|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02525 |
PLN02525 |
phosphatidic acid phosphatase family protein |
72-416 |
0e+00 |
|
phosphatidic acid phosphatase family protein
Pssm-ID: 215288 Cd Length: 352 Bit Score: 676.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 72 FFSGLSCVVSVPFYTAFLPLLFWSGHGRLARQMTLLIAFCDYLGNCIKDVVSAPRPSCPPVRRITATKDEEDNAMEYGLP 151
Cdd:PLN02525 8 FFSGLSCVVSVPFYTAFLPLLFWSGHGKLARQMTLLMAFCDYVGNCIKDVVSAPRPSCPPVRRVTATKDEEENAMEYGLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 152 SSHTLNTVCLSGYLLHYVLSSLEYESVSIQYYGFALACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGLWLTVNEKL 231
Cdd:PLN02525 88 SSHTLNTVCLSGYLLHYVLSYLQNVDASVIFAGLALFCLLVALVGFGRLYLGMHSPIDIIAGLAIGLVILAFWLTVDEYV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 232 DDFITSKQNVSSFWTALSFLLLFAYPTPEHPTPSYEYHTAFNGVTLGIVTGVQQTYSQFHHEAAPRIFSPELPISSYLGR 311
Cdd:PLN02525 168 DAFITSGQNVTPFWAALSFLLLFAYPTPEFPTPSFEYHTAFNGVAFGIVAGVQQTYSQFHHEAAPRIFSPQLPIAAFLGR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 312 VMVGIPTILLVKFCSKSLAKWTLPMVSNALGIPIRSSMYIPKLKGYASGKKTDEPKNSVGYLQKLCEFLSHDSFDIDTGI 391
Cdd:PLN02525 248 VAVGIPTILAVKFCSKALAKWLLPVVCNALGIPIRSTSYVPSLKGSVSGKKSDEPKQSVGYLQKLCFFSSQDSFDVDTGI 327
|
330 340
....*....|....*....|....*
gi 15231046 392 RFFQYAGLAWSVVDLVPSLFSYVNL 416
Cdd:PLN02525 328 RFLQYAGLAWSVVDLVPSIFSYLNL 352
|
|
| PAP2_SPPase1 |
cd03388 |
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ... |
69-225 |
2.15e-58 |
|
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an intracellular enzyme located in the endoplasmic reticulum, which regulates the level of sphingosine-1-phosphate (S1P), a bioactive lipid. S1P acts as a second messenger in the cell, and extracellularly by binding to G-protein coupled receptors of the endothelial differentiation gene family.
Pssm-ID: 239482 Cd Length: 151 Bit Score: 187.82 E-value: 2.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 69 LDAFFSGLSCVVSVPFYTAFLPLLFWSGHGRLARQMTLLIAFCDYLGNCIKDVVSAPRPSCPPVRRITATKdeedNAMEY 148
Cdd:cd03388 3 LDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSS----AALEY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231046 149 GLPSSHTLNTVCLSGYLLHYVLSSLEYesvsIQYYGFALACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGLWL 225
Cdd:cd03388 79 GFPSTHAMNATAISFYLLIYLYDRYQY----PFVLGLILALFYSTLVCLSRIYMGMHSVLDVIAGSLIGVLILLFRF 151
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
108-224 |
1.89e-12 |
|
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.
