|
Name |
Accession |
Description |
Interval |
E-value |
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
33-522 |
1.82e-100 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 311.39 E-value: 1.82e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 33 LGWWPLALPAAALIFLAVWQQR-ARWGLLAGAVAGLAFWGPHISWLTLY----------LGLVPWAGLTAVMTAWFALFG 101
Cdd:COG0815 2 FGLWPLAFVALAPLLLLLRGARsPRRAFLLGWLFGLGFFLAGLYWLYVSlhvfgglpawLAPLAVLLLAAYLALFFALAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 102 LfvgagtrgIARAAVFRSRPALLLVAqaatgAGLWVLRESVQSSWpYGGFAWGRLAHTQA-TGWLAESVSWLGFSGLSGA 180
Cdd:COG0815 82 A--------LARRLRRRGGLLRPLAF-----AALWVLLEWLRGWL-FTGFPWLRLGYSQAdFSPLAQLAPLGGVYGLSFL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 181 IAFaaalcvaagVALWSARVGADRSaiQRPARAAVAGAVVLLVALGLVPAAPLPQDGTLKVAAIQGNSKSAI-FDDRESG 259
Cdd:COG0815 148 VVL---------VNALLALALLRRR--RRLAALALALALLLAALRLSPVPWTEPAGEPLRVALVQGNIPQDLkWDPEQRR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 260 AVFRDHARQTEslldelEAAGESVDLIVWPENSAEFDLPGNTLRDFEVAGLARRAGAPIVAGSILQDPD-GTYTNSVVVW 338
Cdd:COG0815 217 EILDRYLDLTR------ELADDGPDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGgGRYYNSALLL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 339 DARGATGERYDKRFPVPFAEYMPNRDFFHMLAPDLvDLVQLEYTAGTRPAVLNLdtpaGAVAAGLAICFDIIFDQQAEAI 418
Cdd:COG0815 291 DPDGGILGRYDKHHLVPFGEYVPLRDLLRPLIPFL-DLPLGDFSPGTGPPVLDL----GGVRVGPLICYESIFPELVRDA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 419 VDGGAQVILAPTNNADFGRTDESAQQLQIARLRAIETGRALVNISTVGTSAMVSPTGQTLDGLTPFTADAMVAEIPLVSG 498
Cdd:COG0815 366 VRAGADLLVNITNDAWFGDSIGPYQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTG 445
|
490 500
....*....|....*....|....
gi 1198900569 499 ATPALRFGAVIAGAWMLLGALGAA 522
Cdd:COG0815 446 LTPYARWGDWPALLLLLLALLLAL 469
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
239-516 |
2.67e-74 |
|
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: 236.73 E-value: 2.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 239 LKVAAIQGNSKSAIFDDRES-GAVFRDHARQTEslldelEAAGESVDLIVWPENSAEFDLPGNTLRDFEVAGLARRAGAP 317
Cdd:cd07571 1 LRVALVQGNIPQDEKWDPEQrQATLDRYLDLTR------ELADEKPDLVVWPETALPFDLQRDPDALARLARAARAVGAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 318 IVAGSILQDPDG-TYTNSVVVWDARGATGERYDKRFPVPFAEYMPNRDFFHMLAPdLVDLVQLEYTAGTRPAVLNLdtpA 396
Cdd:cd07571 75 LLTGAPRREPGGgRYYNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGL-LFDLPMGDFSPGTGPQPLLL---G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 397 GAVAAGLAICFDIIFDQQAEAIVDGGAQVILAPTNNADFGRTDESAQQLQIARLRAIETGRALVNISTVGTSAMVSPTGQ 476
Cdd:cd07571 151 GGVRVGPLICYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGR 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1198900569 477 TLDGLTPFTADAMVAEIPLVSGATPALRFGAVIAGAWMLL 516
Cdd:cd07571 231 IVARLPLFEAGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
9-536 |
1.91e-61 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 210.12 E-value: 1.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 9 RLRWWTSLLAAAVGGLLLDTAGPGLGWWPLALPAAALIFLAVWQQRARWGLLAGAVAGLAFWGPHISWLTL----YLGLV 84
