|
Name |
Accession |
Description |
Interval |
E-value |
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
21-487 |
2.20e-117 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 353.76 E-value: 2.20e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 21 PHGLWWAGLGGIGMLWLScvpWRGVPvRAGRAALIGFVHALTQYLLMLPWIGE----------LVGTMPYVALALWLSVY 90
Cdd:COG0815 1 PFGLWPLAFVALAPLLLL---LRGAR-SPRRAFLLGWLFGLGFFLAGLYWLYVslhvfgglpaWLAPLAVLLLAAYLALF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 91 ALLLTPGAVLLAR--WRWGWLGFPFFYLAIELLRSSVpFGGFAWVRLAWGQMN-GPLANLAAWGGTALVSLAAALVGtgv 167
Cdd:COG0815 77 FALAAALARRLRRrgGLLRPLAFAALWVLLEWLRGWL-FTGFPWLRLGYSQADfSPLAQLAPLGGVYGLSFLVVLVN--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 168 AALYLAVLRHAWResWAAAAVVLPVVLGLVAGLGVNDPGRTVGTTKVAAIQGNVPRLGLDFNAQRRAVLANHVQATAKAA 247
Cdd:COG0815 153 ALLALALLRRRRR--LAALALALALLLAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKWDPEQRREILDRYLDLTRELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 248 KADPDvdLYIWPENSSDVNPFRDAEAMALIQSAVQAAGAPIVVGTLTVDEVGER--NTMQVFNADGSVGEHHYKKYLQPF 325
Cdd:COG0815 231 DDGPD--LVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRyyNSALLLDPDGGILGRYDKHHLVPF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 326 GETMPWRSFFRTITDLVDLA-GDFKPGNGPGVVHMGGIAVGLATCYEVAFDAAYRTSVRNGAQILATPTNNATFGFSDMT 404
Cdd:COG0815 309 GEYVPLRDLLRPLIPFLDLPlGDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNITNDAWFGDSIGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 405 FQQLAMSRLRAIETDRAVVVAATSGVSAIVHPDGRVSQESGIFEQQYLIEELPLREGITPAVKYGALLQAVAVLIGLAAV 484
Cdd:COG0815 389 YQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLLLLLALLLA 468
|
...
gi 1080393323 485 AAA 487
Cdd:COG0815 469 LLL 471
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
213-479 |
1.10e-90 |
|
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: 277.94 E-value: 1.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 213 KVAAIQGNVPRLGLDFNAQRRAVLANHVQATAKAAKADPDvdLYIWPENSSDVNPFRDAEAMALIQSAVQAAGAPIVVGT 292
Cdd:cd07571 2 RVALVQGNIPQDEKWDPEQRQATLDRYLDLTRELADEKPD--LVVWPETALPFDLQRDPDALARLARAARAVGAPLLTGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 293 LTVDEVGER--NTMQVFNADGSVGEHHYKKYLQPFGETMPWRSFFRTITDLVDLA-GDFKPGNGPGVVHM-GGIAVGLAT 368
Cdd:cd07571 80 PRREPGGGRyyNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPmGDFSPGTGPQPLLLgGGVRVGPLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 369 CYEVAFDAAYRTSVRNGAQILATPTNNATFGFSDMTFQQLAMSRLRAIETDRAVVVAATSGVSAIVHPDGRVSQESGIFE 448
Cdd:cd07571 160 CYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVARLPLFE 239
|
250 260 270
....*....|....*....|....*....|.
