|
Name |
Accession |
Description |
Interval |
E-value |
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
12-475 |
7.13e-124 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 369.94 E-value: 7.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 12 PRGWWWGAIIGIALLYVSLmpwrGRQVRGSVGALLAVTHGLVLYLLSLPWIGE----------LVGTVPYAALSIWLsvy 81
Cdd:COG0815 1 PFGLWPLAFVALAPLLLLL----RGARSPRRAFLLGWLFGLGFFLAGLYWLYVslhvfgglpaWLAPLAVLLLAAYL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 82 AIFLGIFGAAVARWR-----YGFLVFPFVYLAVEVLRSSVpFGGFPWVKLAWGQIE-GPLANLAPWGGTSLITAATVLCA 155
Cdd:COG0815 74 ALFFALAAALARRLRrrgglLRPLAFAALWVLLEWLRGWL-FTGFPWLRLGYSQADfSPLAQLAPLGGVYGLSFLVVLVN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 156 CGLAGLLLRGGrvKVAAAAALILPLIVGLMAGRGIDSAETKVGETKVAAIQGNVPRSGLDFAGQRRAVLNNHVQETEKLA 235
Cdd:COG0815 153 ALLALALLRRR--RRLAALALALALLLAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKWDPEQRREILDRYLDLTRELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 236 rrEDDIDLVIWPENSSDIDPFRDGEAAQAISGAVDAIDAPVLVGTATRDEVGAR--NTMQVFTPGHGVGDHHYKKYLQPF 313
Cdd:COG0815 231 --DDGPDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRyyNSALLLDPDGGILGRYDKHHLVPF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 314 GETMPMRDFFAHFSDYVDLA-GDFKAGDGPGVVSMNSVAVGVATCYEVSFDNAFHESVKNGAQILTTPTNNATFGFSDMT 392
Cdd:COG0815 309 GEYVPLRDLLRPLIPFLDLPlGDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNITNDAWFGDSIGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 393 YQQLAMSRLRALETDRAVVVAATSGVSALVHPDGSVSQSTELFEPAALVESLPLKTGETFSVRYGSLMQWLMVIIGTVCA 472
Cdd:COG0815 389 YQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLLLLLALLLA 468
|
...
gi 2785973803 473 LIA 475
Cdd:COG0815 469 LLL 471
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
201-467 |
3.04e-93 |
|
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.
Pssm-ID: 143595 Cd Length: 270 Bit Score: 284.11 E-value: 3.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 201 KVAAIQGNVPRSGLDFAGQRRAVLNNHVQETEKLArrEDDIDLVIWPENSSDIDPFRDGEAAQAISGAVDAIDAPVLVGT 280
Cdd:cd07571 2 RVALVQGNIPQDEKWDPEQRQATLDRYLDLTRELA--DEKPDLVVWPETALPFDLQRDPDALARLARAARAVGAPLLTGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 281 ATRDEVGAR--NTMQVFTPGHGVGDHHYKKYLQPFGETMPMRDFFAHFSDYVDLA-GDFKAGDGPGVVSM-NSVAVGVAT 356
Cdd:cd07571 80 PRREPGGGRyyNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPmGDFSPGTGPQPLLLgGGVRVGPLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 357 CYEVSFDNAFHESVKNGAQILTTPTNNATFGFSDMTYQQLAMSRLRALETDRAVVVAATSGVSALVHPDGSVSQSTELFE 436
Cdd:cd07571 160 CYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVARLPLFE 239
|
250 260 270
....*....|....*....|....*....|.