Cdd:PRK00302 2 LLRGWLRLLLALLAGALGTLAFAPFDLWPLALLSLAGLLWLLLGASPKQAALIGFLWGFGYFGSGLSWIYVsihtFGGMP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 85 PWA--GLTAVMTAWFALFGLFVGAgtrgIARAAVFRSRPALLLVAqaatgAGLWVLRESVQsSWPYGGFAWGRLAHTQA- 161
Cdd:PRK00302 82 AWLapLLVLLLAAYLALYPALFAA----LWRRLWPKSGLRRALAL-----PALWVLTEWLR-GWLLTGFPWLALGYSQIp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 162 TGWLAESVSWLGFSGLSGAIAFaaalcvaagVALWSARVGADRSAIQRPARAAVAGAVVLLVALGLVPAAPLPQDGTLKV 241
Cdd:PRK00302 152 DGPLAQLAPIFGVYGLSFLVVL---------VNALLALALIKRRWRLALLALLLLLLAALGYGLRRLQWTTPAPEPALKV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 242 AAIQGN-SKSAIFDDRESGAVFRDHARQTESLLDEleaagesVDLIVWPEnSA----EFDLPGNTLRdfEVAGLARRAGA 316
Cdd:PRK00302 223 ALVQGNiPQSLKWDPAGLEATLQKYLDLSRPALGP-------ADLIIWPE-TAipflLEDLPQAFLK--ALDDLAREKGS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 317 PIVAGSILQDPDGT---YTNSVVVWDARGATGeRYDKRFPVPFAEYMPNRDFFHMLAPdLVDLVQLEYTAGTRPAVLnld 393
Cdd:PRK00302 293 ALITGAPRAENKQGrydYYNSIYVLGPYGILN-RYDKHHLVPFGEYVPLESLLRPLAP-FFNLPMGDFSRGPYVQPP--- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 394 TPAGAVAAGLAICFDIIFDQQAEAIVDGGAQVILAPTNNADFGRTDESAQQLQIARLRAIETGRALVNISTVGTSAMVSP 473
Cdd:PRK00302 368 LLAKGLKLAPLICYEIIFPEEVRANVRQGADLLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDP 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198900569 474 TGQTLDGLTPFTADAMVAEIPLVSGATPALRFgaviaGAWMLLGALGAASGILLGYEPRRARK 536
Cdd:PRK00302 448 LGRIIAQLPQFTEGVLDGTVPPTTGLTPYARW-----GDWPLLLLALLLLLLALLLALRRRRK 505
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
66-477 |
1.02e-49 |
|
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: 176.01 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 66 GLAFWGPHISWLT--LYLGLVPWAGLTAVMTAWFALFGLFVGAGTRGIARAAVFRSRPALLlvaqaatgAGLWVLRESVq 143
Cdd:TIGR00546 2 GFGFFLAGLFWLGiaLSVNGFIAFVAGLLVVGLPALLALFPGLAAYLLRRLAPFRKVLLAL--------PLLWTLAEWL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 144 SSWPYGGFAWGRLAHTQATGWLAESVSWLGFSGLS-------GAIAFAAALCVAAGVALWSARVgadrsaiqrparaava 216
Cdd:TIGR00546 73 RSFGFLGFPWGLIGYAQSSLPLIQIASIFGVWGLSflvvflnALLALVLLKKESFKKLLAIAVV---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 217 GAVVLLVALGLVPAAPLPQDG-TLKVAAIQGN-SKSAIFDDRESGAVFRDHarqteslLDELEAAGESVDLIVWPENSAE 294
Cdd:TIGR00546 137 VLLAALGFLLYELKSATPVPGpTLNVALVQPNiPQDLKFDSEGLEAILEIL-------TSLTKQAVEKPDLVVWPETAFP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 295 FDLPGNTLR-DFEVAGLARRAGAPIVAGSILQDPDGT--YTNSVVVWDARGATGERYDKRFPVPFAEYMPNRDFFHMLAP 371
Cdd:TIGR00546 210 FDLENSPQKlADRLKLLVLSKGIPILIGAPDAVPGGPyhYYNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 372 DLVDLVQLEYTAGTRPAVLNLDtpagAVAAGLAICFDIIFDQQAEAIVDGGAQVILAPTNNADFGRTDESAQQLQIARLR 451
Cdd:TIGR00546 290 LFFLLSQEDFSRGPGPQVLKLP----GGKIAPLICYESIFPDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFR 365
|
410 420
....*....|....*....|....*.
