|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
1-557 |
0e+00 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 1172.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 1 MKYIRTMTQQKLSFWLALYIGWFMNVAVFFRRFDGYAQEFNFWKGLSGVVELVATVFVTFFLLRLLSLFGRRIWRILATL 80
Cdd:PRK11560 1 MRYIKSLTQQKLSFLLAVYIGLFLNIAVFYRRFDSYAQDFTVWKGLSAVVELAATVLVTFFLLRLLSLFGRRFWRVLASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 81 IVLFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVIGWHLILWLVAVSAPPLLFIWSNRCRHTLLRQLRTPGQRVKN 160
Cdd:PRK11560 81 LVLFSAAASYYMTFFNVVIGYGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWNNRCRYTLLRQLRTPGQRIRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 161 VLIVVLAGLIVWGPIRLLELRQHDVERHSEVDMPSYGGVIANSYLPSNWLSALGLYAWAQVDESSDNKSLINPAKKFTYV 240
Cdd:PRK11560 161 LAVVVLAGLLVWAPIRLLDIQQKKVERATGVDLPSYGGVVANSYLPSNWLSALGLYAWAQVDESSDNNSLLNPAKKFTYQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 241 APEGLDDTYVVFIIGETTRWDHMGILGYSRNTTPELEKEKNLVAFRGYSCDTATKLSLRCMFVREGGAEDNPQRTLKEQN 320
Cdd:PRK11560 241 APKGVDDTYVVFIIGETTRWDHMGILGYERNTTPKLAQEKNLAAFRGYSCDTATKLSLRCMFVREGGAEDNPQRTLKEQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 321 VFAVLHQLGFSGNLYAMQSEMWFYSNTMANNIAYREQIGAEPRNRGKSVDDMLLVDEMKRGMAQgNASGKHLIILHTKGS 400
Cdd:PRK11560 321 VFAVLKQLGFSSELFAMQSEMWFYNNTMADNYAYREQIGAEPRNRGKPVDDMLLVDEMKQSLGR-NPDGKHLIILHTKGS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 401 HFNYTQRYPRSFAQWKPECVGVDNKCSKAELINSYDNSVTYVDHFIVSVLDQLRDKKAIVFYAADHGESINEREHLHGTP 480
Cdd:PRK11560 400 HYNYTQRYPRSFARYQPECIGVDSGCSKAQLINSYDNSVLYVDHFISSVIDQLRDKKAIVFYAADHGESINEREHLHGTP 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523671330 481 RKMAPPEQFRVPMMVWMSDKYLENPDHAAAFAHLQQQAAMKVPRRHVELYDTIMGCLGYTSPDGGINENNNWCRWKK 557
Cdd:PRK11560 480 REMAPPEQFRVPMMVWMSDKYLANPDNAQAFAQLKKQADMKVPRRHVELFDTILGCLGYTSPDGGINENNNWCHIPD 556
|
|
| 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: 548.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 5 RTMTQQKLSFWLALYIGWFMNVAVFFRRFDGYAQEFNFWKGLSGVVELVATVFVTFFLLRLLSLfgrrIWRILATLIVLF 84
Cdd:COG2194 5 PRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDGVNLLFLLSLPLLLLAALNLLLSLLAWRY----LFKPLLILLLLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 85 SAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVIGWHLILWLVAVSAPPLLFIWSNRCRHTLLrqLRTPGQRVKNVLI- 163
Cdd:COG2194 81 SAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPL--LRELGQRLALLLLa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 164 VVLAGLIVWGPIRLLE--LRQHDVERHsevdmpsyggvianSYLPSNWLSALGLYAWAQVDESS-DNKSLINPAKKftyv 240
Cdd:COG2194 159 LLVIVLLALLFYKDYAsfFRNHKELRY--------------LINPSNFIYALGKYAKARYFAAPlPLQPLGADAKL---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 241 APEGLDDTYVVFIIGETTRWDHMGILGYSRNTTPELEKEKNLVAFR-GYSCDTATKLSLRCMFVREGGAEDNPQRTLKEQ 319
Cdd:COG2194 221 AAAGAKPTLVVLVVGETARADNFSLNGYARDTTPELAKEKNLVSFRdVTSCGTATAVSVPCMFSRLGRADYDPQRALNQE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 320 NVFAVLHQLGFSGNLYAMQSEM-WFYSN-----TMANNiayreqigAEPRNRGKSVDDMLLVDEMKRGMAqgNASGKHLI 393
Cdd:COG2194 301 NLLDVLQRAGVKVLWRDNQSGCkGVCDRvptidLTADN--------LPPLCDGGECLDEVLLDGLDEALA--DLAGDKLI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 394 ILHTKGSH-FNYTQRYPRSFAQWKPEC-VGVDNKCSKAELINSYDNSVTYVDHFIVSVLDQLRDK----KAIVFYAADHG 467
Cdd:COG2194 371 VLHQMGSHgPAYYKRYPPEFRKFTPTCdTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKqdryDTAMLYVSDHG 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 468 ESINERE-HLHGTPRKMAPPEQFRVPMMVWMSDKYLenPDHAAAFAHLQQQAamKVPRRHVELYDTIMGCLGYTSPdgGI 546
Cdd:COG2194 451 ESLGENGlYLHGTPYAIAPDEQTHVPMIMWLSDGYA--QRYGIDFACLKARA--DKPYSHDNLFHTLLGLLDVRTS--VY 524
|
....*..
