|
Name |
Accession |
Description |
Interval |
E-value |
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
25-483 |
6.16e-123 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 367.63 E-value: 6.16e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 25 PRGWWAAGIIGVAMLVAALspwRKPLHLGWAALIAVVHSAVLYLFTLPWIGELV---GNMPY-------IALAIFLSLYS 94
Cdd:COG0815 1 PFGLWPLAFVALAPLLLLL---RGARSPRRAFLLGWLFGLGFFLAGLYWLYVSLhvfGGLPAwlaplavLLLAAYLALFF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 95 ILLGTGGAALLRLNYGFAL--FPFFYVAVEMLRSSVpFGGFAWVRLAWGQIE-GPLANLAPWGGPALISF--AVVCVAAG 169
Cdd:COG0815 78 ALAAALARRLRRRGGLLRPlaFAALWVLLEWLRGWL-FTGFPWLRLGYSQADfSPLAQLAPLGGVYGLSFlvVLVNALLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 170 VVGLARAPRLACAFLAVPLLAGLIASQGVNRPSHITSTITVAAVQGNVPRLGLDFAAQRRAVLDNHVRVTEQAAQDgaRP 249
Cdd:COG0815 157 LALLRRRRRLAALALALALLLAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKWDPEQRREILDRYLDLTRELADD--GP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 250 DIVIWPENSSDINPFANEDARALIDGAAHDIDAPILVGTLTRDEVGAR--NTMQVFNPDGSVGQHHYKKYLQPFGETMPM 327
Cdd:COG0815 235 DLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRyyNSALLLDPDGGILGRYDKHHLVPFGEYVPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 328 REFFRKITDLVDLA-GDMKPGDGSGVVTMAGTAVGVATCYEVSFDQAFRTAIDNGAQILTTPTNNATFSDSDMTYQQLAM 406
Cdd:COG0815 315 RDLLRPLIPFLDLPlGDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNITNDAWFGDSIGPYQHLAI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093433562 407 SRLRAMEADRAVVVAATSGVSAIVHPDGSVSQESGIFEPAYLEEELPLREGRTFAVRYGSLLQWLMTIIGTVCALFA 483
Cdd:COG0815 395 ARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLLLLLALLLALLL 471
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
208-475 |
4.04e-93 |
|
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: 283.72 E-value: 4.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 208 ITVAAVQGNVPRLGLDFAAQRRAVLDNHVRVTEQAAQDgaRPDIVIWPENSSDINPFANEDARALIDGAAHDIDAPILVG 287
Cdd:cd07571 1 LRVALVQGNIPQDEKWDPEQRQATLDRYLDLTRELADE--KPDLVVWPETALPFDLQRDPDALARLARAARAVGAPLLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 288 TLTRDEVGAR--NTMQVFNPDGSVGQHHYKKYLQPFGETMPMREFFRKITDLVDLA-GDMKPGDGSGVVTMAG-TAVGVA 363
Cdd:cd07571 79 APRREPGGGRyyNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPmGDFSPGTGPQPLLLGGgVRVGPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 364 TCYEVSFDQAFRTAIDNGAQILTTPTNNATFSDSDMTYQQLAMSRLRAMEADRAVVVAATSGVSAIVHPDGSVSQESGIF 443
Cdd:cd07571 159 ICYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVARLPLF 238
|
250 260 270
....*....|....*....|....*....|..
gi 1093433562 444 EPAYLEEELPLREGRTFAVRYGSLLQWLMTII 475
Cdd:cd07571 239 EAGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
8-488 |
9.36e-74 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 241.71 E-value: 9.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 8 RLVLAALSGAVTYLSVEPRGWWAAGIIGVAMLVAAL--SPWRKPLHLGWAaliavvHSAVLYLFTLPWIG---ELVGNMP 82
Cdd:PRK00302 8 RLLLALLAGALGTLAFAPFDLWPLALLSLAGLLWLLlgASPKQAALIGFL------WGFGYFGSGLSWIYvsiHTFGGMP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 83 YIA-------LAIFLSLYSiLLGTGGAALLRLNYGFAL---FPFFYVAVEMLRSSVpFGGFAWVRLAWGQIE-GPLANLA 151
Cdd:PRK00302 82 AWLapllvllLAAYLALYP-ALFAALWRRLWPKSGLRRalaLPALWVLTEWLRGWL-LTGFPWLALGYSQIPdGPLAQLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 152 PWGGPALISFAVVCVAAGVVGLARAPRLACAFLAVPLLAGLIASQGVNRPSHIT----STITVAAVQGNVP-RLGLDfAA 226
Cdd:PRK00302 160 PIFGVYGLSFLVVLVNALLALALIKRRWRLALLALLLLLLAALGYGLRRLQWTTpapePALKVALVQGNIPqSLKWD-PA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 227 QRRAVLDNHVRVTEQAAQDGarpDIVIWPENSsdINPFANEDARAL---IDGAAHDIDAPILVGTLTRDEVGAR----NT 299
Cdd:PRK00302 239 GLEATLQKYLDLSRPALGPA---DLIIWPETA--IPFLLEDLPQAFlkaLDDLAREKGSALITGAPRAENKQGRydyyNS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 300 MQVFNPDGSVGqhHYKKY-LQPFGETMPMREFFRKITDLVDL-AGDMKPGDGSGVVTMA-GTAVGVATCYEVSFDQAFRT 376
Cdd:PRK00302 314 IYVLGPYGILN--RYDKHhLVPFGEYVPLESLLRPLAPFFNLpMGDFSRGPYVQPPLLAkGLKLAPLICYEIIFPEEVRA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 377 AIDNGAQILTTPTNNATFSDSDMTYQQLAMSRLRAMEADRAVVVAATSGVSAIVHPDGSVSQESGIFEPAYLEEELPLRE 456
Cdd:PRK00302 392 NVRQGADLLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDPLGRIIAQLPQFTEGVLDGTVPPTT 471
|
490 500 510
....*....|....*....|....*....|..