gi 1198900569 452 AIETGRALVNISTVGTSAMVSPTGQT 477
Cdd:TIGR00546 366 AIENGRPLVRATNTGISAVIDPRGRT 391
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
240-495 |
4.35e-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: 87.03 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 240 KVAAIQGNSKSAifdDRESGAvfrdhaRQTESLLDEleAAGESVDLIVWPE-------NSAEF-----DLPGNTLRdfEV 307
Cdd:pfam00795 1 RVALVQLPQGFW---DLEANL------QKALELIEE--AARYGADLIVLPElfitgypCWAHFleaaeVGDGETLA--GL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 308 AGLARRAGAPIVAGSILQDPD-GTYTNSVVVWDARGATGERYDKRfpvpfaeympnrdffHMLAPDLVDLVQLEYTAGTR 386
Cdd:pfam00795 68 AALARKNGIAIVIGLIERWLTgGRLYNTAVLLDPDGKLVGKYRKL---------------HLFPEPRPPGFRERVLFEPG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 387 PAVLNLDTPAGAVaaGLAICFDIIFDQQAEAIVDGGAQVILAPTNNADFGRTDESAQQLQIARLRAIETGRALVNISTVG 466
Cdd:pfam00795 133 DGGTVFDTPLGKI--GAAICYEIRFPELLRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALENGCFVIAANQVG 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 1198900569 467 T----------SAMVSPTGQTLDGLTPFTADAMVAEIPL 495
Cdd:pfam00795 211 GeedapwpyghSMIIDPDGRILAGAGEWEEGVLIADIDL 249
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
33-522 |
1.82e-100 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 311.39 E-value: 1.82e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 33 LGWWPLALPAAALIFLAVWQQR-ARWGLLAGAVAGLAFWGPHISWLTLY----------LGLVPWAGLTAVMTAWFALFG 101
Cdd:COG0815 2 FGLWPLAFVALAPLLLLLRGARsPRRAFLLGWLFGLGFFLAGLYWLYVSlhvfgglpawLAPLAVLLLAAYLALFFALAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 102 LfvgagtrgIARAAVFRSRPALLLVAqaatgAGLWVLRESVQSSWpYGGFAWGRLAHTQA-TGWLAESVSWLGFSGLSGA 180
Cdd:COG0815 82 A--------LARRLRRRGGLLRPLAF-----AALWVLLEWLRGWL-FTGFPWLRLGYSQAdFSPLAQLAPLGGVYGLSFL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 181 IAFaaalcvaagVALWSARVGADRSaiQRPARAAVAGAVVLLVALGLVPAAPLPQDGTLKVAAIQGNSKSAI-FDDRESG 259
Cdd:COG0815 148 VVL---------VNALLALALLRRR--RRLAALALALALLLAALRLSPVPWTEPAGEPLRVALVQGNIPQDLkWDPEQRR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 260 AVFRDHARQTEslldelEAAGESVDLIVWPENSAEFDLPGNTLRDFEVAGLARRAGAPIVAGSILQDPD-GTYTNSVVVW 338
Cdd:COG0815 217 EILDRYLDLTR------ELADDGPDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGgGRYYNSALLL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 339 DARGATGERYDKRFPVPFAEYMPNRDFFHMLAPDLvDLVQLEYTAGTRPAVLNLdtpaGAVAAGLAICFDIIFDQQAEAI 418
Cdd:COG0815 291 DPDGGILGRYDKHHLVPFGEYVPLRDLLRPLIPFL-DLPLGDFSPGTGPPVLDL----GGVRVGPLICYESIFPELVRDA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 419 VDGGAQVILAPTNNADFGRTDESAQQLQIARLRAIETGRALVNISTVGTSAMVSPTGQTLDGLTPFTADAMVAEIPLVSG 498
Cdd:COG0815 366 VRAGADLLVNITNDAWFGDSIGPYQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTG 445
|
490 500
....*....|....*....|....
