDLTRELADEkpDLVVWPETALPFDLQRDPDALARLARAARAVGAPLLTGAPRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 402 EGKSQRHFNSIAAITDMGEVL-FYHKKHLVPFGEYLPMAGILRGILDFLKIPMSDFSAGPAGQLPFSVAGQSIGASVCYE 480
Cdd:cd07571 83 EPGGGRYYNSALLLDPGGGILgRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPMGDFSPGTGPQPLLLGGGVRVGPLICYE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 481 ASFGENIIASLS-RATLLVNVSNEAWFGDSRGPHQNLQMARMRALESERYLLRATNTGISAIIDPQGRIVGRAPQFQLSV 559
Cdd:cd07571 163 SIFPELVRDAVRqGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVARLPLFEAGV 242
|
250 260
....*....|....*....|....*...
gi 1584356770 560 LTGTVTGMRGVTPYARYGNWIIVSGALL 587
Cdd:cd07571 243 LVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
134-548 |
5.05e-84 |
|
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]
Pssm-ID: 273129 [Multi-domain] Cd Length: 391 Bit Score: 268.07 E-value: 5.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 134 FGLAMFGTGVFWIHESFRFAAVSLPLALLLTGGLIGILAIYPAL-FGFFAALWSRRFAmpsgsaptpasgrllsislgaL 212
Cdd:TIGR00546 1 FGFGFFLAGLFWLGIALSVNGFIAFVAGLLVVGLPALLALFPGLaAYLLRRLAPFRKV---------------------L 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 213 LVFPAGWTLLEWMRGWFLTGFPWLQVGYAHGDSPLAGLAPLLGVYGVG-WAVALSAGLLLVAFRlvmenRNLATKARIIG 291
Cdd:TIGR00546 60 LALPLLWTLAEWLRSFGFLGFPWGLIGYAQSSLPLIQIASIFGVWGLSfLVVFLNALLALVLLK-----KESFKKLLAIA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 292 LSSLLALGGGIwggsswLDQGAWSTPTGAP-IGVALIQGNIPQDEKWLPALRQPTLERYLSLTRREAGR-DLVVWPETAL 369
Cdd:TIGR00546 135 VVVLLAALGFL------LYELKSATPVPGPtLNVALVQPNIPQDLKFDSEGLEAILEILTSLTKQAVEKpDLVVWPETAF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 370 PGSYH-HFTDFIAILRREARFHHMNILFGVPTLEGKSQRH-FNSIAAITDMGEVLF-YHKKHLVPFGEYLPMAGILRGIL 446
Cdd:TIGR00546 209 PFDLEnSPQKLADRLKLLVLSKGIPILIGAPDAVPGGPYHyYNSAYLVDPGGEVVQrYDKVKLVPFGEYIPLGFLFKWLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 447 DFL-KIPMSDFSAGPaGQLPFSVAGQSIGASVCYEASFGENIIASLSR-ATLLVNVSNEAWFGDSRGPHQNLQMARMRAL 524
Cdd:TIGR00546 289 KLFfLLSQEDFSRGP-GPQVLKLPGGKIAPLICYESIFPDLVRASARQgAELLVNLTNDAWFGDSSGPWQHFALARFRAI 367
|
410 420
....*....|....*....|....
gi 1584356770 525 ESERYLLRATNTGISAIIDPQGRI 548
Cdd:TIGR00546 368 ENGRPLVRATNTGISAVIDPRGRT 391
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
324-564 |
2.45e-33 |
|
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.
