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Conserved domains on  [gi|754810822|ref|WP_042173735|]
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MULTISPECIES: apolipoprotein N-acyltransferase [unclassified Streptomyces]

Protein Classification

apolipoprotein N-acyltransferase( domain architecture ID 11435283)

apolipoprotein N-acyltransferase catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
49-523 3.39e-114

Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 346.45  E-value: 3.39e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  49 PRTLWWLALPAFAVFGGLLRG-RSWKAGLGIGYLFGLGFLLPLLVWTGV----------EVGPGPWIALAVIEAVFVALV 117
Cdd:COG0815    1 PFGLWPLAFVALAPLLLLLRGaRSPRRAFLLGWLFGLGFFLAGLYWLYVslhvfgglpaWLAPLAVLLLAAYLALFFALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 118 GAGAAAVSKLPG--SPVWAAALWTAGEAARARVpFSGFPWGKIAFGQAD-GVFLPLAALGGTPVLGFAVVLCGFGLYEIV 194
Cdd:COG0815   81 AALARRLRRRGGllRPLAFAALWVLLEWLRGWL-FTGFPWLRLGYSQADfSPLAQLAPLGGVYGLSFLVVLVNALLALAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 195 RvvldaRRTTTVRRVAAAVGALsvaaplVAAVAARPLVSDTAEDGTATVAVVQGNVPRLGLDFNTQRRAVLDYHARETER 274
Cdd:COG0815  160 L-----RRRRRLAALALALALL------LAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKWDPEQRREILDRYLDLTRE 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 275 LAAavdageaERPDIVLWPENSSDIDPFANADARAVIDRAAQAIGAPVSVGAVV--GKDGKLLNEQVLWDPDKGPVDIYD 352
Cdd:COG0815  229 LAD-------DGPDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRrdGGGGRYYNSALLLDPDGGILGRYD 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 353 KRQIQPFGEYLPLRSLVGAINDeWTSMVRQDFSRGTEPGVFTMAGTGVGLVTCYEAAFDWAVRDTVTEGARLISVPSNNA 432
Cdd:COG0815  302 KHHLVPFGEYVPLRDLLRPLIP-FLDLPLGDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNITNDA 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 433 TFGRSEMTHQQLAMSRVRAVEHSRTVTVPVTSGVSAIIMPDGKVSQRTGMFVADSLVQEVPLRSSLTPATRLGVLPETVL 512
Cdd:COG0815  381 WFGDSIGPYQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLL 460

                        490
                 ....*....|.
gi 754810822 513 VLVAAGGLGWA 523
Cdd:COG0815  461 LLLALLLALLL 471
 
Name Accession Description Interval E-value
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
49-523 3.39e-114

Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 346.45  E-value: 3.39e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  49 PRTLWWLALPAFAVFGGLLRG-RSWKAGLGIGYLFGLGFLLPLLVWTGV----------EVGPGPWIALAVIEAVFVALV 117
Cdd:COG0815    1 PFGLWPLAFVALAPLLLLLRGaRSPRRAFLLGWLFGLGFFLAGLYWLYVslhvfgglpaWLAPLAVLLLAAYLALFFALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 118 GAGAAAVSKLPG--SPVWAAALWTAGEAARARVpFSGFPWGKIAFGQAD-GVFLPLAALGGTPVLGFAVVLCGFGLYEIV 194
Cdd:COG0815   81 AALARRLRRRGGllRPLAFAALWVLLEWLRGWL-FTGFPWLRLGYSQADfSPLAQLAPLGGVYGLSFLVVLVNALLALAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 195 RvvldaRRTTTVRRVAAAVGALsvaaplVAAVAARPLVSDTAEDGTATVAVVQGNVPRLGLDFNTQRRAVLDYHARETER 274
Cdd:COG0815  160 L-----RRRRRLAALALALALL------LAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKWDPEQRREILDRYLDLTRE 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 275 LAAavdageaERPDIVLWPENSSDIDPFANADARAVIDRAAQAIGAPVSVGAVV--GKDGKLLNEQVLWDPDKGPVDIYD 352
Cdd:COG0815  229 LAD-------DGPDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRrdGGGGRYYNSALLLDPDGGILGRYD 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 353 KRQIQPFGEYLPLRSLVGAINDeWTSMVRQDFSRGTEPGVFTMAGTGVGLVTCYEAAFDWAVRDTVTEGARLISVPSNNA 432
Cdd:COG0815  302 KHHLVPFGEYVPLRDLLRPLIP-FLDLPLGDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNITNDA 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 433 TFGRSEMTHQQLAMSRVRAVEHSRTVTVPVTSGVSAIIMPDGKVSQRTGMFVADSLVQEVPLRSSLTPATRLGVLPETVL 512
Cdd:COG0815  381 WFGDSIGPYQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLL 460