gi 1198900569 499 ATPALRFGAVIAGAWMLLGALGAA 522
Cdd:COG0815 446 LTPYARWGDWPALLLLLLALLLAL 469
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
239-516 |
2.67e-74 |
|
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: 236.73 E-value: 2.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 239 LKVAAIQGNSKSAIFDDRES-GAVFRDHARQTEslldelEAAGESVDLIVWPENSAEFDLPGNTLRDFEVAGLARRAGAP 317
Cdd:cd07571 1 LRVALVQGNIPQDEKWDPEQrQATLDRYLDLTR------ELADEKPDLVVWPETALPFDLQRDPDALARLARAARAVGAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 318 IVAGSILQDPDG-TYTNSVVVWDARGATGERYDKRFPVPFAEYMPNRDFFHMLAPdLVDLVQLEYTAGTRPAVLNLdtpA 396
Cdd:cd07571 75 LLTGAPRREPGGgRYYNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGL-LFDLPMGDFSPGTGPQPLLL---G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 397 GAVAAGLAICFDIIFDQQAEAIVDGGAQVILAPTNNADFGRTDESAQQLQIARLRAIETGRALVNISTVGTSAMVSPTGQ 476
Cdd:cd07571 151 GGVRVGPLICYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGR 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1198900569 477 TLDGLTPFTADAMVAEIPLVSGATPALRFGAVIAGAWMLL 516
Cdd:cd07571 231 IVARLPLFEAGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
9-536 |
1.91e-61 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 210.12 E-value: 1.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 9 RLRWWTSLLAAAVGGLLLDTAGPGLGWWPLALPAAALIFLAVWQQRARWGLLAGAVAGLAFWGPHISWLTL----YLGLV 84
Cdd:PRK00302 2 LLRGWLRLLLALLAGALGTLAFAPFDLWPLALLSLAGLLWLLLGASPKQAALIGFLWGFGYFGSGLSWIYVsihtFGGMP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 85 PWA--GLTAVMTAWFALFGLFVGAgtrgIARAAVFRSRPALLLVAqaatgAGLWVLRESVQsSWPYGGFAWGRLAHTQA- 161
Cdd:PRK00302 82 AWLapLLVLLLAAYLALYPALFAA----LWRRLWPKSGLRRALAL-----PALWVLTEWLR-GWLLTGFPWLALGYSQIp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 162 TGWLAESVSWLGFSGLSGAIAFaaalcvaagVALWSARVGADRSAIQRPARAAVAGAVVLLVALGLVPAAPLPQDGTLKV 241
Cdd:PRK00302 152 DGPLAQLAPIFGVYGLSFLVVL---------VNALLALALIKRRWRLALLALLLLLLAALGYGLRRLQWTTPAPEPALKV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 242 AAIQGN-SKSAIFDDRESGAVFRDHARQTESLLDEleaagesVDLIVWPEnSA----EFDLPGNTLRdfEVAGLARRAGA 316
Cdd:PRK00302 223 ALVQGNiPQSLKWDPAGLEATLQKYLDLSRPALGP-------ADLIIWPE-TAipflLEDLPQAFLK--ALDDLAREKGS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 317 PIVAGSILQDPDGT---YTNSVVVWDARGATGeRYDKRFPVPFAEYMPNRDFFHMLAPdLVDLVQLEYTAGTRPAVLnld 393
Cdd:PRK00302 293 ALITGAPRAENKQGrydYYNSIYVLGPYGILN-RYDKHHLVPFGEYVPLESLLRPLAP-FFNLPMGDFSRGPYVQPP--- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 394 TPAGAVAAGLAICFDIIFDQQAEAIVDGGAQVILAPTNNADFGRTDESAQQLQIARLRAIETGRALVNISTVGTSAMVSP 473
Cdd:PRK00302 368 LLAKGLKLAPLICYEIIFPEEVRANVRQGADLLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDP 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198900569 474 TGQTLDGLTPFTADAMVAEIPLVSGATPALRFgaviaGAWMLLGALGAASGILLGYEPRRARK 536
Cdd:PRK00302 448 LGRIIAQLPQFTEGVLDGTVPPTTGLTPYARW-----GDWPLLLLALLLLLLALLLALRRRRK 505
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
66-477 |
1.02e-49 |
|
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: 176.01 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 66 GLAFWGPHISWLT--LYLGLVPWAGLTAVMTAWFALFGLFVGAGTRGIARAAVFRSRPALLlvaqaatgAGLWVLRESVq 143
