|
Name |
Accession |
Description |
Interval |
E-value |
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
11-526 |
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: 619.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 11 SINPFVLMGLVAFFLAATANLTFFEKAMAVYPVSD-NLGFIVSMAVALMGAMLLIVVLLSYRYVLKPVLILLLIMGAVTS 89
Cdd:COG2194 6 RLSPLKLILLLALYFALFLNLPFWGRLLAILPLDGvNLLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLISAAAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 90 YFTDTYGTVYDTTMLQNAMQTDQAESKDLMNLAFFVRIIGLGVLPSLLVAVAKVNYPTWGKSLIQRAMTWGVSLVLLLVP 169
Cdd:COG2194 86 YFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPLLRELGQRLALLLLALLVIVLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 170 IGLFSSQYASFFRVHKPVRFYINPITPIYSVGKLASIEYKKATAPTDTIyhAKDAVQTtkPSERKPRLVVFVVGETARAD 249
Cdd:COG2194 166 ALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPL--GADAKLA--AAGAKPTLVVLVVGETARAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 250 HVQFNGYGRETFPQLAKVDGLANFSQVTSCGTSTAYSVPCMFSYLGQDDYDVDTAKYQENVLDTLDRLGVGILWRDNNSD 329
Cdd:COG2194 242 NFSLNGYARDTTPELAKEKNLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQSG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 330 SKGVMDKLPatqYFDYKSATNNTICNTNpynECRDVGMLVGLDDYVStNNGKDMLIMLHQMGNHGPAYFKRYDEQFAKFT 409
Cdd:COG2194 322 CKGVCDRVP---TIDLTADNLPPLCDGG---ECLDEVLLDGLDEALA-DLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 410 PVCEGNELAKCEHQSLINAYDNALLATDDFIAKSIDWLKTHEANYDVAMLYVSDHGESLGENGVYLHGMPNAFAPKEQRA 489
Cdd:COG2194 395 PTCDTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTH 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1905483320 490 VPAFFWSNNtTFKPT----------ASDTVLTHDAITPTLLKLFDVT 526
Cdd:COG2194 475 VPMIMWLSD-GYAQRygidfaclkaRADKPYSHDNLFHTLLGLLDVR 520
|
|
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
8-495 |
1.21e-139 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 414.46 E-value: 1.21e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 8 YRYSINPFVLMGLVAFFLAATANLTFFEKAMAVYPV--SDNLGFIVSMAVALMGAMLLIVVLLSYRYVLKPVLILLLIMG 85
Cdd:PRK11598 6 KRPSLNLLTFLLLAAFYITLCLNIAFYKQVLQLLPLdsLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACLFILVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 86 AVTSYFTDTYGTVYDTTMLQNAMQTDQAESKDLMNLAFFVRIIGLGVLPSLLVAVAKV-NYPTWGKSLIQRAMTWGVSLV 164
Cdd:PRK11598 86 AAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIrPATPRWRSVLFRLANILVSVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 165 LLLVPIGLFSSQYASFFRVHKPVrfyINPITPIYSVgkLASIEYKK----ATAPTDTIyhAKDAVQTTKPS-ERKPRLVV 239
Cdd:PRK11598 166 LILLVAALFYKDYASLFRNNKEL---VKSLTPSNSI--VASWSWYShqrlANLPLVRI--GEDAHKNPLMQnQKRKNLTI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 240 FVVGETARADHVQFNGYGRETFPQLAKvDGLANFSQVTSCGTSTAYSVPCMFSYLGQDDYDVDTAKYQENVLDTLDRLGV 319
Cdd:PRK11598 239 LVVGETSRAENFSLGGYPRETNPRLAK-DNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 320 GILWRDNNSDSKGVMDKLPATQYFDYKSatnNTICNTNpynECRDVGMLVGLDDYVSTNNGkDMLIMLHQMGNHGPAYFK 399
Cdd:PRK11598 318 NVLWNDNDGGCKGACDRVPHQDVTALNL---PGQCIDG---ECYDEVLFHGLENYINNLQG-DGVIVLHTIGSHGPTYYN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 400 RYDEQFAKFTPVCEGNELAKCEHQSLINAYDNALLATDDFIAKSIDWLKTHEANYDVAMLYVSDHGESLGENGVYLHGMP 479
Cdd:PRK11598 391 RYPPQFRKFTPTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLP 470
|
490
....*....|....*.