gi 1093433562 457 GRTFAVRYGSLLQWLMTIIGTVCALFAIHSTR 488
Cdd:PRK00302 472 GLTPYARWGDWPLLLLALLLLLLALLLALRRR 503
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
66-436 |
3.25e-70 |
|
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: 228.78 E-value: 3.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 66 LYLFTLPWIGE--LVGNMPYIALAIFLSLYSILLG---TGGAALLRLNYGFAL----FPFFYVAVEMLRSSVPFGgFAWV 136
Cdd:TIGR00546 5 FFLAGLFWLGIalSVNGFIAFVAGLLVVGLPALLAlfpGLAAYLLRRLAPFRKvllaLPLLWTLAEWLRSFGFLG-FPWG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 137 RLAWGQIEGPLANLAPWGGPALISFAVVCVAAGVVGLAR-----APRLACAFLAVPLLAGLIASQGVNRPSHITSTITVA 211
Cdd:TIGR00546 84 LIGYAQSSLPLIQIASIFGVWGLSFLVVFLNALLALVLLkkesfKKLLAIAVVVLLAALGFLLYELKSATPVPGPTLNVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 212 AVQGNVPRLGLDFAAQRRAVLDNHVRVTEQAAQdgaRPDIVIWPENSSDINPFANEDARAL-IDGAAHDIDAPILVGTLT 290
Cdd:TIGR00546 164 LVQPNIPQDLKFDSEGLEAILEILTSLTKQAVE---KPDLVVWPETAFPFDLENSPQKLADrLKLLVLSKGIPILIGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 291 RDEVGAR---NTMQVFNPDGSVGQHHYKKYLQPFGETMPMREFFRKITDLVDLA--GDMKPGDGSGVVTMAGTAVGVATC 365
Cdd:TIGR00546 241 AVPGGPYhyyNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSKLFFLLsqEDFSRGPGPQVLKLPGGKIAPLIC 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093433562 366 YEVSFDQAFRTAIDNGAQILTTPTNNATFSDSDMTYQQLAMSRLRAMEADRAVVVAATSGVSAIVHPDGSV 436
Cdd:TIGR00546 321 YESIFPDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFRAIENGRPLVRATNTGISAVIDPRGRT 391
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
209-454 |
7.97e-20 |
|
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: 88.95 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 209 TVAAVQGNVPrlgldfAAQRRAVLDNHVRVTEQAAQDGArpDIVIWPENS-----SDINPFANEDAR-----ALIDGAAH 278
Cdd:pfam00795 1 RVALVQLPQG------FWDLEANLQKALELIEEAARYGA--DLIVLPELFitgypCWAHFLEAAEVGdgetlAGLAALAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 279 DIDAPILVGTLTRDEVGAR--NTMQVFNPDGSVGQHHYKKYLqpFGETMPMREFFRKItdlvdlagdMKPGDGSGVVTMA 356
Cdd:pfam00795 73 KNGIAIVIGLIERWLTGGRlyNTAVLLDPDGKLVGKYRKLHL--FPEPRPPGFRERVL---------FEPGDGGTVFDTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 357 GTAVGVATCYEVSFDQAFRTAIDNGAQILTTPTNNATFSDSDMTYQQLAMSRLRAMEADRAVVVAATSGV---------- 426
Cdd:pfam00795 142 LGKIGAAICYEIRFPELLRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGeedapwpygh 221
|
250 260
....*....|....*....|....*...