                        490
                 ....*....|.
gi 754810822 513 VLVAAGGLGWA 523
Cdd:COG0815  461 LLLALLLALLL 471
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
 242-515 4.16e-87

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: 269.47  E-value: 4.16e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 242 TVAVVQGNVPRLGLDFNTQRRAVLDYHARETERLAAavdageaERPDIVLWPENSSDIDPFANADARAVIDRAAQAIGAP 321
Cdd:cd07571    2 RVALVQGNIPQDEKWDPEQRQATLDRYLDLTRELAD-------EKPDLVVWPETALPFDLQRDPDALARLARAARAVGAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 322 VSVGAV--VGKDGKLLNEQVLWDPDKGPVDIYDKRQIQPFGEYLPLRSLVGAINDEWTSMVRqDFSRGTEPGVFTMAGTG 399
Cdd:cd07571   75 LLTGAPrrEPGGGRYYNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPMG-DFSPGTGPQPLLLGGGV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 400 -VGLVTCYEAAFDWAVRDTVTEGARLISVPSNNATFGRSEMTHQQLAMSRVRAVEHSRTVTVPVTSGVSAIIMPDGKVSQ 478
Cdd:cd07571  154 rVGPLICYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVA 233

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 754810822 479 RTGMFVADSLVQEVPLRSSLTPATRLGVLPETVLVLV 515
Cdd:cd07571  234 RLPLFEAGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
 98-476 1.70e-65

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: 217.61  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822   98 VGPGPWIALAVIEAVFVALVGAGAAAVSKLPG---SPVWAAALWTAGEAARARVPFsGFPWGKIAFGQADGVFLPLAALG 174
Cdd:TIGR00546  23 IAFVAGLLVVGLPALLALFPGLAAYLLRRLAPfrkVLLALPLLWTLAEWLRSFGFL-GFPWGLIGYAQSSLPLIQIASIF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  175 GTPVLGFAVVLCGFGLYEIVRVVLDARRTTTVRRVAAAVGALSVAAplvaavaaRPLVSDTAEDGTATVAVVQGNVPRLG 254
Cdd:TIGR00546 102 GVWGLSFLVVFLNALLALVLLKKESFKKLLAIAVVVLLAALGFLLY--------ELKSATPVPGPTLNVALVQPNIPQDL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  255 LDFNTQRRAVLDYHARETERLAaavdageaERPDIVLWPENSSDIDPFANADARAV-IDRAAQAIGAPVSVGA---VVGK 330
Cdd:TIGR00546 174 KFDSEGLEAILEILTSLTKQAV--------EKPDLVVWPETAFPFDLENSPQKLADrLKLLVLSKGIPILIGApdaVPGG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  331 DGKLLNEQVLWDPDKGPVDIYDKRQIQPFGEYLPLRSLVGAINDEWTSMVRQDFSRGTEPGVFTMAGTGVGLVTCYEAAF 410
Cdd:TIGR00546 246 PYHYYNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSKLFFLLSQEDFSRGPGPQVLKLPGGKIAPLICYESIF 325

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754810822  411 DWAVRDTVTEGARLISVPSNNATFGRSEMTHQQLAMSRVRAVEHSRTVTVPVTSGVSAIIMPDGKV 476
Cdd:TIGR00546 326 PDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFRAIENGRPLVRATNTGISAVIDPRGRT 391
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
 45-533 2.48e-54