gi 2785973803 437 PAALVESLPLKTGETFSVRYGSLMQWLMVII 467
Cdd:cd07571 240 AGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
51-428 |
1.82e-75 |
|
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: 242.65 E-value: 1.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 51 GLVLYLLSLPWIGELVGTVPYAALSIWLSV---YAIFLGIFGAAV------ARWRYGFLVFPFVYLAVEVLRSSVPFGgF 121
Cdd:TIGR00546 2 GFGFFLAGLFWLGIALSVNGFIAFVAGLLVvglPALLALFPGLAAyllrrlAPFRKVLLALPLLWTLAEWLRSFGFLG-F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 122 PWVKLAWGQIEGPLANLAPWGGTSLITAATVLCACGLAGLLLRGGRVKVAAAAALILPLIVGLMAGRGIDSAETKVGET- 200
Cdd:TIGR00546 81 PWGLIGYAQSSLPLIQIASIFGVWGLSFLVVFLNALLALVLLKKESFKKLLAIAVVVLLAALGFLLYELKSATPVPGPTl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 201 KVAAIQGNVPRSGLDFAGQRRAVLNNHVQETEKLARReddIDLVIWPENSSDIDPFR-DGEAAQAISGAVDAIDAPVLVG 279
Cdd:TIGR00546 161 NVALVQPNIPQDLKFDSEGLEAILEILTSLTKQAVEK---PDLVVWPETAFPFDLENsPQKLADRLKLLVLSKGIPILIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 280 TATRDEVGAR---NTMQVFTPGHGVGDHHYKKYLQPFGETMPMRDFFAHFSDYVDLA--GDFKAGDGPGVVSMNSVAVGV 354
Cdd:TIGR00546 238 APDAVPGGPYhyyNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSKLFFLLsqEDFSRGPGPQVLKLPGGKIAP 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2785973803 355 ATCYEVSFDNAFHESVKNGAQILTTPTNNATFGFSDMTYQQLAMSRLRALETDRAVVVAATSGVSALVHPDGSV 428
Cdd:TIGR00546 318 LICYESIFPDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFRAIENGRPLVRATNTGISAVIDPRGRT 391
|
|
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
2-480 |
4.35e-69 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 229.38 E-value: 4.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 2 SGALTFTAVEPRGWWWGAIIGIALLYvslmpWRGRQVRGSVGALLAVTHGLVLYLLSLPWIGelVGTVPYAALSIWLSV- 80
Cdd:PRK00302 15 AGALGTLAFAPFDLWPLALLSLAGLL-----WLLLGASPKQAALIGFLWGFGYFGSGLSWIY--VSIHTFGGMPAWLAPl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 81 --------YAIFLGIFGAAVARWR-----YGFLVFPFVYLAVEVLRSSVpFGGFPWVKLAWGQIE-GPLANLAPWGGTSL 146
Cdd:PRK00302 88 lvlllaayLALYPALFAALWRRLWpksglRRALALPALWVLTEWLRGWL-LTGFPWLALGYSQIPdGPLAQLAPIFGVYG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 147 ITAATVLCACGLAGLLLRGGRVKVAAAAALILPLIVGLMAGRGIDSAETKVGETKVAAIQGNVPRSgLDF-AGQRRAVLN 225
Cdd:PRK00302 167 LSFLVVLVNALLALALIKRRWRLALLALLLLLLAALGYGLRRLQWTTPAPEPALKVALVQGNIPQS-LKWdPAGLEATLQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 226 NHVQETEKLARredDIDLVIWPENSsdIDPFRDGEA---AQAISGAVDAIDAPVLVGTATRDEVGAR----NTMQVFTPG 298
Cdd:PRK00302 246 KYLDLSRPALG---PADLIIWPETA--IPFLLEDLPqafLKALDDLAREKGSALITGAPRAENKQGRydyyNSIYVLGPY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 299 HGVGdhHYKKY-LQPFGETMPMRDFFAHFSDYVDL-AGDFKAGDGPGVV-SMNSVAVGVATCYEVSFDNAFHESVKNGAQ 375
Cdd:PRK00302 321 GILN--RYDKHhLVPFGEYVPLESLLRPLAPFFNLpMGDFSRGPYVQPPlLAKGLKLAPLICYEIIFPEEVRANVRQGAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 376 ILTTPTNNATFGFSDMTYQQLAMSRLRALETDRAVVVAATSGVSALVHPDGSVSQSTELFEPAALVESLPLKTGETFSVR 455