gi 1093433562 427 SAIVHPDGSVSQESGIFEPAYLEEELPL 454
Cdd:pfam00795 222 SMIIDPDGRILAGAGEWEEGVLIADIDL 249
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
25-483 |
6.16e-123 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 367.63 E-value: 6.16e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 25 PRGWWAAGIIGVAMLVAALspwRKPLHLGWAALIAVVHSAVLYLFTLPWIGELV---GNMPY-------IALAIFLSLYS 94
Cdd:COG0815 1 PFGLWPLAFVALAPLLLLL---RGARSPRRAFLLGWLFGLGFFLAGLYWLYVSLhvfGGLPAwlaplavLLLAAYLALFF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 95 ILLGTGGAALLRLNYGFAL--FPFFYVAVEMLRSSVpFGGFAWVRLAWGQIE-GPLANLAPWGGPALISF--AVVCVAAG 169
Cdd:COG0815 78 ALAAALARRLRRRGGLLRPlaFAALWVLLEWLRGWL-FTGFPWLRLGYSQADfSPLAQLAPLGGVYGLSFlvVLVNALLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 170 VVGLARAPRLACAFLAVPLLAGLIASQGVNRPSHITSTITVAAVQGNVPRLGLDFAAQRRAVLDNHVRVTEQAAQDgaRP 249
Cdd:COG0815 157 LALLRRRRRLAALALALALLLAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKWDPEQRREILDRYLDLTRELADD--GP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 250 DIVIWPENSSDINPFANEDARALIDGAAHDIDAPILVGTLTRDEVGAR--NTMQVFNPDGSVGQHHYKKYLQPFGETMPM 327
Cdd:COG0815 235 DLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRyyNSALLLDPDGGILGRYDKHHLVPFGEYVPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 328 REFFRKITDLVDLA-GDMKPGDGSGVVTMAGTAVGVATCYEVSFDQAFRTAIDNGAQILTTPTNNATFSDSDMTYQQLAM 406
Cdd:COG0815 315 RDLLRPLIPFLDLPlGDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNITNDAWFGDSIGPYQHLAI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093433562 407 SRLRAMEADRAVVVAATSGVSAIVHPDGSVSQESGIFEPAYLEEELPLREGRTFAVRYGSLLQWLMTIIGTVCALFA 483
Cdd:COG0815 395 ARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLLLLLALLLALLL 471
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
208-475 |
4.04e-93 |
|
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: 283.72 E-value: 4.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 208 ITVAAVQGNVPRLGLDFAAQRRAVLDNHVRVTEQAAQDgaRPDIVIWPENSSDINPFANEDARALIDGAAHDIDAPILVG 287
Cdd:cd07571 1 LRVALVQGNIPQDEKWDPEQRQATLDRYLDLTRELADE--KPDLVVWPETALPFDLQRDPDALARLARAARAVGAPLLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 288 TLTRDEVGAR--NTMQVFNPDGSVGQHHYKKYLQPFGETMPMREFFRKITDLVDLA-GDMKPGDGSGVVTMAG-TAVGVA 363
Cdd:cd07571 79 APRREPGGGRyyNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPmGDFSPGTGPQPLLLGGgVRVGPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 364 TCYEVSFDQAFRTAIDNGAQILTTPTNNATFSDSDMTYQQLAMSRLRAMEADRAVVVAATSGVSAIVHPDGSVSQESGIF 443
Cdd:cd07571 159 ICYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVARLPLF 238
|
250 260 270
....*....|....*....|....*....|..
gi 1093433562 444 EPAYLEEELPLREGRTFAVRYGSLLQWLMTII 475
Cdd:cd07571 239 EAGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
8-488 |
9.36e-74 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 241.71 E-value: 9.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 8 RLVLAALSGAVTYLSVEPRGWWAAGIIGVAMLVAAL--SPWRKPLHLGWAaliavvHSAVLYLFTLPWIG---ELVGNMP 82
Cdd:PRK00302 8 RLLLALLAGALGTLAFAPFDLWPLALLSLAGLLWLLlgASPKQAALIGFL------WGFGYFGSGLSWIYvsiHTFGGMP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 83 YIA-------LAIFLSLYSiLLGTGGAALLRLNYGFAL---FPFFYVAVEMLRSSVpFGGFAWVRLAWGQIE-GPLANLA 151
Cdd:PRK00302 82 AWLapllvllLAAYLALYP-ALFAALWRRLWPKSGLRRalaLPALWVLTEWLRGWL-LTGFPWLALGYSQIPdGPLAQLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 152 PWGGPALISFAVVCVAAGVVGLARAPRLACAFLAVPLLAGLIASQGVNRPSHIT----STITVAAVQGNVP-RLGLDfAA 226
Cdd:PRK00302 160 PIFGVYGLSFLVVLVNALLALALIKRRWRLALLALLLLLLAALGYGLRRLQWTTpapePALKVALVQGNIPqSLKWD-PA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 227 QRRAVLDNHVRVTEQAAQDGarpDIVIWPENSsdINPFANEDARAL---IDGAAHDIDAPILVGTLTRDEVGAR----NT 299
Cdd:PRK00302 239 GLEATLQKYLDLSRPALGPA---DLIIWPETA--IPFLLEDLPQAFlkaLDDLAREKGSALITGAPRAENKQGRydyyNS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 300 MQVFNPDGSVGqhHYKKY-LQPFGETMPMREFFRKITDLVDL-AGDMKPGDGSGVVTMA-GTAVGVATCYEVSFDQAFRT 376
Cdd:PRK00302 314 IYVLGPYGILN--RYDKHhLVPFGEYVPLESLLRPLAPFFNLpMGDFSRGPYVQPPLLAkGLKLAPLICYEIIFPEEVRA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 377 AIDNGAQILTTPTNNATFSDSDMTYQQLAMSRLRAMEADRAVVVAATSGVSAIVHPDGSVSQESGIFEPAYLEEELPLRE 456
Cdd:PRK00302 392 NVRQGADLLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDPLGRIIAQLPQFTEGVLDGTVPPTT 471
|
490 500 510
....*....|....*....|....*....|..