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 190.86  E-value: 2.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  45 VSFPPRTLWWLALPAFAVFGGLLRGRSWKAGLGIGYLFGLGFLLPLLVWTGVEV---GPGPWIA-----------LAVIE 110
Cdd:PRK00302  21 LAFAPFDLWPLALLSLAGLLWLLLGASPKQAALIGFLWGFGYFGSGLSWIYVSIhtfGGMPAWLapllvlllaayLALYP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 111 AVFVALVGAGAAAVSKlpGSPVWAAALWTAGEAARARVpFSGFPWGKIAFGQA-DGVFLPLAALGGTPVLGFAVVLCGFG 189
Cdd:PRK00302 101 ALFAALWRRLWPKSGL--RRALALPALWVLTEWLRGWL-LTGFPWLALGYSQIpDGPLAQLAPIFGVYGLSFLVVLVNAL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 190 LYEIVrvvldarrtTTVRRVAAAVGALSVAAPLVAAVAARPLVSDTAEDGTATVAVVQGNVP-RLGLDfNTQRRAVLDYH 268
Cdd:PRK00302 178 LALAL---------IKRRWRLALLALLLLLLAALGYGLRRLQWTTPAPEPALKVALVQGNIPqSLKWD-PAGLEATLQKY 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 269 ARETERLAAAVdageaerpDIVLWPENSSDIDPFANADA-RAVIDRAAQAIGAPVSVGAVV----GKDGKLLNEQVLWDP 343
Cdd:PRK00302 248 LDLSRPALGPA--------DLIIWPETAIPFLLEDLPQAfLKALDDLAREKGSALITGAPRaenkQGRYDYYNSIYVLGP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 344 DKGpVDIYDKRQIQPFGEYLPLRSLVGAINDeWTSMVRQDFSRGTEPGVFTMAGTG-VGLVTCYEAAFDWAVRDTVTEGA 422
Cdd:PRK00302 320 YGI-LNRYDKHHLVPFGEYVPLESLLRPLAP-FFNLPMGDFSRGPYVQPPLLAKGLkLAPLICYEIIFPEEVRANVRQGA 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 423 RLISVPSNNATFGRSEMTHQQLAMSRVRAVEHSRTVtVPVT-SGVSAIIMPDGKVSQRTGMFVADSLVQEVPLRSSLTPA 501
Cdd:PRK00302 398 DLLLNISNDAWFGDSIGPYQHFQMARMRALELGRPL-IRATnTGITAVIDPLGRIIAQLPQFTEGVLDGTVPPTTGLTPY 476

                        490       500       510
                 ....*....|....*....|....*....|..
gi 754810822 502 TRLGVLPetvLVLVAAGGLGWAVATGVRGRVR 533
Cdd:PRK00302 477 ARWGDWP---LLLLALLLLLLALLLALRRRRK 505
LNT_N pfam20154
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal ...
 44-187 4.67e-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: 4.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822   44 YVSFPPRTLWWLALPAFAVFGGLLRGR-SWKAGLGIGYLFGLGFLLPLLVWTGV-----EVGPGPW-IALAVIEAVFVAL 116
Cdd:pfam20154   5 SLAFPPFGLWPLAWVALAPLLLALEARsSPRRAFLLGFLFGLGFFGLGLYWLGVslhtfGGAPLPLaLLLLLLLALYLAL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754810822  117 VGAGAAAVSKLPGS--PVWAAALWTAGEAARArVPFSGFPWGKIAFGQADG-VFLPLAALGGTPVLGFAVVLCG 187
Cdd:pfam20154  85 FALAAWLLKRLWGLfrALLFAALWVGLEYLRG-WPFGGFPWGLLGYSQADGpPLIQLAPLGGVYGVSFLVVLVN 157
 
Name Accession Description Interval E-value
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
49-523 3.39e-114

Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 346.45  E-value: 3.39e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  49 PRTLWWLALPAFAVFGGLLRG-RSWKAGLGIGYLFGLGFLLPLLVWTGV----------EVGPGPWIALAVIEAVFVALV 117
Cdd:COG0815    1 PFGLWPLAFVALAPLLLLLRGaRSPRRAFLLGWLFGLGFFLAGLYWLYVslhvfgglpaWLAPLAVLLLAAYLALFFALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 118 GAGAAAVSKLPG--SPVWAAALWTAGEAARARVpFSGFPWGKIAFGQAD-GVFLPLAALGGTPVLGFAVVLCGFGLYEIV 194
Cdd:COG0815   81 AALARRLRRRGGllRPLAFAALWVLLEWLRGWL-FTGFPWLRLGYSQADfSPLAQLAPLGGVYGLSFLVVLVNALLALAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 195 RvvldaRRTTTVRRVAAAVGALsvaaplVAAVAARPLVSDTAEDGTATVAVVQGNVPRLGLDFNTQRRAVLDYHARETER 274
Cdd:COG0815  160 L-----RRRRRLAALALALALL------LAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKWDPEQRREILDRYLDLTRE 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 275 LAAavdageaERPDIVLWPENSSDIDPFANADARAVIDRAAQAIGAPVSVGAVV--GKDGKLLNEQVLWDPDKGPVDIYD 352
Cdd:COG0815  229 LAD-------DGPDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRrdGGGGRYYNSALLLDPDGGILGRYD 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 353 KRQIQPFGEYLPLRSLVGAINDeWTSMVRQDFSRGTEPGVFTMAGTGVGLVTCYEAAFDWAVRDTVTEGARLISVPSNNA 432
Cdd:COG0815  302 KHHLVPFGEYVPLRDLLRPLIP-FLDLPLGDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNITNDA 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 433 TFGRSEMTHQQLAMSRVRAVEHSRTVTVPVTSGVSAIIMPDGKVSQRTGMFVADSLVQEVPLRSSLTPATRLGVLPETVL 512
Cdd:COG0815  381 WFGDSIGPYQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLL 460