Cdd:TIGR00546 2 GFGFFLAGLFWLGiaLSVNGFIAFVAGLLVVGLPALLALFPGLAAYLLRRLAPFRKVLLAL--------PLLWTLAEWL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 144 SSWPYGGFAWGRLAHTQATGWLAESVSWLGFSGLS-------GAIAFAAALCVAAGVALWSARVgadrsaiqrparaava 216
Cdd:TIGR00546 73 RSFGFLGFPWGLIGYAQSSLPLIQIASIFGVWGLSflvvflnALLALVLLKKESFKKLLAIAVV---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 217 GAVVLLVALGLVPAAPLPQDG-TLKVAAIQGN-SKSAIFDDRESGAVFRDHarqteslLDELEAAGESVDLIVWPENSAE 294
Cdd:TIGR00546 137 VLLAALGFLLYELKSATPVPGpTLNVALVQPNiPQDLKFDSEGLEAILEIL-------TSLTKQAVEKPDLVVWPETAFP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 295 FDLPGNTLR-DFEVAGLARRAGAPIVAGSILQDPDGT--YTNSVVVWDARGATGERYDKRFPVPFAEYMPNRDFFHMLAP 371
Cdd:TIGR00546 210 FDLENSPQKlADRLKLLVLSKGIPILIGAPDAVPGGPyhYYNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 372 DLVDLVQLEYTAGTRPAVLNLDtpagAVAAGLAICFDIIFDQQAEAIVDGGAQVILAPTNNADFGRTDESAQQLQIARLR 451
Cdd:TIGR00546 290 LFFLLSQEDFSRGPGPQVLKLP----GGKIAPLICYESIFPDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFR 365
|
410 420
....*....|....*....|....*.
gi 1198900569 452 AIETGRALVNISTVGTSAMVSPTGQT 477
Cdd:TIGR00546 366 AIENGRPLVRATNTGISAVIDPRGRT 391
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
238-493 |
5.26e-22 |
|
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 95.70 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 238 TLKVAAIQGNSksaIFDDREsgavfrDHARQTESLLDEleAAGESVDLIVWPENS-------------AEFDLPGNTLRd 304
Cdd:COG0388 1 TMRIALAQLNP---TVGDIE------ANLAKIEELIRE--AAAQGADLVVFPELFltgyppedddlleLAEPLDGPALA- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 305 fEVAGLARRAGAPIVAGSILQDPDGTYTNSVVVWDARGATGERYDKRFPVPFAEYMPNRDFfhmlapdlvdlvqleyTAG 384
Cdd:COG0388 69 -ALAELARELGIAVVVGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPNYGVFDEKRYF----------------TPG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 385 TRPAVlnLDTPAGAVaaGLAICFDIIFDQQAEAIVDGGAQVILAPTNnadFGRTDESAQQLQIARLRAIETGRALVNIST 464
Cdd:COG0388 132 DELVV--FDTDGGRI--GVLICYDLWFPELARALALAGADLLLVPSA---SPFGRGKDHWELLLRARAIENGCYVVAANQ 204
|
250 260 270
....*....|....*....|....*....|....*...
gi 1198900569 465 VGT---------SAMVSPTGQTLDGLtPFTADAMVAEI 493
Cdd:COG0388 205 VGGedglvfdggSMIVDPDGEVLAEA-GDEEGLLVADI 241
|
|
| nitrilase |
cd07197 |
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
241-495 |
1.03e-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: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 241 VAAIQGNSKSAIFDDResgavfrdhARQTESLLDEleAAGESVDLIVWPE--------------NSAEFDLPGNTLRdfE 306
Cdd:cd07197 1 IAAVQLAPKIGDVEAN---------LAKALRLIKE--AAEQGADLIVLPElfltgysfesakedLDLAEELDGPTLE--A 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 307 VAGLARRAGAPIVAGSILQDPDGTYtNSVVVWDARGATGERYDKRFPVPFAEympnrdffhmlapdlvdlvQLEYTAGTR 386
Cdd:cd07197 68 LAELAKELGIYIVAGIAEKDGDKLY-NTAVVIDPDGEIIGKYRKIHLFDFGE-------------------RRYFSPGDE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 387 PAVLnlDTPAGAVaaGLAICFDIIFDQQAEAIVDGGAQVILAPTNnadfGRTDESAQQLQIARLRAIETGRALVNISTVG 466
Cdd:cd07197 128 FPVF--DTPGGKI--GLLICYDLRFPELARELALKGADIILVPAA----WPTARREHWELLLRARAIENGVYVVAANRVG 199
|
250 260 270
....*....|....*....|....*....|....*...