gi 1093433562 457 GRTFAVRYGSLLQWLMTIIGTVCALFAIHSTR 488
Cdd:PRK00302 472 GLTPYARWGDWPLLLLALLLLLLALLLALRRR 503
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
66-436 |
3.25e-70 |
|
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: 228.78 E-value: 3.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 66 LYLFTLPWIGE--LVGNMPYIALAIFLSLYSILLG---TGGAALLRLNYGFAL----FPFFYVAVEMLRSSVPFGgFAWV 136
Cdd:TIGR00546 5 FFLAGLFWLGIalSVNGFIAFVAGLLVVGLPALLAlfpGLAAYLLRRLAPFRKvllaLPLLWTLAEWLRSFGFLG-FPWG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 137 RLAWGQIEGPLANLAPWGGPALISFAVVCVAAGVVGLAR-----APRLACAFLAVPLLAGLIASQGVNRPSHITSTITVA 211
Cdd:TIGR00546 84 LIGYAQSSLPLIQIASIFGVWGLSFLVVFLNALLALVLLkkesfKKLLAIAVVVLLAALGFLLYELKSATPVPGPTLNVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 212 AVQGNVPRLGLDFAAQRRAVLDNHVRVTEQAAQdgaRPDIVIWPENSSDINPFANEDARAL-IDGAAHDIDAPILVGTLT 290
Cdd:TIGR00546 164 LVQPNIPQDLKFDSEGLEAILEILTSLTKQAVE---KPDLVVWPETAFPFDLENSPQKLADrLKLLVLSKGIPILIGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 291 RDEVGAR---NTMQVFNPDGSVGQHHYKKYLQPFGETMPMREFFRKITDLVDLA--GDMKPGDGSGVVTMAGTAVGVATC 365
Cdd:TIGR00546 241 AVPGGPYhyyNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSKLFFLLsqEDFSRGPGPQVLKLPGGKIAPLIC 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093433562 366 YEVSFDQAFRTAIDNGAQILTTPTNNATFSDSDMTYQQLAMSRLRAMEADRAVVVAATSGVSAIVHPDGSV 436
Cdd:TIGR00546 321 YESIFPDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFRAIENGRPLVRATNTGISAVIDPRGRT 391
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
209-454 |
7.97e-20 |
|
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: 88.95 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 209 TVAAVQGNVPrlgldfAAQRRAVLDNHVRVTEQAAQDGArpDIVIWPENS-----SDINPFANEDAR-----ALIDGAAH 278
Cdd:pfam00795 1 RVALVQLPQG------FWDLEANLQKALELIEEAARYGA--DLIVLPELFitgypCWAHFLEAAEVGdgetlAGLAALAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 279 DIDAPILVGTLTRDEVGAR--NTMQVFNPDGSVGQHHYKKYLqpFGETMPMREFFRKItdlvdlagdMKPGDGSGVVTMA 356
Cdd:pfam00795 73 KNGIAIVIGLIERWLTGGRlyNTAVLLDPDGKLVGKYRKLHL--FPEPRPPGFRERVL---------FEPGDGGTVFDTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 357 GTAVGVATCYEVSFDQAFRTAIDNGAQILTTPTNNATFSDSDMTYQQLAMSRLRAMEADRAVVVAATSGV---------- 426
Cdd:pfam00795 142 LGKIGAAICYEIRFPELLRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGeedapwpygh 221
|
250 260
....*....|....*....|....*...
