|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
1-558 |
0e+00 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 1170.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 1 MTYIKAMTQQKLSFLLAIYIGLFMNCAVFYRRFDGYAQAFTVLKGISAVVELIGTVLVTFFLLRLLSLLGRRVWRVLASL 80
Cdd:PRK11560 1 MRYIKSLTQQKLSFLLAVYIGLFLNIAVFYRRFDSYAQDFTVWKGLSAVVELAATVLVTFFLLRLLSLFGRRFWRVLASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 81 VVIFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVVGWQLIAWVVLVSALPLLSIWSNRCRDTLLRQLSTPGARIRS 160
Cdd:PRK11560 81 LVLFSAAASYYMTFFNVVIGYGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWNNRCRYTLLRQLRTPGQRIRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 161 VSIVLLAGLMVWGPIRLLDLQQKNAERTSGVDMPSYGGVVANSYLPSNWLSALGLYAWAQVDESSDYKSLINPAKKFTYV 240
Cdd:PRK11560 161 LAVVVLAGLLVWAPIRLLDIQQKKVERATGVDLPSYGGVVANSYLPSNWLSALGLYAWAQVDESSDNNSLLNPAKKFTYQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 241 APKDIDDTMVVFIIGETTRWDHMGMLGYSRDTTPKLAQEKNLVAFRGYSCDTATKLSLRCMFVREGGADDNPQRTLKEQN 320
Cdd:PRK11560 241 APKGVDDTYVVFIIGETTRWDHMGILGYERNTTPKLAQEKNLAAFRGYSCDTATKLSLRCMFVREGGAEDNPQRTLKEQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 321 VFAVLKQLGFSSDLYAMQSEMWFYSNTMADNIAYREQIGAEPRNRGKNVDDMLLINELQASLDKGTRGKRLIIMHTKGSH 400
Cdd:PRK11560 321 VFAVLKQLGFSSELFAMQSEMWFYNNTMADNYAYREQIGAEPRNRGKPVDDMLLVDEMKQSLGRNPDGKHLIILHTKGSH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 401 FNYTQRYPRDFAKWTPECVSVDDKCSKEELINSFDNSVTYVDHFIDTVIDKVRDRKAIVFYAADHGESINEKEHLHGTPR 480
Cdd:PRK11560 401 YNYTQRYPRSFARYQPECIGVDSGCSKAQLINSYDNSVLYVDHFISSVIDQLRDKKAIVFYAADHGESINEREHLHGTPR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291418 481 KMAPPEQFRVPMMVWMSDKYLQDPQKAQMFAQLKQQAAFKTPRRHVELYDTIMGCLGYTSPNGGINENNNWCHLPSQT 558
Cdd:PRK11560 481 EMAPPEQFRVPMMVWMSDKYLANPDNAQAFAQLKKQADMKVPRRHVELFDTILGCLGYTSPDGGINENNNWCHIPDAK 558
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
5-553 |
0e+00 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 572.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 5 KAMTQQKLSFLLAIYIGLFMNCAVFYRRFDGYAQAFtvlKGISAVVELIGTVLVTFFLLRLLSLLGRrVWRVLASLVVIF 84
Cdd:COG2194 5 PRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDG---VNLLFLLSLPLLLLAALNLLLSLLAWRY-LFKPLLILLLLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 85 SAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVVGWQLIAWVVLVSALPLLSIWSNRCRDT-LLRQLstpGARIRSVSI 163
Cdd:COG2194 81 SAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRpLLREL---GQRLALLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 164 VLL-AGLMVWGPIRLLDLQQKNAErtsgvdmpsyggVVANSYLPSNWLSALGLYAWAQVDESS-DYKSLINPAKKftyvA 241
Cdd:COG2194 158 ALLvIVLLALLFYKDYASFFRNHK------------ELRYLINPSNFIYALGKYAKARYFAAPlPLQPLGADAKL----A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 242 PKDIDDTMVVFIIGETTRWDHMGMLGYSRDTTPKLAQEKNLVAFR-GYSCDTATKLSLRCMFVREGGADDNPQRTLKEQN 320
