|
Name |
Accession |
Description |
Interval |
E-value |
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
45-215 |
4.31e-58 |
|
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. Most likely membrane-associated phosphatidic acid phosphatases. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity, they may have a more generic housekeeping role in lipid metabolism.
Pssm-ID: 239484 [Multi-domain] Cd Length: 193 Bit Score: 182.80 E-value: 4.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 45 VNVLYPYRDS-TFSEAVAGIVIYASTILIIIAFQIK-RLSFKHTIFTFIGLGASVTTWLMFVQGGKIYAGRPRPNMYALV 122
Cdd:cd03390 1 PSISYPFAESeTVPTWLLVIISVGIPLLVIILISLFfRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 123 AQGKE--------------------KDAWKSFPSGHSAASFCGYTYLSLYIAGELRIFSDRPELWRMIPVIIPMFLAGII 182
Cdd:cd03390 81 FPDGGtpsdtlvgidicctgdpgvlKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILV 160
|
170 180 190
....*....|....*....|....*....|...
gi 56466456 183 VLTRTRDYYHNFSDVLAGSIIGILSACIGYFSK 215
Cdd:cd03390 161 AVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PLN02715 |
PLN02715 |
lipid phosphate phosphatase |
14-212 |
1.25e-26 |
|
lipid phosphate phosphatase
Pssm-ID: 178317 [Multi-domain] Cd Length: 327 Bit Score: 105.14 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 14 DIIYIIVTGAVAAVLTFIDGFHMEVpGGENNVNVLYPYRDSTFSeaVAGIVIYAS--TILIIIAFQIKRLSFKHTIFTFI 91
Cdd:PLN02715 50 DWIILVILIAIEIGLNLISPFYRYV-GKDMMTDLKYPFKDNTVP--IWSVPVYAVllPIILFVCFYLKRRCVYDLHHSIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 92 GLGASVTTWLMFVQGGKIYAGRPRPNMY---------------ALVAQGKE---KDAWKSFPSGHSAASFCGYTYLSLYI 153
Cdd:PLN02715 127 GLLFAVLITGVITDSIKVATGRPRPNFYwrcfpdgkelydalgGVICHGKAaevKEGHKSFPSGHTSWSFAGLTFLSLYL 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 56466456 154 AGELRIFSDRPELWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGY 212
Cdd:PLN02715 207 SGKIKAFNGEGHVAKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFCY 265
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
93-212 |
2.28e-18 |
|
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: 78.23 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 93 LGASVTTWLMFVQGGKIYAGRPRPNMYAL-----VAQGKEKDAWKSFPSGHSAASFCGYTYLSLYIAGelrifsdRPELW 167
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLegglvPAPSTLPGLGYSFPSGHSATAFALALLLALLLRR-------LRKIV 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 56466456 168 RMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGY 212
Cdd:pfam01569 75 RVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVY 119
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
59-212 |
2.68e-15 |
|
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: 71.99 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 59 AVAGIVIYASTILIIIAFQIKRLSFKHTIFTFIGLGASVTTWLMFVQGGKIYAGRPRPNMYALVAQGKEKDAWKSFPSGH 138
Cdd:COG0671 44 LLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGH 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56466456 139 SAASFCGYTYLSLYiagelrifsdrpeLWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGY 212
Cdd:COG0671 124 AAAAFALALVLALL-------------LPRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLL 184
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
108-210 |
5.26e-14 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 66.22 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 108 KIYAGRPRP------NMYALVAQGKEKDAWKSFPSGHSAASFCGYTYLSLYIagelrifsdRPELWRMIPVIIPMFLAGI 181
Cdd:smart00014 15 KNYFGRPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL---------PARAGRKLLIFLLLLLALV 85
|
90 100
....*....|....*....|....*....
gi 56466456 182 IVLTRTRDYYHNFSDVLAGSIIGILSACI 210
Cdd:smart00014 86 VGFSRVYLGAHWPSDVLAGSLLGILIAAV 114
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
45-215 |
4.31e-58 |
|
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. Most likely membrane-associated phosphatidic acid phosphatases. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity, they may have a more generic housekeeping role in lipid metabolism.