gi 1198900569 467 T---------SAMVSPTGQTLDgLTPFTADAMVAEIPL 495
Cdd:cd07197 200 EegglefaggSMIVDPDGEVLA-EASEEEGILVAELDL 236
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
240-495 |
4.35e-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: 87.03 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 240 KVAAIQGNSKSAifdDRESGAvfrdhaRQTESLLDEleAAGESVDLIVWPE-------NSAEF-----DLPGNTLRdfEV 307
Cdd:pfam00795 1 RVALVQLPQGFW---DLEANL------QKALELIEE--AARYGADLIVLPElfitgypCWAHFleaaeVGDGETLA--GL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 308 AGLARRAGAPIVAGSILQDPD-GTYTNSVVVWDARGATGERYDKRfpvpfaeympnrdffHMLAPDLVDLVQLEYTAGTR 386
Cdd:pfam00795 68 AALARKNGIAIVIGLIERWLTgGRLYNTAVLLDPDGKLVGKYRKL---------------HLFPEPRPPGFRERVLFEPG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 387 PAVLNLDTPAGAVaaGLAICFDIIFDQQAEAIVDGGAQVILAPTNNADFGRTDESAQQLQIARLRAIETGRALVNISTVG 466
Cdd:pfam00795 133 DGGTVFDTPLGKI--GAAICYEIRFPELLRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALENGCFVIAANQVG 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 1198900569 467 T----------SAMVSPTGQTLDGLTPFTADAMVAEIPL 495
Cdd:pfam00795 211 GeedapwpyghSMIIDPDGRILAGAGEWEEGVLIADIDL 249
|
|
| LNT_N |
pfam20154 |
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal ... |
23-181 |
1.11e-16 |
|
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: 77.28 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 23 GLLLDTAGPGLGWWPLALPAAALIFLAVWQQRARW-GLLAGAVAGLAFWGPHISWLTLYLglvPWAGLTAVMTAWFALFG 101
Cdd:pfam20154 1 GLLLSLAFPPFGLWPLAWVALAPLLLALEARSSPRrAFLLGFLFGLGFFGLGLYWLGVSL---HTFGGAPLPLALLLLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 102 LFVGAGTRGIARAAVFRsrpaLLLVAQAATGAGLWVLRESVQsSWPYGGFAWGRLAHTQA-TGWLAESVSWLGFSGLSGA 180
Cdd:pfam20154 78 LALYLALFALAAWLLKR----LWGLFRALLFAALWVGLEYLR-GWPFGGFPWGLLGYSQAdGPPLIQLAPLGGVYGVSFL 152
|
.
gi 1198900569 181 I 181
Cdd:pfam20154 153 V 153
|
|
| nitrilase_5 |
cd07583 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
240-478 |
1.68e-14 |
|
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: 73.34 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 240 KVAAIQGNSKSAIFDDREsgavfrdhaRQTESLLDEleAAGESVDLIVWPE------------NSAEfDLPGNTLRdfEV 307
Cdd:cd07583 1 KIALIQLDIVWGDPEANI---------ERVESLIEE--AAAAGADLIVLPEmwntgyflddlyELAD-EDGGETVS--FL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 308 AGLARRAGAPIVAGSILQDPDGTYTNSVVVWDARGATGERYDKRFPVPFA---EYMpnrdffhmlapdlvdlvqleyTAG 384
Cdd:cd07583 67 SELAKKHGVNIVAGSVAEKEGGKLYNTAYVIDPDGELIATYRKIHLFGLMgedKYL---------------------TAG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 385 TRPAVLNLDtpagAVAAGLAICFDIIFDQQAEAIVDGGAQVILAPTN----NADFGRTdesaqqLQIArlRAIETGRALV 460
Cdd:cd07583 126 DELEVFELD----GGKVGLFICYDLRFPELFRKLALEGAEILFVPAEwpaaRIEHWRT------LLRA--RAIENQAFVV 193
|
250 260
....*....|....*....|....*..