gi 523671330 547 NENNNWC 553
Cdd:COG2194 525 DPELDIL 531
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
246-540 |
3.07e-92 |
|
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: 284.13 E-value: 3.07e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 246 DDTYVVFIIGETTRWDHMGILGYSRNTTPELEKEK-NLVAFRG-YSCDTATKLSLRCMFVREGgaEDNPQRTLKEQNVFA 323
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKkNLIVFDNvISCGTSTAVSLPCMLSFAN--RENYDRAYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 324 VLHQLGFSGNLYAMQSEMWFYSNTMANNIAYREQIGAEPRNRGKSVDDMLLVDEMKRgmAQGNASGKHLIILHTKGSHFN 403
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDE--ALADSSKKKLIVLHLMGSHGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 404 YTQRYPRSFAQWKPECVGVDNKCSKAELINSYDNSVTYVDHFIVSVLDQLR--DKKAIVFYAADHGESINEREH-LHGTP 480
Cdd:cd16017 157 YYDRYPEEFAKFTPDCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKkkDKDAALIYFSDHGESLGENGLyLHGAP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 481 RkmAPPEQFRVPMMVWMSDKYLENPDHAAAFAHLQQqaamkvPRRHVELYDTIMGCLGYT 540
Cdd:cd16017 237 Y--APKEQYHVPFIIWSSDSYKQRYPVERLRANKDR------PFSHDNLFHTLLGLLGIK 288
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
250-539 |
8.00e-58 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 194.95 E-value: 8.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 250 VVFIIGETTRWDHMGILGYSRNTTPELEKE-KNLVAF-RGYSCDTATKLSLRCMFVR------EGGAEDNPQRTLKEQNV 321
Cdd:pfam00884 3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRLaEEGLLFsNFYSGGTLTAPSRFALLTGlpphnfGSYVSTPVGLPRTEPSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 322 FAVLHQLGFSGNLYAMQSEMWFYSNTMAN--------NIAYREQIGAEPRN----RGKSVDDMLLVDEMKRgmAQGNASG 389
Cdd:pfam00884 83 PDLLKRAGYNTGAIGKWHLGWYNNQSPCNlgfdkffgRNTGSDLYADPPDVpyncSGGGVSDEALLDEALE--FLDNNDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 390 KHLIILHTKGSH--FNYTQRYPRSFAQWKPecvgvdNKCSKAELINSYDNSVTYVDHFIVSVLDQLR----DKKAIVFYA 463
Cdd:pfam00884 161 PFFLVLHTLGSHgpPYYPDRYPEKYATFKP------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEenglLDNTLVVYT 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523671330 464 ADHGESINEREH-LHGTPRKMAPPEQFRVPMMVWMSDKYlenpdhaaafahlQQQAAMKVPRRHVELYDTIMGCLGY 539
Cdd:pfam00884 235 SDHGESLGEGGGyLHGGKYDNAPEGGYRVPLLIWSPGGK-------------AKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
1-557 |
0e+00 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 1172.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 1 MKYIRTMTQQKLSFWLALYIGWFMNVAVFFRRFDGYAQEFNFWKGLSGVVELVATVFVTFFLLRLLSLFGRRIWRILATL 80
Cdd:PRK11560 1 MRYIKSLTQQKLSFLLAVYIGLFLNIAVFYRRFDSYAQDFTVWKGLSAVVELAATVLVTFFLLRLLSLFGRRFWRVLASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 81 IVLFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVIGWHLILWLVAVSAPPLLFIWSNRCRHTLLRQLRTPGQRVKN 160
Cdd:PRK11560 81 LVLFSAAASYYMTFFNVVIGYGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWNNRCRYTLLRQLRTPGQRIRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 161 VLIVVLAGLIVWGPIRLLELRQHDVERHSEVDMPSYGGVIANSYLPSNWLSALGLYAWAQVDESSDNKSLINPAKKFTYV 240