gi 1905483320 480 NAFAPKEQRAVPAFFW 495
Cdd:PRK11598 471 YAIAPDQQTHVPMLLW 486
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
234-526 |
2.13e-99 |
|
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: 302.23 E-value: 2.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 234 KPRLVVFVVGETARADHVQFNGYGRETFPQLAKV-DGLANFSQVTSCGTSTAYSVPCMFSYLGQDDYDvdTAKYQENVLD 312
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkKNLIVFDNVISCGTSTAVSLPCMLSFANRENYD--RAYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 313 TLDRLGVGILWRDNNSDSKGVMDKLPATQYFDYKSaTNNTICNtnpYNECRDVGMLVGLDDYVStNNGKDMLIMLHQMGN 392
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIAKIETVF-TNKGSCN---SSNCYDEALLPLLDEALA-DSSKKKLIVLHLMGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 393 HGPaYFKRYDEQFAKFTPVCEgNELAKCEHQSLINAYDNALLATDDFIAKSIDWLKthEANYDVAMLYVSDHGESLGENG 472
Cdd:cd16017 154 HGP-YYDRYPEEFAKFTPDCD-NELQSCSKEELINAYDNSILYTDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENG 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1905483320 473 VYLHGMPNafAPKEQRAVPAFFWSNNTTFKP-------TASDTVLTHDAITPTLLKLFDVT 526
Cdd:cd16017 230 LYLHGAPY--APKEQYHVPFIIWSSDSYKQRypverlrANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
236-525 |
1.05e-55 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 189.17 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 236 RLVVFVVGETARADHVQFNGYGRETFPQLAK-VDGLANFSQVTSCGTSTAYSVPCMFSYLGQDDYDVDT------AKYQE 308
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRlAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVstpvglPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 309 NVLDTLDRLGV--------GILWRDNNSDSKGVMDKL---PATQYFDYKSATNNTICntnPYNECRDVGMLVGLDDYVSt 377
Cdd:pfam00884 81 SLPDLLKRAGYntgaigkwHLGWYNNQSPCNLGFDKFfgrNTGSDLYADPPDVPYNC---SGGGVSDEALLDEALEFLD- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 378 NNGKDMLIMLHQMGNHGP-AYFKRYDEQFAKFTPVcegnelaKCEHQSLINAYDNALLATDDFIAKSIDWLKTHEANYDV 456
Cdd:pfam00884 157 NNDKPFFLVLHTLGSHGPpYYPDRYPEKYATFKPS-------SCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNT 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1905483320 457 AMLYVSDHGESLGENGVYLHGMPNAFAPKEQRAVPAFFWSNNTTFKPTASDTVLTHDAITPTLLKLFDV 525
Cdd:pfam00884 230 LVVYTSDHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
11-526 |
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: 619.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 11 SINPFVLMGLVAFFLAATANLTFFEKAMAVYPVSD-NLGFIVSMAVALMGAMLLIVVLLSYRYVLKPVLILLLIMGAVTS 89
Cdd:COG2194 6 RLSPLKLILLLALYFALFLNLPFWGRLLAILPLDGvNLLFLLSLPLLLLAALNLLLSLLAWRYLFKPLLILLLLISAAAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 90 YFTDTYGTVYDTTMLQNAMQTDQAESKDLMNLAFFVRIIGLGVLPSLLVAVAKVNYPTWGKSLIQRAMTWGVSLVLLLVP 169