gi 1080393323 449 QQYLIEELPLREGITPAVKYGALLQAVAVLI 479
Cdd:cd07571 240 AGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
64-440 |
3.60e-72 |
|
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: 234.18 E-value: 3.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 64 YLLMLPWIGE--LVGTMPY-------VALALWLSVYALLLTPGAVLLARWRWGWLGFPFFYLAIELLRSSVPFGgFAWVR 134
Cdd:TIGR00546 6 FLAGLFWLGIalSVNGFIAfvagllvVGLPALLALFPGLAAYLLRRLAPFRKVLLALPLLWTLAEWLRSFGFLG-FPWGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 135 LAWGQMNGPLANLAAWGGTALVSLAAALVGtgvAALYLAVLRHAWRESWAAAAVVLPVVLGLVAGLGVNDPGRTVGTT-K 213
Cdd:TIGR00546 85 IGYAQSSLPLIQIASIFGVWGLSFLVVFLN---ALLALVLLKKESFKKLLAIAVVVLLAALGFLLYELKSATPVPGPTlN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 214 VAAIQGNVPRLGLDFNAQRRAVLANHVQATAKAAkadPDVDLYIWPENSSDVNPFR-DAEAMALIQSAVQAAGAPIVVGT 292
Cdd:TIGR00546 162 VALVQPNIPQDLKFDSEGLEAILEILTSLTKQAV---EKPDLVVWPETAFPFDLENsPQKLADRLKLLVLSKGIPILIGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 293 LTVDEVGER---NTMQVFNADGSVGEHHYKKYLQPFGETMPWRSFFRTITDLVDLA--GDFKPGNGPGVVHMGGIAVGLA 367
Cdd:TIGR00546 239 PDAVPGGPYhyyNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSKLFFLLsqEDFSRGPGPQVLKLPGGKIAPL 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080393323 368 TCYEVAFDAAYRTSVRNGAQILATPTNNATFGFSDMTFQQLAMSRLRAIETDRAVVVAATSGVSAIVHPDGRV 440
Cdd:TIGR00546 319 ICYESIFPDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFRAIENGRPLVRATNTGISAVIDPRGRT 391
|
|
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
17-492 |
9.60e-68 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 225.91 E-value: 9.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 17 FSYEPHGLWWAGLGGIGMLWLScvpWRGVPVRagRAALIGFVHALTQYLLMLPWIG---ELVGTMPYVA-------LALW 86
Cdd:PRK00302 21 LAFAPFDLWPLALLSLAGLLWL---LLGASPK--QAALIGFLWGFGYFGSGLSWIYvsiHTFGGMPAWLapllvllLAAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 87 LSVYALLLTPGAVLLARWRWGW--LGFPFFYLAIELLRSSVpFGGFAWVRLAWGQM-NGPLANLAAWGGTALVSLAAALV 163
Cdd:PRK00302 96 LALYPALFAALWRRLWPKSGLRraLALPALWVLTEWLRGWL-LTGFPWLALGYSQIpDGPLAQLAPIFGVYGLSFLVVLV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 164 GtgvAALYLAVLRHAWReswaAAAVVLPVVLGLVAGLGV-------NDPGRTVgttKVAAIQGNVP-RLGLDfNAQRRAV 235
Cdd:PRK00302 175 N---ALLALALIKRRWR----LALLALLLLLLAALGYGLrrlqwttPAPEPAL---KVALVQGNIPqSLKWD-PAGLEAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 236 LANHVQATAKAAKadpDVDLYIWPENSSDVNPFRDAEAMAL-IQSAVQAAGAPIVVGTLTVDEVGER----NTMQVFNAD 310
Cdd:PRK00302 244 LQKYLDLSRPALG---PADLIIWPETAIPFLLEDLPQAFLKaLDDLAREKGSALITGAPRAENKQGRydyyNSIYVLGPY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 311 GSVGehHYKKY-LQPFGETMPWRSFFRTITDLVDL-AGDFKPGNGPGVV-HMGGIAVGLATCYEVAFDAAYRTSVRNGAQ 387
Cdd:PRK00302 321 GILN--RYDKHhLVPFGEYVPLESLLRPLAPFFNLpMGDFSRGPYVQPPlLAKGLKLAPLICYEIIFPEEVRANVRQGAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 388 ILATPTNNATFGFSDMTFQQLAMSRLRAIETDRAVVVAATSGVSAIVHPDGRVSQESGIFEQQYLIEELPLREGITPAVK 467
Cdd:PRK00302 399 LLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDPLGRIIAQLPQFTEGVLDGTVPPTTGLTPYAR 478
|
490 500
....*....|....*....|....*.