Cdd:PRK11560 161 LAVVVLAGLLVWAPIRLLDIQQKKVERATGVDLPSYGGVVANSYLPSNWLSALGLYAWAQVDESSDNNSLLNPAKKFTYQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 241 APEGLDDTYVVFIIGETTRWDHMGILGYSRNTTPELEKEKNLVAFRGYSCDTATKLSLRCMFVREGGAEDNPQRTLKEQN 320
Cdd:PRK11560 241 APKGVDDTYVVFIIGETTRWDHMGILGYERNTTPKLAQEKNLAAFRGYSCDTATKLSLRCMFVREGGAEDNPQRTLKEQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 321 VFAVLHQLGFSGNLYAMQSEMWFYSNTMANNIAYREQIGAEPRNRGKSVDDMLLVDEMKRGMAQgNASGKHLIILHTKGS 400
Cdd:PRK11560 321 VFAVLKQLGFSSELFAMQSEMWFYNNTMADNYAYREQIGAEPRNRGKPVDDMLLVDEMKQSLGR-NPDGKHLIILHTKGS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 401 HFNYTQRYPRSFAQWKPECVGVDNKCSKAELINSYDNSVTYVDHFIVSVLDQLRDKKAIVFYAADHGESINEREHLHGTP 480
Cdd:PRK11560 400 HYNYTQRYPRSFARYQPECIGVDSGCSKAQLINSYDNSVLYVDHFISSVIDQLRDKKAIVFYAADHGESINEREHLHGTP 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523671330 481 RKMAPPEQFRVPMMVWMSDKYLENPDHAAAFAHLQQQAAMKVPRRHVELYDTIMGCLGYTSPDGGINENNNWCRWKK 557
Cdd:PRK11560 480 REMAPPEQFRVPMMVWMSDKYLANPDNAQAFAQLKKQADMKVPRRHVELFDTILGCLGYTSPDGGINENNNWCHIPD 556
|
|
| 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: 548.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 5 RTMTQQKLSFWLALYIGWFMNVAVFFRRFDGYAQEFNFWKGLSGVVELVATVFVTFFLLRLLSLfgrrIWRILATLIVLF 84
Cdd:COG2194 5 PRLSPLKLILLLALYFALFLNLPFWGRLLAILPLDGVNLLFLLSLPLLLLAALNLLLSLLAWRY----LFKPLLILLLLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 85 SAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVIGWHLILWLVAVSAPPLLFIWSNRCRHTLLrqLRTPGQRVKNVLI- 163
Cdd:COG2194 81 SAAASYFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPL--LRELGQRLALLLLa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 164 VVLAGLIVWGPIRLLE--LRQHDVERHsevdmpsyggvianSYLPSNWLSALGLYAWAQVDESS-DNKSLINPAKKftyv 240
Cdd:COG2194 159 LLVIVLLALLFYKDYAsfFRNHKELRY--------------LINPSNFIYALGKYAKARYFAAPlPLQPLGADAKL---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 241 APEGLDDTYVVFIIGETTRWDHMGILGYSRNTTPELEKEKNLVAFR-GYSCDTATKLSLRCMFVREGGAEDNPQRTLKEQ 319
Cdd:COG2194 221 AAAGAKPTLVVLVVGETARADNFSLNGYARDTTPELAKEKNLVSFRdVTSCGTATAVSVPCMFSRLGRADYDPQRALNQE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 320 NVFAVLHQLGFSGNLYAMQSEM-WFYSN-----TMANNiayreqigAEPRNRGKSVDDMLLVDEMKRGMAqgNASGKHLI 393
Cdd:COG2194 301 NLLDVLQRAGVKVLWRDNQSGCkGVCDRvptidLTADN--------LPPLCDGGECLDEVLLDGLDEALA--DLAGDKLI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 394 ILHTKGSH-FNYTQRYPRSFAQWKPEC-VGVDNKCSKAELINSYDNSVTYVDHFIVSVLDQLRDK----KAIVFYAADHG 467
Cdd:COG2194 371 VLHQMGSHgPAYYKRYPPEFRKFTPTCdTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKqdryDTAMLYVSDHG 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 468 ESINERE-HLHGTPRKMAPPEQFRVPMMVWMSDKYLenPDHAAAFAHLQQQAamKVPRRHVELYDTIMGCLGYTSPdgGI 546
Cdd:COG2194 451 ESLGENGlYLHGTPYAIAPDEQTHVPMIMWLSDGYA--QRYGIDFACLKARA--DKPYSHDNLFHTLLGLLDVRTS--VY 524
|
....*..