Cdd:COG2194 222 AAGAKPTLVVLVVGETARADNFSLNGYARDTTPELAKEKNLVSFRdVTSCGTATAVSVPCMFSRLGRADYDPQRALNQEN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 321 VFAVLKQLGFSSDLYAMQSEM-WFYSN-----TMADNiayreqigAEPRNRGKNVDDMLLINELQASLDKgTRGKRLIIM 394
Cdd:COG2194 302 LLDVLQRAGVKVLWRDNQSGCkGVCDRvptidLTADN--------LPPLCDGGECLDEVLLDGLDEALAD-LAGDKLIVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 395 HTKGSH-FNYTQRYPRDFAKWTPEC-VSVDDKCSKEELINSFDNSVTYVDHFIDTVIDKVRDR----KAIVFYAADHGES 468
Cdd:COG2194 373 HQMGSHgPAYYKRYPPEFRKFTPTCdTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKqdryDTAMLYVSDHGES 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 469 INEKE-HLHGTPRKMAPPEQFRVPMMVWMSDKYLQDpqKAQMFAQLKQQAafKTPRRHVELYDTIMGCLGYTSPngGINE 547
Cdd:COG2194 453 LGENGlYLHGTPYAIAPDEQTHVPMIMWLSDGYAQR--YGIDFACLKARA--DKPYSHDNLFHTLLGLLDVRTS--VYDP 526
|
....*.
gi 521291418 548 NNNWCH 553
Cdd:COG2194 527 ELDILA 532
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
250-539 |
3.48e-95 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 291.83 E-value: 3.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 250 VVFIIGETTRWDHMGMLGYSRDTTPKLAQEK-NLVAFRG-YSCDTATKLSLRCMFVREGGadDNPQRTLKEQNVFAVLKQ 327
Cdd:cd16017 5 VVLVIGESARRDHMSLYGYPRDTTPFLSKLKkNLIVFDNvISCGTSTAVSLPCMLSFANR--ENYDRAYYQENLIDLAKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 328 LGFSSDLYAMQSEMWFYSNTMADNIAYREQIGAEPRNRGKNVDDMLLINELQASLDKGTrGKRLIIMHTKGSHFNYTQRY 407
Cdd:cd16017 83 AGYKTYWISNQGGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEALADSS-KKKLIVLHLMGSHGPYYDRY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 408 PRDFAKWTPECVSVDDKCSKEELINSFDNSVTYVDHFIDTVIDKVR--DRKAIVFYAADHGESINEKEH-LHGTPRkmAP 484
Cdd:cd16017 162 PEEFAKFTPDCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKkkDKDAALIYFSDHGESLGENGLyLHGAPY--AP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 521291418 485 PEQFRVPMMVWMSDKYLQDPQKAQmfaqlkQQAAFKTPRRHVELYDTIMGCLGYT 539
Cdd:cd16017 240 KEQYHVPFIIWSSDSYKQRYPVER------LRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
250-538 |
3.21e-57 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 193.41 E-value: 3.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 250 VVFIIGETTRWDHMGMLGYSRDTTPKLAQE-KNLVAF-RGYSCDTATKLSLRCMFVREGGADDN------PQRTLKEQNV 321
Cdd:pfam00884 3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRLaEEGLLFsNFYSGGTLTAPSRFALLTGLPPHNFGsyvstpVGLPRTEPSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 322 FAVLKQLGFSSDLYAMQSEMWFYSNT--------MADNIAYREQIGAEPRN----RGKNVDDMLLINELQASLDKGTRgK 389