                        490
                 ....*....|.
gi 754810822 513 VLVAAGGLGWA 523
Cdd:COG0815  461 LLLALLLALLL 471
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
 242-515 4.16e-87

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: 269.47  E-value: 4.16e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 242 TVAVVQGNVPRLGLDFNTQRRAVLDYHARETERLAAavdageaERPDIVLWPENSSDIDPFANADARAVIDRAAQAIGAP 321
Cdd:cd07571    2 RVALVQGNIPQDEKWDPEQRQATLDRYLDLTRELAD-------EKPDLVVWPETALPFDLQRDPDALARLARAARAVGAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 322 VSVGAV--VGKDGKLLNEQVLWDPDKGPVDIYDKRQIQPFGEYLPLRSLVGAINDEWTSMVRqDFSRGTEPGVFTMAGTG 399
Cdd:cd07571   75 LLTGAPrrEPGGGRYYNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPMG-DFSPGTGPQPLLLGGGV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 400 -VGLVTCYEAAFDWAVRDTVTEGARLISVPSNNATFGRSEMTHQQLAMSRVRAVEHSRTVTVPVTSGVSAIIMPDGKVSQ 478
Cdd:cd07571  154 rVGPLICYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVA 233

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 754810822 479 RTGMFVADSLVQEVPLRSSLTPATRLGVLPETVLVLV 515
Cdd:cd07571  234 RLPLFEAGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
 98-476 1.70e-65

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: 217.61  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822   98 VGPGPWIALAVIEAVFVALVGAGAAAVSKLPG---SPVWAAALWTAGEAARARVPFsGFPWGKIAFGQADGVFLPLAALG 174
Cdd:TIGR00546  23 IAFVAGLLVVGLPALLALFPGLAAYLLRRLAPfrkVLLALPLLWTLAEWLRSFGFL-GFPWGLIGYAQSSLPLIQIASIF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  175 GTPVLGFAVVLCGFGLYEIVRVVLDARRTTTVRRVAAAVGALSVAAplvaavaaRPLVSDTAEDGTATVAVVQGNVPRLG 254
Cdd:TIGR00546 102 GVWGLSFLVVFLNALLALVLLKKESFKKLLAIAVVVLLAALGFLLY--------ELKSATPVPGPTLNVALVQPNIPQDL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  255 LDFNTQRRAVLDYHARETERLAaavdageaERPDIVLWPENSSDIDPFANADARAV-IDRAAQAIGAPVSVGA---VVGK 330
Cdd:TIGR00546 174 KFDSEGLEAILEILTSLTKQAV--------EKPDLVVWPETAFPFDLENSPQKLADrLKLLVLSKGIPILIGApdaVPGG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  331 DGKLLNEQVLWDPDKGPVDIYDKRQIQPFGEYLPLRSLVGAINDEWTSMVRQDFSRGTEPGVFTMAGTGVGLVTCYEAAF 410
Cdd:TIGR00546 246 PYHYYNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSKLFFLLSQEDFSRGPGPQVLKLPGGKIAPLICYESIF 325

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754810822  411 DWAVRDTVTEGARLISVPSNNATFGRSEMTHQQLAMSRVRAVEHSRTVTVPVTSGVSAIIMPDGKV 476
Cdd:TIGR00546 326 PDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFRAIENGRPLVRATNTGISAVIDPRGRT 391
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
 45-533 2.48e-54