gi 523671330 547 NENNNWC 553
Cdd:COG2194 525 DPELDIL 531
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
246-540 |
3.07e-92 |
|
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: 284.13 E-value: 3.07e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 246 DDTYVVFIIGETTRWDHMGILGYSRNTTPELEKEK-NLVAFRG-YSCDTATKLSLRCMFVREGgaEDNPQRTLKEQNVFA 323
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKkNLIVFDNvISCGTSTAVSLPCMLSFAN--RENYDRAYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 324 VLHQLGFSGNLYAMQSEMWFYSNTMANNIAYREQIGAEPRNRGKSVDDMLLVDEMKRgmAQGNASGKHLIILHTKGSHFN 403
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIAKIETVFTNKGSCNSSNCYDEALLPLLDE--ALADSSKKKLIVLHLMGSHGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 404 YTQRYPRSFAQWKPECVGVDNKCSKAELINSYDNSVTYVDHFIVSVLDQLR--DKKAIVFYAADHGESINEREH-LHGTP 480
Cdd:cd16017 157 YYDRYPEEFAKFTPDCDNELQSCSKEELINAYDNSILYTDYVLSQIIERLKkkDKDAALIYFSDHGESLGENGLyLHGAP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 481 RkmAPPEQFRVPMMVWMSDKYLENPDHAAAFAHLQQqaamkvPRRHVELYDTIMGCLGYT 540
Cdd:cd16017 237 Y--APKEQYHVPFIIWSSDSYKQRYPVERLRANKDR------PFSHDNLFHTLLGLLGIK 288
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
250-539 |
8.00e-58 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 194.95 E-value: 8.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 250 VVFIIGETTRWDHMGILGYSRNTTPELEKE-KNLVAF-RGYSCDTATKLSLRCMFVR------EGGAEDNPQRTLKEQNV 321
Cdd:pfam00884 3 VVLVLGESLRAPDLGLYGYPRPTTPFLDRLaEEGLLFsNFYSGGTLTAPSRFALLTGlpphnfGSYVSTPVGLPRTEPSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 322 FAVLHQLGFSGNLYAMQSEMWFYSNTMAN--------NIAYREQIGAEPRN----RGKSVDDMLLVDEMKRgmAQGNASG 389
Cdd:pfam00884 83 PDLLKRAGYNTGAIGKWHLGWYNNQSPCNlgfdkffgRNTGSDLYADPPDVpyncSGGGVSDEALLDEALE--FLDNNDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 390 KHLIILHTKGSH--FNYTQRYPRSFAQWKPecvgvdNKCSKAELINSYDNSVTYVDHFIVSVLDQLR----DKKAIVFYA 463
Cdd:pfam00884 161 PFFLVLHTLGSHgpPYYPDRYPEKYATFKP------SSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEenglLDNTLVVYT 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523671330 464 ADHGESINEREH-LHGTPRKMAPPEQFRVPMMVWMSDKYlenpdhaaafahlQQQAAMKVPRRHVELYDTIMGCLGY 539
Cdd:pfam00884 235 SDHGESLGEGGGyLHGGKYDNAPEGGYRVPLLIWSPGGK-------------AKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
75-557 |
4.41e-45 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 166.88 E-value: 4.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 75 RILATLIVLFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVIGWHLILWLVAVSAPPLLFIWSNRCRHTLLRQLrtp 154
Cdd:PRK09598 75 RLSAIVFSLLNSIAFYFINTYKVFLNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKNSSKKAP--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 155 gqrVKNVLIVVLAgLIVWgpirLLELRQHD--VERHSEVdmpsYGGVIansyLPSNWLSALGLYAwAQVDESSDNKSLIN 232