gi 1093433562 427 SAIVHPDGSVSQESGIFEPAYLEEELPL 454
Cdd:pfam00795 222 SMIIDPDGRILAGAGEWEEGVLIADIDL 249
|
|
| LNT_N |
pfam20154 |
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal ... |
16-161 |
8.29e-20 |
|
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: 86.14 E-value: 8.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 16 GAVTYLSVEPRGWWAAGIIGVAMLVAALSPWRKPlhlGWAALIAVVHSAVLYLFTLPWIGELV---GNMP---YIALAIF 89
Cdd:pfam20154 1 GLLLSLAFPPFGLWPLAWVALAPLLLALEARSSP---RRAFLLGFLFGLGFFGLGLYWLGVSLhtfGGAPlplALLLLLL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093433562 90 LSLYSILLGTGGAALLRLN--YGFALFPFFYVAVEMLRSsVPFGGFAWVRLAWGQIEGP-LANLAPWGGPALISF 161
Cdd:pfam20154 78 LALYLALFALAAWLLKRLWglFRALLFAALWVGLEYLRG-WPFGGFPWGLLGYSQADGPpLIQLAPLGGVYGVSF 151
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
207-436 |
1.05e-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: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 207 TITVAAVQGNVPrlgldfAAQRRAVLDNHVRVTEQAAQDGArpDIVIWPENSsdINPFANEDARAL-----IDG------ 275
Cdd:COG0388 1 TMRIALAQLNPT------VGDIEANLAKIEELIREAAAQGA--DLVVFPELF--LTGYPPEDDDLLelaepLDGpalaal 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 276 --AAHDIDAPILVGTLTRDEVGA-RNTMQVFNPDGSVGQHHYKKYL---QPFGEtmpmREFFRkitdlvdlagdmkPGDG 349
Cdd:COG0388 71 aeLARELGIAVVVGLPERDEGGRlYNTALVIDPDGEILGRYRKIHLpnyGVFDE----KRYFT-------------PGDE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 350 SGVVTMAGTAVGVATCYEVSFDQAFRTAIDNGAQILTTPTNnatfSDSDMTYQQ-LAMSRLRAMEADRAVVVAATSGV-- 426
Cdd:COG0388 134 LVVFDTDGGRIGVLICYDLWFPELARALALAGADLLLVPSA----SPFGRGKDHwELLLRARAIENGCYVVAANQVGGed 209
|
250
....*....|....*..
gi 1093433562 427 -------SAIVHPDGSV 436
Cdd:COG0388 210 glvfdggSMIVDPDGEV 226
|
|
| nitrilase |
cd07197 |
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
210-456 |
2.58e-19 |
|
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: 87.38 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 210 VAAVQGNVPrlgldfAAQRRAVLDNHVRVTEQAAQDGArpDIVIWPE---------NSSDINPFANEDARALIDG---AA 277
Cdd:cd07197 1 IAAVQLAPK------IGDVEANLAKALRLIKEAAEQGA--DLIVLPElfltgysfeSAKEDLDLAEELDGPTLEAlaeLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 278 HDIDAPILVGTLTRDEVGARNTMQVFNPDGSVGQHHYKKYLQPFGEtmpmREFFrkitdlvdlagdmKPGDGSGVVTMAG 357
Cdd:cd07197 73 KELGIYIVAGIAEKDGDKLYNTAVVIDPDGEIIGKYRKIHLFDFGE----RRYF-------------SPGDEFPVFDTPG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 358 TAVGVATCYEVSFDQAFRTAIDNGAQILTTPTNNATFSdsdmTYQQLAMSRLRAMEADRAVVVAATSGV---------SA 428
Cdd:cd07197 136 GKIGLLICYDLRFPELARELALKGADIILVPAAWPTAR----REHWELLLRARAIENGVYVVAANRVGEegglefaggSM 211
|
250 260
....*....|....*....|....*...
gi 1093433562 429 IVHPDGSVsQESGIFEPAYLEEELPLRE 456
Cdd:cd07197 212 IVDPDGEV-LAEASEEEGILVAELDLDE 238
|
|
| nitrilase_3 |
cd07581 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
236-456 |
4.67e-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: 143605 Cd Length: 255 Bit Score: 60.28 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 236 VRVTEQAAQDGArpDIVIWPENSSDINPFANEDARAL---IDG--------AAHDIDAPILVGTLTRDEVG-ARNTMQVF 303
Cdd:cd07581 20 RRLLAEAAAAGA--DLVVFPEYTMARFGDGLDDYARVaepLDGpfvsalarLARELGITVVAGMFEPAGDGrVYNTLVVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 304 NPDGSVgQHHYKK---YlQPFGetmpMREffrkiTDLVdLAGDMKPgdgSGVVTMAGTAVGVATCYEVSFDQAFRTAIDN 380
Cdd:cd07581 98 GPDGEI-IAVYRKihlY-DAFG----FRE-----SDTV-APGDELP---PVVFVVGGVKVGLATCYDLRFPELARALALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 381 GAQILTTPTnnATFSDSDMTYQQLAMSRLRAMEADRAVVVAAT-----SGVSAIVHPDGSVSQESGiFEPAYLEEELPLR 455
Cdd:cd07581 163 GADVIVVPA--AWVAGPGKEEHWETLLRARALENTVYVAAAGQagprgIGRSMVVDPLGVVLADLG-EREGLLVADIDPE 239
|
.