Pssm-ID: 425873 [Multi-domain] Cd Length: 257 Bit Score: 128.24 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 324 VALIQGNIPQDEKWlpalrqPTLERYLSLTRR--EAGRDLVVWPETALPG--SYHHFTD--------FIAILRREARFHH 391
Cdd:pfam00795 2 VALVQLPQGFWDLE------ANLQKALELIEEaaRYGADLIVLPELFITGypCWAHFLEaaevgdgeTLAGLAALARKNG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 392 MNILFGVPTLEGKSQRHFNSIAAITDMGEVLF-YHKKHLVPfgEYLPMAGILRGIldflkipmsdFSAGPAGQlPFSVAG 470
Cdd:pfam00795 76 IAIVIGLIERWLTGGRLYNTAVLLDPDGKLVGkYRKLHLFP--EPRPPGFRERVL----------FEPGDGGT-VFDTPL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 471 QSIGASVCYEASFGEN-IIASLSRATLLVNVSNEAWFGDSRGPHQNLQMARMRALESERYLLRATNTGI----------S 539
Cdd:pfam00795 143 GKIGAAICYEIRFPELlRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGeedapwpyghS 222
|
250 260
....*....|....*....|....*
gi 1584356770 540 AIIDPQGRIVGRAPQFQLSVLTGTV 564
Cdd:pfam00795 223 MIIDPDGRILAGAGEWEEGVLIADI 247
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
82-598 |
2.47e-171 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 496.32 E-value: 2.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 82 AMGDVVALAAGFLMPFAFAPFGFYGLTIVALALLFQVLLVASAGRGFWRGWIFGLAMFGTGVFWIHESF-RFAAVSLPLA 160
Cdd:PRK00302 6 WLRLLLALLAGALGTLAFAPFDLWPLALLSLAGLLWLLLGASPKQAALIGFLWGFGYFGSGLSWIYVSIhTFGGMPAWLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 161 LLLTGGLIGILAIYPALFGFFAALWSRRFampsgsaptpasgrllsiSLGALLVFPAGWTLLEWMRGWFLTGFPWLQVGY 240
Cdd:PRK00302 86 PLLVLLLAAYLALYPALFAALWRRLWPKS------------------GLRRALALPALWVLTEWLRGWLLTGFPWLALGY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 241 AH-GDSPLAGLAPLLGVYGVGWAVALSAGLLLVAFRlvmenrnlATKARIIGLSSLLALGGGIWGGSSWLdqgAWSTPTG 319
Cdd:PRK00302 148 SQiPDGPLAQLAPIFGVYGLSFLVVLVNALLALALI--------KRRWRLALLALLLLLLAALGYGLRRL---QWTTPAP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 320 A-PIGVALIQGNIPQDEKWLPALRQPTLERYLSLTRREAGR-DLVVWPETALPGSYHHFTD-FIAILRREARFHHMNILF 396
Cdd:PRK00302 217 EpALKVALVQGNIPQSLKWDPAGLEATLQKYLDLSRPALGPaDLIIWPETAIPFLLEDLPQaFLKALDDLAREKGSALIT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 397 GVP--TLEGKSQRHFNSIAAITDMGEVLFYHKKHLVPFGEYLPMAGILRGILDFLKIPMSDFSAGPAGQLPFSVAGQSIG 474
Cdd:PRK00302 297 GAPraENKQGRYDYYNSIYVLGPYGILNRYDKHHLVPFGEYVPLESLLRPLAPFFNLPMGDFSRGPYVQPPLLAKGLKLA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 475 ASVCYEASFGENIIASL-SRATLLVNVSNEAWFGDSRGPHQNLQMARMRALESERYLLRATNTGISAIIDPQGRIVGRAP 553
Cdd:PRK00302 377 PLICYEIIFPEEVRANVrQGADLLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDPLGRIIAQLP 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1584356770 554 QFQLSVLTGTVTGMRGVTPYARYGNWIIVSGALLVLMIGIVIGAF 598
Cdd:PRK00302 457 QFTEGVLDGTVPPTTGLTPYARWGDWPLLLLALLLLLLALLLALR 501
|
|
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
101-595 |
6.92e-170 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 491.67 E-value: 6.92e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 101 PFGFYGLTIVALALLFQVLL-VASAGRGFWRGWIFGLAMFGTGVFWIHESF-RFAAVSLPLALLLTGGLIGILAIYPALF 178
Cdd:COG0815 1 PFGLWPLAFVALAPLLLLLRgARSPRRAFLLGWLFGLGFFLAGLYWLYVSLhVFGGLPAWLAPLAVLLLAAYLALFFALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 179 GFFAALWSRRFampsgsaptpasgrllsiSLGALLVFPAGWTLLEWMRGWFLTGFPWLQVGYAHGD-SPLAGLAPLLGVY 257
Cdd:COG0815 81 AALARRLRRRG------------------GLLRPLAFAALWVLLEWLRGWLFTGFPWLRLGYSQADfSPLAQLAPLGGVY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 258 GVGWAVALSAGLLLVAFRlvmenrnlATKARIIGLSSLLALGGGIWGgsswLDQGAWSTPTGAPIGVALIQGNIPQDEKW 337
Cdd:COG0815 143 GLSFLVVLVNALLALALL--------RRRRRLAALALALALLLAALR----LSPVPWTEPAGEPLRVALVQGNIPQDLKW 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 338 LPALRQPTLERYLSLTRREAGR--DLVVWPETALPGSYHHFTDFIAILRREARFHHMNILFGVPTLEGKSQRHFNSIAAI 415
Cdd:COG0815 211 DPEQRREILDRYLDLTRELADDgpDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRYYNSALLL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 416 TDMGEVL-FYHKKHLVPFGEYLPMAGILRGILDFLKIPMSDFSAGPaGQLPFSVAGQSIGASVCYEASFGENIIASL-SR 493
Cdd:COG0815 291 DPDGGILgRYDKHHLVPFGEYVPLRDLLRPLIPFLDLPLGDFSPGT-GPPVLDLGGVRVGPLICYESIFPELVRDAVrAG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 494 ATLLVNVSNEAWFGDSRGPHQNLQMARMRALESERYLLRATNTGISAIIDPQGRIVGRAPQFQLSVLTGTVTGMRGVTPY 573
Cdd:COG0815 370 ADLLVNITNDAWFGDSIGPYQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPY 449
|
490 500
....*....|....*....|..