Cdd:PRK09598 152 ---FAAILALVLI-FLAS----AFANSKNWlwFDKHAKF----LGGLI----LPWSYSVNTFRVS-AHKFFAPTIKPLLP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 233 PAKkftyvaPEGLDDTYVVFIIGETTRWDHMGILGYSRNTTPELEKEKN---LVAFRGYSCDTATKLSLRCM----FVRE 305
Cdd:PRK09598 215 PLF------SPNHSKSVVVLVIGESARKHNYALYGYEKPTNPRLSKRLAtheLTLFNATSCATYTTASLECIldssFKNT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 306 GGAEDNPQRTLKEQNVFAVlhqlgfsgnlyaMQSEMWFYSNTMANNIAYREQIGAEPRNRGKSVDDMLLVDEMKRgmAQG 385
Cdd:PRK09598 289 SNAYENLPTYLTRAGIKVF------------WRSANDGEPNVKVTSYLKNYELIQKCPNCEAPYDESLLYNLPEL--IKA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 386 NASGKHLIILHTKGSHF-NYTQRYPRSFAQWKPECVGVD-NKCSKAELINSYDNSVTYVDHF---IVSVLDQLRDKKAIV 460
Cdd:PRK09598 355 SSNENVLLILHLAGSHGpNYDNKYPLNFRVFKPVCSSVElSSCSKESLINAYDNTIFYNDYLldkIISMLKNLKQPALMI 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 461 fYAADHGESINERE-HLHGTPRKMAPPEQFRVPMMVWMSDKYLENpdhaaafaHLQQQAAMKVPRRHVelYDTIMGCLGY 539
Cdd:PRK09598 435 -YLSDHGESLGEGAfYLHGIPKSIAPKEQYEIPFIVWASDSFKKQ--------HSIIQTQTPINQNVI--FHSVLGVFDF 503
|
490
....*....|....*...
gi 523671330 540 TSPDGGINENNNWCRWKK 557
Cdd:PRK09598 504 KNPSAVYRPSLDLFKHKK 521
|
|
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
75-538 |
2.52e-43 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 162.15 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 75 RILATLIVLFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVIGWHLILWLVAVSAPPLLFIWSNRCRHTLLRqLRTP 154
Cdd:PRK11598 75 RPLACLFILVGAAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIRPATPR-WRSV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 155 GQRVKNVLIVVLAGLIVwgpirllelrqhdverhSEVDMPSYGGVIAN------SYLPSNWLSALGLYA---------WA 219
Cdd:PRK11598 154 LFRLANILVSVLLILLV-----------------AALFYKDYASLFRNnkelvkSLTPSNSIVASWSWYshqrlanlpLV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 220 QVDESSDNKSLINPAKKftyvapegldDTYVVFIIGETTRWDHMGILGYSRNTTPELEKEkNLVAF-RGYSCDTATKLSL 298
Cdd:PRK11598 217 RIGEDAHKNPLMQNQKR----------KNLTILVVGETSRAENFSLGGYPRETNPRLAKD-NVIYFpHTTSCGTATAVSV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 299 RCMFvreggaEDNPQRTLKEQnvfAVLHQLGFsgnLYAMQSEmwfysntmANNIAYREQIGA--EPRNR----------- 365
Cdd:PRK11598 286 PCMF------SNMPRKHYDEE---LAHHQEGL---LDIIQRA--------GINVLWNDNDGGckGACDRvphqdvtalnl 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 366 ------GKSVDDMLL--VDEMKRGMAQGNasgkhLIILHTKGSHF-NYTQRYPRSFAQWKPECvgvDNK----CSKAELI 432
Cdd:PRK11598 346 pgqcidGECYDEVLFhgLENYINNLQGDG-----VIVLHTIGSHGpTYYNRYPPQFRKFTPTC---DTNeiqtCTQQQLV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 433 NSYDNSVTYVDHFI---VSVLDQLRDK--KAIVfYAADHGESINERE-HLHGTPRKMAPPEQFRVPMMVWMSdkylenPD 506
Cdd:PRK11598 418 NTYDNTILYVDYIVdkaINLLKQHQDKfnTSLV-YLSDHGESLGENGiYLHGLPYAIAPDQQTHVPMLLWLS------PD 490
|
490 500 510
....*....|....*....|....*....|....*....