Pssm-ID: 239484 [Multi-domain] Cd Length: 193 Bit Score: 182.80 E-value: 4.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 45 VNVLYPYRDS-TFSEAVAGIVIYASTILIIIAFQIK-RLSFKHTIFTFIGLGASVTTWLMFVQGGKIYAGRPRPNMYALV 122
Cdd:cd03390 1 PSISYPFAESeTVPTWLLVIISVGIPLLVIILISLFfRRSLWDLHTSLLGLLLSVSLNGVITNVLKNYAGRPRPDFLARC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 123 AQGKE--------------------KDAWKSFPSGHSAASFCGYTYLSLYIAGELRIFSDRPELWRMIPVIIPMFLAGII 182
Cdd:cd03390 81 FPDGGtpsdtlvgidicctgdpgvlKEGRKSFPSGHSSFAFAGLGFLSLYLAGKLHIFDPRGSSWRLLLALLPLLLAILV 160
|
170 180 190
....*....|....*....|....*....|...
gi 56466456 183 VLTRTRDYYHNFSDVLAGSIIGILSACIGYFSK 215
Cdd:cd03390 161 AVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQY 193
|
|
| PLN02715 |
PLN02715 |
lipid phosphate phosphatase |
14-212 |
1.25e-26 |
|
lipid phosphate phosphatase
Pssm-ID: 178317 [Multi-domain] Cd Length: 327 Bit Score: 105.14 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 14 DIIYIIVTGAVAAVLTFIDGFHMEVpGGENNVNVLYPYRDSTFSeaVAGIVIYAS--TILIIIAFQIKRLSFKHTIFTFI 91
Cdd:PLN02715 50 DWIILVILIAIEIGLNLISPFYRYV-GKDMMTDLKYPFKDNTVP--IWSVPVYAVllPIILFVCFYLKRRCVYDLHHSIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 92 GLGASVTTWLMFVQGGKIYAGRPRPNMY---------------ALVAQGKE---KDAWKSFPSGHSAASFCGYTYLSLYI 153
Cdd:PLN02715 127 GLLFAVLITGVITDSIKVATGRPRPNFYwrcfpdgkelydalgGVICHGKAaevKEGHKSFPSGHTSWSFAGLTFLSLYL 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 56466456 154 AGELRIFSDRPELWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGY 212
Cdd:PLN02715 207 SGKIKAFNGEGHVAKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGILVAAFCY 265
|
|
| PLN02250 |
PLN02250 |
lipid phosphate phosphatase |
14-222 |
5.22e-25 |
|
lipid phosphate phosphatase
Pssm-ID: 215139 Cd Length: 314 Bit Score: 100.39 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 14 DIIYIIVTGAVAAVLTFIDGFHMEVpGGENNVNVLYPYRDSTFS-EAVAGIVIYASTILIIIAFQIKR--LSFKHTIftf 90
Cdd:PLN02250 25 DWLILLLLVVIEVVLNVIEPFHRFV-GKDMLTDLSYPLQDNTIPfWAVPLIAILLPFAVILVYYFIRRdvYDLHHAI--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 91 IGLGASVTTWLMFVQGGKIYAGRPRPNMY-----------------ALVAQGKE--KDAWKSFPSGHSAASFCGYTYLSL 151
Cdd:PLN02250 101 LGLLFSVLITGVITDAIKDAVGRPRPDFFwrcfpdgkgvfhpvttdVLCTGAKSviKEGHKSFPSGHTSWSFAGLGFLSL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56466456 152 YIAGELRIFSDRPELWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGYFSKFESLFSP 222
Cdd:PLN02250 181 YLSGKIRVFDRRGHVAKLCIVFLPLLVAALVGVSRVDDYWHHWQDVFAGALIGLTVASFCYLQFFPPPYDI 251
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
88-212 |
6.77e-22 |
|
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: 87.52 E-value: 6.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 88 FTFIGLGASVTTWLMFVQGGKIYAGRPRPNMYALV----AQGKEKDAWKSFPSGHSAASFCGYTYLSLYIagelrifsdR 163
Cdd:cd01610 3 LLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCgpdgDPLLLTEGGYSFPSGHAAFAFALALFLALLL---------P 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 56466456 164 PELWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGY 212
Cdd:cd01610 74 RRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
|
|
| PLN02731 |
PLN02731 |
Putative lipid phosphate phosphatase |
14-216 |
8.58e-20 |
|
Putative lipid phosphate phosphatase
Pssm-ID: 178332 Cd Length: 333 Bit Score: 86.62 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 14 DIIYIIVTGAVAAVLTFIDGFHMEVpGGENNVNVLYPYRDSTFSeaVAGIVIYAS--TILIIIAFQIKRLSFKHTIFTFI 91