gi 1093433562 456 E 456
Cdd:cd07581 240 R 240
|
|
| R-amidase_like |
cd07576 |
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
209-436 |
5.91e-10 |
|
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: 59.90 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 209 TVAAVQGnvprlgldfAAQRRAVLDNHVRVTEQAAQ-DGARPDIVIWPE------NSSDINP----FANEDARALIDGAA 277
Cdd:cd07576 1 RLALYQG---------PARDGDVAANLARLDEAAARaAAAGADLLVFPElfltgyNIGDAVArlaePADGPALQALRAIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 278 HDIDAPILVGTLTRDEVGARNTMQVFNPDGSVGQHHYKKYLqpFGEtmPMREFFRkitdlvdlagdmkPGDGSGVVTMAG 357
Cdd:cd07576 72 RRHGIAIVVGYPERAGGAVYNAAVLIDEDGTVLANYRKTHL--FGD--SERAAFT-------------PGDRFPVVELRG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 358 TAVGVATCYEVSFDQAFRTAIDNGAQILTTPTNNatfsDSDMTYQQLAMSRLRAME-------ADRAVVVAATS--GVSA 428
Cdd:cd07576 135 LRVGLLICYDVEFPELVRALALAGADLVLVPTAL----MEPYGFVARTLVPARAFEnqifvayANRCGAEDGLTyvGLSS 210
|
....*...
gi 1093433562 429 IVHPDGSV 436
Cdd:cd07576 211 IAGPDGTV 218
|
|
| nitrilase_5 |
cd07583 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
240-441 |
9.74e-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: 59.09 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 240 EQAAQDGArpDIVIWPE--NSSdinpFANEDARALIDGA-----------AHDIDAPILVGTL-TRDEVGARNTMQVFNP 305
Cdd:cd07583 26 EEAAAAGA--DLIVLPEmwNTG----YFLDDLYELADEDggetvsflselAKKHGVNIVAGSVaEKEGGKLYNTAYVIDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 306 DGSVgQHHYKKyLQPFGetmPMREffrkitDLVdlagdMKPGDGSGVVTMAGTAVGVATCYEVSFDQAFRTAIDNGAQIL 385
Cdd:cd07583 100 DGEL-IATYRK-IHLFG---LMGE------DKY-----LTAGDELEVFELDGGKVGLFICYDLRFPELFRKLALEGAEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093433562 386 TTPTnnatfsdsdmtyqQLAMSRL---------RAMEaDRAVVVAATS----------GVSAIVHPDGSVSQESG 441
Cdd:cd07583 164 FVPA-------------EWPAARIehwrtllraRAIE-NQAFVVACNRvgtdggnefgGHSMVIDPWGEVLAEAG 224
|
|
| nitrilase_Rim1_like |
cd07574 |
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ... |
208-445 |
2.43e-09 |
|
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an N-terminal RimI domain (class 12 nitrilases); Some members of this subgroup are implicated in post-translational modification, as they contain an N-terminal GCN5-related N-acetyltransferase (GNAT) protein RimI family domain. 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), this subgroup corresponds to class 12. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143598 Cd Length: 280 Bit Score: 58.37 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 208 ITVAAVQGNVPRLG--LDFAAQRRAVLDnhvrvteQAAQDGArpDIVIWPENS-----SDINPFANEDARALIDGAAH-- 278
Cdd:cd07574 1 VRVAAAQYPLRRYAsfEEFAAKVEYWVA-------EAAGYGA--DLLVFPEYFtmellSLLPEAIDGLDEAIRALAALtp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 279 DIDAP-----------ILVGT-LTRDEVGARNTMQVFNPDGSVGqHHYKKYLQPFgetmpMREffrkitdlvdlAGDMKP 346
Cdd:cd07574 72 DYVALfselarkyginIIAGSmPVREDGRLYNRAYLFGPDGTIG-HQDKLHMTPF-----ERE-----------EWGISG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 347 GDGSGVVTMAGTAVGVATCYEVSFDQAFRTAIDNGAQILTTPTNNATFSdsdmtYQQLAM--SRLRAMEADRAVVVAATS 424
Cdd:cd07574 135 GDKLKVFDTDLGKIGILICYDSEFPELARALAEAGADLLLVPSCTDTRA-----GYWRVRigAQARALENQCYVVQSGTV 209
|
250 260
....*....|....*....|..
gi 1093433562 425 GVSAIVHP-DGSVSQeSGIFEP 445
Cdd:cd07574 210 GNAPWSPAvDVNYGQ-AAVYTP 230
|
|
| nitrilase_2 |
cd07580 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
209-434 |
3.28e-07 |
|
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: 143604 Cd Length: 268 Bit Score: 51.58 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 209 TVAAVQGNvPRLGlDFAAQRRAVLdnhvRVTEQAAQDGARpdIVIWPENSSDINPFANED-----ARALIDGA------- 276
Cdd:cd07580 1 RVACVQFD-PRVG-DLDANLARSI----ELIREAADAGAN--LVVLPELANTGYVFESRDeafalAEEVPDGAstrawae 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 277 -AHDIDAPILVGTLTRDEVGARNTMQVFNPDGSVGQhhYKKyLQPFGETmpmREFFRkitdlvdlagdmkPGD-GSGVVT 354
Cdd:cd07580 73 lAAELGLYIVAGFAERDGDRLYNSAVLVGPDGVIGT--YRK-AHLWNEE---KLLFE-------------PGDlGLPVFD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 355 MAGTAVGVATCYEVSFDQAFRTAIDNGAQILTTPTnNATFSDSDMTYqQLAMSRLRAMEADRA--VVVAATS-------- 424
Cdd:cd07580 134 TPFGRIGVAICYDGWFPETFRLLALQGADIVCVPT-NWVPMPRPPEG-GPPMANILAMAAAHSngLFIACADrvgtergq 211
|
250
....*....|...