gi 523671330 507 HAAAFA----HLQQQAAMKvprrHVE---LYDTIMGCLG 538
Cdd:PRK11598 491 YQKRYGvdqqCLQKQAQTQ----DYSqdnLFSTLLGLTG 525
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
75-512 |
1.58e-27 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 116.73 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 75 RILATLI--VLFS---AAASYYmtflnVVIGYGIIASVM----TTDIDLSKEVIGWHLILWLVavsapPLLFIWSNRC-- 143
Cdd:PRK10649 68 RIIAAVIgvVLWAaslAALCYY-----VIYGQEFSQSVLfvmfETNTNEASEYLSQYFSLKIV-----LIALAYTAVAvl 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 144 RHTLLRQLRTPGQRVKNVLIVVLAGLIVwGPIRLLELRQHD--------VERHSEVDMPsyggviansylpsnWLSALGL 215
Cdd:PRK10649 138 LWTRLRPVYIPWPWRYVVSFALLYGLIL-HPIAMNTFIKHKpfektldkLASRMEPAAP--------------WQFLTGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 216 YAWAQVDESSDNksLINPAKKFTYVApeGLDDTY------VVFIIGETTRWDHMGILGYSRNTTPELEK----EKNLVAF 285
Cdd:PRK10649 203 YQYRQQLNSLQK--LLNENAALPPLA--NLKDESgnaprtLVLVIGESTQRGRMSLYGYPRETTPELDAlhktDPGLTVF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 286 RG-YSCDTATKLSLR--CMFvregGAEDNPQRTLKEQNVFAVLHQLGFSGNLYAMQSEMwFYSNTMANNIAyrEQIGAE- 361
Cdd:PRK10649 279 NNvVTSRPYTIEILQqaLTF----ADEKNPDLYLTQPSLMNMMKQAGYKTFWITNQQTM-TARNTMLTVFS--RQTDKQy 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 362 ----PRNRGKSVDDMLLVDEMKRGMAqgNASGKHLIILHTKGSHFNYTQRYPRSFAQWK--PECV--GVDNKcsKAELIN 433
Cdd:PRK10649 352 ymnqQRTQNAREYDTNVLKPFSEVLA--DPAPKKFIIVHLLGTHIKYKYRYPENQGKFDdrTGHVppGLNAD--ELESYN 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 434 SYDNSVTYVDHFIVSVLDQLR--DKKAIVFYAADHGESI-NEREHL-----HGTP-RKMappeqFRVPMMVWMSDKYLEN 504
Cdd:PRK10649 428 DYDNANLYNDHVVASLIKDFKatDPNGFLVYFSDHGEEVyDTPPHKtqgrnEDNPtRHM-----YTIPFLLWTSEKWQAA 502
|
....*...
gi 523671330 505 PDHAAAFA 512
Cdd:PRK10649 503 HPRDFSQD 510
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
75-171 |
1.35e-16 |
|
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: 76.79 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 75 RILATLIVLFSAAASYYMTFLNVVIGYGIIASVMTTDIDLSKEVIGWHLILWLVAVSAPPLLFIWSNRCRHTLLrqLRTP 154
Cdd:pfam08019 19 KPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPALLLWRVRIRYRPW--LREL 96
|
90
....*....|....*...