Cdd:pfam00884 83 PDLLKRAGYNTGAIGKWHLGWYNNQSpcnlgfdkFFGRNTGSDLYADPPDVpyncSGGGVSDEALLDEALEFLDNNDK-P 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 390 RLIIMHTKGSH--FNYTQRYPRDFAKWTPEcvsvddKCSKEELINSFDNSVTYVDHFIDTVIDKVR----DRKAIVFYAA 463
Cdd:pfam00884 162 FFLVLHTLGSHgpPYYPDRYPEKYATFKPS------SCSEEQLLNSYDNTLLYTDDAIGRVLDKLEenglLDNTLVVYTS 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291418 464 DHGESINEKEH-LHGTPRKMAPPEQFRVPMMVWMSDKYlqdpqkaqmfaqlKQQAAFKTPRRHVELYDTIMGCLGY 538
Cdd:pfam00884 236 DHGESLGEGGGyLHGGKYDNAPEGGYRVPLLIWSPGGK-------------AKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
1-558 |
0e+00 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 1170.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 1 MTYIKAMTQQKLSFLLAIYIGLFMNCAVFYRRFDGYAQAFTVLKGISAVVELIGTVLVTFFLLRLLSLLGRRVWRVLASL 80
Cdd:PRK11560 1 MRYIKSLTQQKLSFLLAVYIGLFLNIAVFYRRFDSYAQDFTVWKGLSAVVELAATVLVTFFLLRLLSLFGRRFWRVLASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 81 VVIFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVVGWQLIAWVVLVSALPLLSIWSNRCRDTLLRQLSTPGARIRS 160
Cdd:PRK11560 81 LVLFSAAASYYMTFFNVVIGYGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWNNRCRYTLLRQLRTPGQRIRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 161 VSIVLLAGLMVWGPIRLLDLQQKNAERTSGVDMPSYGGVVANSYLPSNWLSALGLYAWAQVDESSDYKSLINPAKKFTYV 240
Cdd:PRK11560 161 LAVVVLAGLLVWAPIRLLDIQQKKVERATGVDLPSYGGVVANSYLPSNWLSALGLYAWAQVDESSDNNSLLNPAKKFTYQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 241 APKDIDDTMVVFIIGETTRWDHMGMLGYSRDTTPKLAQEKNLVAFRGYSCDTATKLSLRCMFVREGGADDNPQRTLKEQN 320
Cdd:PRK11560 241 APKGVDDTYVVFIIGETTRWDHMGILGYERNTTPKLAQEKNLAAFRGYSCDTATKLSLRCMFVREGGAEDNPQRTLKEQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 321 VFAVLKQLGFSSDLYAMQSEMWFYSNTMADNIAYREQIGAEPRNRGKNVDDMLLINELQASLDKGTRGKRLIIMHTKGSH 400
Cdd:PRK11560 321 VFAVLKQLGFSSELFAMQSEMWFYNNTMADNYAYREQIGAEPRNRGKPVDDMLLVDEMKQSLGRNPDGKHLIILHTKGSH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 401 FNYTQRYPRDFAKWTPECVSVDDKCSKEELINSFDNSVTYVDHFIDTVIDKVRDRKAIVFYAADHGESINEKEHLHGTPR 480
Cdd:PRK11560 401 YNYTQRYPRSFARYQPECIGVDSGCSKAQLINSYDNSVLYVDHFISSVIDQLRDKKAIVFYAADHGESINEREHLHGTPR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291418 481 KMAPPEQFRVPMMVWMSDKYLQDPQKAQMFAQLKQQAAFKTPRRHVELYDTIMGCLGYTSPNGGINENNNWCHLPSQT 558
Cdd:PRK11560 481 EMAPPEQFRVPMMVWMSDKYLANPDNAQAFAQLKKQADMKVPRRHVELFDTILGCLGYTSPDGGINENNNWCHIPDAK 558
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
5-553 |
0e+00 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 572.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 5 KAMTQQKLSFLLAIYIGLFMNCAVFYRRFDGYAQAFtvlKGISAVVELIGTVLVTFFLLRLLSLLGRrVWRVLASLVVIF 84
Cdd:COG2194 5 PRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDG---VNLLFLLSLPLLLLAALNLLLSLLAWRY-LFKPLLILLLLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 85 SAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVVGWQLIAWVVLVSALPLLSIWSNRCRDT-LLRQLstpGARIRSVSI 163