gi 1584356770 574 ARYGNWIIVSGALLVLMIGIVI 595
Cdd:COG0815 450 ARWGDWPALLLLLLALLLALLL 471
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
324-587 |
3.56e-108 |
|
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.
Pssm-ID: 143595 Cd Length: 270 Bit Score: 326.09 E-value: 3.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 324 VALIQGNIPQDEKWLPALRQPTLERYLSLTRREAGR--DLVVWPETALPGSYHHFTDFIAILRREARFHHMNILFGVPTL 401
Cdd:cd07571 3 VALVQGNIPQDEKWDPEQRQATLDRYLDLTRELADEkpDLVVWPETALPFDLQRDPDALARLARAARAVGAPLLTGAPRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 402 EGKSQRHFNSIAAITDMGEVL-FYHKKHLVPFGEYLPMAGILRGILDFLKIPMSDFSAGPAGQLPFSVAGQSIGASVCYE 480
Cdd:cd07571 83 EPGGGRYYNSALLLDPGGGILgRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPMGDFSPGTGPQPLLLGGGVRVGPLICYE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 481 ASFGENIIASLS-RATLLVNVSNEAWFGDSRGPHQNLQMARMRALESERYLLRATNTGISAIIDPQGRIVGRAPQFQLSV 559
Cdd:cd07571 163 SIFPELVRDAVRqGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVARLPLFEAGV 242
|
250 260
....*....|....*....|....*...
gi 1584356770 560 LTGTVTGMRGVTPYARYGNWIIVSGALL 587
Cdd:cd07571 243 LVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
134-548 |
5.05e-84 |
|
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]
Pssm-ID: 273129 [Multi-domain] Cd Length: 391 Bit Score: 268.07 E-value: 5.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 134 FGLAMFGTGVFWIHESFRFAAVSLPLALLLTGGLIGILAIYPAL-FGFFAALWSRRFAmpsgsaptpasgrllsislgaL 212
Cdd:TIGR00546 1 FGFGFFLAGLFWLGIALSVNGFIAFVAGLLVVGLPALLALFPGLaAYLLRRLAPFRKV---------------------L 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 213 LVFPAGWTLLEWMRGWFLTGFPWLQVGYAHGDSPLAGLAPLLGVYGVG-WAVALSAGLLLVAFRlvmenRNLATKARIIG 291
Cdd:TIGR00546 60 LALPLLWTLAEWLRSFGFLGFPWGLIGYAQSSLPLIQIASIFGVWGLSfLVVFLNALLALVLLK-----KESFKKLLAIA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 292 LSSLLALGGGIwggsswLDQGAWSTPTGAP-IGVALIQGNIPQDEKWLPALRQPTLERYLSLTRREAGR-DLVVWPETAL 369
Cdd:TIGR00546 135 VVVLLAALGFL------LYELKSATPVPGPtLNVALVQPNIPQDLKFDSEGLEAILEILTSLTKQAVEKpDLVVWPETAF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 370 PGSYH-HFTDFIAILRREARFHHMNILFGVPTLEGKSQRH-FNSIAAITDMGEVLF-YHKKHLVPFGEYLPMAGILRGIL 446
Cdd:TIGR00546 209 PFDLEnSPQKLADRLKLLVLSKGIPILIGAPDAVPGGPYHyYNSAYLVDPGGEVVQrYDKVKLVPFGEYIPLGFLFKWLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 447 DFL-KIPMSDFSAGPaGQLPFSVAGQSIGASVCYEASFGENIIASLSR-ATLLVNVSNEAWFGDSRGPHQNLQMARMRAL 524
Cdd:TIGR00546 289 KLFfLLSQEDFSRGP-GPQVLKLPGGKIAPLICYESIFPDLVRASARQgAELLVNLTNDAWFGDSSGPWQHFALARFRAI 367
|
410 420
....*....|....*....|....