gi 1080393323 468 YG-ALLQAVAVLIGLAAVAAAWRSNR 492
Cdd:PRK00302 479 WGdWPLLLLALLLLLLALLLALRRRR 504
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
213-458 |
1.48e-19 |
|
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: 88.18 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 213 KVAAIQGNVPRLGLDFNAQRravlanHVQATAKAAKADpdVDLYIWPENSSDVNPFR----------DAEAMALIQSAVQ 282
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQK------ALELIEEAARYG--ADLIVLPELFITGYPCWahfleaaevgDGETLAGLAALAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 283 AAGAPIVVGTLTVDEVGER--NTMQVFNADGSVGEHHYKKYLqpFGETMPWRSFFRTItdlvdlagdFKPGNGPGVVHMG 360
Cdd:pfam00795 73 KNGIAIVIGLIERWLTGGRlyNTAVLLDPDGKLVGKYRKLHL--FPEPRPPGFRERVL---------FEPGDGGTVFDTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 361 GIAVGLATCYEVAFDAAYRTSVRNGAQILATPTNNATFGFSDMTFQQLAMSRLRAIETDRAVVVAATSGV---------- 430
Cdd:pfam00795 142 LGKIGAAICYEIRFPELLRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGeedapwpygh 221
|
250 260
....*....|....*....|....*...
gi 1080393323 431 SAIVHPDGRVSQESGIFEQQYLIEELPL 458
Cdd:pfam00795 222 SMIIDPDGRILAGAGEWEEGVLIADIDL 249
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
21-487 |
2.20e-117 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 353.76 E-value: 2.20e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 21 PHGLWWAGLGGIGMLWLScvpWRGVPvRAGRAALIGFVHALTQYLLMLPWIGE----------LVGTMPYVALALWLSVY 90
Cdd:COG0815 1 PFGLWPLAFVALAPLLLL---LRGAR-SPRRAFLLGWLFGLGFFLAGLYWLYVslhvfgglpaWLAPLAVLLLAAYLALF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 91 ALLLTPGAVLLAR--WRWGWLGFPFFYLAIELLRSSVpFGGFAWVRLAWGQMN-GPLANLAAWGGTALVSLAAALVGtgv 167
Cdd:COG0815 77 FALAAALARRLRRrgGLLRPLAFAALWVLLEWLRGWL-FTGFPWLRLGYSQADfSPLAQLAPLGGVYGLSFLVVLVN--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 168 AALYLAVLRHAWResWAAAAVVLPVVLGLVAGLGVNDPGRTVGTTKVAAIQGNVPRLGLDFNAQRRAVLANHVQATAKAA 247
Cdd:COG0815 153 ALLALALLRRRRR--LAALALALALLLAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKWDPEQRREILDRYLDLTRELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 248 KADPDvdLYIWPENSSDVNPFRDAEAMALIQSAVQAAGAPIVVGTLTVDEVGER--NTMQVFNADGSVGEHHYKKYLQPF 325
Cdd:COG0815 231 DDGPD--LVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRyyNSALLLDPDGGILGRYDKHHLVPF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 326 GETMPWRSFFRTITDLVDLA-GDFKPGNGPGVVHMGGIAVGLATCYEVAFDAAYRTSVRNGAQILATPTNNATFGFSDMT 404
Cdd:COG0815 309 GEYVPLRDLLRPLIPFLDLPlGDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNITNDAWFGDSIGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 405 FQQLAMSRLRAIETDRAVVVAATSGVSAIVHPDGRVSQESGIFEQQYLIEELPLREGITPAVKYGALLQAVAVLIGLAAV 484
Cdd:COG0815 389 YQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLLLLLALLLA 468
|
...