Cdd:COG2194 86 YFMDFYGVVIDYGMIQNVLETDPAEASELLSPKLILWLLLLGVLPALLLWRVRIRYRPLLRELGQRLALLLLALLVIVLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 170 IGLFSSQYASFFRVHKPVRFYINPITPIYSVGKLASIEYKKATAPTDTIyhAKDAVQTtkPSERKPRLVVFVVGETARAD 249
Cdd:COG2194 166 ALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPL--GADAKLA--AAGAKPTLVVLVVGETARAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 250 HVQFNGYGRETFPQLAKVDGLANFSQVTSCGTSTAYSVPCMFSYLGQDDYDVDTAKYQENVLDTLDRLGVGILWRDNNSD 329
Cdd:COG2194 242 NFSLNGYARDTTPELAKEKNLVSFRDVTSCGTATAVSVPCMFSRLGRADYDPQRALNQENLLDVLQRAGVKVLWRDNQSG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 330 SKGVMDKLPatqYFDYKSATNNTICNTNpynECRDVGMLVGLDDYVStNNGKDMLIMLHQMGNHGPAYFKRYDEQFAKFT 409
Cdd:COG2194 322 CKGVCDRVP---TIDLTADNLPPLCDGG---ECLDEVLLDGLDEALA-DLAGDKLIVLHQMGSHGPAYYKRYPPEFRKFT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 410 PVCEGNELAKCEHQSLINAYDNALLATDDFIAKSIDWLKTHEANYDVAMLYVSDHGESLGENGVYLHGMPNAFAPKEQRA 489
Cdd:COG2194 395 PTCDTNDLQNCSREELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENGLYLHGTPYAIAPDEQTH 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1905483320 490 VPAFFWSNNtTFKPT----------ASDTVLTHDAITPTLLKLFDVT 526
Cdd:COG2194 475 VPMIMWLSD-GYAQRygidfaclkaRADKPYSHDNLFHTLLGLLDVR 520
|
|
| PRK11598 |
PRK11598 |
putative metal dependent hydrolase; Provisional |
8-495 |
1.21e-139 |
|
putative metal dependent hydrolase; Provisional
Pssm-ID: 183224 [Multi-domain] Cd Length: 545 Bit Score: 414.46 E-value: 1.21e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 8 YRYSINPFVLMGLVAFFLAATANLTFFEKAMAVYPV--SDNLGFIVSMAVALMGAMLLIVVLLSYRYVLKPVLILLLIMG 85
Cdd:PRK11598 6 KRPSLNLLTFLLLAAFYITLCLNIAFYKQVLQLLPLdsLHNVLVFASMPVVAFSVINIVFTLLSFPWLRRPLACLFILVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 86 AVTSYFTDTYGTVYDTTMLQNAMQTDQAESKDLMNLAFFVRIIGLGVLPSLLVAVAKV-NYPTWGKSLIQRAMTWGVSLV 164
Cdd:PRK11598 86 AAAQYFMMTYGIVIDRSMIQNIFETTPAESFALMTPQMLLWLGLSGVLPALIACWIKIrPATPRWRSVLFRLANILVSVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 165 LLLVPIGLFSSQYASFFRVHKPVrfyINPITPIYSVgkLASIEYKK----ATAPTDTIyhAKDAVQTTKPS-ERKPRLVV 239
Cdd:PRK11598 166 LILLVAALFYKDYASLFRNNKEL---VKSLTPSNSI--VASWSWYShqrlANLPLVRI--GEDAHKNPLMQnQKRKNLTI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 240 FVVGETARADHVQFNGYGRETFPQLAKvDGLANFSQVTSCGTSTAYSVPCMFSYLGQDDYDVDTAKYQENVLDTLDRLGV 319
Cdd:PRK11598 239 LVVGETSRAENFSLGGYPRETNPRLAK-DNVIYFPHTTSCGTATAVSVPCMFSNMPRKHYDEELAHHQEGLLDIIQRAGI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 320 GILWRDNNSDSKGVMDKLPATQYFDYKSatnNTICNTNpynECRDVGMLVGLDDYVSTNNGkDMLIMLHQMGNHGPAYFK 399
Cdd:PRK11598 318 NVLWNDNDGGCKGACDRVPHQDVTALNL---PGQCIDG---ECYDEVLFHGLENYINNLQG-DGVIVLHTIGSHGPTYYN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 400 RYDEQFAKFTPVCEGNELAKCEHQSLINAYDNALLATDDFIAKSIDWLKTHEANYDVAMLYVSDHGESLGENGVYLHGMP 479
Cdd:PRK11598 391 RYPPQFRKFTPTCDTNEIQTCTQQQLVNTYDNTILYVDYIVDKAINLLKQHQDKFNTSLVYLSDHGESLGENGIYLHGLP 470
|
490
....*....|....*.