Cdd:PLN02731 44 DWIILVLLVILECVLLIIHPFYRFV-GKDMMTDLSYPLKSNTVP--IWSVPVYAMllPLVIFIFIYFRRRDVYDLHHAVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 92 GLGASVTTWLMFVQGGKIYAGRPRPNMY---------------ALVAQGKE---KDAWKSFPSGHSAASFCGYTYLSLYI 153
Cdd:PLN02731 121 GLLYSVLVTAVLTDAIKNAVGRPRPDFFwrcfpdgkalydslgDVICHGDKsviREGHKSFPSGHTSWSFSGLGFLSLYL 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56466456 154 AGELRIFSDRPELWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGYFSKF 216
Cdd:PLN02731 201 SGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQFF 263
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
93-212 |
2.28e-18 |
|
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: 78.23 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 93 LGASVTTWLMFVQGGKIYAGRPRPNMYAL-----VAQGKEKDAWKSFPSGHSAASFCGYTYLSLYIAGelrifsdRPELW 167
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLegglvPAPSTLPGLGYSFPSGHSATAFALALLLALLLRR-------LRKIV 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 56466456 168 RMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGY 212
Cdd:pfam01569 75 RVLLALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVY 119
|
|
| PAP2_wunen |
cd03384 |
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid ... |
83-208 |
3.39e-16 |
|
PAP2, wunen subfamily. Most likely a family of membrane associated phosphatidic acid phosphatases. Wunen is a drosophila protein expressed in the central nervous system, which provides repellent activity towards primordial germ cells (PGCs), controls the survival of PGCs and is essential in the migration process of these cells towards the somatic gonadal precursors.
Pssm-ID: 239479 Cd Length: 150 Bit Score: 73.05 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 83 FKHTIFTFIGLGAsvtTWLmFVQGGKIYAGRPRP--------NMYALVAQGKE----------------KDAWKSFPSGH 138
Cdd:cd03384 3 YRFVGVFLFGLFA---TQL-LTDLGKYVTGRLRPhfldvckpNYTDLTCSLDHqyiadctcctgdpdliREARLSFPSGH 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56466456 139 SAASFCGYTYLSLYIagELRIFSDRPELwrMIPVIIPMFLA-GIIV-LTRTRDYYHNFSDVLAGSIIGILSA 208
Cdd:cd03384 79 ASLSMYAAVFLALYL--QARLKLRGSRL--LRPLLQFLLLAlALYVgLSRISDYKHHWSDVLAGALLGSVIA 146
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
59-212 |
2.68e-15 |
|
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: 71.99 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 59 AVAGIVIYASTILIIIAFQIKRLSFKHTIFTFIGLGASVTTWLMFVQGGKIYAGRPRPNMYALVAQGKEKDAWKSFPSGH 138
Cdd:COG0671 44 LLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLLLLKYLFGRPRPFVVPDLELLLGTAGGYSFPSGH 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56466456 139 SAASFCGYTYLSLYiagelrifsdrpeLWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGY 212
Cdd:COG0671 124 AAAAFALALVLALL-------------LPRRWLAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLL 184
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
108-210 |
5.26e-14 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 66.22 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 108 KIYAGRPRP------NMYALVAQGKEKDAWKSFPSGHSAASFCGYTYLSLYIagelrifsdRPELWRMIPVIIPMFLAGI 181
Cdd:smart00014 15 KNYFGRPRPfflsigDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL---------PARAGRKLLIFLLLLLALV 85
|
90 100
....*....|....*....|....*....