gi 1080393323 485 AAA 487
Cdd:COG0815 469 LLL 471
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
213-479 |
1.10e-90 |
|
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: 277.94 E-value: 1.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 213 KVAAIQGNVPRLGLDFNAQRRAVLANHVQATAKAAKADPDvdLYIWPENSSDVNPFRDAEAMALIQSAVQAAGAPIVVGT 292
Cdd:cd07571 2 RVALVQGNIPQDEKWDPEQRQATLDRYLDLTRELADEKPD--LVVWPETALPFDLQRDPDALARLARAARAVGAPLLTGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 293 LTVDEVGER--NTMQVFNADGSVGEHHYKKYLQPFGETMPWRSFFRTITDLVDLA-GDFKPGNGPGVVHM-GGIAVGLAT 368
Cdd:cd07571 80 PRREPGGGRyyNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPmGDFSPGTGPQPLLLgGGVRVGPLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 369 CYEVAFDAAYRTSVRNGAQILATPTNNATFGFSDMTFQQLAMSRLRAIETDRAVVVAATSGVSAIVHPDGRVSQESGIFE 448
Cdd:cd07571 160 CYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVARLPLFE 239
|
250 260 270
....*....|....*....|....*....|.
gi 1080393323 449 QQYLIEELPLREGITPAVKYGALLQAVAVLI 479
Cdd:cd07571 240 AGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
64-440 |
3.60e-72 |
|
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: 234.18 E-value: 3.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 64 YLLMLPWIGE--LVGTMPY-------VALALWLSVYALLLTPGAVLLARWRWGWLGFPFFYLAIELLRSSVPFGgFAWVR 134
Cdd:TIGR00546 6 FLAGLFWLGIalSVNGFIAfvagllvVGLPALLALFPGLAAYLLRRLAPFRKVLLALPLLWTLAEWLRSFGFLG-FPWGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 135 LAWGQMNGPLANLAAWGGTALVSLAAALVGtgvAALYLAVLRHAWRESWAAAAVVLPVVLGLVAGLGVNDPGRTVGTT-K 213
Cdd:TIGR00546 85 IGYAQSSLPLIQIASIFGVWGLSFLVVFLN---ALLALVLLKKESFKKLLAIAVVVLLAALGFLLYELKSATPVPGPTlN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 214 VAAIQGNVPRLGLDFNAQRRAVLANHVQATAKAAkadPDVDLYIWPENSSDVNPFR-DAEAMALIQSAVQAAGAPIVVGT 292
Cdd:TIGR00546 162 VALVQPNIPQDLKFDSEGLEAILEILTSLTKQAV---EKPDLVVWPETAFPFDLENsPQKLADRLKLLVLSKGIPILIGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 293 LTVDEVGER---NTMQVFNADGSVGEHHYKKYLQPFGETMPWRSFFRTITDLVDLA--GDFKPGNGPGVVHMGGIAVGLA 367
Cdd:TIGR00546 239 PDAVPGGPYhyyNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSKLFFLLsqEDFSRGPGPQVLKLPGGKIAPL 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080393323 368 TCYEVAFDAAYRTSVRNGAQILATPTNNATFGFSDMTFQQLAMSRLRAIETDRAVVVAATSGVSAIVHPDGRV 440
Cdd:TIGR00546 319 ICYESIFPDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFRAIENGRPLVRATNTGISAVIDPRGRT 391
|
|
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
17-492 |
9.60e-68 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 225.91 E-value: 9.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 17 FSYEPHGLWWAGLGGIGMLWLScvpWRGVPVRagRAALIGFVHALTQYLLMLPWIG---ELVGTMPYVA-------LALW 86
Cdd:PRK00302 21 LAFAPFDLWPLALLSLAGLLWL---LLGASPK--QAALIGFLWGFGYFGSGLSWIYvsiHTFGGMPAWLapllvllLAAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 87 LSVYALLLTPGAVLLARWRWGW--LGFPFFYLAIELLRSSVpFGGFAWVRLAWGQM-NGPLANLAAWGGTALVSLAAALV 163
