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Conserved domains on  [gi|1826788846|gb|KAF3816965|]
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hypothetical protein GH733_014313 [Mirounga leonina]

Protein Classification

glucose-6-phosphatase( domain architecture ID 10130180)

glucose-6-phosphatase is a type 2 phosphatidic acid phosphatase (PAP2) family protein that catalyzes the hydrolysis of glucose-6-phosphate to glucose and phosphate

CATH:  1.20.144.10
EC:  3.1.3.9
Gene Ontology:  GO:0004346|GO:0016311|GO:0051156
PubMed:  12192101|11879177|9122162|12447906|9260289
SCOP:  3001110|4001226

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
 42-280 1.16e-140

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


:

Pssm-ID: 239476  Cd Length: 235  Bit Score: 398.29  E-value: 1.16e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  42 AFYVLFPIWFHLREAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVMDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAM 121
Cdd:cd03381     1 LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCETGPGSPSGHAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846 122 GTAGVYYVMVTSTLAIFRGKrkptYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVIAGVLSGIAVAETFRHIQSI 201
Cdd:cd03381    81 GTTAVLLVMVTALLSHLAGR----KRSRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGIAVAETFSHIRYI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1826788846 202 YNASLKKYFLITFFLFGFAIGFYLLLKGLGVDLLWTLEKAKRWCERPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMY 280
Cdd:cd03381   157 YSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDTTPFASLLRNLGTLLGLGLALNSSMY 235
 
Name Accession Description Interval E-value
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
 42-280 1.16e-140

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


Pssm-ID: 239476  Cd Length: 235  Bit Score: 398.29  E-value: 1.16e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  42 AFYVLFPIWFHLREAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVMDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAM 121
Cdd:cd03381     1 LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCETGPGSPSGHAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846 122 GTAGVYYVMVTSTLAIFRGKrkptYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVIAGVLSGIAVAETFRHIQSI 201
Cdd:cd03381    81 GTTAVLLVMVTALLSHLAGR----KRSRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGIAVAETFSHIRYI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1826788846 202 YNASLKKYFLITFFLFGFAIGFYLLLKGLGVDLLWTLEKAKRWCERPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMY 280
Cdd:cd03381   157 YSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDTTPFASLLRNLGTLLGLGLALNSSMY 235
acidPPc smart00014
Acid phosphatase homologues;
62-195 1.18e-23

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 93.95  E-value: 1.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846   62 LWVAVIGDWLNLVFKWILFGQRPYWWvmdtdyySNTSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTLAIFRgk 141
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFL-------SIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAG-- 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1826788846  142 rkptyrfrclNVILWLGFWAVQLNVCLSRIYLAAHFPHQVIAGVLSGIAVAETF 195
Cdd:smart00014  72 ----------RKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 61-192 1.17e-11

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: 61.28  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  61 LLWVAVIGDWLNLVFKWILFGQRPYWWVMDTDYYSNTSVPLikqfpvtcETGPGSPSGHAMGTAGVYYVmvtstLAIFRG 140
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLP--------GLGYSFPSGHSATAFALALL-----LALLLR 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1826788846 141 KRKPTYRFRCLNVILWLGFWavqlnVCLSRIYLAAHFPHQVIAGVLSGIAVA 192
Cdd:pfam01569  69 RLRKIVRVLLALLLLVLALL-----VGLSRLYLGVHFPSDVLAGALIGILLA 115
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 5-198 9.08e-07

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: 48.88  E-value: 9.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846   5 MNALHDFGIQSTHYLQVNYQDSQDWFILVSMIADLRNAFYVLFPIWFHLREAVGIKLLWVAVIGDWLNLV--FKWILFGQ 82
Cdd:COG0671    20 LALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLllLKYLFGRP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  83 RPYWWvmdtdyysntsvPLIKQFpVTCETGPGSPSGHAMGTAGVYYVMVtstlaifrgkrkptYRFRCLNVILWLGFWAV 162
Cdd:COG0671   100 RPFVV------------PDLELL-LGTAGGYSFPSGHAAAAFALALVLA--------------LLLPRRWLAALLLALAL 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1826788846 163 QlnVCLSRIYLAAHFPHQVIAGVLSGIAVAETFRHI 198
Cdd:COG0671   153 L--VGLSRVYLGVHYPSDVLAGALLGLAIALLLLAL 186
 