Pssm-ID: 426329 [Multi-domain] Cd Length: 124 Bit Score: 63.98 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 108 IAFCDYLGNCIKDVVSAPRPSCPPVRRITATKDEEDNAMEYGLPSSHTLNTVCLSGYLLHYVLSSLEYESVSIqyygFAL 187
Cdd:pfam01569 6 LALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLL----ALL 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 15231046 188 ACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGLW 224
Cdd:pfam01569 82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLV 118
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
69-227 |
2.91e-10 |
|
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 440435 [Multi-domain] Cd Length: 189 Bit Score: 59.28 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 69 LDAFFSGLSCVVSVPFYTAFLPLLFWSGHGRLARQMTLLIAFCDYLGNC------IKDVVSAPRPSCPPVRRITATkdee 142
Cdd:COG0671 37 LLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLllllllLKYLFGRPRPFVVPDLELLLG---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 143 dNAMEYGLPSSHTLNTVCLSGYLLHYVLssleyesvsiQYYGFALACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILG 222
Cdd:COG0671 113 -TAGGYSFPSGHAAAAFALALVLALLLP----------RRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIAL 181
|
....*
gi 15231046 223 LWLTV 227
Cdd:COG0671 182 LLLAL 186
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
106-220 |
1.00e-08 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 53.12 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 106 LLIAFCDYLGNCIKDVVSAPRP-SCPPVRRITATKDEEDNAMEYGLPSSHTLNTVCLSGYLLHYVLSSLEYESVSIQYYg 184
Cdd:smart00014 2 LLAVVSQLFNGVIKNYFGRPRPfFLSIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLLIFLLL- 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 15231046 185 falacLLVALIAFGRVYLGMHSVVDIVSGLAIGVLI 220
Cdd:smart00014 81 -----LLALVVGFSRVYLGAHWPSDVLAGSLLGILI 111
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02525 |
PLN02525 |
phosphatidic acid phosphatase family protein |
72-416 |
0e+00 |
|
phosphatidic acid phosphatase family protein
Pssm-ID: 215288 Cd Length: 352 Bit Score: 676.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 72 FFSGLSCVVSVPFYTAFLPLLFWSGHGRLARQMTLLIAFCDYLGNCIKDVVSAPRPSCPPVRRITATKDEEDNAMEYGLP 151
Cdd:PLN02525 8 FFSGLSCVVSVPFYTAFLPLLFWSGHGKLARQMTLLMAFCDYVGNCIKDVVSAPRPSCPPVRRVTATKDEEENAMEYGLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 152 SSHTLNTVCLSGYLLHYVLSSLEYESVSIQYYGFALACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGLWLTVNEKL 231
Cdd:PLN02525 88 SSHTLNTVCLSGYLLHYVLSYLQNVDASVIFAGLALFCLLVALVGFGRLYLGMHSPIDIIAGLAIGLVILAFWLTVDEYV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 232 DDFITSKQNVSSFWTALSFLLLFAYPTPEHPTPSYEYHTAFNGVTLGIVTGVQQTYSQFHHEAAPRIFSPELPISSYLGR 311
Cdd:PLN02525 168 DAFITSGQNVTPFWAALSFLLLFAYPTPEFPTPSFEYHTAFNGVAFGIVAGVQQTYSQFHHEAAPRIFSPQLPIAAFLGR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 312 VMVGIPTILLVKFCSKSLAKWTLPMVSNALGIPIRSSMYIPKLKGYASGKKTDEPKNSVGYLQKLCEFLSHDSFDIDTGI 391
Cdd:PLN02525 248 VAVGIPTILAVKFCSKALAKWLLPVVCNALGIPIRSTSYVPSLKGSVSGKKSDEPKQSVGYLQKLCFFSSQDSFDVDTGI 327
|
330 340
....*....|....*....|....*
gi 15231046 392 RFFQYAGLAWSVVDLVPSLFSYVNL 416
Cdd:PLN02525 328 RFLQYAGLAWSVVDLVPSIFSYLNL 352
|
|
| PAP2_SPPase1 |
cd03388 |
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ... |
69-225 |
2.15e-58 |
|
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an intracellular enzyme located in the endoplasmic reticulum, which regulates the level of sphingosine-1-phosphate (S1P), a bioactive lipid. S1P acts as a second messenger in the cell, and extracellularly by binding to G-protein coupled receptors of the endothelial differentiation gene family.
Pssm-ID: 239482 Cd Length: 151 Bit Score: 187.82 E-value: 2.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 69 LDAFFSGLSCVVSVPFYTAFLPLLFWSGHGRLARQMTLLIAFCDYLGNCIKDVVSAPRPSCPPVRRITATKdeedNAMEY 148
Cdd:cd03388 3 LDYYFAFTALLGTHTFYILFLPFLFWNGDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPSSPPVVRLTMSS----AALEY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231046 149 GLPSSHTLNTVCLSGYLLHYVLSSLEYesvsIQYYGFALACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGLWL 225
Cdd:cd03388 79 GFPSTHAMNATAISFYLLIYLYDRYQY----PFVLGLILALFYSTLVCLSRIYMGMHSVLDVIAGSLIGVLILLFRF 151
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
99-225 |
2.47e-14 |
|
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.