gi 1905483320 480 NAFAPKEQRAVPAFFW 495
Cdd:PRK11598 471 YAIAPDQQTHVPMLLW 486
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
234-526 |
2.13e-99 |
|
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: 302.23 E-value: 2.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 234 KPRLVVFVVGETARADHVQFNGYGRETFPQLAKV-DGLANFSQVTSCGTSTAYSVPCMFSYLGQDDYDvdTAKYQENVLD 312
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkKNLIVFDNVISCGTSTAVSLPCMLSFANRENYD--RAYYQENLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 313 TLDRLGVGILWRDNNSDSKGVMDKLPATQYFDYKSaTNNTICNtnpYNECRDVGMLVGLDDYVStNNGKDMLIMLHQMGN 392
Cdd:cd16017 79 LAKKAGYKTYWISNQGGCGGYDTRISAIAKIETVF-TNKGSCN---SSNCYDEALLPLLDEALA-DSSKKKLIVLHLMGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 393 HGPaYFKRYDEQFAKFTPVCEgNELAKCEHQSLINAYDNALLATDDFIAKSIDWLKthEANYDVAMLYVSDHGESLGENG 472
Cdd:cd16017 154 HGP-YYDRYPEEFAKFTPDCD-NELQSCSKEELINAYDNSILYTDYVLSQIIERLK--KKDKDAALIYFSDHGESLGENG 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1905483320 473 VYLHGMPNafAPKEQRAVPAFFWSNNTTFKP-------TASDTVLTHDAITPTLLKLFDVT 526
Cdd:cd16017 230 LYLHGAPY--APKEQYHVPFIIWSSDSYKQRypverlrANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| PRK09598 |
PRK09598 |
phosphoethanolamine--lipid A transferase EptA; |
24-525 |
6.00e-78 |
|
phosphoethanolamine--lipid A transferase EptA;
Pssm-ID: 236581 [Multi-domain] Cd Length: 522 Bit Score: 254.32 E-value: 6.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 24 FLAATANLTFFEKAMAVYPV--SDNLGFIVSMAVALM---GAMLLIVVLLSyRYVLKPVLILLLIMGAVTSYFTDTYGTV 98
Cdd:PRK09598 20 LLYSLLNGVLYHFPLFAYVYkeSNQVSFIAMLVVLLFcvnGLLFLLLGLLS-RRLMRLSAIVFSLLNSIAFYFINTYKVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 99 YDTTMLQNAMQTDQAESKDLMNLAFFVRIIGLGVLPSLLVAVAKVNYptwgKSLIQRAMTWGVSLVLLLVPIglFSSQyA 178
Cdd:PRK09598 99 LNKSMMGNVLNTNTAESSGFLSVKLFIYIVVLGVLPGYIIYKIPLKN----SSKKAPFAAILALVLIFLASA--FANS-K 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 179 SFFRVHKPVRFYINPITPIYSVGKLASIEYKKATAPTDTIYHAkDAvqttKPSERKPRLVVFVVGETARADHVQFNGYGR 258
Cdd:PRK09598 172 NWLWFDKHAKFLGGLILPWSYSVNTFRVSAHKFFAPTIKPLLP-PL----FSPNHSKSVVVLVIGESARKHNYALYGYEK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 259 ETFPQLAK---VDGLANFSqVTSCGTSTAYSVPCMFSYLGQDDYDVDtakyqENVLDTLDRLGVGILWRDNNSDSKGVmd 335
Cdd:PRK09598 247 PTNPRLSKrlaTHELTLFN-ATSCATYTTASLECILDSSFKNTSNAY-----ENLPTYLTRAGIKVFWRSANDGEPNV-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 336 klPATQYFDYKSATNNTICNTNPYNECrdvgMLVGLDDYVSTNNGKDMLIMLHQMGNHGPAYFKRYDEQFAKFTPVCEGN 415
Cdd:PRK09598 319 --KVTSYLKNYELIQKCPNCEAPYDES----LLYNLPELIKASSNENVLLILHLAGSHGPNYDNKYPLNFRVFKPVCSSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 416 ELAKCEHQSLINAYDNALLATDDFIAKSIDWLKthEANYDVAMLYVSDHGESLGENGVYLHGMPNAFAPKEQRAVPAFFW 495
Cdd:PRK09598 393 ELSSCSKESLINAYDNTIFYNDYLLDKIISMLK--NLKQPALMIYLSDHGESLGEGAFYLHGIPKSIAPKEQYEIPFIVW 470
|
490 500 510
....*....|....*....|....*....|...