gi 1198900569 461 NISTVGT---------SAMVSPTGQTL 478
Cdd:cd07583 194 ACNRVGTdggnefgghSMVIDPWGEVL 220
|
|
| nit |
cd07572 |
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ... |
240-429 |
2.37e-13 |
|
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: 70.15 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 240 KVAAIQ---GNSKSAIFddresgavfrdhaRQTESLLDEleAAGESVDLIVWPENS-------------AEFDLPGNTLR 303
Cdd:cd07572 1 RVALIQmtsTADKEANL-------------ARAKELIEE--AAAQGAKLVVLPECFnypggtdafklalAEEEGDGPTLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 304 dfEVAGLARRAGAPIVAGSI--LQDPDGTYTNSVVVWDARGATGERYDKrfpvpfaeympnrdfFHMLAPDLVDLVQL-E 380
Cdd:cd07572 66 --ALSELAKEHGIWLVGGSIpeRDDDDGKVYNTSLVFDPDGELVARYRK---------------IHLFDVDVPGGISYrE 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1198900569 381 ---YTAGTRPAVlnLDTPAGAVaaGLAICFDIIFDQQAEAIVDGGAQVILAP 429
Cdd:cd07572 129 sdtLTPGDEVVV--VDTPFGKI--GLGICYDLRFPELARALARQGADILTVP 176
|
|
| Ph0642_like |
cd07577 |
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ... |
268-493 |
4.03e-10 |
|
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: 60.39 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 268 QTESLLDELEAagesvDLIVWPE---------------NSAEFDLPGNTLRDFEvaGLARRAGAPIVAGSILQDPDGTYt 332
Cdd:cd07577 20 KVESLIKGVEA-----DLIVLPElfntgyaftskeevaSLAESIPDGPTTRFLQ--ELARETGAYIVAGLPERDGDKFY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 333 NSVVVWDARGATGeRYDKR--FpvpFAEympnRDFFhmlapdlvdlvqleyTAG-TRPAVLNLdtpaGAVAAGLAICFDI 409
Cdd:cd07577 92 NSAVVVGPEGYIG-IYRKThlF---YEE----KLFF---------------EPGdTGFRVFDI----GDIRIGVMICFDW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 410 IFDQQAEAIVDGGAQVILAPTNNA-DFGRtdesaqqlQIARLRAIE----------TG---RALVNISTVGTSAMVSPTG 475
Cdd:cd07577 145 YFPEAARTLALKGADIIAHPANLVlPYCP--------KAMPIRALEnrvftitanrIGteeRGGETLRFIGKSQITSPKG 216
|
250
....*....|....*...
gi 1198900569 476 QTLDGLTPFTADAMVAEI 493
Cdd:cd07577 217 EVLARAPEDGEEVLVAEI 234
|
|
| nitrilase_Rim1_like |
cd07574 |
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ... |
262-466 |
3.76e-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: 57.98 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 262 FRDHARQTESLLDEleAAGESVDLIVWPENSAE----FDLPGNTLRDFEV--------------AGLARRAGAPIVAGSI 323
Cdd:cd07574 16 FEEFAAKVEYWVAE--AAGYGADLLVFPEYFTMellsLLPEAIDGLDEAIralaaltpdyvalfSELARKYGINIIAGSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 324 LQDPDGTYTNSVVVWdARGATGERYDKRFPVPFAEYmpnrdffhmlapdlvdlvQLEYTAGTRPAVLnlDTPAGAVaaGL 403
Cdd:cd07574 94 PVREDGRLYNRAYLF-GPDGTIGHQDKLHMTPFERE------------------EWGISGGDKLKVF--DTDLGKI--GI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1198900569 404 AICFDIIFDQQAEAIVDGGAQVILAPTNNAD---FGRTDESAQQlqiarlRAIETGRALVNISTVG 466
Cdd:cd07574 151 LICYDSEFPELARALAEAGADLLLVPSCTDTragYWRVRIGAQA------RALENQCYVVQSGTVG 210
|
|
| R-amidase_like |
cd07576 |
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
260-478 |
8.47e-08 |
|
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: 53.35 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 260 AVFRDHARQTESLLDEL-EAAGESVDLIVWPE----------NSAEFDLP--GNTLRdfEVAGLARRAGAPIVAGSILQD 326
Cdd:cd07576 9 ARDGDVAANLARLDEAAaRAAAAGADLLVFPElfltgynigdAVARLAEPadGPALQ--ALRAIARRHGIAIVVGYPERA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 327 PDGTYtNSVVVWDARGATGERYDKRfpvpfaeympnrdffHMLAPDLVDLvqleYTAGTRPAVLNLDtpagAVAAGLAIC 406
Cdd:cd07576 87 GGAVY-NAAVLIDEDGTVLANYRKT---------------HLFGDSERAA----FTPGDRFPVVELR----GLRVGLLIC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 407 FDIIFDQQAEAIVDGGAQVILAPTNNAD-FGRTDESaqqlqIARLRAIETG--RALVN-------ISTVGTSAMVSPTGQ 476
Cdd:cd07576 143 YDVEFPELVRALALAGADLVLVPTALMEpYGFVART-----LVPARAFENQifVAYANrcgaedgLTYVGLSSIAGPDGT 217
|
..