Pssm-ID: 238813 [Multi-domain] Cd Length: 122 Bit Score: 69.03 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 99 RLARQMTLLIAFCDYLGNCIKDVVSAPRPSCPPVRRITATKDEEDNAmEYGLPSSHTLNTVCLSGYLLHYVLSSLeyesv 178
Cdd:cd01610 3 LLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLLLTEG-GYSFPSGHAAFAFALALFLALLLPRRL----- 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15231046 179 sIQYYGFALACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGLWL 225
Cdd:cd01610 77 -LRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
108-224 |
1.89e-12 |
|
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.
Pssm-ID: 426329 [Multi-domain] Cd Length: 124 Bit Score: 63.98 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 108 IAFCDYLGNCIKDVVSAPRPSCPPVRRITATKDEEDNAMEYGLPSSHTLNTVCLSGYLLHYVLSSLEYESVSIqyygFAL 187
Cdd:pfam01569 6 LALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLL----ALL 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 15231046 188 ACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGLW 224
Cdd:pfam01569 82 LLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLV 118
|
|
| PAP2_like_3 |
cd03393 |
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
87-223 |
9.39e-12 |
|
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria and archaea, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239487 [Multi-domain] Cd Length: 125 Bit Score: 62.00 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 87 AFLPLLFWSGHGRLARQMTLLIAFCDYLGNCIKDVVSAPRPSCPPVRRITATKDEEDnameYGLPSSHT-LNTVCLSGYL 165
Cdd:cd03393 1 IVLSLIYWLVDKRLGRYLGLALCASGYLNAALKEVFKIPRPFTYDGIQAIYEESAGG----YGFPSGHAqTSATFWGSLM 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231046 166 LHYVLSSLEYesvsiqyygfaLACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGL 223
Cdd:cd03393 77 LHVRKKWFTL-----------IGVVLVVLISFSRLYLGVHWPSDVIGGVLIGLLVLVL 123
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
56-231 |
8.38e-11 |
|
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239486 Cd Length: 182 Bit Score: 60.70 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 56 PLILRIQKCQNGVLDAFFSGL----SCVVSVPFYTAFLPLLFWSGHGRLARQMTLLIAFCDYLGNCIKDVVSAPRPSCPP 131
Cdd:cd03392 15 SVLSLLRSLRTPLLTAFMTAItflgSPAVLLIIVLLLALLLLLKRRRRAALFLLLALLGGGALNTLLKLLVQRPRPPLHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 132 VRRITAtkdeednameYGLPSSHTLNTVCLSGYLLhyVLSSLEYESVSIQYYGFALACLLVALIAFGRVYLGMHSVVDIV 211
Cdd:cd03392 95 LVPEGG----------YSFPSGHAMGATVLYGFLA--YLLARRLPRRRVRILLLILAAILILLVGLSRLYLGVHYPSDVL 162
|
170 180
....*....|....*....|
gi 15231046 212 SGLAIGVLILGLWLTVNEKL 231
Cdd:cd03392 163 AGWLLGLAWLALLILLYRRL 182
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
69-227 |
2.91e-10 |
|
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 440435 [Multi-domain] Cd Length: 189 Bit Score: 59.28 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 69 LDAFFSGLSCVVSVPFYTAFLPLLFWSGHGRLARQMTLLIAFCDYLGNC------IKDVVSAPRPSCPPVRRITATkdee 142
Cdd:COG0671 37 LLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLllllllLKYLFGRPRPFVVPDLELLLG---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 143 dNAMEYGLPSSHTLNTVCLSGYLLHYVLssleyesvsiQYYGFALACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILG 222
Cdd:COG0671 113 -TAGGYSFPSGHAAAAFALALVLALLLP----------RRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIAL 181