gi 1584356770 525 ESERYLLRATNTGISAIIDPQGRI 548
Cdd:TIGR00546 368 ENGRPLVRATNTGISAVIDPRGRT 391
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
324-564 |
2.45e-33 |
|
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.
Pssm-ID: 425873 [Multi-domain] Cd Length: 257 Bit Score: 128.24 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 324 VALIQGNIPQDEKWlpalrqPTLERYLSLTRR--EAGRDLVVWPETALPG--SYHHFTD--------FIAILRREARFHH 391
Cdd:pfam00795 2 VALVQLPQGFWDLE------ANLQKALELIEEaaRYGADLIVLPELFITGypCWAHFLEaaevgdgeTLAGLAALARKNG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 392 MNILFGVPTLEGKSQRHFNSIAAITDMGEVLF-YHKKHLVPfgEYLPMAGILRGIldflkipmsdFSAGPAGQlPFSVAG 470
Cdd:pfam00795 76 IAIVIGLIERWLTGGRLYNTAVLLDPDGKLVGkYRKLHLFP--EPRPPGFRERVL----------FEPGDGGT-VFDTPL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 471 QSIGASVCYEASFGEN-IIASLSRATLLVNVSNEAWFGDSRGPHQNLQMARMRALESERYLLRATNTGI----------S 539
Cdd:pfam00795 143 GKIGAAICYEIRFPELlRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGeedapwpyghS 222
|
250 260
....*....|....*....|....*
gi 1584356770 540 AIIDPQGRIVGRAPQFQLSVLTGTV 564
Cdd:pfam00795 223 MIIDPDGRILAGAGEWEEGVLIADI 247
|
|
| LNT_N |
pfam20154 |
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal ... |
92-269 |
2.86e-33 |
|
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal transmembrane region of the apolipoprotein N-acyltransferase enzyme. The enzyme catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. This entry does not represent the enzymatic domain found at the C-terminus of the protein.
Pssm-ID: 466311 [Multi-domain] Cd Length: 159 Bit Score: 124.66 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 92 GFLMPFAFAPFGFYGLTIVALALLFQVLLV-ASAGRGFWRGWIFGLAMFGTGVFWIHESFR-FAAVSLPLALLLTGglig 169
Cdd:pfam20154 1 GLLLSLAFPPFGLWPLAWVALAPLLLALEArSSPRRAFLLGFLFGLGFFGLGLYWLGVSLHtFGGAPLPLALLLLL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 170 ILAIYPALFGFFAALWSRRfampsgsaptpasgrllsISLGALLVFPAGWTLLEWMRGWFLTGFPWLQVGYAHGDSP-LA 248
Cdd:pfam20154 77 LLALYLALFALAAWLLKRL------------------WGLFRALLFAALWVGLEYLRGWPFGGFPWGLLGYSQADGPpLI 138
|
170 180
....*....|....*....|.
gi 1584356770 249 GLAPLLGVYGVGWAVALSAGL 269
Cdd:pfam20154 139 QLAPLGGVYGVSFLVVLVNAL 159
|
|
| nitrilase |
cd07197 |
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
324-553 |
1.57e-21 |
|
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.