Cdd:PRK00302 399 LLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDPLGRIIAQLPQFTEGVLDGTVPPTTGLTPYAR 478
|
490 500
....*....|....*....|....*
gi 2785973803 456 YGSLMQWLMVIIGTVCALIAVRTNR 480
Cdd:PRK00302 479 WGDWPLLLLALLLLLLALLLALRRR 503
|
|
| LNT_N |
pfam20154 |
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal ... |
3-156 |
1.22e-22 |
|
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: 94.23 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 3 GALTFTAVEPRGWWWGAIIGIALLYVSLmpwRGRQVRGSVgALLAVTHGLVLYLLSLPWIGELVGTVPYA------ALSI 76
Cdd:pfam20154 1 GLLLSLAFPPFGLWPLAWVALAPLLLAL---EARSSPRRA-FLLGFLFGLGFFGLGLYWLGVSLHTFGGAplplalLLLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 77 WLSVYAIFLGIFGAAVARW--RYGFLVFPFVYLAVEVLRSsVPFGGFPWVKLAWGQIEGP-LANLAPWGGTSLITAATVL 153
Cdd:pfam20154 77 LLALYLALFALAAWLLKRLwgLFRALLFAALWVGLEYLRG-WPFGGFPWGLLGYSQADGPpLIQLAPLGGVYGVSFLVVL 155
|
...
gi 2785973803 154 CAC 156
Cdd:pfam20154 156 VNA 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lnt |
COG0815 |
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
12-475 |
7.13e-124 |
|
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 369.94 E-value: 7.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 12 PRGWWWGAIIGIALLYVSLmpwrGRQVRGSVGALLAVTHGLVLYLLSLPWIGE----------LVGTVPYAALSIWLsvy 81
Cdd:COG0815 1 PFGLWPLAFVALAPLLLLL----RGARSPRRAFLLGWLFGLGFFLAGLYWLYVslhvfgglpaWLAPLAVLLLAAYL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 82 AIFLGIFGAAVARWR-----YGFLVFPFVYLAVEVLRSSVpFGGFPWVKLAWGQIE-GPLANLAPWGGTSLITAATVLCA 155
Cdd:COG0815 74 ALFFALAAALARRLRrrgglLRPLAFAALWVLLEWLRGWL-FTGFPWLRLGYSQADfSPLAQLAPLGGVYGLSFLVVLVN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 156 CGLAGLLLRGGrvKVAAAAALILPLIVGLMAGRGIDSAETKVGETKVAAIQGNVPRSGLDFAGQRRAVLNNHVQETEKLA 235
Cdd:COG0815 153 ALLALALLRRR--RRLAALALALALLLAALRLSPVPWTEPAGEPLRVALVQGNIPQDLKWDPEQRREILDRYLDLTRELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 236 rrEDDIDLVIWPENSSDIDPFRDGEAAQAISGAVDAIDAPVLVGTATRDEVGAR--NTMQVFTPGHGVGDHHYKKYLQPF 313
Cdd:COG0815 231 --DDGPDLVVWPETALPFLLDEDPDALARLAAAAREAGAPLLTGAPRRDGGGGRyyNSALLLDPDGGILGRYDKHHLVPF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 314 GETMPMRDFFAHFSDYVDLA-GDFKAGDGPGVVSMNSVAVGVATCYEVSFDNAFHESVKNGAQILTTPTNNATFGFSDMT 392
Cdd:COG0815 309 GEYVPLRDLLRPLIPFLDLPlGDFSPGTGPPVLDLGGVRVGPLICYESIFPELVRDAVRAGADLLVNITNDAWFGDSIGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 393 YQQLAMSRLRALETDRAVVVAATSGVSALVHPDGSVSQSTELFEPAALVESLPLKTGETFSVRYGSLMQWLMVIIGTVCA 472
Cdd:COG0815 389 YQHLAIARLRAIETGRPVVRATNTGISAVIDPDGRVLARLPLFTRGVLVAEVPLRTGLTPYARWGDWPALLLLLLALLLA 468
|
...
gi 2785973803 473 LIA 475
Cdd:COG0815 469 LLL 471
|
|
| ALP_N-acyl_transferase |
cd07571 |
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
201-467 |
3.04e-93 |
|
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.