Cdd:PRK00302 96 LALYPALFAALWRRLWPKSGLRraLALPALWVLTEWLRGWL-LTGFPWLALGYSQIpDGPLAQLAPIFGVYGLSFLVVLV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 164 GtgvAALYLAVLRHAWReswaAAAVVLPVVLGLVAGLGV-------NDPGRTVgttKVAAIQGNVP-RLGLDfNAQRRAV 235
Cdd:PRK00302 175 N---ALLALALIKRRWR----LALLALLLLLLAALGYGLrrlqwttPAPEPAL---KVALVQGNIPqSLKWD-PAGLEAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 236 LANHVQATAKAAKadpDVDLYIWPENSSDVNPFRDAEAMAL-IQSAVQAAGAPIVVGTLTVDEVGER----NTMQVFNAD 310
Cdd:PRK00302 244 LQKYLDLSRPALG---PADLIIWPETAIPFLLEDLPQAFLKaLDDLAREKGSALITGAPRAENKQGRydyyNSIYVLGPY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 311 GSVGehHYKKY-LQPFGETMPWRSFFRTITDLVDL-AGDFKPGNGPGVV-HMGGIAVGLATCYEVAFDAAYRTSVRNGAQ 387
Cdd:PRK00302 321 GILN--RYDKHhLVPFGEYVPLESLLRPLAPFFNLpMGDFSRGPYVQPPlLAKGLKLAPLICYEIIFPEEVRANVRQGAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 388 ILATPTNNATFGFSDMTFQQLAMSRLRAIETDRAVVVAATSGVSAIVHPDGRVSQESGIFEQQYLIEELPLREGITPAVK 467
Cdd:PRK00302 399 LLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDPLGRIIAQLPQFTEGVLDGTVPPTTGLTPYAR 478
|
490 500
....*....|....*....|....*.
gi 1080393323 468 YG-ALLQAVAVLIGLAAVAAAWRSNR 492
Cdd:PRK00302 479 WGdWPLLLLALLLLLLALLLALRRRR 504
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
213-465 |
2.59e-20 |
|
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 90.69 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 213 KVAAIQGNVPRLGLDFNAQRravlanHVQATAKAAKADpdVDLYIWPENSS-----------DVNPFRDAEAMALIQSAV 281
Cdd:COG0388 3 RIALAQLNPTVGDIEANLAK------IEELIREAAAQG--ADLVVFPELFLtgyppedddllELAEPLDGPALAALAELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 282 QAAGAPIVVGTLTVDEVGE-RNTMQVFNADGSVGEHHYKKYLqpFGETMPWRSFFrtitdlvdlagdFKPGNGPGVVHMG 360
Cdd:COG0388 75 RELGIAVVVGLPERDEGGRlYNTALVIDPDGEILGRYRKIHL--PNYGVFDEKRY------------FTPGDELVVFDTD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 361 GIAVGLATCYEVAFDAAYRTSVRNGAQILATPTNnatFGFSDMTFQQLAMSRLRAIETDRAVVVAATSGV---------S 431
Cdd:COG0388 141 GGRIGVLICYDLWFPELARALALAGADLLLVPSA---SPFGRGKDHWELLLRARAIENGCYVVAANQVGGedglvfdggS 217
|
250 260 270
....*....|....*....|....*....|....
gi 1080393323 432 AIVHPDGRVsqesgifeqqylIEELPLREGITPA 465
Cdd:COG0388 218 MIVDPDGEV------------LAEAGDEEGLLVA 239
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
213-458 |
1.48e-19 |
|
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: 88.18 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 213 KVAAIQGNVPRLGLDFNAQRravlanHVQATAKAAKADpdVDLYIWPENSSDVNPFR----------DAEAMALIQSAVQ 282
Cdd:pfam00795 1 RVALVQLPQGFWDLEANLQK------ALELIEEAARYG--ADLIVLPELFITGYPCWahfleaaevgDGETLAGLAALAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 283 AAGAPIVVGTLTVDEVGER--NTMQVFNADGSVGEHHYKKYLqpFGETMPWRSFFRTItdlvdlagdFKPGNGPGVVHMG 360
Cdd:pfam00795 73 KNGIAIVIGLIERWLTGGRlyNTAVLLDPDGKLVGKYRKLHL--FPEPRPPGFRERVL---------FEPGDGGTVFDTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 361 GIAVGLATCYEVAFDAAYRTSVRNGAQILATPTNNATFGFSDMTFQQLAMSRLRAIETDRAVVVAATSGV---------- 430
Cdd:pfam00795 142 LGKIGAAICYEIRFPELLRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGeedapwpygh 221
|
250 260
....*....|....*....|....*...