Pssm-ID: 143587 [Multi-domain] Cd Length: 253 Bit Score: 94.31 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 324 VALIQGNIPQDEKwlpalrQPTLERYLSLTRR--EAGRDLVVWPETALPGSYHHFTDFIAI------------LRREARF 389
Cdd:cd07197 1 IAAVQLAPKIGDV------EANLAKALRLIKEaaEQGADLIVLPELFLTGYSFESAKEDLDlaeeldgptleaLAELAKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 390 HHMNILFGVPtlEGKSQRHFNSIAAITDMGEVLF-YHKKHLVPFGEYLPmagilrgildflkipmsdFSAGpAGQLPFSV 468
Cdd:cd07197 75 LGIYIVAGIA--EKDGDKLYNTAVVIDPDGEIIGkYRKIHLFDFGERRY------------------FSPG-DEFPVFDT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 469 AGQSIGASVCYEASFGENI-IASLSRATLLVNVSNeawFGDSRGPHQNLqMARMRALESERYLLRATNTGI--------- 538
Cdd:cd07197 134 PGGKIGLLICYDLRFPELArELALKGADIILVPAA---WPTARREHWEL-LLRARAIENGVYVVAANRVGEegglefagg 209
|
250
....*....|....*
gi 1584356770 539 SAIIDPQGRIVGRAP 553
Cdd:cd07197 210 SMIVDPDGEVLAEAS 224
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
324-554 |
1.48e-19 |
|
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 88.77 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 324 VALIQGNIPQDEKwlpalrQPTLERYLSLTRR--EAGRDLVVWPETALPG------SYHHFTD-----FIAILRREARFH 390
Cdd:COG0388 4 IALAQLNPTVGDI------EANLAKIEELIREaaAQGADLVVFPELFLTGyppeddDLLELAEpldgpALAALAELAREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 391 HMNILFGVPtLEGKSQRHFNSIAAITDMGEVL-FYHKKHLVPFGEYlpmagilrgildflkipmsD----FSAGPAgQLP 465
Cdd:COG0388 78 GIAVVVGLP-ERDEGGRLYNTALVIDPDGEILgRYRKIHLPNYGVF-------------------DekryFTPGDE-LVV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 466 FSVAGQSIGASVCYEASFGENI-IASLSRATLLVNVSNeawFGDSRGPHQNLQMARMRALESERYLLRATNTGI------ 538
Cdd:COG0388 137 FDTDGGRIGVLICYDLWFPELArALALAGADLLLVPSA---SPFGRGKDHWELLLRARAIENGCYVVAANQVGGedglvf 213
|
250
....*....|....*....
gi 1584356770 539 ---SAIIDPQGRIVGRAPQ 554
Cdd:COG0388 214 dggSMIVDPDGEVLAEAGD 232
|
|
| PRK12291 |
PRK12291 |
apolipoprotein N-acyltransferase; Reviewed |
93-544 |
4.31e-18 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 237042 [Multi-domain] Cd Length: 418 Bit Score: 86.95 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 93 FLMPFaFAPFGFYgltivalallfqVLLVASAGRGFWRGWIFGLAMFgtgvFWIHESFRFAAVS--LPLALLLTGGLIGI 170
Cdd:PRK12291 40 FLSSL-LALLGLY------------LLLKSPRNSAFASGFFVGILWF----YWIGLSFRYYDLTylIPLIIILIGLVYGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 171 LaIYPALFGFFAALwsrRFAMpsgsaptpasgrLLSISlgallvfpagwtllewmrgwFLT--GFPWLQVGyahgdspla 248
Cdd:PRK12291 103 L-FYLLLFLKNPYL---RLLL------------LFGLS--------------------FIHpfGFDWLNPE--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 249 glapLLGVYGVGWAVALSAGLLLVAFRLVMENRnlATKARIIGLSSLLALgggiwggsswLDQGAWSTPTGAPIGVALIQ 328
Cdd:PRK12291 138 ----IFFVYSYFDVSKLSLALIFLAAIFLYKKY--KKKYKIIGVLLLLFA----------LDFKPFKTSDLPLVNIELVN 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 329 GNIPQDEKWLPALRQPTLERYLSLTRR--EAGRDLVVWPETALPGSYHHFTDFIAILrrEARFHHMNILFGVPTLEGKSq 406
Cdd:PRK12291 202 TNIPQDLKWDKENLKSIINENLKEIDKaiDEKKDLIVLPETAFPLALNNSPILLDKL--KELSHKITIITGALRVEDGH- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 407 rHFNSiAAITDMGEVLFYHKKHLVPFGEYLPMAgilrgilDFLKIPM--------SDFSAGPAgQLPFSVAGQSIGASVC 478