gi 1093433562 425 ---GVSAIVHPDG 434
Cdd:cd07580 212 pfiGQSLIVGPDG 224
|
|
| nit |
cd07572 |
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ... |
240-388 |
2.60e-06 |
|
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); This subgroup includes mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor, fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong 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 10.
Pssm-ID: 143596 Cd Length: 265 Bit Score: 48.96 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 240 EQAAQDGArpDIVIWPENSSdinpFANEDARALIDGAAHDIDAPIL---------------VGTL-TRDEVGAR--NTMQ 301
Cdd:cd07572 25 EEAAAQGA--KLVVLPECFN----YPGGTDAFKLALAEEEGDGPTLqalselakehgiwlvGGSIpERDDDDGKvyNTSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 302 VFNPDGSVGQHHykkylqpfgetmpmreffRKIT--DlVDLAGDMK--------PGDGSGVVTMAGTAVGVATCYEVSFD 371
Cdd:cd07572 99 VFDPDGELVARY------------------RKIHlfD-VDVPGGISyresdtltPGDEVVVVDTPFGKIGLGICYDLRFP 159
|
170
....*....|....*..
gi 1093433562 372 QAFRTAIDNGAQILTTP 388
Cdd:cd07572 160 ELARALARQGADILTVP 176
|
|
| PRK12291 |
PRK12291 |
apolipoprotein N-acyltransferase; Reviewed |
278-432 |
5.79e-06 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 237042 [Multi-domain] Cd Length: 418 Bit Score: 48.44 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 278 HDIDapILVGTLTRDEVGARNTMQVFNpDGSVgQHHYKKYLQPFGETMPMREFFRK-ITDL-----VDLAGDMKPGDgsg 351
Cdd:PRK12291 263 HKIT--IITGALRVEDGHIYNSTYIFS-KGNV-QIADKVILVPFGEEIPLPKFFKKpINKLffggaSDFSKASKFSD--- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 352 vVTMAGTAVGVATCYEVSFDQAFrtaiDNGAQILTTPTNNATFSDSDM-TYQQLAMsRLRAMEADRAVVVAATSGVSAIV 430
Cdd:PRK12291 336 -FTLDGVKFRNAICYEATSEELY----EGNPKIVIAISNNAWFVPSIEpTLQKLLL-KYYARKYGKTIYHSANGSPSYII 409
|
..
gi 1093433562 431 HP 432
Cdd:PRK12291 410 TP 411
|
|
| nitrilase_7 |
cd07585 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
237-455 |
1.07e-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: 46.93 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 237 RVTEQAAQDGArpDIVIWPENS-----SDINPFANEDA------RALIDgAAHDIDAPILVGTLTRDEVGARNTMQVFNP 305
Cdd:cd07585 23 RWTRKAAAQGA--ELVCFPEMCitgytHVRALSREAEVpdgpstQALSD-LARRYGLTILAGLIEKAGDRPYNTYLVCLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 306 DGSVgqHHYKKyLQPFGETMPMreffrkitdlvdlagdMKPGDGSGVVTMAGTAVGVATCYEVSFDQAFRTAIDNGAQIL 385
Cdd:cd07585 100 DGLV--HRYRK-LHLFRREHPY----------------IAAGDEYPVFATPGVRFGILICYDNHFPENVRATALLGAEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 386 TTPtnNATFSDSDMTYQQLAMSRLRAMEADRAVVVAAT-----------SGVSAIVHPDGSVSQESGIFEPAYLEEELPL 454
Cdd:cd07585 161 FAP--HATPGTTSPKGREWWMRWLPARAYDNGVFVAACngvgrdggevfPGGAMILDPYGRVLAETTSGGDGMVVADLDL 238
|
.