gi 1080393323 431 SAIVHPDGRVSQESGIFEQQYLIEELPL 458
Cdd:pfam00795 222 SMIIDPDGRILAGAGEWEEGVLIADIDL 249
|
|
| nitrilase |
cd07197 |
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
214-460 |
1.58e-18 |
|
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: 85.07 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 214 VAAIQGNVPRLGLDFNAQRravlanHVQATAKAAKADpdVDLYIWPE-------NSSDVNPFRDAE-----AMALIQSAV 281
Cdd:cd07197 1 IAAVQLAPKIGDVEANLAK------ALRLIKEAAEQG--ADLIVLPElfltgysFESAKEDLDLAEeldgpTLEALAELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 282 QAAGAPIVVGTLTVDEVGERNTMQVFNADGSVGEHHYKKYLQPFGETMPwrsffrtitdlvdlagdFKPGNGPGVVHMGG 361
Cdd:cd07197 73 KELGIYIVAGIAEKDGDKLYNTAVVIDPDGEIIGKYRKIHLFDFGERRY-----------------FSPGDEFPVFDTPG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 362 IAVGLATCYEVAFDAAYRTSVRNGAQILATPTNnatFGFSDMTFQQLaMSRLRAIETDRAVVVAATSGV---------SA 432
Cdd:cd07197 136 GKIGLLICYDLRFPELARELALKGADIILVPAA---WPTARREHWEL-LLRARAIENGVYVVAANRVGEegglefaggSM 211
|
250 260
....*....|....*....|....*...
gi 1080393323 433 IVHPDGRVsQESGIFEQQYLIEELPLRE 460
Cdd:cd07197 212 IVDPDGEV-LAEASEEEGILVAELDLDE 238
|
|
| LNT_N |
pfam20154 |
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal ... |
16-164 |
3.84e-17 |
|
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: 78.44 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 16 YFSYEPHGLWWAGLGGIGMLWLSCVPWrgvpVRAGRAALIGFVHALTQYLLMLPWI-------GELVGTMPYVALALWLS 88
Cdd:pfam20154 5 SLAFPPFGLWPLAWVALAPLLLALEAR----SSPRRAFLLGFLFGLGFFGLGLYWLgvslhtfGGAPLPLALLLLLLLAL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080393323 89 VYALLLTPGAVLLARWRWGW-LGFPFFYLAIELLRSsVPFGGFAWVRLAWGQMNGP-LANLAAWGGTALVSLAAALVG 164
Cdd:pfam20154 81 YLALFALAAWLLKRLWGLFRaLLFAALWVGLEYLRG-WPFGGFPWGLLGYSQADGPpLIQLAPLGGVYGVSFLVVLVN 157
|
|
| R-amidase_like |
cd07576 |
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
213-440 |
6.98e-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: 65.68 E-value: 6.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 213 KVAAIQGNvprlgldfnAQRRAVLANHVQATAKAAKADPD-VDLYIWPE------NSSDVNP----FRDAEAMALIQSAV 281
Cdd:cd07576 1 RLALYQGP---------ARDGDVAANLARLDEAAARAAAAgADLLVFPElfltgyNIGDAVArlaePADGPALQALRAIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 282 QAAGAPIVVGTLTVDEVGERNTMQVFNADGSVGEHHYKKYLqpFGEtmpwrsffrtitdlvDLAGDFKPGNGPGVVHMGG 361
Cdd:cd07576 72 RRHGIAIVVGYPERAGGAVYNAAVLIDEDGTVLANYRKTHL--FGD---------------SERAAFTPGDRFPVVELRG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 362 IAVGLATCYEVAFDAAYRTSVRNGAQILATPTNNATfgfsDMTFQQLAMSRLRAIETDRAVVVAATSGV---------SA 432
Cdd:cd07576 135 LRVGLLICYDVEFPELVRALALAGADLVLVPTALME----PYGFVARTLVPARAFENQIFVAYANRCGAedgltyvglSS 210
|
....*...