gi 1905483320 496 SNNTTFK---PTASDTVLTHDAITPTLLKLFDV 525
Cdd:PRK09598 471 ASDSFKKqhsIIQTQTPINQNVIFHSVLGVFDF 503
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
236-525 |
1.05e-55 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 189.17 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 236 RLVVFVVGETARADHVQFNGYGRETFPQLAK-VDGLANFSQVTSCGTSTAYSVPCMFSYLGQDDYDVDT------AKYQE 308
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRlAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVstpvglPRTEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 309 NVLDTLDRLGV--------GILWRDNNSDSKGVMDKL---PATQYFDYKSATNNTICntnPYNECRDVGMLVGLDDYVSt 377
Cdd:pfam00884 81 SLPDLLKRAGYntgaigkwHLGWYNNQSPCNLGFDKFfgrNTGSDLYADPPDVPYNC---SGGGVSDEALLDEALEFLD- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 378 NNGKDMLIMLHQMGNHGP-AYFKRYDEQFAKFTPVcegnelaKCEHQSLINAYDNALLATDDFIAKSIDWLKTHEANYDV 456
Cdd:pfam00884 157 NNDKPFFLVLHTLGSHGPpYYPDRYPEKYATFKPS-------SCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNT 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1905483320 457 AMLYVSDHGESLGENGVYLHGMPNAFAPKEQRAVPAFFWSNNTTFKPTASDTVLTHDAITPTLLKLFDV 525
Cdd:pfam00884 230 LVVYTSDHGESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| EptA_B_N |
pfam08019 |
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ... |
57-205 |
3.76e-52 |
|
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: 174.63 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 57 LMGAMLLIVVLLSYRYVLKPVLILLLIMGAVTSYFTDTYGTVYDTTMLQNAMQTDQAESKDLMNLAFFVRIIGLGVLPSL 136
Cdd:pfam08019 1 LFAALNLLLSLLSWRYLLKPLLILLLLLSAAASYFMDTYGVVIDRDMIQNVLETDVAEASDLLSPKLLLYLLLLGVLPAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1905483320 137 LVAVAKVNYPTWGKSLIQRAMTWGVSLVLLLVPIGLFSSQYASFFRVHKPVRFYINPITPIYSVGKLAS 205
Cdd:pfam08019 81 LLWRVRIRYRPWLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKYAK 149
|
|
| PRK11560 |
PRK11560 |
kdo(2)-lipid A phosphoethanolamine 7''-transferase; |
20-495 |
1.85e-44 |
|
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
Pssm-ID: 183198 [Multi-domain] Cd Length: 558 Bit Score: 165.21 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 20 LVAFFLAATANLTFFEKAMAVYPVSDNLGFIVSMAVALMGAMLL---IVVLLSY--RYVLKPVLILLLIMGAVTSYFTDT 94
Cdd:PRK11560 15 LLAVYIGLFLNIAVFYRRFDSYAQDFTVWKGLSAVVELAATVLVtffLLRLLSLfgRRFWRVLASLLVLFSAAASYYMTF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 95 YGTVYDTTMLQNAMQTDQAESKDLMNLAFFVRIIGLGVLPSLLVAVAKVNYPTWG-----KSLIQRAMTWGVSLVLLLVP 169
Cdd:PRK11560 95 FNVVIGYGIIASVMTTDIDLSKEVVGLHFILWLVAVSALPLILIWNNRCRYTLLRqlrtpGQRIRSLAVVVLAGLLVWAP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 170 IGLFSSQYASFFR---VHKP-----VRFYINPITPIYSVGKLASIEYKKATAPTDTIYHAKDAVQTTkPSERKPRLVVFV 241
Cdd:PRK11560 175 IRLLDIQQKKVERatgVDLPsyggvVANSYLPSNWLSALGLYAWAQVDESSDNNSLLNPAKKFTYQA-PKGVDDTYVVFI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 242 VGETARADHVQFNGYGRETFPQLAKVDGLANFsQVTSCGTSTAYSVPCMFSYL-GQDDYDVDTAKYQeNVLDTLDRLGVg 320
Cdd:PRK11560 254 IGETTRWDHMGILGYERNTTPKLAQEKNLAAF-RGYSCDTATKLSLRCMFVREgGAEDNPQRTLKEQ-NVFAVLKQLGF- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 321 ilwrdnNSDskgvmdkLPATQ---YFdYksatNNTICNTNPYNEC-----RDVG-----MLV------GLDDYvstNNGK 381
Cdd:PRK11560 331 ------SSE-------LFAMQsemWF-Y----NNTMADNYAYREQigaepRNRGkpvddMLLvdemkqSLGRN---PDGK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 382 DmLIMLHQMGNHGpAYFKRYDEQFAKFTPVCEGNElAKCEHQSLINAYDNALLATDDFIAKSIDWLKTHEAnydvAMLYV 461
Cdd:PRK11560 390 H-LIILHTKGSHY-NYTQRYPRSFARYQPECIGVD-SGCSKAQLINSYDNSVLYVDHFISSVIDQLRDKKA----IVFYA 462
|
490 500 510
....*....|....*....|....*....|....