Cdd:PRK12291 279 -IYNS-TYIFSKGNVQIADKVILVPFGEEIPLP-------KFFKKPInklffggaSDFSKASK-FSDFTLDGVKFRNAIC 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1584356770 479 YEASfGENIIASLSRAtlLVNVSNEAWFGDSRGPH-QNLQMaRMRALESERYLLRATNTGISAIIDP 544
Cdd:PRK12291 349 YEAT-SEELYEGNPKI--VIAISNNAWFVPSIEPTlQKLLL-KYYARKYGKTIYHSANGSPSYIITP 411
|
|
| nitrilase_3 |
cd07581 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
346-552 |
1.20e-12 |
|
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143605 Cd Length: 255 Bit Score: 68.37 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 346 LERYLSLTRR--EAGRDLVVWPETAL---PGSYHHFTD--------FIAILRREARFHHMNILFGVPTlEGKSQRHFNSI 412
Cdd:cd07581 16 LEKVRRLLAEaaAAGADLVVFPEYTMarfGDGLDDYARvaepldgpFVSALARLARELGITVVAGMFE-PAGDGRVYNTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 413 AAITDMGEVL-FYHKKHLvpfgeYlpmagilrgilDFLKIPMSDFSAgPAGQLP---FSVAGQSIGASVCYEASFGEnii 488
Cdd:cd07581 95 VVVGPDGEIIaVYRKIHL-----Y-----------DAFGFRESDTVA-PGDELPpvvFVVGGVKVGLATCYDLRFPE--- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584356770 489 asLSR------ATLLVNVSneAWFgdsRGP---HQNLQMARMRALESERYLLRA-----TNTGISAIIDPQGRIVGRA 552
Cdd:cd07581 155 --LARalalagADVIVVPA--AWV---AGPgkeEHWETLLRARALENTVYVAAAgqagpRGIGRSMVVDPLGVVLADL 225
|
|
| R-amidase_like |
cd07576 |
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
324-553 |
3.34e-12 |
|
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer.
Pssm-ID: 143600 Cd Length: 254 Bit Score: 66.83 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 324 VALIQGNIPqdekwlPALRQPTLERYLSLTRR--EAGRDLVVWPETALPGsYH-----------HFTDFIAILRREARFH 390
Cdd:cd07576 2 LALYQGPAR------DGDVAANLARLDEAAARaaAAGADLLVFPELFLTG-YNigdavarlaepADGPALQALRAIARRH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 391 HMNILFGVPtlEGKSQRHFNSIAAITDMGEVLF-YHKKHLvpFGEYlpmagiLRGIldflkipmsdFSAGpAGQLPFSVA 469
Cdd:cd07576 75 GIAIVVGYP--ERAGGAVYNAAVLIDEDGTVLAnYRKTHL--FGDS------ERAA----------FTPG-DRFPVVELR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 470 GQSIGASVCYEASFGENI-IASLSRATL-LVNVSNEAWFGDSrgpHQNLQMArmRALESERYLLRA---------TNTGI 538
Cdd:cd07576 134 GLRVGLLICYDVEFPELVrALALAGADLvLVPTALMEPYGFV---ARTLVPA--RAFENQIFVAYAnrcgaedglTYVGL 208
|
250
....*....|....*
gi 1584356770 539 SAIIDPQGRIVGRAP 553
Cdd:cd07576 209 SSIAGPDGTVLARAG 223
|
|
| nitrilase_5 |
cd07583 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
324-549 |
8.26e-10 |
|
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143607 Cd Length: 253 Bit Score: 59.86 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 324 VALIQGNIpQDEKwlPALRQPTLERYLSLTRrEAGRDLVVWPETALPGsYHHFTDF----------IAILRREARFHHMN 393
Cdd:cd07583 2 IALIQLDI-VWGD--PEANIERVESLIEEAA-AAGADLIVLPEMWNTG-YFLDDLYeladedggetVSFLSELAKKHGVN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 394 ILFG-VPTLEGKsqRHFNSIAAITDMGEVLF-YHKKHLVPFG---EYlpmagilrgildflkipmsdFSAGpAGQLPFSV 468
Cdd:cd07583 77 IVAGsVAEKEGG--KLYNTAYVIDPDGELIAtYRKIHLFGLMgedKY--------------------LTAG-DELEVFEL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 469 AGQSIGASVCYEASFGENI-IASLSRATLLVNVSNeaWfGDSRGPH-QNLQMARmrALESERYLLrATNT---------- 536
Cdd:cd07583 134 DGGKVGLFICYDLRFPELFrKLALEGAEILFVPAE--W-PAARIEHwRTLLRAR--AIENQAFVV-ACNRvgtdggnefg 207
|
250
....*....|...