gi 1080393323 433 IVHPDGRV 440
Cdd:cd07576 211 IAGPDGTV 218
|
|
| nitrilase_5 |
cd07583 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
213-460 |
8.51e-09 |
|
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: 56.39 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 213 KVAAIQGNVPrLGlDFNAQRRAVlanhVQATAKAAKADPDVDLY--IWPENSSDVNPFRDAEAM-----ALIQSAVQAAG 285
Cdd:cd07583 1 KIALIQLDIV-WG-DPEANIERV----ESLIEEAAAAGADLIVLpeMWNTGYFLDDLYELADEDggetvSFLSELAKKHG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 286 APIVVGTLTVDEVGE-RNTMQVFNADGSVgEHHYKKyLQPFGetmpwrsffrtitdlvdLAGD---FKPGNGPGVVHMGG 361
Cdd:cd07583 75 VNIVAGSVAEKEGGKlYNTAYVIDPDGEL-IATYRK-IHLFG-----------------LMGEdkyLTAGDELEVFELDG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 362 IAVGLATCYEVAFDAAYRTSVRNGAQILATPTnnatfgfsdmtfqQLAMSRL---------RAIETDrAVVVAATS---- 428
Cdd:cd07583 136 GKVGLFICYDLRFPELFRKLALEGAEILFVPA-------------EWPAARIehwrtllraRAIENQ-AFVVACNRvgtd 201
|
250 260 270
....*....|....*....|....*....|....*...
gi 1080393323 429 ------GVSAIVHPDGRVSQESGIfEQQYLIEELPLRE 460
Cdd:cd07583 202 ggnefgGHSMVIDPWGEVLAEAGE-EEEILTAEIDLEE 238
|
|
| nitrilase_3 |
cd07581 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
348-445 |
5.90e-08 |
|
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: 53.73 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 348 FKPGNG--PGVVHMGGIAVGLATCYEVAFDAAYRTSVRNGAQILATPtnnATFGFSDMTFQQL-AMSRLRAIETDRAVVV 424
Cdd:cd07581 124 VAPGDElpPVVFVVGGVKVGLATCYDLRFPELARALALAGADVIVVP---AAWVAGPGKEEHWeTLLRARALENTVYVAA 200
|
90 100
....*....|....*....|....*.
gi 1080393323 425 AAT-----SGVSAIVHPDGRVSQESG 445
Cdd:cd07581 201 AGQagprgIGRSMVVDPLGVVLADLG 226
|
|
| PRK12291 |
PRK12291 |
apolipoprotein N-acyltransferase; Reviewed |
288-410 |
1.32e-07 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 237042 [Multi-domain] Cd Length: 418 Bit Score: 53.83 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 288 IVVGTLTVDEVGERNTMQVFNaDGSVgEHHYKKYLQPFGETMPWRSFFRT-ITDL-VDLAGDFKPGNGPGVVHMGGIAVG 365
Cdd:PRK12291 267 IITGALRVEDGHIYNSTYIFS-KGNV-QIADKVILVPFGEEIPLPKFFKKpINKLfFGGASDFSKASKFSDFTLDGVKFR 344
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1080393323 366 LATCYEVAFDAAYRTSVRNgaqILATpTNNATFGFSDM-TFQQLAM 410
Cdd:PRK12291 345 NAICYEATSEELYEGNPKI---VIAI-SNNAWFVPSIEpTLQKLLL 386
|
|
| nit |
cd07572 |
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ... |
213-441 |
1.46e-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: 49.73 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 213 KVAAIQGNVPrlgldfnAQRRAVLANHVQATAKAAKADPDvdLYIWPENS---SDVNPFRDAEAMALIQSAVQAA----- 284
Cdd:cd07572 1 RVALIQMTST-------ADKEANLARAKELIEEAAAQGAK--LVVLPECFnypGGTDAFKLALAEEEGDGPTLQAlsela 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 285 ---GAPIVVGTL-TVDEVGER--NTMQVFNADGSVGEHHYKKYLqpFGetmpwrsffrtitdlVDLAGD--------FKP 350
Cdd:cd07572 72 kehGIWLVGGSIpERDDDDGKvyNTSLVFDPDGELVARYRKIHL--FD---------------VDVPGGisyresdtLTP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 351 GNGPGVVHMGGIAVGLATCYEVAFDAAYRTSVRNGAQILATPtnnATFgfsDMT-----FQQLAmsRLRAIETDRAVVVA 425
Cdd:cd07572 135 GDEVVVVDTPFGKIGLGICYDLRFPELARALARQGADILTVP---AAF---TMTtgpahWELLL--RARAIENQCYVVAA 206
|
250
....*....|....*.