Cdd:COG2194 81 SAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRpLLREL---GQRLALLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 164 VLL-AGLMVWGPIRLLDLQQKNAErtsgvdmpsyggVVANSYLPSNWLSALGLYAWAQVDESS-DYKSLINPAKKftyvA 241
Cdd:COG2194 158 ALLvIVLLALLFYKDYASFFRNHK------------ELRYLINPSNFIYALGKYAKARYFAAPlPLQPLGADAKL----A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 242 PKDIDDTMVVFIIGETTRWDHMGMLGYSRDTTPKLAQEKNLVAFR-GYSCDTATKLSLRCMFVREGGADDNPQRTLKEQN 320
Cdd:COG2194 222 AAGAKPTLVVLVVGETARADNFSLNGYARDTTPELAKEKNLVSFRdVTSCGTATAVSVPCMFSRLGRADYDPQRALNQEN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 321 VFAVLKQLGFSSDLYAMQSEM-WFYSN-----TMADNiayreqigAEPRNRGKNVDDMLLINELQASLDKgTRGKRLIIM 394
Cdd:COG2194 302 LLDVLQRAGVKVLWRDNQSGCkGVCDRvptidLTADN--------LPPLCDGGECLDEVLLDGLDEALAD-LAGDKLIVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 395 HTKGSH-FNYTQRYPRDFAKWTPEC-VSVDDKCSKEELINSFDNSVTYVDHFIDTVIDKVRDR----KAIVFYAADHGES 468
Cdd:COG2194 373 HQMGSHgPAYYKRYPPEFRKFTPTCdTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKqdryDTAMLYVSDHGES 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 469 INEKE-HLHGTPRKMAPPEQFRVPMMVWMSDKYLQDpqKAQMFAQLKQQAafKTPRRHVELYDTIMGCLGYTSPngGINE 547
Cdd:COG2194 453 LGENGlYLHGTPYAIAPDEQTHVPMIMWLSDGYAQR--YGIDFACLKARA--DKPYSHDNLFHTLLGLLDVRTS--VYDP 526
|
....*.
gi 521291418 548 NNNWCH 553
Cdd:COG2194 527 ELDILA 532
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
250-539 |
3.48e-95 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 291.83 E-value: 3.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 250 VVFIIGETTRWDHMGMLGYSRDTTPKLAQEK-NLVAFRG-YSCDTATKLSLRCMFVREGGadDNPQRTLKEQNVFAVLKQ 327
Cdd:cd16017 5 VVLVIGESARRDHMSLYGYPRDTTPFLSKLKkNLIVFDNvISCGTSTAVSLPCMLSFANR--ENYDRAYYQENLIDLAKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 328 LGFSSDLYAMQSEMWFYSNTMADNIAYREQIGAEPRNRGKNVDDMLLINELQASLDKGTrGKRLIIMHTKGSHFNYTQRY 407
Cdd:cd16017 83 AGYKTYWISNQGGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDEALADSS-KKKLIVLHLMGSHGPYYDRY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 408 PRDFAKWTPECVSVDDKCSKEELINSFDNSVTYVDHFIDTVIDKVR--DRKAIVFYAADHGESINEKEH-LHGTPRkmAP 484
Cdd:cd16017 162 PEEFAKFTPDCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKkkDKDAALIYFSDHGESLGENGLyLHGAPY--AP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 521291418 485 PEQFRVPMMVWMSDKYLQDPQKAQmfaqlkQQAAFKTPRRHVELYDTIMGCLGYT 539
Cdd:cd16017 240 KEQYHVPFIIWSSDSYKQRYPVER------LRANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
250-538 |
3.21e-57 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 193.41 E-value: 3.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 250 VVFIIGETTRWDHMGMLGYSRDTTPKLAQE-KNLVAF-RGYSCDTATKLSLRCMFVREGGADDN------PQRTLKEQNV 321