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 190.86  E-value: 2.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  45 VSFPPRTLWWLALPAFAVFGGLLRGRSWKAGLGIGYLFGLGFLLPLLVWTGVEV---GPGPWIA-----------LAVIE 110
Cdd:PRK00302  21 LAFAPFDLWPLALLSLAGLLWLLLGASPKQAALIGFLWGFGYFGSGLSWIYVSIhtfGGMPAWLapllvlllaayLALYP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 111 AVFVALVGAGAAAVSKlpGSPVWAAALWTAGEAARARVpFSGFPWGKIAFGQA-DGVFLPLAALGGTPVLGFAVVLCGFG 189
Cdd:PRK00302 101 ALFAALWRRLWPKSGL--RRALALPALWVLTEWLRGWL-LTGFPWLALGYSQIpDGPLAQLAPIFGVYGLSFLVVLVNAL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 190 LYEIVrvvldarrtTTVRRVAAAVGALSVAAPLVAAVAARPLVSDTAEDGTATVAVVQGNVP-RLGLDfNTQRRAVLDYH 268
Cdd:PRK00302 178 LALAL---------IKRRWRLALLALLLLLLAALGYGLRRLQWTTPAPEPALKVALVQGNIPqSLKWD-PAGLEATLQKY 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 269 ARETERLAAAVdageaerpDIVLWPENSSDIDPFANADA-RAVIDRAAQAIGAPVSVGAVV----GKDGKLLNEQVLWDP 343
Cdd:PRK00302 248 LDLSRPALGPA--------DLIIWPETAIPFLLEDLPQAfLKALDDLAREKGSALITGAPRaenkQGRYDYYNSIYVLGP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 344 DKGpVDIYDKRQIQPFGEYLPLRSLVGAINDeWTSMVRQDFSRGTEPGVFTMAGTG-VGLVTCYEAAFDWAVRDTVTEGA 422
Cdd:PRK00302 320 YGI-LNRYDKHHLVPFGEYVPLESLLRPLAP-FFNLPMGDFSRGPYVQPPLLAKGLkLAPLICYEIIFPEEVRANVRQGA 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 423 RLISVPSNNATFGRSEMTHQQLAMSRVRAVEHSRTVtVPVT-SGVSAIIMPDGKVSQRTGMFVADSLVQEVPLRSSLTPA 501
Cdd:PRK00302 398 DLLLNISNDAWFGDSIGPYQHFQMARMRALELGRPL-IRATnTGITAVIDPLGRIIAQLPQFTEGVLDGTVPPTTGLTPY 476

                        490       500       510
                 ....*....|....*....|....*....|..
gi 754810822 502 TRLGVLPetvLVLVAAGGLGWAVATGVRGRVR 533
Cdd:PRK00302 477 ARWGDWP---LLLLALLLLLLALLLALRRRRK 505
LNT_N pfam20154
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal ...
 44-187 4.67e-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: 4.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822   44 YVSFPPRTLWWLALPAFAVFGGLLRGR-SWKAGLGIGYLFGLGFLLPLLVWTGV-----EVGPGPW-IALAVIEAVFVAL 116
Cdd:pfam20154   5 SLAFPPFGLWPLAWVALAPLLLALEARsSPRRAFLLGFLFGLGFFGLGLYWLGVslhtfGGAPLPLaLLLLLLLALYLAL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754810822  117 VGAGAAAVSKLPGS--PVWAAALWTAGEAARArVPFSGFPWGKIAFGQADG-VFLPLAALGGTPVLGFAVVLCG 187
Cdd:pfam20154  85 FALAAWLLKRLWGLfrALLFAALWVGLEYLRG-WPFGGFPWGLLGYSQADGpPLIQLAPLGGVYGVSFLVVLVN 157
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 243-486 1.24e-15

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: 76.59  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 243 VAVVQGNVPRLGLDFNTQRraVLDYhareterLAAAVDAGeaerPDIVLWPE---------NSSDIDPFANADARAVIDR 313
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAK--ALRL-------IKEAAEQG----ADLIVLPElfltgysfeSAKEDLDLAEELDGPTLEA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 314 ---AAQAIGAPVSVGAVVGKDGKLLNEQVLWDPDKGPVDIYDKRQIQPFGEylplrslvgainDEWtsmvrqdFSRGTEP 390
Cdd:cd07197   68 laeLAKELGIYIVAGIAEKDGDKLYNTAVVIDPDGEIIGKYRKIHLFDFGE------------RRY-------FSPGDEF 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 391 GVFTMAGTGVGLVTCYEAAFDWAVRDTVTEGARLISVPSNNATFGRsemtHQQLAMSRVRAVEHsrtvTVPVTS------ 464
Cdd:cd07197  129 PVFDTPGGKIGLLICYDLRFPELARELALKGADIILVPAAWPTARR----EHWELLLRARAIEN----GVYVVAanrvge 200