Name Accession Description Interval E-value
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
 42-280 1.16e-140

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


Pssm-ID: 239476  Cd Length: 235  Bit Score: 398.29  E-value: 1.16e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  42 AFYVLFPIWFHLREAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVMDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAM 121
Cdd:cd03381     1 LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCETGPGSPSGHAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846 122 GTAGVYYVMVTSTLAIFRGKrkptYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVIAGVLSGIAVAETFRHIQSI 201
Cdd:cd03381    81 GTTAVLLVMVTALLSHLAGR----KRSRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGIAVAETFSHIRYI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1826788846 202 YNASLKKYFLITFFLFGFAIGFYLLLKGLGVDLLWTLEKAKRWCERPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMY 280
Cdd:cd03381   157 YSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDTTPFASLLRNLGTLLGLGLALNSSMY 235
acidPPc smart00014
Acid phosphatase homologues;
62-195 1.18e-23

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 93.95  E-value: 1.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846   62 LWVAVIGDWLNLVFKWILFGQRPYWWvmdtdyySNTSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTLAIFRgk 141
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFL-------SIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAG-- 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1826788846  142 rkptyrfrclNVILWLGFWAVQLNVCLSRIYLAAHFPHQVIAGVLSGIAVAETF 195
Cdd:smart00014  72 ----------RKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 54-196 3.81e-17

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: 76.73  E-value: 3.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  54 REAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVMDTDYYsntsvplikQFPVTCETGPGSPSGHAMGTAGVYYVMVTS 133
Cdd:cd01610     1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDG---------DPLLLTEGGYSFPSGHAAFAFALALFLALL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1826788846 134 tlaifrgkrkptYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVIAGVLSGIAVAETFR 196
Cdd:cd01610    72 ------------LPRRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 61-192 1.17e-11

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: 61.28  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  61 LLWVAVIGDWLNLVFKWILFGQRPYWWVMDTDYYSNTSVPLikqfpvtcETGPGSPSGHAMGTAGVYYVmvtstLAIFRG 140
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLP--------GLGYSFPSGHSATAFALALL-----LALLLR 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1826788846 141 KRKPTYRFRCLNVILWLGFWavqlnVCLSRIYLAAHFPHQVIAGVLSGIAVA 192
Cdd:pfam01569  69 RLRKIVRVLLALLLLVLALL-----VGLSRLYLGVHFPSDVLAGALIGILLA 115
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 5-198 9.08e-07

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: 48.88  E-value: 9.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846   5 MNALHDFGIQSTHYLQVNYQDSQDWFILVSMIADLRNAFYVLFPIWFHLREAVGIKLLWVAVIGDWLNLV--FKWILFGQ 82
Cdd:COG0671    20 LALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLllLKYLFGRP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  83 RPYWWvmdtdyysntsvPLIKQFpVTCETGPGSPSGHAMGTAGVYYVMVtstlaifrgkrkptYRFRCLNVILWLGFWAV 162
Cdd:COG0671   100 RPFVV------------PDLELL-LGTAGGYSFPSGHAAAAFALALVLA--------------LLLPRRWLAALLLALAL 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1826788846 163 QlnVCLSRIYLAAHFPHQVIAGVLSGIAVAETFRHI 198
Cdd:COG0671   153 L--VGLSRVYLGVHYPSDVLAGALLGLAIALLLLAL 186
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 45-192 3.21e-06