Cdd:pfam00884 3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRLaEEGLLFsNFYSGGTLTAPSRFALLTGLPPHNFGsyvstpVGLPRTEPSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 322 FAVLKQLGFSSDLYAMQSEMWFYSNT--------MADNIAYREQIGAEPRN----RGKNVDDMLLINELQASLDKGTRgK 389
Cdd:pfam00884 83 PDLLKRAGYNTGAIGKWHLGWYNNQSpcnlgfdkFFGRNTGSDLYADPPDVpyncSGGGVSDEALLDEALEFLDNNDK-P 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 390 RLIIMHTKGSH--FNYTQRYPRDFAKWTPEcvsvddKCSKEELINSFDNSVTYVDHFIDTVIDKVR----DRKAIVFYAA 463
Cdd:pfam00884 162 FFLVLHTLGSHgpPYYPDRYPEKYATFKPS------SCSEEQLLNSYDNTLLYTDDAIGRVLDKLEenglLDNTLVVYTS 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291418 464 DHGESINEKEH-LHGTPRKMAPPEQFRVPMMVWMSDKYlqdpqkaqmfaqlKQQAAFKTPRRHVELYDTIMGCLGY 538
Cdd:pfam00884 236 DHGESLGEGGGyLHGGKYDNAPEGGYRVPLLIWSPGGK-------------AKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
1-550 |
3.57e-54 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 191.53 E-value: 3.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 1 MTYIKAMTQQKLSFLLAIYIGLFMNCAVFyrrfdgyAQAFTVLKGISAVVELIGT-VLVTFFLLRLLSLLGRRVWRVLAS 79
Cdd:PRK09598 7 LKFLKPLSCLQAGLLYSLLNGVLYHFPLF-------AYVYKESNQVSFIAMLVVLlFCVNGLLFLLLGLLSRRLMRLSAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 80 LVVIFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVVGWQLIAWVVLVSALPLLSIWSNRCRDTLLRQlstPGARIR 159
Cdd:PRK09598 80 VFSLLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSSKKA---PFAAIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 160 SVSIVLLAGLM------VWgpirlLDlqqKNAERTSGVDMP-SYggvVANSYLPSNwlsalgLYAWAQVdessdYKSLIN 232
Cdd:PRK09598 157 ALVLIFLASAFansknwLW-----FD---KHAKFLGGLILPwSY---SVNTFRVSA------HKFFAPT-----IKPLLP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 233 PAKkftyvaPKDIDDTMVVFIIGETTRWDHMGMLGYSRDTTPKLAQEKN---LVAFRGYSCDTATKLSLRCM----FVRE 305
Cdd:PRK09598 215 PLF------SPNHSKSVVVLVIGESARKHNYALYGYEKPTNPRLSKRLAtheLTLFNATSCATYTTASLECIldssFKNT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 306 GGADDNPQRTLKEQNVFAVlkqlgfssdlyamqsemWFYSNTMADNIAY-----REQIGAEPRNRGKNVDDMLLIN---E 377
Cdd:PRK09598 289 SNAYENLPTYLTRAGIKVF-----------------WRSANDGEPNVKVtsylkNYELIQKCPNCEAPYDESLLYNlpeL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 378 LQASldkgTRGKRLIIMHTKGSHF-NYTQRYPRDFAKWTPECVSVD-DKCSKEELINSFDNSVTYVDHFIDTVIDKVRDR 455
Cdd:PRK09598 352 IKAS----SNENVLLILHLAGSHGpNYDNKYPLNFRVFKPVCSSVElSSCSKESLINAYDNTIFYNDYLLDKIISMLKNL 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 456 K--AIVFYAADHGESINEKE-HLHGTPRKMAPPEQFRVPMMVWMSDKYLQDPQKAQMFAQLKQQAAFktprrHvelydTI 532
Cdd:PRK09598 428 KqpALMIYLSDHGESLGEGAfYLHGIPKSIAPKEQYEIPFIVWASDSFKKQHSIIQTQTPINQNVIF-----H-----SV 497
|
570
....*....|....*...