Pssm-ID: 143595 Cd Length: 270 Bit Score: 284.11 E-value: 3.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 201 KVAAIQGNVPRSGLDFAGQRRAVLNNHVQETEKLArrEDDIDLVIWPENSSDIDPFRDGEAAQAISGAVDAIDAPVLVGT 280
Cdd:cd07571 2 RVALVQGNIPQDEKWDPEQRQATLDRYLDLTRELA--DEKPDLVVWPETALPFDLQRDPDALARLARAARAVGAPLLTGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 281 ATRDEVGAR--NTMQVFTPGHGVGDHHYKKYLQPFGETMPMRDFFAHFSDYVDLA-GDFKAGDGPGVVSM-NSVAVGVAT 356
Cdd:cd07571 80 PRREPGGGRyyNSALLLDPGGGILGRYDKHHLVPFGEYVPLRDLLRFLGLLFDLPmGDFSPGTGPQPLLLgGGVRVGPLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 357 CYEVSFDNAFHESVKNGAQILTTPTNNATFGFSDMTYQQLAMSRLRALETDRAVVVAATSGVSALVHPDGSVSQSTELFE 436
Cdd:cd07571 160 CYESIFPELVRDAVRQGADLLVNITNDAWFGDSAGPYQHLAMARLRAIETGRPLVRAANTGISAVIDPDGRIVARLPLFE 239
|
250 260 270
....*....|....*....|....*....|.
gi 2785973803 437 PAALVESLPLKTGETFSVRYGSLMQWLMVII 467
Cdd:cd07571 240 AGVLVAEVPLRTGLTPYVRWGDWPLLLLLLL 270
|
|
| lnt |
TIGR00546 |
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
51-428 |
1.82e-75 |
|
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: 242.65 E-value: 1.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 51 GLVLYLLSLPWIGELVGTVPYAALSIWLSV---YAIFLGIFGAAV------ARWRYGFLVFPFVYLAVEVLRSSVPFGgF 121
Cdd:TIGR00546 2 GFGFFLAGLFWLGIALSVNGFIAFVAGLLVvglPALLALFPGLAAyllrrlAPFRKVLLALPLLWTLAEWLRSFGFLG-F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 122 PWVKLAWGQIEGPLANLAPWGGTSLITAATVLCACGLAGLLLRGGRVKVAAAAALILPLIVGLMAGRGIDSAETKVGET- 200
Cdd:TIGR00546 81 PWGLIGYAQSSLPLIQIASIFGVWGLSFLVVFLNALLALVLLKKESFKKLLAIAVVVLLAALGFLLYELKSATPVPGPTl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 201 KVAAIQGNVPRSGLDFAGQRRAVLNNHVQETEKLARReddIDLVIWPENSSDIDPFR-DGEAAQAISGAVDAIDAPVLVG 279
Cdd:TIGR00546 161 NVALVQPNIPQDLKFDSEGLEAILEILTSLTKQAVEK---PDLVVWPETAFPFDLENsPQKLADRLKLLVLSKGIPILIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 280 TATRDEVGAR---NTMQVFTPGHGVGDHHYKKYLQPFGETMPMRDFFAHFSDYVDLA--GDFKAGDGPGVVSMNSVAVGV 354
Cdd:TIGR00546 238 APDAVPGGPYhyyNSAYLVDPGGEVVQRYDKVKLVPFGEYIPLGFLFKWLSKLFFLLsqEDFSRGPGPQVLKLPGGKIAP 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2785973803 355 ATCYEVSFDNAFHESVKNGAQILTTPTNNATFGFSDMTYQQLAMSRLRALETDRAVVVAATSGVSALVHPDGSV 428
Cdd:TIGR00546 318 LICYESIFPDLVRASARQGAELLVNLTNDAWFGDSSGPWQHFALARFRAIENGRPLVRATNTGISAVIDPRGRT 391
|
|
| lnt |
PRK00302 |
apolipoprotein N-acyltransferase; Reviewed |