gi 1905483320 462 SDHGESLGENGvYLHGMPNAFAPKEQRAVPAFFW 495
Cdd:PRK11560 463 ADHGESINERE-HLHGTPREMAPPEQFRVPMMVW 495
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
15-525 |
2.57e-13 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 72.38 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 15 FVLMGLVAFFLAATanLTFFEKAMAVYPVSDNLGFIVSMAVALMGAMLLIVVLLSYRYVLKP---------VLILLLIMG 85
Cdd:COG1368 1 FFLLFLLLLSLRLV--FLLFNFDLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPklrwiylllVLLLLLLLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 86 AVTSYFTDTYGTVYDTTMLQNAMQTDQAeSKDLMNLAFFVRIIGLGVLPSLLVAVAKVNYPTWGK-SLIQRAMTWGVSLV 164
Cdd:COG1368 79 VADILYYRFFGDRLNFSDLDYLGDTGEV-LGSLLSSYDLLLLLDLLLLLLLLLLLYRLLKKLRKSlPWRKRLALLLLLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 165 LLLVPIGLFSSQYASFFRVHKPVRFYIN-PITPIYSVGKLASIEYKKATAPTDTIYHAKDAVQTTKPSER-----KPRLV 238
Cdd:COG1368 158 LLLLGIRLGEDRPLNLSDAFSRNNFVNElGLNGPYSFYDALRNNKAPATYSEEEALEIKKYLKSNRPTPNpfgpaKKPNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 239 VFVVGETARADHVQFNGYGRETFPQLakvDGLAN----FSQVTSCGTSTAYSVPCMF-SYLGQDDYDVdtakYQENVLDT 313
Cdd:COG1368 238 VVILLESFSDFFIGALGNGKDVTPFL---DSLAKeslyFGNFYSQGGRTSRGEFAVLtGLPPLPGGSP----YKRPGQNN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 314 LDRLGvGILwRDNNSDS-------------KGVMDKLPATQYFDYKSatnnticntnpYNECRDVGMlvGLDDYVSTNNG 380
Cdd:COG1368 311 FPSLP-SIL-KKQGYETsffhggdgsfwnrDSFYKNLGFDEFYDRED-----------FDDPFDGGW--GVSDEDLFDKA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 381 KDMLIMLHQ--------MGNHGPayFKrYDEQFAKFTPvcegnelakcEHQSLINAYDNALLATDDFIAKSIDWLKTHEA 452
Cdd:COG1368 376 LEELEKLKKpffaflitLSNHGP--YT-LPEEDKKIPD----------YGKTTLNNYLNAVRYADQALGEFIEKLKKSGW 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1905483320 453 NYDVAMLYVSDHGESLGENGVYLHgmpnafaPKEQRAVPAFFWSNNTTfKPTASDTVLTHDAITPTLLKLFDV 525
Cdd:COG1368 443 YDNTIFVIYGDHGPRSPGKTDYEN-------PLERYRVPLLIYSPGLK-KPKVIDTVGSQIDIAPTLLDLLGI 507
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