gi 521291418 533 MGCLGYTSPNGGINENNN 550
Cdd:PRK09598 498 LGVFDFKNPSAVYRPSLD 515
|
|
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
1-537 |
9.30e-51 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 182.95 E-value: 9.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 1 MTYIKAMTQQKLSFLL--AIYIGLFMNCAvFYRR---------FDGYAQAFTVLKGISAVVELIGTVLVTFFLLrllsll 69
Cdd:PRK11598 2 KRLLKRPSLNLLTFLLlaAFYITLCLNIA-FYKQvlqllpldsLHNVLVFASMPVVAFSVINIVFTLLSFPWLR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 70 grrvwRVLASLVVIFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVVGWQLIAWVVLVSALPLLSIWSNRCRDTLLR 149
Cdd:PRK11598 75 -----RPLACLFILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 150 QLSTpGARIRSVSIVLLAGLMVwGPIRLLD---LQQKNAERTSGVDmPSYGGVVANSYLPSNWLSALGLyawAQVDESSD 226
Cdd:PRK11598 150 WRSV-LFRLANILVSVLLILLV-AALFYKDyasLFRNNKELVKSLT-PSNSIVASWSWYSHQRLANLPL---VRIGEDAH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 227 YKSLINPAKKftyvapkdidDTMVVFIIGETTRWDHMGMLGYSRDTTPKLAQEkNLVAF-RGYSCDTATKLSLRCMFVRE 305
Cdd:PRK11598 224 KNPLMQNQKR----------KNLTILVVGETSRAENFSLGGYPRETNPRLAKD-NVIYFpHTTSCGTATAVSVPCMFSNM 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 306 GGADDNPQRTLKEQNVFAVLKQLGFssdlyamqsemwfysntmadNIAYREQ----IGAEPRNRGKNV------------ 369
Cdd:PRK11598 293 PRKHYDEELAHHQEGLLDIIQRAGI--------------------NVLWNDNdggcKGACDRVPHQDVtalnlpgqcidg 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 370 ---DDMLLiNELQASLDkGTRGKRLIIMHTKGSHF-NYTQRYPRDFAKWTPECVS--VDDkCSKEELINSFDNSVTYVDH 443
Cdd:PRK11598 353 ecyDEVLF-HGLENYIN-NLQGDGVIVLHTIGSHGpTYYNRYPPQFRKFTPTCDTneIQT-CTQQQLVNTYDNTILYVDY 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 444 FIDTVIDKVRDRK-----AIVfYAADHGESINEKE-HLHGTPRKMAPPEQFRVPMMVWMSDKYlqdpqkAQMFAQ----L 513
Cdd:PRK11598 430 IVDKAINLLKQHQdkfntSLV-YLSDHGESLGENGiYLHGLPYAIAPDQQTHVPMLLWLSPDY------QKRYGVdqqcL 502
|
570 580
....*....|....*....|....
gi 521291418 514 KQQAAFKTPRRHvELYDTIMGCLG 537
Cdd:PRK11598 503 QKQAQTQDYSQD-NLFSTLLGLTG 525
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
126-503 |
1.49e-25 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 110.57 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 126 WVVLVS-ALPLLSIWsnrcRDTLLRQLSTPGARIRSVSIVLLAGLMVWGPIRLLDLQQKNAERTsgvdmpsYGGVVANSY 204
Cdd:PRK10649 123 KIVLIAlAYTAVAVL----LWTRLRPVYIPWPWRYVVSFALLYGLILHPIAMNTFIKHKPFEKT-------LDKLASRME 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 205 LPSNWLSALGLYAWAQ----VDESSDYKSLINPAKKFtyvapKDIDDT---MVVFIIGETTRWDHMGMLGYSRDTTPKL- 276
Cdd:PRK10649 192 PAAPWQFLTGYYQYRQqlnsLQKLLNENAALPPLANL-----KDESGNaprTLVLVIGESTQRGRMSLYGYPRETTPELd 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 277 ---AQEKNLVAFRGY-SCDTATKLSLR--CMFVREggadDNPQRTLKEQNVFAVLKQLGFSSDLYAMQSEMwFYSNTM-- 348
Cdd:PRK10649 267 alhKTDPGLTVFNNVvTSRPYTIEILQqaLTFADE----KNPDLYLTQPSLMNMMKQAGYKTFWITNQQTM-TARNTMlt 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 349 -----ADNIAYREQigaeprNRGKNVD--DMLLINELQASLDKGTRgKRLIIMHTKGSHFNYTQRYPRDFAKWT------ 415
Cdd:PRK10649 342 vfsrqTDKQYYMNQ------QRTQNAReyDTNVLKPFSEVLADPAP-KKFIIVHLLGTHIKYKYRYPENQGKFDdrtghv 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 416 PECVSVDDKcskeELINSFDNSVTYVDHFIDTVIDKVR--DRKAIVFYAADHGESI-----------NEkehlhGTP-RK 481
Cdd:PRK10649 415 PPGLNADEL----ESYNDYDNANLYNDHVVASLIKDFKatDPNGFLVYFSDHGEEVydtpphktqgrNE-----DNPtRH 485
|
410 420
....*....|....*....|..