2-480 |
4.35e-69 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 234721 [Multi-domain] Cd Length: 505 Bit Score: 229.38 E-value: 4.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 2 SGALTFTAVEPRGWWWGAIIGIALLYvslmpWRGRQVRGSVGALLAVTHGLVLYLLSLPWIGelVGTVPYAALSIWLSV- 80
Cdd:PRK00302 15 AGALGTLAFAPFDLWPLALLSLAGLL-----WLLLGASPKQAALIGFLWGFGYFGSGLSWIY--VSIHTFGGMPAWLAPl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 81 --------YAIFLGIFGAAVARWR-----YGFLVFPFVYLAVEVLRSSVpFGGFPWVKLAWGQIE-GPLANLAPWGGTSL 146
Cdd:PRK00302 88 lvlllaayLALYPALFAALWRRLWpksglRRALALPALWVLTEWLRGWL-LTGFPWLALGYSQIPdGPLAQLAPIFGVYG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 147 ITAATVLCACGLAGLLLRGGRVKVAAAAALILPLIVGLMAGRGIDSAETKVGETKVAAIQGNVPRSgLDF-AGQRRAVLN 225
Cdd:PRK00302 167 LSFLVVLVNALLALALIKRRWRLALLALLLLLLAALGYGLRRLQWTTPAPEPALKVALVQGNIPQS-LKWdPAGLEATLQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 226 NHVQETEKLARredDIDLVIWPENSsdIDPFRDGEA---AQAISGAVDAIDAPVLVGTATRDEVGAR----NTMQVFTPG 298
Cdd:PRK00302 246 KYLDLSRPALG---PADLIIWPETA--IPFLLEDLPqafLKALDDLAREKGSALITGAPRAENKQGRydyyNSIYVLGPY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 299 HGVGdhHYKKY-LQPFGETMPMRDFFAHFSDYVDL-AGDFKAGDGPGVV-SMNSVAVGVATCYEVSFDNAFHESVKNGAQ 375
Cdd:PRK00302 321 GILN--RYDKHhLVPFGEYVPLESLLRPLAPFFNLpMGDFSRGPYVQPPlLAKGLKLAPLICYEIIFPEEVRANVRQGAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 376 ILTTPTNNATFGFSDMTYQQLAMSRLRALETDRAVVVAATSGVSALVHPDGSVSQSTELFEPAALVESLPLKTGETFSVR 455
Cdd:PRK00302 399 LLLNISNDAWFGDSIGPYQHFQMARMRALELGRPLIRATNTGITAVIDPLGRIIAQLPQFTEGVLDGTVPPTTGLTPYAR 478
|
490 500
....*....|....*....|....*
gi 2785973803 456 YGSLMQWLMVIIGTVCALIAVRTNR 480
Cdd:PRK00302 479 WGDWPLLLLALLLLLLALLLALRRR 503
|
|
| LNT_N |
pfam20154 |
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal ... |
3-156 |
1.22e-22 |
|
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: 94.23 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 3 GALTFTAVEPRGWWWGAIIGIALLYVSLmpwRGRQVRGSVgALLAVTHGLVLYLLSLPWIGELVGTVPYA------ALSI 76
Cdd:pfam20154 1 GLLLSLAFPPFGLWPLAWVALAPLLLAL---EARSSPRRA-FLLGFLFGLGFFGLGLYWLGVSLHTFGGAplplalLLLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 77 WLSVYAIFLGIFGAAVARW--RYGFLVFPFVYLAVEVLRSsVPFGGFPWVKLAWGQIEGP-LANLAPWGGTSLITAATVL 153
Cdd:pfam20154 77 LLALYLALFALAAWLLKRLwgLFRALLFAALWVGLEYLRG-WPFGGFPWGLLGYSQADGPpLIQLAPLGGVYGVSFLVVL 155
|
...