238-527 |
1.94e-11 |
|
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: 64.49 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 238 VVFVVGETARADHVQFNGYGRETFPQLakvDGLAN----FSQVTSCGTSTAYSVPCMFSylGQD--DYDVDTAKYQENVl 311
Cdd:cd16148 3 VILIVIDSLRADHLGCYGYDRVTTPNL---DRLAAegvvFDNHYSGSNPTLPSRFSLFT--GLYpfYHGVWGGPLEPDD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 312 DTL-DRLgvgilwRDNNSDSKGVMDKLPATQYFDY--------KSATNNTICNTNPYNECRDVgMLVGLDdYVSTN-NGK 381
Cdd:cd16148 77 PTLaEIL------RKAGYYTAAVSSNPHLFGGPGFdrgfdtfeDFRGQEGDPGEEGDERAERV-TDRALE-WLDRNaDDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 382 DMLIMLHQMGNHGPayfkrYdeqfakftpvcegnelakcehqslinAYDNALLATDDFIAKSIDWLKTHEAnYDVAMLYV 461
Cdd:cd16148 149 PFFLFLHYFDPHEP-----Y--------------------------LYDAEVRYVDEQIGRLLDKLKELGL-LEDTLVIV 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905483320 462 -SDHGESLGENGVYL-HGMPnafAPKEQRAVPAFFWSNNTTFKPTASDTVLTHDaITPTLLKLFDVTA 527
Cdd:cd16148 197 tSDHGEEFGEHGLYWgHGSN---LYDEQLHVPLIIRWPGKEPGKRVDALVSHID-IAPTLLDLLGVEP 260
|
|
| PRK10649 |
PRK10649 |
phosphoethanolamine transferase CptA; |
234-466 |
2.29e-08 |
|
phosphoethanolamine transferase CptA;
Pssm-ID: 182617 [Multi-domain] Cd Length: 577 Bit Score: 56.64 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 234 KPRLVVFVVGETARADHVQFNGYGRETFPQLAKV----DGLANFSQVTscgTSTAYSVPCM-----FSYLGQDDyDVDTa 304
Cdd:PRK10649 235 APRTLVLVIGESTQRGRMSLYGYPRETTPELDALhktdPGLTVFNNVV---TSRPYTIEILqqaltFADEKNPD-LYLT- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 305 kyQENVLDTLDRLGVGILWRDNNsdsKGVMDKLPATQYFDyKSATNNTICNTNPYNECR--DVGMLVGLDDyVSTNNGKD 382
Cdd:PRK10649 310 --QPSLMNMMKQAGYKTFWITNQ---QTMTARNTMLTVFS-RQTDKQYYMNQQRTQNAReyDTNVLKPFSE-VLADPAPK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 383 MLIMLHQMGNHgPAYFKRYDEQFAKFT-------PVCEGNELakcehqSLINAYDNALLATDDFIAKSIDWLKTHEANyd 455
Cdd:PRK10649 383 KFIIVHLLGTH-IKYKYRYPENQGKFDdrtghvpPGLNADEL------ESYNDYDNANLYNDHVVASLIKDFKATDPN-- 453
|
250
....*....|.