gi 1584356770 537 GISAIIDPQGRIV 549
Cdd:cd07583 208 GHSMVIDPWGEVL 220
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
355-561 |
1.57e-06 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 50.93 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 355 REAGRDLVVWPETALPGS------YHhfTDFIAILRRE----ARFHHMN--ILFGVPTLEGksQRHFNSIAAITDmGEVL 422
Cdd:PRK13981 30 ADAGADLLLFPELFLSGYppedllLR--PAFLAACEAAlerlAAATAGGpaVLVGHPWREG--GKLYNAAALLDG-GEVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 423 -FYHKKHLVPFGEYlpmagilrgildflkipmsD----FSAGPAGqLPFSVAGQSIGASVCYEASFGEnIIASLSR--AT 495
Cdd:PRK13981 105 aTYRKQDLPNYGVF-------------------DekryFAPGPEP-GVVELKGVRIGVPICEDIWNPE-PAETLAEagAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1584356770 496 LLVNVSNEAWfgdSRG-PHQNLQMARMRALESERYLLRATNT---------GISAIIDPQGRIVGRAPQFQLSVLT 561
Cdd:PRK13981 164 LLLVPNASPY---HRGkPDLREAVLRARVRETGLPLVYLNQVggqdelvfdGASFVLNADGELAARLPAFEEQIAV 236
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
80-298 |
6.35e-06 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 49.23 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 80 GLAMGDVVALAAGFLMPFAFAPFGFYGLTIVALALLFQVLLV-----ASAGRGFWRGWIFGLAMFGTGVFWIHESFRFAA 154
Cdd:COG5373 440 LLQLAPLAALLAAYWPVANLAGSYLWALLALALAALFAALALrlarrRSAGLRLWGAAWWALAALAAIALALTLLLEEAA 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 155 VSLPLALL-LTGGLIGILAIYPALFGFFAALWS----RRFAMPS-GSAPTPASGRLLSISLGALLVFPAGWTLL------ 222
Cdd:COG5373 520 LTLALALLvLSLAWLARRLDWPLLRWLAALLLPlvllRLLWDPGlVGGPLAGFNWLLWGYGGPLLALAAAAWLLrrrrlr 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1584356770 223 ---EWMRGWFLTGFPWLQVGYAhgdspLAGLAPLLGVYGVGWAVALSAGLLLVAfrLVMENRNLATKARIIGLSSLLAL 298
Cdd:COG5373 600 rwlEAAALWLLVLLLALELRYL-----LWGGDLFASEWSLAEAGLLALLWLALA--LALLRRWLRRAGRVYRLAALALG 671
|
|
| Ph0642_like |
cd07577 |
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ... |
324-561 |
5.79e-05 |
|
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This subgroup was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143601 Cd Length: 259 Bit Score: 44.98 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 324 VALIQGNipqdekwlPALRQPT--LERYLSLTR-REAgrDLVVWPETALPGsyHHFTD---------------FIAILRR 385
Cdd:cd07577 2 VGYVQFN--------PKFGEVEknLKKVESLIKgVEA--DLIVLPELFNTG--YAFTSkeevaslaesipdgpTTRFLQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 386 EARFHHMNILFGVPTLEGKsqRHFNSIAAITDMGEVLFYHKKHLvpfgeylpmagilrgildFLKIPMSdFSAGPAGQLP 465
Cdd:cd07577 70 LARETGAYIVAGLPERDGD--KFYNSAVVVGPEGYIGIYRKTHL------------------FYEEKLF-FEPGDTGFRV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 466 FSVAGQSIGASVCYEASFGENI-IASLSRATLLVNVSNEAWfgdsrgPHQNLQMaRMRALESERYLLRA----------- 533
Cdd:cd07577 129 FDIGDIRIGVMICFDWYFPEAArTLALKGADIIAHPANLVL------PYCPKAM-PIRALENRVFTITAnrigteergge 201
|
250 260 270
....*....|....*....|....*....|
gi 1584356770 534 --TNTGISAIIDPQGRIVGRAPQFQLSVLT 561
Cdd:cd07577 202 tlRFIGKSQITSPKGEVLARAPEDGEEVLV 231
|
|
| nitrilase_7 |
cd07585 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
355-549 |
6.34e-05 |
|
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143609 Cd Length: 261 Bit Score: 45.00 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 355 REAGRDLVVWPETALPGsYHHFTDF-----------IAILRREARFHHMNILFGvpTLEGKSQRHFNSIAAITDMGEVLF 423