gi 2785973803 154 CAC 156
Cdd:pfam20154 156 VNA 158
|
|
| CN_hydrolase |
pfam00795 |
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
201-428 |
1.22e-14 |
|
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: 73.93 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 201 KVAAIQGNVPrsGLDFAGQRRAVLNnHVQEteklARREDdIDLVIWPENSS----------DIDPFRDGEAAQAISGAVD 270
Cdd:pfam00795 1 RVALVQLPQG--FWDLEANLQKALE-LIEE----AARYG-ADLIVLPELFItgypcwahflEAAEVGDGETLAGLAALAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 271 AIDAPVLVGTATRDEVGAR--NTMQVFTPGHGVGDHHYKKYLqpFGETMPMRDFFAHFsdyvdlagdFKAGDGPGVVSMN 348
Cdd:pfam00795 73 KNGIAIVIGLIERWLTGGRlyNTAVLLDPDGKLVGKYRKLHL--FPEPRPPGFRERVL---------FEPGDGGTVFDTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 349 SVAVGVATCYEVSFDNAFHESVKNGAQILTTPTNNATFGFSDMTYQQLAMSRLRALETDRAVVVAATSGV---------- 418
Cdd:pfam00795 142 LGKIGAAICYEIRFPELLRALALKGAEILINPSARAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGeedapwpygh 221
|
250
....*....|
gi 2785973803 419 SALVHPDGSV 428
Cdd:pfam00795 222 SMIIDPDGRI 231
|
|
| Nit2 |
COG0388 |
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
201-428 |
1.23e-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: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 201 KVAAIQGNVprSGLDFAGqrravlnNhVQETEKLARR--EDDIDLVIWPENSS-----------DIDPFRDGEAAQAISG 267
Cdd:COG0388 3 RIALAQLNP--TVGDIEA-------N-LAKIEELIREaaAQGADLVVFPELFLtgyppedddllELAEPLDGPALAALAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 268 AVDAIDAPVLVGTATRDEVGA-RNTMQVFTPGHGVGDHHYKKYL---QPFGEtmpmrdffahfSDYvdlagdFKAGDGPG 343
Cdd:COG0388 73 LARELGIAVVVGLPERDEGGRlYNTALVIDPDGEILGRYRKIHLpnyGVFDE-----------KRY------FTPGDELV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 344 VVSMNSVAVGVATCYEVSFDNAFHESVKNGAQILTTPTNnatFGFSDMTYQQLAMSRLRALETDRAVVVAATSGV----- 418
Cdd:COG0388 136 VFDTDGGRIGVLICYDLWFPELARALALAGADLLLVPSA---SPFGRGKDHWELLLRARAIENGCYVVAANQVGGedglv 212
|
250
....*....|....
gi 2785973803 419 ----SALVHPDGSV 428
Cdd:COG0388 213 fdggSMIVDPDGEV 226
|
|
| nitrilase |
cd07197 |
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
202-428 |
2.01e-12 |
|
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: 66.96 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 202 VAAIQGNVPrsgldfAGQRRAVLNNHVQETEKLArrEDDIDLVIWPE-------NSSDIDPFR-----DGEAAQAISGAV 269
Cdd:cd07197 1 IAAVQLAPK------IGDVEANLAKALRLIKEAA--EQGADLIVLPElfltgysFESAKEDLDlaeelDGPTLEALAELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 270 DAIDAPVLVGTATRDEVGARNTMQVFTP-GHGVGDHHyKKYLQPFGETMPmrdffahfsdyvdlagdFKAGDGPGVVSMN 348
Cdd:cd07197 73 KELGIYIVAGIAEKDGDKLYNTAVVIDPdGEIIGKYR-KIHLFDFGERRY-----------------FSPGDEFPVFDTP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 349 SVAVGVATCYEVSFDNAFHESVKNGAQILTTPTNNATFGFsdmtYQQLAMSRLRALETDRAVVVAATSGV---------S 419
Cdd:cd07197 135 GGKIGLLICYDLRFPELARELALKGADIILVPAAWPTARR----EHWELLLRARAIENGVYVVAANRVGEegglefaggS 210
|
....*....