|
....*
gi 15231046 223 LWLTV 227
Cdd:COG0671 182 LLLAL 186
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
106-220 |
1.00e-08 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 53.12 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 106 LLIAFCDYLGNCIKDVVSAPRP-SCPPVRRITATKDEEDNAMEYGLPSSHTLNTVCLSGYLLHYVLSSLEYESVSIQYYg 184
Cdd:smart00014 2 LLAVVSQLFNGVIKNYFGRPRPfFLSIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRKLLIFLLL- 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 15231046 185 falacLLVALIAFGRVYLGMHSVVDIVSGLAIGVLI 220
Cdd:smart00014 81 -----LLALVVGFSRVYLGAHWPSDVLAGSLLGILI 111
|
|
| PAP2_like_4 |
cd03395 |
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
69-220 |
4.82e-08 |
|
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239489 Cd Length: 177 Bit Score: 52.65 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 69 LDAFFSGLSCVV-SVPF-YTAFLPLLFWSGHGRLAR--QMTLLIAFCDYL-GNCIKDVVSAPRPSCPPVRRITATKDEED 143
Cdd:cd03395 22 LDDLMPFLTGKKlSVPIfLLLALFILFRKGPIGLLIllLVLLAVGFADQLaSGFLKPLVARLRPCNALDGVRLVVLGDQG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 144 naMEYGLPSSHTLN--TVCLSGYLLHYvlssleyesvsiqYYGFALACLLVA-LIAFGRVYLGMHSVVDIVSGLAIGVLI 220
Cdd:cd03395 102 --GSYSFASSHAANsfALALFIWLFFR-------------RGLFSPVLLLWAlLVGYSRVYVGVHYPGDVIAGALIGIIS 166
|
|
| PAP2_dolichyldiphosphatase |
cd03382 |
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ... |
85-224 |
7.30e-07 |
|
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a membrane-associated protein located in the endoplasmic reticulum and hydrolyzes dolichyl pyrophosphate, as well as dolichylmonophosphate at a low rate. The enzyme is necessary for maintaining proper levels of dolichol-linked oligosaccharides and protein N-glycosylation, and might play a role in re-utilization of the glycosyl carrier lipid for additional rounds of lipid intermediate biosynthesis after its release during protein N-glycosylation reactions.
Pssm-ID: 239477 Cd Length: 159 Bit Score: 48.81 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231046 85 YTAFLP---LLFWSGHGRLARQMTLLIAF-----CDYLGNCIKDVVSAPRPSCPPVRRITatkdeednamEYGLPSSHTL 156
Cdd:cd03382 20 YLSLLPvaiLVGYATLILFRRELEAIYLFigllaNEALNYVLKRIIKEPRPCSGAYFVRS----------GYGMPSSHSQ 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231046 157 NTVCLSGYLLHYVLSSLEYESVSIQYYGFALACLLVA-LIAFGRVYLGMHSVVDIVSGLAIGVLILGLW 224
Cdd:cd03382 90 FMGFFAVYLLLFIYLRLGRLNSLVSRFLLSLGLLLLAlLVSYSRVYLGYHTVSQVVVGAIVGILLGILW 158
|
|
| PAP2_BcrC_like |
cd03385 |
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ... |
151-223 |
4.36e-03 |
|
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as bacitracin transport permeases, as it was suspected that they form the permease component of an ABC transporter system. It was shown, however, that BcrC from Bacillus subtilis posesses undecaprenyl pyrophosphate (UPP) phospatase activity, and it is hypothesized that it competes with bacitracin for UPP, increasing the cell's resistance to bacitracin.
Pssm-ID: 239480 Cd Length: 144 Bit Score: 37.24 E-value: 4.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231046 151 PSSHTLN--TVCLSGYLLHYVLSSLeyesvsiqyygfaLACLLVALIAFGRVYLGMHSVVDIVSGLAIGVLILGL 223
Cdd:cd03385 80 PSDHTTLffSIAFSLLLRRRKWAGW-------------ILLILALLVAWSRIYLGVHYPLDMLGAALVAVLSALL 141
|
|
| |