                        250       260       270
                 ....*....|....*....|....*....|...
gi 754810822 465 -------GVSAIIMPDGKV----SQRTGMFVAD 486
Cdd:cd07197  201 egglefaGGSMIVDPDGEVlaeaSEEEGILVAE 233
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
240-486 1.70e-14

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 73.74  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 240 TATVAVVQGNVPRLGLDFNTqrravldyharetERLAAAVDAGEAERPDIVLWPENSS---DIDPFANADARAVID---- 312
Cdd:COG0388    1 TMRIALAQLNPTVGDIEANL-------------AKIEELIREAAAQGADLVVFPELFLtgyPPEDDDLLELAEPLDgpal 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 313 ----RAAQAIGAPVSVGAVV-GKDGKLLNEQVLWDPDKGPVDIYDKRQIQPFGEYlplrslvgainDEwtsmvRQDFSRG 387
Cdd:COG0388   68 aalaELARELGIAVVVGLPErDEGGRLYNTALVIDPDGEILGRYRKIHLPNYGVF-----------DE-----KRYFTPG 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 388 TEPGVFTMAGTGVGLVTCYEAAFDWAVRDTVTEGARLISVPSNNaTFGRSEMTHQQLAmsRVRAVEHsrtvTVPV----- 462
Cdd:COG0388  132 DELVVFDTDGGRIGVLICYDLWFPELARALALAGADLLLVPSAS-PFGRGKDHWELLL--RARAIEN----GCYVvaanq 204

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 754810822 463 --------TSGVSAIIMPDGKV----SQRTGMFVAD 486
Cdd:COG0388  205 vggedglvFDGGSMIVDPDGEVlaeaGDEEGLLVAD 240
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 242-476 1.86e-12

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: 67.38  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  242 TVAVVQGNVPRLGLDFNTQRraVLDYHAReterlAAAVDAgeaerpDIVLWPENS-----SDIDPFANADARAV-----I 311
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQK--ALELIEE-----AARYGA------DLIVLPELFitgypCWAHFLEAAEVGDGetlagL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  312 DRAAQAIGAPVSVGAV--VGKDGKLLNEQVLWDPDKGPVDIYDKRQIqpFGEYLPLrslvgaindewTSMVRQDFSRGTE 389
Cdd:pfam00795  68 AALARKNGIAIVIGLIerWLTGGRLYNTAVLLDPDGKLVGKYRKLHL--FPEPRPP-----------GFRERVLFEPGDG 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  390 PGVFTMAGTGVGLVTCYEAAFDWAVRDTVTEGARLISVPSNNATFGRSEMTHQQLAMSRVRAVEhSRTVTVPVTS----- 464
Cdd:pfam00795 135 GTVFDTPLGKIGAAICYEIRFPELLRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALE-NGCFVIAANQvggee 213

                         250
                  ....*....|....*...
gi 754810822  465 ------GVSAIIMPDGKV 476
Cdd:pfam00795 214 dapwpyGHSMIIDPDGRI 231
PRK12291 PRK12291
apolipoprotein N-acyltransferase; Reviewed
 324-472 1.30e-08

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 237042 [Multi-domain]  Cd Length: 418  Bit Score: 56.91  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 324 VGAVVGKDGKLLNEQVLWDpdKGPVDIYDKRQIQPFGEYLPL-RSLVGAINDEWTSMVrQDFSRGTEPGVFTMAGTGVGL 402
Cdd:PRK12291 269 TGALRVEDGHIYNSTYIFS--KGNVQIADKVILVPFGEEIPLpKFFKKPINKLFFGGA-SDFSKASKFSDFTLDGVKFRN 345

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754810822 403 VTCYEAAfdwavRDTVTEG-ARLISVPSNNATFGRS-EMTHQQLAMsRVRAVEHSRTVTVPVTSGVSAIIMP 472
Cdd:PRK12291 346 AICYEAT-----SEELYEGnPKIVIAISNNAWFVPSiEPTLQKLLL-KYYARKYGKTIYHSANGSPSYIITP 411
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
 331-433 6.42e-07

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: 51.05  E-value: 6.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 331 DGKLLNEQVLWDPDkGPVDIYDKRQIQPFGEylplrslvgainDEWtsmvrqDFSRGTEPGVFTMAGTGVGLVTCYEAAF 410
Cdd:cd07574   98 DGRLYNRAYLFGPD-GTIGHQDKLHMTPFER------------EEW------GISGGDKLKVFDTDLGKIGILICYDSEF 158