gi 1093433562 455 R 455
Cdd:cd07585 239 D 239
|
|
| Ph0642_like |
cd07577 |
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ... |
245-458 |
3.74e-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: 45.37 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 245 DGARPDIVIWPE---------NSSDINPFANEDA-----RALIdGAAHDIDAPILVGTLTRDEVGARNTMQVFNPDGSVG 310
Cdd:cd07577 26 KGVEADLIVLPElfntgyaftSKEEVASLAESIPdgpttRFLQ-ELARETGAYIVAGLPERDGDKFYNSAVVVGPEGYIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 311 QhhYKKYLQPFGEtmpmREFFrkitdlvdlagdmKPGD-GSGVVTMAGTAVGVATCYEVSFDQAFRTAIDNGAQILTTPT 389
Cdd:cd07577 105 I--YRKTHLFYEE----KLFF-------------EPGDtGFRVFDIGDIRIGVMICFDWYFPEAARTLALKGADIIAHPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 390 NNAtfsdsdMTYQQLAMsRLRAMEADRAVVVAATSGV-------------SAIVHPDGSVSQESGIFEPAYLEEELPLRE 456
Cdd:cd07577 166 NLV------LPYCPKAM-PIRALENRVFTITANRIGTeerggetlrfigkSQITSPKGEVLARAPEDGEEVLVAEIDPRL 238
|
..
gi 1093433562 457 GR 458
Cdd:cd07577 239 AR 240
|
|
| GAT_Gln-NAD-synth |
cd07570 |
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
209-452 |
4.11e-04 |
|
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain 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 classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer.
Pssm-ID: 143594 [Multi-domain] Cd Length: 261 Bit Score: 42.07 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 209 TVAAVQGNvPRLGlDFAAQRRAVLDnhvrVTEQAAQDGArpDIVIWPE-------------NSSDINpfANEDARALIDG 275
Cdd:cd07570 1 RIALAQLN-PTVG-DLEGNAEKILE----AIREAKAQGA--DLVVFPElsltgyppedlllRPDFLE--AAEEALEELAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 276 AAHDIDAPILVGTLTRDEVGARNTMQVFNpDGSVGQHHYKKYLQPFGETMPMREFfrkitdlvdlagdmKPGDGSGVVTM 355
Cdd:cd07570 71 ATADLDIAVVVGLPLRHDGKLYNAAAVLQ-NGKILGVVPKQLLPNYGVFDEKRYF--------------TPGDKPDVLFF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 356 AGTAVGVATCYEVSFDQA-FRTAIDNGAQILTTPtnNAtfSDSDMTYQQL--AMSRLRAMEADRAVVVAAT--------- 423
Cdd:cd07570 136 KGLRIGVEICEDLWVPDPpSAELALAGADLILNL--SA--SPFHLGKQDYrrELVSSRSARTGLPYVYVNQvggqddlvf 211
|
250 260
....*....|....*....|....*....
gi 1093433562 424 SGVSAIVHPDGSVSQESGIFEPAYLEEEL 452
Cdd:cd07570 212 DGGSFIADNDGELLAEAPRFEEDLADVDL 240
|
|
| PLN02798 |
PLN02798 |
nitrilase |
208-436 |
4.51e-03 |
|
nitrilase
Pssm-ID: 215428 Cd Length: 286 Bit Score: 38.96 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 208 ITVAAVQGNVPRLGldfAAQRRAVLDNHV------RVTEQAAQDGARpdIVIWPENSSDInpfANEDARALidGAAHDID 281
Cdd:PLN02798 1 MSTAATAGSSVRVA---VAQMTSTNDLAAnfatcsRLAKEAAAAGAK--LLFLPECFSFI---GDKDGESL--AIAEPLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 282 APILVG--TLTRdEVGARNTMQVFNPDGSVGQHHYKKYL--QPFGEtmpMREFFRKITDL-VDLAGDM--------KPGD 348
Cdd:PLN02798 71 GPIMQRyrSLAR-ESGLWLSLGGFQEKGPDDSHLYNTHVliDDSGE---IRSSYRKIHLFdVDVPGGPvlkessftAPGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 349 GSGVVTMAGTAVGVATCYEVSFDQAF-RTAIDNGAQILTTPtnnATFSDSDMTYQQLAMSRLRAMEADRAVVVAATSGV- 426
Cdd:PLN02798 147 TIVAVDSPVGRLGLTVCYDLRFPELYqQLRFEHGAQVLLVP---SAFTKPTGEAHWEVLLRARAIETQCYVIAAAQAGKh 223
|
250
....*....|....*....
gi 1093433562 427 ---------SAIVHPDGSV 436
Cdd:PLN02798 224 nekresyghALIIDPWGTV 242
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
240-388 |
6.08e-03 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 38.98 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093433562 240 EQAAQDGArpDIVIWPENS------SDI--NP-FANEDARALIDGAAHDIDAP-ILVGTLTRDEVGARNTMQVFNpDGSV 309
Cdd:PRK13981 27 AEAADAGA--DLLLFPELFlsgyppEDLllRPaFLAACEAALERLAAATAGGPaVLVGHPWREGGKLYNAAALLD-GGEV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093433562 310 GQHHYKKYLQPFGETMPMREFfrkitdlvdlagdmKPGDGSGVVTMAGTAVGVATCYEVSFDQAFRTAIDNGAQILTTP 388
Cdd:PRK13981 104 LATYRKQDLPNYGVFDEKRYF--------------APGPEPGVVELKGVRIGVPICEDIWNPEPAETLAEAGAELLLVP 168
|
|
| |