gi 56466456 182 IVLTRTRDYYHNFSDVLAGSIIGILSACI 210
Cdd:smart00014 86 VGFSRVYLGAHWPSDVLAGSLLGILIAAV 114
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
63-216 |
4.86e-12 |
|
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: 62.63 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 63 IVIYASTILIIIAFQIKRLSFKHTIFTFIGLGASVTTWLMfvqggKIYAGRPRP-NMYALVAQGKekdawkSFPSGHSAA 141
Cdd:cd03392 42 AVLLIIVLLLALLLLLKRRRRAALFLLLALLGGGALNTLL-----KLLVQRPRPpLHLLVPEGGY------SFPSGHAMG 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56466456 142 SFCGYTYLSLYIAGELrifsdRPELWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGI--LSACIGYFSKF 216
Cdd:cd03392 111 ATVLYGFLAYLLARRL-----PRRRVRILLLILAAILILLVGLSRLYLGVHYPSDVLAGWLLGLawLALLILLYRRL 182
|
|
| PAP2_like_5 |
cd03394 |
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
93-212 |
2.13e-11 |
|
PAP2_like_5 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: 239488 [Multi-domain] Cd Length: 106 Bit Score: 58.88 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 93 LGASVTTWLMFVQGGKIYAGRPRPNMYAlvaqgkekDAWKSFPSGHSAASFCGYTYLSlyiageLRIFSDRPELWRMIpv 172
Cdd:cd03394 8 LAEAAALTAAVTEGLKFAVGRARPDGSN--------NGYRSFPSGHTASAFAAATFLQ------YRYGWRWYGIPAYA-- 71
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 56466456 173 iipmfLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGY 212
Cdd:cd03394 72 -----LASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
|
|
| PAP2_containing_2_like |
cd03391 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ... |
101-208 |
1.09e-06 |
|
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to eukaryota, lacks functional characterization and may act as a membrane-associated phosphatidic acid phosphatase.
Pssm-ID: 239485 [Multi-domain] Cd Length: 159 Bit Score: 47.31 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 101 LMFVQGGKIYAGRPRP-----NMYALVAQgkekDAWkSFPSGHSAASFCGYTYL--SLYIAGELRIfsdrpelwrmiPVI 173
Cdd:cd03391 60 IITVAILKALVRRRRPaynspDMLDYVAV----DKY-SFPSGHASRAAFVARFLlnHLVLAVPLRV-----------LLV 123
|
90 100 110
....*....|....*....|....*....|....*
gi 56466456 174 IpmfLAGIIVLTRTRDYYHNFSDVLAGSIIGILSA 208
Cdd:cd03391 124 L---WATVVGISRVLLGRHHVLDVLAGAFLGYLEA 155
|
|
| PAP2_lipid_A_1_phosphatase |
cd03389 |
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ... |
108-213 |
1.41e-05 |
|
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from Francisella novicida selectively dephosphorylates lipid A at the 1-position. Lipid A is the membrane-anchor component of lipopolysaccharides (LPS), the major constituents of the outer membrane in many gram-negative bacteria.