                         90       100
                 ....*....|....*....|...
gi 754810822 411 DWAVRDTVTEGARLISVPSNNAT 433
Cdd:cd07574  159 PELARALAEAGADLLLVPSCTDT 181
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 273-476 1.74e-06

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: 49.46  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 273 ERLAAAVDAGEAERPDIVLWPE--NSSdidpFANADARAVIDRAAQAIGAPVSVGA------------VVGKDGKLLNEQ 338
Cdd:cd07583   19 ERVESLIEEAAAAGADLIVLPEmwNTG----YFLDDLYELADEDGGETVSFLSELAkkhgvnivagsvAEKEGGKLYNTA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 339 VLWDPDKGPVDIYDKrqIQPFGeYLplrslvgainDEwtsmvRQDFSRGTEPGVFTMAGTGVGLVTCYEAAF-DWAvRDT 417
Cdd:cd07583   95 YVIDPDGELIATYRK--IHLFG-LM----------GE-----DKYLTAGDELEVFELDGGKVGLFICYDLRFpELF-RKL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 418 VTEGARLISVPSN--NAtfgRsemTHQQLAMSRVRAVEH-------SRTVTVPVT--SGVSAIIMPDGKV 476
Cdd:cd07583  156 ALEGAEILFVPAEwpAA---R---IEHWRTLLRARAIENqafvvacNRVGTDGGNefGGHSMVIDPWGEV 219
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 274-453 4.40e-06

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: 48.34  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 274 RLAAAVDAGEAERPDIVLWPE------NSSDIDPFANADARAVIDRAAQAIGAPVSVGAVVG----KDGKLLNEQVLWDP 343
Cdd:cd07576   20 RLDEAAARAAAAGADLLVFPElfltgyNIGDAVARLAEPADGPALQALRAIARRHGIAIVVGyperAGGAVYNAAVLIDE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 344 DKGPVDIYDKRQIqpFGEYlplrslvgaindEwtsmvRQDFSRGTEPGVFTMAGTGVGLVTCYEAAFDWAVRDTVTEGAR 423
Cdd:cd07576  100 DGTVLANYRKTHL--FGDS------------E-----RAAFTPGDRFPVVELRGLRVGLLICYDVEFPELVRALALAGAD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 754810822 424 LISVPSNNATfgrsEMTHQQLAMSRVRAVE 453
Cdd:cd07576  161 LVLVPTALME----PYGFVARTLVPARAFE 186
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 243-486 3.36e-05

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143609  Cd Length: 261  Bit Score: 45.77  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 243 VAVVQGNVPRLGLDFNTQRravldyhARETERLAAAVDAgeaerpDIVLWPENS-----SDIDPFANA---DARAV--ID 312
Cdd:cd07585    2 IALVQFEARVGDKARNLAV-------IARWTRKAAAQGA------ELVCFPEMCitgytHVRALSREAevpDGPSTqaLS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 313 RAAQAIGAPVSVGAVVGKDGKLLNEQVLWDPDkGPVDIYdkRQIQPFgeylplrslvgaindewtSMVRQDFSRGTEPGV 392
Cdd:cd07585   69 DLARRYGLTILAGLIEKAGDRPYNTYLVCLPD-GLVHRY--RKLHLF------------------RREHPYIAAGDEYPV 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 393 FTMAGTGVGLVTCYEAAFDWAVRDTVTEGARLISVPsnNATFGRSEMTHQQLAMSRVRAVEHSRTVTV-----------P 461
Cdd:cd07585  128 FATPGVRFGILICYDNHFPENVRATALLGAEILFAP--HATPGTTSPKGREWWMRWLPARAYDNGVFVaacngvgrdggE 205

                        250       260       270
                 ....*....|....*....|....*....|
gi 754810822 462 VTSGVSAIIMPDGKV-----SQRTGMFVAD 486
Cdd:cd07585  206 VFPGGAMILDPYGRVlaettSGGDGMVVAD 235
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 21-533 1.91e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.48  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822   21 GAWRRRLVRL--VPFAAAALSGLLLYVSFPPRTLWWLALPAFAVFGGLLRGRSWKAGLGIGYLFGLGFLLPLLVWTGVEV 98
Cdd:COG3321   854 PGRGRRRVPLptYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822   99 GPGPWIALAVIEAVFVALVGAGAAAVSKLPGSPVWAAALWTAGEAARARVPFSGfPWGKIAFGQADGVFLPLAALGGTPV 178
Cdd:COG3321   934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAA-AAAAAAAALAAAAALALLAAAALLL 1012