gi 2785973803 420 ALVHPDGSV 428
Cdd:cd07197 211 MIVDPDGEV 219
|
|
| nitrilase_3 |
cd07581 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
232-428 |
1.86e-08 |
|
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143605 Cd Length: 255 Bit Score: 55.27 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 232 EKLARR--EDDIDLVIWPENSS-----DIDPFR------DGEAAQAISGAVDAIDAPVLVGTATRDEVG-ARNTMqVFTP 297
Cdd:cd07581 20 RRLLAEaaAAGADLVVFPEYTMarfgdGLDDYArvaeplDGPFVSALARLARELGITVVAGMFEPAGDGrVYNTL-VVVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 298 GHGVGDHHYKKylqpfgetMPMRDFFAHF-SDYVdLAGDfkaGDGPGVVSMNSVAVGVATCYEVSFDNAFHESVKNGAQI 376
Cdd:cd07581 99 PDGEIIAVYRK--------IHLYDAFGFReSDTV-APGD---ELPPVVFVVGGVKVGLATCYDLRFPELARALALAGADV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2785973803 377 LTTPTnnATFGFSDMTYQQLAMSRLRALETDRAVVVAAT-----SGVSALVHPDGSV 428
Cdd:cd07581 167 IVVPA--AWVAGPGKEEHWETLLRARALENTVYVAAAGQagprgIGRSMVVDPLGVV 221
|
|
| PRK12291 |
PRK12291 |
apolipoprotein N-acyltransferase; Reviewed |
307-398 |
2.15e-06 |
|
apolipoprotein N-acyltransferase; Reviewed
Pssm-ID: 237042 [Multi-domain] Cd Length: 418 Bit Score: 49.98 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 307 KKYLQPFGETMPMRDFFAHFSD--YVDLAGDFKAGDGPGVVSMNSVAVGVATCYEVSFDNAFHESVKNgaqILTTpTNNA 384
Cdd:PRK12291 296 KVILVPFGEEIPLPKFFKKPINklFFGGASDFSKASKFSDFTLDGVKFRNAICYEATSEELYEGNPKI---VIAI-SNNA 371
|
90
....*....|....*
gi 2785973803 385 TFGFSDM-TYQQLAM 398
Cdd:PRK12291 372 WFVPSIEpTLQKLLL 386
|
|
| nitrilase_7 |
cd07585 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
228-448 |
1.17e-05 |
|
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
Pssm-ID: 143609 Cd Length: 261 Bit Score: 46.93 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 228 VQETEKLARR--EDDIDLVIWPE----------NSSDIDPFRDGEAAQAISGAVDAIDAPVLVGTATRDEVGARNTMQVF 295
Cdd:cd07585 18 LAVIARWTRKaaAQGAELVCFPEmcitgythvrALSREAEVPDGPSTQALSDLARRYGLTILAGLIEKAGDRPYNTYLVC 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 296 TPGHGVgdHHYKKyLQPFGETMPmrdffaHFSdyvdlagdfkAGDGPGVVSMNSVAVGVATCYevsfDNAFHESVKN--- 372
Cdd:cd07585 98 LPDGLV--HRYRK-LHLFRREHP------YIA----------AGDEYPVFATPGVRFGILICY----DNHFPENVRAtal 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 373 -GAQILTTPtnNATFGFSDMTYQQLAMSRLRALETDRAVVVAAT-----------SGVSALVHPDGSVSQSTELFEPAAL 440
Cdd:cd07585 155 lGAEILFAP--HATPGTTSPKGREWWMRWLPARAYDNGVFVAACngvgrdggevfPGGAMILDPYGRVLAETTSGGDGMV 232
|
....*...