gi 1080393323 426 ATSGvsaiVHPDGRVS 441
Cdd:cd07572 207 AQAG----DHEAGRET 218
|
|
| nitrilase_Rim1_like |
cd07574 |
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ... |
285-447 |
1.51e-06 |
|
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: 49.89 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 285 GAPIVVGTLTVDEVGE-RNTMQVFNADGSVGeHHYKKYLQPFgETMPWrsffrtitdlvdlagDFKPGNGPGVVHMGGIA 363
Cdd:cd07574 85 GINIIAGSMPVREDGRlYNRAYLFGPDGTIG-HQDKLHMTPF-EREEW---------------GISGGDKLKVFDTDLGK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 364 VGLATCYEVAFDAAYRTSVRNGAQILATPTNNAT-FGFSdmtfQQLAMSRLRAIETDRAVVVAATSGVSAIVHP-DGRVS 441
Cdd:cd07574 148 IGILICYDSEFPELARALAEAGADLLLVPSCTDTrAGYW----RVRIGAQARALENQCYVVQSGTVGNAPWSPAvDVNYG 223
|
....*.
gi 1080393323 442 QeSGIF 447
Cdd:cd07574 224 Q-AAVY 228
|
|
| Ph0642_like |
cd07577 |
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ... |
348-460 |
4.18e-06 |
|
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: 48.06 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 348 FKPGN-GPGVVHMGGIAVGLATCYEVAFDAAYRTSVRNGAQILATPTNNAtfgfsdMTFQQLAMsRLRAIETDRAVVVAA 426
Cdd:cd07577 119 FEPGDtGFRVFDIGDIRIGVMICFDWYFPEAARTLALKGADIIAHPANLV------LPYCPKAM-PIRALENRVFTITAN 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1080393323 427 TSGV-------------SAIVHPDGRVSQESGIFEQQYLIEELPLRE 460
Cdd:cd07577 192 RIGTeerggetlrfigkSQITSPKGEVLARAPEDGEEVLVAEIDPRL 238
|
|
| nitrilase_2 |
cd07580 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
348-453 |
9.14e-03 |
|
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: 38.10 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393323 348 FKPGN-GPGVVHMGGIAVGLATCYEVAFDAAYRTSVRNGAQILATPTNnatfgFSDMTFQQLAMsrlRAIETDRAVVVAA 426
Cdd:cd07580 122 FEPGDlGLPVFDTPFGRIGVAICYDGWFPETFRLLALQGADIVCVPTN-----WVPMPRPPEGG---PPMANILAMAAAH 193
|
90 100
....*....|....*....|....*...
gi 1080393323 427 TSGVsAIVHPDgRVSQESGI-FEQQYLI 453
Cdd:cd07580 194 SNGL-FIACAD-RVGTERGQpFIGQSLI 219
|
|
| |