gi 521291418 482 MappeqFRVPMMVWMSDKYLQD 503
Cdd:PRK10649 486 M-----YTIPFLLWTSEKWQAA 502
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
250-541 |
1.48e-16 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 79.90 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 250 VVFIIGETTRWDHMGMLGYSRDTTP---KLAQEkNLVAFRGYSCDTATKLSLRCMFV-------REGGADDNPQRTLkeq 319
Cdd:cd16148 3 VILIVIDSLRADHLGCYGYDRVTTPnldRLAAE-GVVFDNHYSGSNPTLPSRFSLFTglypfyhGVWGGPLEPDDPT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 320 nVFAVLKQLGFS----SDLYAMQSEMWFysntmadniayreqigaeprNRGKNVDDMLLINELQASLDKGTRGKRLIimh 395
Cdd:cd16148 79 -LAEILRKAGYYtaavSSNPHLFGGPGF--------------------DRGFDTFEDFRGQEGDPGEEGDERAERVT--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 396 tkgshfnytqrypRDFAKWtpecvsVDDKCSKEEL---INSFD--------NSVTYVDHFIDTVIDKVRDRK-----AIV 459
Cdd:cd16148 135 -------------DRALEW------LDRNADDDPFflfLHYFDphepylydAEVRYVDEQIGRLLDKLKELGlledtLVI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 460 FyAADHGESINEKEHLHGTPRKMApPEQFRVPMMVWmsdkylqDPQKAqmfaqlkQQAAFKTPRRHVELYDTIMGCLGYT 539
Cdd:cd16148 196 V-TSDHGEEFGEHGLYWGHGSNLY-DEQLHVPLIIR-------WPGKE-------PGKRVDALVSHIDIAPTLLDLLGVE 259
|
..
gi 521291418 540 SP 541
Cdd:cd16148 260 PP 261
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
14-542 |
7.25e-16 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 80.47 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 14 FLLAIYIGLFMNCAVFYRRFDGYAQAF-TVLKGISAVVELIGTVLVTFFLLRLLSLLGRRVWRVLASLVVIFSAAASY-Y 91
Cdd:COG1368 5 FLLLLSLRLVFLLFNFDLSLGEILQAFlYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLVADIlY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 92 MTFLNVVIGYGIIASVMTTDiDLSKEVVGWQLIAWVVLVSALPLLSIWSNRcrdtLLRQLSTPGARIRSVSIVLLAGLMV 171
Cdd:COG1368 85 YRFFGDRLNFSDLDYLGDTG-EVLGSLLSSYDLLLLLDLLLLLLLLLLLYR----LLKKLRKSLPWRKRLALLLLLLALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 172 WGPIRLLDLQQKNAERT-SGVDMPSYGGVVANSYLpsnwLSALGLYAWAQVDESSDYKSLINPAKKFTYVAPKDIDDTM- 249
Cdd:COG1368 160 LLGIRLGEDRPLNLSDAfSRNNFVNELGLNGPYSF----YDALRNNKAPATYSEEEALEIKKYLKSNRPTPNPFGPAKKp 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 250 -VVFIIGETTRWDHMGMLGYSRDTTP---KLAQE----KNLVAfrgyscdTATKlSLRCMFVREGGADDNPQR----TLK 317
Cdd:COG1368 236 nVVVILLESFSDFFIGALGNGKDVTPfldSLAKEslyfGNFYS-------QGGR-TSRGEFAVLTGLPPLPGGspykRPG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 318 EQNVFA---VLKQLGFSSdlYAMQS-EMWFYS-NTMADNIAYREQIGAE----PRNRGKNVDDMLLINELQASLDKGTRg 388
Cdd:COG1368 308 QNNFPSlpsILKKQGYET--SFFHGgDGSFWNrDSFYKNLGFDEFYDREdfddPFDGGWGVSDEDLFDKALEELEKLKK- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 389 KRLIIMHTKGSHFNYTqrYPRDFAKWTPEcvsvddkcsKEELINSFDNSVTYVDHFIDTVIDKVRDRKA-----IVFYaA 463
Cdd:COG1368 385 PFFAFLITLSNHGPYT--LPEEDKKIPDY---------GKTTLNNYLNAVRYADQALGEFIEKLKKSGWydntiFVIY-G 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291418 464 DHGESINekehlhGTPRKMAPPEQFRVPMMVWMSDkylqdpqkaqmfaqLKQQAAFKTPRRHVELYDTIMGCLGYTSPN 542
Cdd:COG1368 453 DHGPRSP------GKTDYENPLERYRVPLLIYSPG--------------LKKPKVIDTVGSQIDIAPTLLDLLGIDYPS 511
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
75-169 |
1.35e-14 |
|
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of bacterial phosphoethanolamine transferases, including eptA from Helicobacter pylori and eptB from Escherichia coli EC:2.7.8.42. This domain is found immediately N-terminal to the sulphatase domain in many sulphatases.