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: 46.83  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  45 VLFPIWFHLREAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVMDTdyysntsvplikqfpvtcETGPGSPSGHAMGTA 124
Cdd:cd03392    51 LALLLLLKRRRRAALFLLLALLGGGALNTLLKLLVQRPRPPLHLLVP------------------EGGYSFPSGHAMGAT 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1826788846 125 GVYyvmvtSTLAIFRGKRKPTYRFRCLNVILWLGFWavqLNVCLSRIYLAAHFPHQVIAGVLSGIAVA 192
Cdd:cd03392   113 VLY-----GFLAYLLARRLPRRRVRILLLILAAILI---LLVGLSRLYLGVHYPSDVLAGWLLGLAWL 172
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 43-190 5.09e-05

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: 42.99  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  43 FYVLF-PIWFHL---REAVGIKLLWVAV--IGDWLNLVFKWilfgQRPYwwvmdtdyysntSVPLIKQFPVTCETGPGSP 116
Cdd:cd03388    18 FYILFlPFLFWNgdpYVGRDLVVVLALGmyIGQFIKDLFCL----PRPS------------SPPVVRLTMSSAALEYGFP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1826788846 117 SGHAMGTAGVYYVMVTSTLaifrgKRKPTYRFRCLNVILwlgFWAVqlNVCLSRIYLAAHFPHQVIAGVLSGIA 190
Cdd:cd03388    82 STHAMNATAISFYLLIYLY-----DRYQYPFVLGLILAL---FYST--LVCLSRIYMGMHSVLDVIAGSLIGVL 145
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 111-192 1.61e-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: 41.49  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846 111 TGPGSPSGHA--MGTAGVYyvmvtSTLAIFrgKRKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVIAGVLSG 188
Cdd:cd03382    79 SGYGMPSSHSqfMGFFAVY-----LLLFIY--LRLGRLNSLVSRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVG 151


                  ....
gi 1826788846 189 IAVA 192
Cdd:cd03382   152 ILLG 155
PAP2_like_1 cd03380
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ...
 76-192 2.80e-04

PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium chloroperoxidases and vanadium bromoperoxidases.


Pssm-ID: 239475  Cd Length: 209  Bit Score: 41.65  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  76 KWILFGQRPYWWvmdtdyYSNTSVPLIKQFPVTcETGPGSPSGHAMgTAGvyyvMVTSTLAIFRGKRKPTyrfrclnvil 155
Cdd:cd03380   113 KYHYNRPRPFVA------IRLQWLPICTPEEGT-PKHPSYPSGHAT-FGG----AAALVLAELFPERAAE---------- 170

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1826788846 156 wlgFWAVQLNVCLSRIYLAAHFPHQVIAGVLSGIAVA 192
Cdd:cd03380   171 ---LLARAAEAGNSRVVAGVHWPSDVEAGRILGEAIA 204
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 58-192 2.87e-04

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: 40.05  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846  58 GIKLLWVAVIGDWLNLVFKWILFGQRPYwwvmdtdyysnTSVPLIKQFPVTcETGPGSPSGHAMGTAGVYyvmvtSTLAI 137
Cdd:cd03393    15 GRYLGLALCASGYLNAALKEVFKIPRPF-----------TYDGIQAIYEES-AGGYGFPSGHAQTSATFW-----GSLML 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1826788846 138 FRgkRKPTYRFRCLNVILWLGFwavqlnvclSRIYLAAHFPHQVIAGVLSGIAVA 192
Cdd:cd03393    78 HV--RKKWFTLIGVVLVVLISF---------SRLYLGVHWPSDVIGGVLIGLLVL 121
PAP2_haloperoxidase cd03398
PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as ...
 113-193 2.29e-03

PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles.


Pssm-ID: 239492  Cd Length: 232  Bit Score: 38.94  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826788846 113 PGSPSGHAMgTAGVY-----------YVMVTSTLAIFRGKRKPTYRFrclnvilWLGFWAVQLNVCLSRIYLAAHFPHQV 181
Cdd:cd03398   145 PSYPSGHAT-FAGAAatvlkalfgsdKVPDTVSEPDEGGPSTGVTRV-------WAELNELADEVAISRVYAGVHFRSDD 216

                          90
                  ....*....|..
gi 1826788846 182 IAGVLSGIAVAE 193
Cdd:cd03398   217 AAGAALGEQIGA 228
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
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