gi 523671330 155 GQRVKNVLI-VVLAGLIV 171
Cdd:pfam08019 97 LSRLALILVsLLVIGLVA 114
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
250-543 |
7.25e-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: 77.97 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 250 VVFIIGETTRWDHMGILGYSRNTTPELEK--EKNLVAFRGYSCDTATKLSLRCMF---------VREGGAEDNPQ---RT 315
Cdd:cd16148 3 VILIVIDSLRADHLGCYGYDRVTTPNLDRlaAEGVVFDNHYSGSNPTLPSRFSLFtglypfyhgVWGGPLEPDDPtlaEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 316 LKEQNVFAVLhqlgFSGNLYAmqSEMWFYSNTMANNIAYREQIGAEPRNRGKSVDDMllvdeMKRGMA--QGNASGK--- 390
Cdd:cd16148 83 LRKAGYYTAA----VSSNPHL--FGGPGFDRGFDTFEDFRGQEGDPGEEGDERAERV-----TDRALEwlDRNADDDpff 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 391 -HLiilHTKGSHFNYtqryprsfaqwkpecvgvdnkcskaelinSYDNSVTYVDHFIVSVLDQLRDKK-----AIVFyAA 464
Cdd:cd16148 152 lFL---HYFDPHEPY-----------------------------LYDAEVRYVDEQIGRLLDKLKELGlledtLVIV-TS 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523671330 465 DHGESINEREHLHGTPRKMApPEQFRVPMMVWMSDKYlenpdHAAAFAHLQQqaamkvprrHVELYDTIMGCLGYTSPD 543
Cdd:cd16148 199 DHGEEFGEHGLYWGHGSNLY-DEQLHVPLIIRWPGKE-----PGKRVDALVS---------HIDIAPTLLDLLGVEPPD 262
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
14-496 |
8.26e-12 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 67.76 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 14 FWLALYIGWFMNVAVFFRRFdgyaqeFNFWKGLSGVVELVATVFV---TFFLLRLLSLFGRRIWRILATLIVLFSAAASY 90
Cdd:COG1368 9 LSLRLVFLLFNFDLSLGEIL------QAFLYGLRFILYLLLLLLLlllLLLPLLFRRPKLRWIYLLLVLLLLLLLLVADI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 91 -YMTFLNVVIGYGIIASVMTTDiDLSKEVIGWHLILWLVAVSAPPLLFIWSnrcrHTLLRQLRTPGQRVKNVLIVVLAGL 169
Cdd:COG1368 83 lYYRFFGDRLNFSDLDYLGDTG-EVLGSLLSSYDLLLLLDLLLLLLLLLLL----YRLLKKLRKSLPWRKRLALLLLLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 170 IVWGPIRLLELRQHDVERH-SEVDMPSYGGVIANSYLpsnwLSALGLYAWAQVDESSDNKSLINPAKKFTYVAPEGLDDT 248
Cdd:COG1368 158 LLLLGIRLGEDRPLNLSDAfSRNNFVNELGLNGPYSF----YDALRNNKAPATYSEEEALEIKKYLKSNRPTPNPFGPAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 249 Y--VVFIIGETTRWDHMGILGYSRNTTPELEK-EKNLVAF-RGYScdTATKlSLRCMFVREGGAEDNPQR----TLKEQN 320
Cdd:COG1368 234 KpnVVVILLESFSDFFIGALGNGKDVTPFLDSlAKESLYFgNFYS--QGGR-TSRGEFAVLTGLPPLPGGspykRPGQNN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 321 VFA---VLHQLG-----FSGNlyamqsEMWFYS-NTMANNIAYREQIGAE----PRNRGKSVDDMLLVDEMKRGMaqgNA 387
Cdd:COG1368 311 FPSlpsILKKQGyetsfFHGG------DGSFWNrDSFYKNLGFDEFYDREdfddPFDGGWGVSDEDLFDKALEEL---EK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 388 SGKH-LIILHTKGSHFNYTqrYPRSFAQWKPEcvgvdnkcsKAELINSYDNSVTYVDHFIVSVLDQLRDKKA-----IVF 461
Cdd:COG1368 382 LKKPfFAFLITLSNHGPYT--LPEEDKKIPDY---------GKTTLNNYLNAVRYADQALGEFIEKLKKSGWydntiFVI 450
|
490 500 510
....*....|....*....|....*....|....*
gi 523671330 462 YaADHGESINerehlhGTPRKMAPPEQFRVPMMVW 496
Cdd:COG1368 451 Y-GDHGPRSP------GKTDYENPLERYRVPLLIY 478
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
250-496 |
9.69e-06 |
|
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: 47.68 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 250 VVFIIGETTRWDHMGILGYSRNTTPELEK--EKNLV-------AFRGYSCDT--ATKLSLRCMFVREGGAEDNPQRTLke 318
Cdd:cd16015 3 VIVILLESFSDPYIDKDVGGEDLTPNLNKlaKEGLYfgnfyspGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLNPL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 319 QNVFAVLHQLGFsgNLYAMQ-SEMWFYS-NTMANNIAYREQIGAE------PRNRGKSVDDMLLVDEMKRGMAQgNASGK 390
Cdd:cd16015 81 PSLPSILKEQGY--ETIFIHgGDASFYNrDSVYPNLGFDEFYDLEdfpddeKETNGWGVSDESLFDQALEELEE-LKKKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 391 HLIILHTKGSHFNYTqrYPrsfaqwKPECVGVDNKCSKAELINSYDNSVTYVDHFIVSVLDQLRDKKA-----IVFYaAD 465
Cdd:cd16015 158 FFIFLVTMSNHGPYD--LP------EEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLyentiIVIY-GD 228
|
250 260 270
....*....|....*....|....*....|.