gi 1198900569 477 TL 478
Cdd:cd07576 218 VL 219
|
|
| nitrilase_3 |
cd07581 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
260-478 |
1.72e-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: 143605 Cd Length: 255 Bit Score: 52.58 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 260 AVFRDHARQTESLLDEL-EAAGESVDLIVWPENSAEFDLPGNTLRD---------F--EVAGLARRAGAPIVAGSILQDP 327
Cdd:cd07581 7 ASSGDKEENLEKVRRLLaEAAAAGADLVVFPEYTMARFGDGLDDYArvaepldgpFvsALARLARELGITVVAGMFEPAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 328 DGTYTNSVVVWDARGATGERYDKR--FpvpfaeympnrDFFHMLAPDLVDlvqleytAGTRPAVLNldTPAGAVAAGLAI 405
Cdd:cd07581 87 DGRVYNTLVVVGPDGEIIAVYRKIhlY-----------DAFGFRESDTVA-------PGDELPPVV--FVVGGVKVGLAT 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1198900569 406 CFDIIFDQQAEAIVDGGAQVILAPtnnADFGRTDESAQQLQI-ARLRAIETGRALVNIST-----VGTSAMVSPTGQTL 478
Cdd:cd07581 147 CYDLRFPELARALALAGADVIVVP---AAWVAGPGKEEHWETlLRARALENTVYVAAAGQagprgIGRSMVVDPLGVVL 222
|
|
| PRK13981 |
PRK13981 |
NAD synthetase; Provisional |
277-466 |
5.32e-07 |
|
NAD synthetase; Provisional
Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 52.08 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 277 EAAGESVDLIVWPENSaefdLPGNTLRD------F------EVAGLAR--RAGAPIVAGSILQDPDGTYtNSVVVWDaRG 342
Cdd:PRK13981 28 EAADAGADLLLFPELF----LSGYPPEDlllrpaFlaaceaALERLAAatAGGPAVLVGHPWREGGKLY-NAAALLD-GG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 343 ATGERYDKRFpvpfaeyMPNRDFFhmlapdlvDLVQLeYTAGTRPAVLNLDTpagaVAAGLAICFDIIFDQQAEAIVDGG 422
Cdd:PRK13981 102 EVLATYRKQD-------LPNYGVF--------DEKRY-FAPGPEPGVVELKG----VRIGVPICEDIWNPEPAETLAEAG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1198900569 423 AQVILAPtnNADFGRTDESAQQLQIARLRAIETGRALVNISTVG 466
Cdd:PRK13981 162 AELLLVP--NASPYHRGKPDLREAVLRARVRETGLPLVYLNQVG 203
|
|
| PRK12291 |
PRK12291 |
apolipoprotein N-acyltransferase; Reviewed |
265-435 |
1.15e-03 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 237042 [Multi-domain] Cd Length: 418 Bit Score: 41.50 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 265 HARQTESLLDELEAA-GESVDLIVWPEnSAeFDLPGNTLRDFEVAGLARRAGAPIVAGSILQDpDGTYTNSVVVWDarGA 343
Cdd:PRK12291 215 LKSIINENLKEIDKAiDEKKDLIVLPE-TA-FPLALNNSPILLDKLKELSHKITIITGALRVE-DGHIYNSTYIFS--KG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198900569 344 TGERYDKRFPVPFAEYMPNRDFFhmlapdlVDLVQ-------LEYTAGTRPAVLNLDtpagAVAAGLAICFdiifdqqaE 416
Cdd:PRK12291 290 NVQIADKVILVPFGEEIPLPKFF-------KKPINklffggaSDFSKASKFSDFTLD----GVKFRNAICY--------E 350
|
170 180
....*....|....*....|...
gi 1198900569 417 AIVD----GGAQVILAPTNNADF 435
Cdd:PRK12291 351 ATSEelyeGNPKIVIAISNNAWF 373
|
|
| |