gi 2785973803 441 VESLPLKT 448
Cdd:cd07585 233 VADLDLDL 240
|
|
| nitrilase_5 |
cd07583 |
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
201-382 |
1.62e-04 |
|
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: 43.30 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 201 KVAAIQGNVPrsgldfAGQRRAVLNNHVQETEKLArrEDDIDLVIWPE---------NSSDIDPFRDGEAAQAISGAVDA 271
Cdd:cd07583 1 KIALIQLDIV------WGDPEANIERVESLIEEAA--AAGADLIVLPEmwntgyfldDLYELADEDGGETVSFLSELAKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 272 IDAPVLVGT-ATRDEVGARNTMQVFTPGhGVGDHHYKKyLQPFGetmpmrdfFAHFSDYvdlagdFKAGDGPGVVSMNSV 350
Cdd:cd07583 73 HGVNIVAGSvAEKEGGKLYNTAYVIDPD-GELIATYRK-IHLFG--------LMGEDKY------LTAGDELEVFELDGG 136
|
170 180 190
....*....|....*....|....*....|..
gi 2785973803 351 AVGVATCYEVSFDNAFHESVKNGAQILTTPTN 382
Cdd:cd07583 137 KVGLFICYDLRFPELFRKLALEGAEILFVPAE 168
|
|
| nitrilase_Rim1_like |
cd07574 |
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ... |
289-431 |
2.98e-04 |
|
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: 42.57 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 289 RNTMQVFTPGhGVGDHHYKKYLQPFgetmpMRDffahfsdyvdlAGDFKAGDGPGVVSMNSVAVGVATCYEVSFDNAFHE 368
Cdd:cd07574 102 YNRAYLFGPD-GTIGHQDKLHMTPF-----ERE-----------EWGISGGDKLKVFDTDLGKIGILICYDSEFPELARA 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2785973803 369 SVKNGAQILTTPTNNAT-FGFSDMTYQQLAmsrlRALETDRAVVVAATSGVSALVHP-DGSVSQS 431
Cdd:cd07574 165 LAEAGADLLLVPSCTDTrAGYWRVRIGAQA----RALENQCYVVQSGTVGNAPWSPAvDVNYGQA 225
|
|
| Exosortase_EpsH |
pfam09721 |
Transmembrane exosortase (Exosortase_EpsH); Members of this family are designated exosortase, ... |
13-128 |
5.87e-03 |
|
Transmembrane exosortase (Exosortase_EpsH); Members of this family are designated exosortase, analogous to sortase in cell wall sorting mediated by LPXTG domains in Gram-positive bacteria. The phylogenetic distribution of the proteins in this entry is nearly perfectly correlated with the distribution of the proteins having the PEP-CTERM anchor motif, IPR013424. Members of this entry are integral membrane proteins with eight predicted transmembrane helices in common. Some members of this family have long trailing sequences past the region described by this model. This model does not include the region of the first predicted transmembrane region. The best characterized member is EpsH of Methylobacillus sp. 12S, where it is part of a locus associated with biosynthesis of the exopolysaccharide methanol-an.
Pssm-ID: 430773 Cd Length: 250 Bit Score: 38.43 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973803 13 RGWW------WGAIIGIALLYVSLMPWRGRQVRGSVGALLAVthgLVLYLLSLPW-IGELVGTVPYAALSIWLSVYAIFL 85
Cdd:pfam09721 11 DIWLasedysHGLLVPPLALYLVWRRWRRAALPPRPSWLGLL---LLLAGLGLLWlLGRLAGVLLLAQLSLVLLLAGLVL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2785973803 86 GIFGAAVARWrygfLVFPFVYLAVevlrsSVPFGGFPWVKLAW 128
Cdd:pfam09721 88 LLLGWRALRA----LWFPLLLLLF-----AVPLPDFLITALTL 121
|
|
| |