Pssm-ID: 239483 Cd Length: 186 Bit Score: 44.23 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 108 KIYAGRPRP------NMYALVAQGKEkDAWKSFPSGHSAASFCGYTYLSLyiagelrIFsdrPELWrmipviiPMFLAGI 181
Cdd:cd03389 89 KFIIGRARPkllfddGLYGFDPFHAD-YAFTSFPSGHSATAGAAAAALAL-------LF---PRYR-------WAFILLA 150
|
90 100 110
....*....|....*....|....*....|....
gi 56466456 182 IVLTRTR--DYYHNFSDVLAGSIIGILSACIGYF 213
Cdd:cd03389 151 LLIAFSRviVGAHYPSDVIAGSLLGAVTALALYQ 184
|
|
| PAP2_like_4 |
cd03395 |
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
70-213 |
1.71e-05 |
|
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: 44.18 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 70 ILIIIAFQIKRLSFKH--TIFTFIGLGASVTTWLmfvQGG--KIYAGRPRP----NMYALVAQGKEKDAWkSFPSGHSAA 141
Cdd:cd03395 38 IFLLLALFILFRKGPIglLILLLVLLAVGFADQL---ASGflKPLVARLRPcnalDGVRLVVLGDQGGSY-SFASSHAAN 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56466456 142 SFCGYTYLSLyiagelrIFSDRPELWRMIPviipmfLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIGYF 213
Cdd:cd03395 114 SFALALFIWL-------FFRRGLFSPVLLL------WALLVGYSRVYVGVHYPGDVIAGALIGIISGLLFYL 172
|
|
| PAP2_like_6 |
cd03396 |
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
63-212 |
3.00e-04 |
|
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which mainly contains bacterial proteins, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239490 Cd Length: 197 Bit Score: 40.75 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 63 IVIYASTILIIIAFQIKRLSFKHTIFTFIGLGASVTTWLMFVQGGKIYAGRPRPNMYALVAQGKEKDAW----------- 131
Cdd:cd03396 42 SIALAVLLLALALLFFRRKRLRRRRRALLLLILVIGLGLLVVAILKSHWGRPRPWDLTEFGGDAPYTPLfsgpsngcgkg 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 132 KSFPSGHSAAsfcGYTYLSLYIAgelriFSDRPELWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIGILSACIG 211
Cdd:cd03396 122 CSFPSGHASA---GFALLALYFL-----FRRRRPRLARLVLAAGLALGALMGLARMARGAHFLSDVLWSLLLVWLIALLL 193
|
.
gi 56466456 212 Y 212
Cdd:cd03396 194 Y 194
|
|
| PAP2_dolichyldiphosphatase |
cd03382 |
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ... |
47-206 |
7.37e-04 |
|
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: 39.18 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 47 VLYPYRDS-TFSEAVAGIVIYASTILIIIAFQIKRLsfKHTIFTFIGLGAS-VTTWLMfvqggKIYAGRPRPNMYALVAQ 124
Cdd:cd03382 6 VLYDPGDLlSFLLAYLSLLPVAILVGYATLILFRRE--LEAIYLFIGLLANeALNYVL-----KRIIKEPRPCSGAYFVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 125 gkekdAWKSFPSGHSAASFCGYTYLSLYIAGELRIFSDRpeLWRMIPVIIPMFLAGIIVLTRTRDYYHNFSDVLAGSIIG 204
Cdd:cd03382 79 -----SGYGMPSSHSQFMGFFAVYLLLFIYLRLGRLNSL--VSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVG 151
|
..
gi 56466456 205 IL 206
Cdd:cd03382 152 IL 153
|
|
| PAP2_acid_phosphatase |
cd03397 |
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ... |
108-204 |
3.35e-03 |
|
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes catalyze phosphomonoester hydrolysis, with optimal activity in low pH conditions. They are secreted into the periplasmic space, and their physiological role remains to be determined.
Pssm-ID: 239491 Cd Length: 232 Bit Score: 37.70 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56466456 108 KIYAGRPRP-NMYALVAQGKEKDAW----KSFPSGHSAAsfcGYTY-LSL-YIAGELrifsdRPELwrmipviipmflag 180
Cdd:cd03397 121 KKYYNRPRPfVLNDEPICTPPDESGlakdGSYPSGHTAA---GYAWaLILaELVPER-----ADEI-------------- 178
|
90 100 110
....*....|....*....|....*....|..
gi 56466456 181 iivLTRTRDY--------YHNFSDVLAGSIIG 204
Cdd:cd03397 179 ---LARGSEYgqsrivcgVHWPSDVMGGRIMA 207
|
|
|