Cdd:cd07585 29 AAQGAELVCFPEMCITG-YTHVRALsreaevpdgpsTQALSDLARRYGLTILAG--LIEKAGDRPYNTYLVCLPDGLVHR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 424 YHKKHLVPFGEYLPMAGilrgilDFLKIpmsdfsagpagqlpFSVAGQSIGASVCYEASFGENI-IASLSRATLLvnvsn 502
Cdd:cd07585 106 YRKLHLFRREHPYIAAG------DEYPV--------------FATPGVRFGILICYDNHFPENVrATALLGAEIL----- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1584356770 503 eawFGDSRGPHQNLQMAR---MRALESERY----LLRATN----------TGISAIIDPQGRIV 549
Cdd:cd07585 161 ---FAPHATPGTTSPKGRewwMRWLPARAYdngvFVAACNgvgrdggevfPGGAMILDPYGRVL 221
|
|
| PRK13825 |
PRK13825 |
conjugal transfer protein TraB; Provisional |
112-536 |
8.44e-04 |
|
conjugal transfer protein TraB; Provisional
Pssm-ID: 237523 [Multi-domain] Cd Length: 388 Bit Score: 41.92 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 112 LALLFQVLLVASAGRGFWRG--WIFGLAMFgTGVFWIHESFRFAAVSLPLALLLT---GGLIGILAIYPALFGFFAALW- 185
Cdd:PRK13825 6 LQALALILAGAAIGFLGWSGhvLLLPLALA-FPVLWANSPSRLAAALVSAGYFLAasrGLPQGVAAFFGSDLWPGLALWl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 186 --SRRFAMPSGSAPTPASGRllsislgallvFPAGWTLLewmrGWFLTGFPWLQ-VGYAHGDSPLAGLAPLLGVYGVGWA 262
Cdd:PRK13825 85 aaSLSFVLVHAALWTAPRGR-----------ARALRYLL----AAVLMAVPPFGiTGWAHPLTAAGVLFPGWGWWGLGAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 263 VALSAGLllVAFRLvmenrnlatKARIIGLSSLLALGGGiwggsswldqgAWSTPTGAP--IGVALIQGNIPQDEKWLPA 340
Cdd:PRK13825 150 AAGLAGL--TTRLW---------PAVAIALVGLWLWSAA-----------AWTLPRAPAgwVGVDTQLGRSLGRDASLER 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 341 LRQpTLERYLSltRREAGRDLVVWPETALpGSYHHFTDFIaiLRREARFHHMNILFGVPTLEgkSQRHFNSIAAITDMGE 420
Cdd:PRK13825 208 RRE-LIATVRA--AAAAGARVVVLPESAL-GFWTPTTERL--WRESLRGSDVTVIAGAAVVD--PGGYDNVLVAISAGGG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 421 VLFYHKKHLVPFGEYLPMaGILRGILDFLkipMSDFSAGPAgqlpFSVAGQSIGASVCYEA-SFGENIIASLSRATLLVN 499
Cdd:PRK13825 280 RILYRERMPVPVSMWQPW-RPWTGQGGGA---RAHFFANPV----VEIDGRRAAPLICYEQlLVWPVLQSMLHSPDVIVA 351
|
410 420 430
....*....|....*....|....*....|....*..
gi 1584356770 500 VSNEAWFGDSRGPHQNLQMARMRALESERYLLRATNT 536
Cdd:PRK13825 352 VGNGWWTKGTSIVAIQRASAEAWARLFGVPLVRAFNR 388
|
|
| DCase |
cd07569 |
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ... |
322-429 |
1.52e-03 |
|
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses N-carbamyl-D-amino acids to produce D-amino acids. It is an important biocatalyst in the pharmaceutical industry, producing useful D-amino acids for example in the preparation of beta-lactam antibiotics. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 6. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Agrobacterium radiobacter DCase forms a tetramer (dimer of dimers). Some DCases may form trimers.
Pssm-ID: 143593 Cd Length: 302 Bit Score: 40.76 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584356770 322 IGVALIQ-GNIPQDEKwlpalRQPTLERYLSLTRREA--GRDLVVWPETAL-----------PGSYHHF------TDFIA 381
Cdd:cd07569 4 VILAAAQmGPIARAET-----RESVVARLIALLEEAAsrGAQLVVFPELALttffprwyfpdEAELDSFfetempNPETQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1584356770 382 ILRREARFHHMNILFGVP--TLEGKSQRHFNSIAAITDMGEVLF-YHKKHL 429
Cdd:cd07569 79 PLFDRAKELGIGFYLGYAelTEDGGVKRRFNTSILVDKSGKIVGkYRKVHL 129
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