gi 523671330 466 HGESINErehlHGTPRKMAPPEQFRVPMMVW 496
Cdd:cd16015 229 HLPSLGS----DYDETDEDPLDLYRTPLLIY 255
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
439-496 |
1.29e-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: 43.58 E-value: 1.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523671330 439 VTYVDHFIVSVLDQLRDKKA----IVFYAADHGESINEReHLHGtpRKMAPPEQ-FRVPMMVW 496
Cdd:cd16022 137 VSAIDDQIGRILDALEELGLldntLIVFTSDHGDMLGDH-GLRG--KKGSLYEGgIRVPFIVR 196
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
431-495 |
2.59e-04 |
|
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: 43.35 E-value: 2.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523671330 431 LINSYDNSVTYVDHFIVSVLDQLRD----KKAIVFYAADHGEsinerehL---HGTPRKMAPP--EQFRVPMMV 495
Cdd:cd16035 165 FRNFYYNLIRDVDRQIGRVLDALDAsglaDNTIVVFTSDHGE-------MggaHGLRGKGFNAyeEALHVPLII 231
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
250-496 |
5.04e-04 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. 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. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 42.02 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 250 VVFIIGETTRWDHMGILGYSRNTTPELEKEKNLVA---FRGYSCDTATKLSLRCMFvreGGAedNPqrtlkeqnvfaVLH 326
Cdd:cd00016 3 VVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGAtfnFRSVSPPTSSAPNHAALL---TGA--YP-----------TLH 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 327 QLGFsgnlyamqsemWFYSNTMANNIAYREQ-----IGAEPRNRGKSVDDMLLVDEMKRgmaqgNASGKH-LIILHTKGS 400
Cdd:cd00016 67 GYTG-----------NGSADPELPSRAAGKDedgptIPELLKQAGYRTGVIGLLKAIDE-----TSKEKPfVLFLHFDGP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523671330 401 HFNYTQRYPRSfaqwkpecvgvdnkcskaeliNSYDNSVTYVDHFIVSVLDQLRDKK----AIVFYAADHGesiNEREHL 476
Cdd:cd00016 131 DGPGHAYGPNT---------------------PEYYDAVEEIDERIGKVLDALKKAGdaddTVIIVTADHG---GIDKGH 186
|
250 260
....*....|....*....|....
gi 523671330 477 HGTPRKMAPPEQF----RVPMMVW 496
Cdd:cd00016 187 GGDPKADGKADKShtgmRVPFIAY 210
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
429-496 |
7.60e-04 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 42.17 E-value: 7.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523671330 429 AELINSYDNSVTYVDHFIVSVLDQLRDKKA----IVFYAADHGESINErehlHGTP-RKMAPPEQ-FRVPMMVW 496
Cdd:COG3119 196 RRARAAYAAMIEEVDDQVGRLLDALEELGLadntIVVFTSDNGPSLGE----HGLRgGKGTLYEGgIRVPLIVR 265
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
429-495 |
7.72e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 38.74 E-value: 7.72e-03
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gi 523671330 429 AELINSYDNSVTYVDHFIVSVLDQLRDK----KAIVFYAADHGESINErehlHGTPRKMAPP--EQFRVPMMV 495
Cdd:cd16033 213 KEIIAHYWGYITLIDDAIGRILDALEELgladDTLVIFTSDHGDALGA----HRLWDKGPFMyeETYRIPLII 281
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