gi 1905483320 456 VAMLYVSDHGE 466
Cdd:PRK10649 454 GFLVYFSDHGE 464
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
238-523 |
3.28e-06 |
|
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: 48.57 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 238 VVFVVGETARADHVQFNGYGRETFPQLAKVD---GLANFSQVTScGTSTAYSVPCMFSYLGQDDYDVdtakYQENVLDTL 314
Cdd:cd00016 3 VVLIVLDGLGADDLGKAGNPAPTTPNLKRLAsegATFNFRSVSP-PTSSAPNHAALLTGAYPTLHGY----TGNGSADPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 315 DRLGVGILWRDNNSdskgVMDKLPATQYfdyksatnnticntnpynecrDVGMlVGLDDYVS-TNNGKDMLIMLHQMGNH 393
Cdd:cd00016 78 LPSRAAGKDEDGPT----IPELLKQAGY---------------------RTGV-IGLLKAIDeTSKEKPFVLFLHFDGPD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 394 GPAYfkrydeQFAKFTPVcegnelakcehqslinaYDNALLATDDFIAKSIDWLKTHEANYDVAMLYVSDHGESLGENGV 473
Cdd:cd00016 132 GPGH------AYGPNTPE-----------------YYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGG 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1905483320 474 YLHGMPNAFAPKEQRAVPAFFWSNNtTFKPTASDTVLTHDAITPTLLKLF 523
Cdd:cd00016 189 DPKADGKADKSHTGMRVPFIAYGPG-VKKGGVKHELISQYDIAPTLADLL 237
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
371-524 |
8.68e-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: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 371 LDDYVSTNNGKDMLIMLHqMGNHGPayFKRYDEQFAKFTPVCEGNELakcehqslINAYDNALLATDDFIAKSIDWLKTH 450
Cdd:cd16015 147 LEELEELKKKPFFIFLVT-MSNHGP--YDLPEEKKDEPLKVEEDKTE--------LENYLNAIHYTDKALGEFIEKLKKS 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1905483320 451 EANYDVAMLYVSDHGESLGENGVYlhgmpNAFAPKEQRAVPAFFWSNNTTfKPTASDTVLTHDAITPTLLKLFD 524
Cdd:cd16015 216 GLYENTIIVIYGDHLPSLGSDYDE-----TDEDPLDLYRTPLLIYSPGLK-KPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
437-530 |
3.64e-05 |
|
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; 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: 293775 [Multi-domain] Cd Length: 468 Bit Score: 46.22 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 437 DDFIAKSIDWLKthEANYDVAMLYVSDHGESLGENGVYLHGmPNAFapKEQRAVPAFFWSNNTTFKPTASDTVLTHDAIT 516
Cdd:cd16156 251 DYEIGRVLDAAD--EIAEDAWVIYTSDHGDMLGAHKLWAKG-PAVY--DEITNIPLIIRGKGGEKAGTVTDTPVSHIDLA 325
|
90
....*....|....
gi 1905483320 517 PTLLKLFDVTAGKV 530
Cdd:cd16156 326 PTILDYAGIPQPKV 339
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
373-527 |
2.57e-04 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 43.33 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 373 DYVSTNNGKD--MLIMLHQMGNHGP-----AYFKRYDEQFAKFTPVCEGNELAKCEHQSLINAYDNALLATDDFIAKSID 445
Cdd:COG3119 139 DFLERQADKDkpFFLYLAFNAPHAPyqapeEYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLD 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 446 WLKthEANYD----VamLYVSDHGESLGENG-------VYLHGMpnafapkeqrAVPAFFWSNNTTFKPTASDT-VLTHD 513
Cdd:COG3119 219 ALE--ELGLAdntiV--VFTSDNGPSLGEHGlrggkgtLYEGGI----------RVPLIVRWPGKIKAGSVSDAlVSLID 284
|
170
....*....|....
gi 1905483320 514 aITPTLLKLFDVTA 527
Cdd:COG3119 285 -LLPTLLDLAGVPI 297
|
|
| 7tm_GPCRs |
cd14964 |
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ... |
15-188 |
4.55e-03 |
|
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.
Pssm-ID: 410628 [Multi-domain] Cd Length: 267 Bit Score: 38.95 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 15 FVLMGLV-AFFLAATANLTFFEKAMAVYPVSDNLGFIVSMAVALMGAMLLIVVLLSYRYVLKPVLILLLIMGA-VTSYFT 92
Cdd:cd14964 9 TCLGLLGnLLVLLSLVRLRKRPRSTRLLLASLAACDLLASLVVLVLFFLLGLTEASSRPQALCYLIYLLWYGAnLASIWT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905483320 93 DTYGTVYDTTMLQNA--MQTDQAESKDLMNLAFFVRIIGLGVLPSLLVAVAKVNYPTWGKSLI----QRAMTWGVSLVLL 166
Cdd:cd14964 89 TLVLTYHRYFALCGPlkYTRLSSPGKTRVIILGCWGVSLLLSIPPLVGKGAIPRYNTLTGSCYlictTIYLTWGFLLVSF 168
|
170 180
....*....|....*....|..
gi 1905483320 167 LVPIGLFSsqYASFFRVHKPVR 188
Cdd:cd14964 169 LLPLVAFL--VIFSRIVLRLRR 188
|
|
| |