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  179 LGFAVVLCGFGLYEIVRVVLDARRTTTVRRVAAAVGALSVAAPLVAAVAARPLVSDTAEDGTATVAVVQGNVPRLGLDFN 258
Cdd:COG3321  1013 AAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAA 1092

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  259 TQRRAVLDYHARETERLAAAVDAGEAERPDIVLWPENSSDIDPFANADARAVIDRAAQAIGAPVSVGAVVGKDGKLLNEQ 338
Cdd:COG3321  1093 AALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAA 1172

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  339 VLWDPDKGPVDIYDKRQIQPFGEYLPLRSLVGAINDEWTSMVRQDFSRGTEPGVFTMAGTGVGLVtcyEAAFDWAVRDTV 418
Cdd:COG3321  1173 LLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLA---LAAAAAAVAALA 1249

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  419 TEGARLISVPSNNATFGRSEMTHQQLAMSRVRAVEHSRTVTVPVTSGVSAIIMPDGKVSQRTGMFVADSLVQEVPLRSSL 498
Cdd:COG3321  1250 AAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAA 1329

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 754810822  499 TPATRLGVLPETVLVLVAAGGLGWAVATGVRGRVR 533
Cdd:COG3321  1330 LAALAAAVAAALALAAAAAAAAAAAAAAAAAAALA 1364
PRK13981 PRK13981
NAD synthetase; Provisional
 272-454 4.13e-04

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 42.84  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 272 TERLAAAVDAGEAERPDIVLWPENS------SDI--DPFANADARAVIDRAAQ--AIGAPVSVGAVVGKDGKLLNEQVLW 341
Cdd:PRK13981  19 AAKILAAAAEAADAGADLLLFPELFlsgyppEDLllRPAFLAACEAALERLAAatAGGPAVLVGHPWREGGKLYNAAALL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822 342 DpdKGPV-DIYDKRQIQPFGEYlplrslvgainDEwtsmvRQDFSRGTEPGVFTMAGTGVGLVTCYEAAFDWAVRDTVTE 420
Cdd:PRK13981  99 D--GGEVlATYRKQDLPNYGVF-----------DE-----KRYFAPGPEPGVVELKGVRIGVPICEDIWNPEPAETLAEA 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 754810822 421 GARLISVPsnNATFGRSEMTHQQLAMSRVRAVEH 454
Cdd:PRK13981 161 GAELLLVP--NASPYHRGKPDLREAVLRARVRET 192
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 96-534 2.24e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 41.01  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822   96 VEVGPGPWIALAVIEAVfvALVGAGAAAVSKLPGSPVWA------AALWTAG----------EAARARVPFSGFPWGKIA 159
Cdd:COG3321   795 LEVGPGPVLTGLVRQCL--AAAGDAVVLPSLRRGEDELAqlltalAQLWVAGvpvdwsalypGRGRRRVPLPTYPFQRED 872

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  160 FGQADGVFLPLAALGGTPVLGFAVVLCGFGLYEIVRVVLDARRTTTVRRVAAAVGALSVAAPLVAAVAARPLVSDTAEDG 239
Cdd:COG3321   873 AAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAA 952

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  240 TATVAVVQGNVPRLGLDFNTQRRAVLDYHARETERLAAAVDAGEAERPDIVLWPENSSDIDPFANADARAVIDRAAQAIG 319
Cdd:COG3321   953 AAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAA 1032

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  320 APVSVGAVVGKDGKLLNEQVLWDPDKGPVDIYDKRQIQPFGEYLPLRSLVGAindewtSMVRQDFSRGTEPGVFTMAGTG 399
Cdd:COG3321  1033 AALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAAL------ALAAALAAAALALALAALAAAL 1106

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754810822  400 VGLVTCYEAAFDWAVRDTVTEGARLISVPSNNATFGRSEMTHQQLAMSRVRAVEHSRTVTVPVTSGVSAIIMPDGKVSQR 479
Cdd:COG3321  1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALA 1186

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 754810822  480 TGMFVADSLVQEVPLRSSLTPATRLGVLPETVLVLVAAGGLGWAVATGVRGRVRR 534
Cdd:COG3321  1187 AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAA 1241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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