Pssm-ID: 429788 [Multi-domain] Cd Length: 151 Bit Score: 71.40 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 75 RVLASLVVIFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVVGWQLIAWVVLVSALPLLSIWSNRCRD-TLLRQLst 153
Cdd:pfam08019 19 KPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPALLLWRVRIRYrPWLREL-- 96
|
90
....*....|....*...
gi 521291418 154 pGARIRS--VSIVLLAGL 169
Cdd:pfam08019 97 -LSRLALilVSLLVIGLV 113
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
250-537 |
2.15e-08 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 55.77 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 250 VVFIIGETTRWDHMGMLGYSRDTTP---KLAQE----KNLVA--FRGYSCDT--ATKLSLRCMFVREGGADDNPQRTLke 318
Cdd:cd16015 3 VIVILLESFSDPYIDKDVGGEDLTPnlnKLAKEglyfGNFYSpgFGGGTANGefEVLTGLPPLPLGSGSYTLYKLNPL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 319 QNVFAVLKQLGFSSdlYAMQ-SEMWFYS-NTMA-----DNIAYREQIGAEPRNRGKN-VDDMLLINELQASLDKGTRGKR 390
Cdd:cd16015 81 PSLPSILKEQGYET--IFIHgGDASFYNrDSVYpnlgfDEFYDLEDFPDDEKETNGWgVSDESLFDQALEELEELKKKPF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 391 LIIMHTKGSHFNYTqrYPRDfakwtpECVSVDDKCSKEELINSFDNSVTYVDHFIDTVIDKVRDRKA-----IVFYAaDH 465
Cdd:cd16015 159 FIFLVTMSNHGPYD--LPEE------KKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLyentiIVIYG-DH 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521291418 466 GESINEKEHlhgtPRKMAPPEQFRVPMMVWmsDKYLQDPQKAQMFAQlkqqaafktprrHVELYDTIMGCLG 537
Cdd:cd16015 230 LPSLGSDYD----ETDEDPLDLYRTPLLIY--SPGLKKPKKIDRVGS------------QIDIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
438-495 |
2.82e-04 |
|
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 42.81 E-value: 2.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521291418 438 VTYVDHFIDTVIDKVRDRKA----IVFYAADHGESINEkehlHGTP-RKMAPPEQ-FRVPMMVW 495
Cdd:cd16022 137 VSAIDDQIGRILDALEELGLldntLIVFTSDHGDMLGD----HGLRgKKGSLYEGgIRVPFIVR 196
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
403-495 |
3.06e-03 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 40.25 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291418 403 YTQRY-PRDFAKWTPECVSVDDKCSKEELINSFDNSVTYVDHFIDTVIDKVRDRKA----IVFYAADHGESINEkehlHG 477
Cdd:COG3119 170 YLDKYdGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLadntIVVFTSDNGPSLGE----HG 245
|
90 100
....*....|....*....|
gi 521291418 478 TP-RKMAPPEQ-FRVPMMVW 495
Cdd:COG3119 246 LRgGKGTLYEGgIRVPLIVR 265
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
436-494 |
8.99e-03 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 38.34 E-value: 8.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291418 436 NSVTYVDHFIDTVIDKVRD----RKAIVFYAADHGEsinekehL---HGTPRKMAPP--EQFRVPMMV 494
Cdd:cd16035 171 NLIRDVDRQIGRVLDALDAsglaDNTIVVFTSDHGE-------MggaHGLRGKGFNAyeEALHVPLII 231
|
|
| |
