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Conserved domains on  [gi|1176198877|gb|OQY10995|]
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MAG: hypothetical protein B6I29_00105 [Marinitoga sp. 4572_148]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 11444094)

metallophosphatase family protein containing an active site consisting of two metal ions

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0016787|GO:0046872|GO:0042578
PubMed:  25837850
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
13-165 5.11e-30

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


:

Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 111.32  E-value: 5.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  13 FKGLNSFYYPILGNHE---KNSKIYYEAFdlpkGGGNYNKQWYSFSYGKCHFIILDSIISTKSE-IFKNETI-WMINEFK 87
Cdd:COG1409    60 LARLGVPVYVVPGNHDiraAMAEAYREYF----GDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSgELGPEQLaWLEEELA 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176198877  88 NNKGKNFFVFFHYPFWNNSSISWRKQFDkLEKAWRPIFERYNVKIVFNGHVHAYERFEKNGIIYITTGGGGAPFDHGA 165
Cdd:COG1409   136 AAPAKPVIVFLHHPPYSTGSGSDRIGLR-NAEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRLPP 212
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
13-165 5.11e-30

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 111.32  E-value: 5.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  13 FKGLNSFYYPILGNHE---KNSKIYYEAFdlpkGGGNYNKQWYSFSYGKCHFIILDSIISTKSE-IFKNETI-WMINEFK 87
Cdd:COG1409    60 LARLGVPVYVVPGNHDiraAMAEAYREYF----GDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSgELGPEQLaWLEEELA 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176198877  88 NNKGKNFFVFFHYPFWNNSSISWRKQFDkLEKAWRPIFERYNVKIVFNGHVHAYERFEKNGIIYITTGGGGAPFDHGA 165
Cdd:COG1409   136 AAPAKPVIVFLHHPPYSTGSGSDRIGLR-NAEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRLPP 212
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 20-182 2.19e-19

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 84.27  E-value: 2.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  20 YYPILGNHE-----KNSKIY---YEAFDLPKGGGNYNKQWYSFSYGKCHFIILDS-IISTKSEIFKNETIWMINEFKNNK 90
Cdd:cd00839    71 YMVAPGNHEadyngSTSKIKffmPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTeTDFLKGDNISPQYDWLEADLAKVD 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  91 GKN---FFVFFHYPFWNNSSISWR-KQFDKLEKAWRPIFERYNVKIVFNGHVHAYERFEK-----------------NGI 149
Cdd:cd00839   151 RSRtpwIIVMGHRPMYCSNDDDADcIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPvynntvanskdniytnpKGP 230

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1176198877 150 IYITTGGGGAPFDH------GAKKEILPHTKKYAYGILE 182
Cdd:cd00839   231 VHIVIGAAGNDEGLddafsyPQPEWSAFRSSDFGFGRLT 269
PLN02533 PLN02533
probable purple acid phosphatase
 25-158 2.60e-11

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 62.39  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  25 GNH--EKNSKIYYEAFDlpkgggNYNKQW--------------YSFSYGKCHFIILDSI--ISTKSEIFKnetiWMINEF 86
Cdd:PLN02533  206 GNHelEKIPILHPEKFT------AYNARWrmpfeesgstsnlyYSFNVYGVHIIMLGSYtdFEPGSEQYQ----WLENNL 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  87 KNNKGKN---FFVFFHYPFWN-NSSISWRKQFDKLEKAWRPIFERYNVKIVFNGHVHAYERF--------EKNGIIYITT 154
Cdd:PLN02533  276 KKIDRKTtpwVVAVVHAPWYNsNEAHQGEKESVGMKESMETLLYKARVDLVFAGHVHAYERFdrvyqgktDKCGPVYITI 355


                  ....
gi 1176198877 155 GGGG 158
Cdd:PLN02533  356 GDGG 359
 
Name Accession Description Interval E-value
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
13-165 5.11e-30

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 111.32  E-value: 5.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  13 FKGLNSFYYPILGNHE---KNSKIYYEAFdlpkGGGNYNKQWYSFSYGKCHFIILDSIISTKSE-IFKNETI-WMINEFK 87
Cdd:COG1409    60 LARLGVPVYVVPGNHDiraAMAEAYREYF----GDLPPGGLYYSFDYGGVRFIGLDSNVPGRSSgELGPEQLaWLEEELA 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176198877  88 NNKGKNFFVFFHYPFWNNSSISWRKQFDkLEKAWRPIFERYNVKIVFNGHVHAYERFEKNGIIYITTGGGGAPFDHGA 165
Cdd:COG1409   136 AAPAKPVIVFLHHPPYSTGSGSDRIGLR-NAEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRLPP 212
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 20-182 2.19e-19

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 84.27  E-value: 2.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  20 YYPILGNHE-----KNSKIY---YEAFDLPKGGGNYNKQWYSFSYGKCHFIILDS-IISTKSEIFKNETIWMINEFKNNK 90
Cdd:cd00839    71 YMVAPGNHEadyngSTSKIKffmPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTeTDFLKGDNISPQYDWLEADLAKVD 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  91 GKN---FFVFFHYPFWNNSSISWR-KQFDKLEKAWRPIFERYNVKIVFNGHVHAYERFEK-----------------NGI 149
Cdd:cd00839   151 RSRtpwIIVMGHRPMYCSNDDDADcIEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPvynntvanskdniytnpKGP 230

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1176198877 150 IYITTGGGGAPFDH------GAKKEILPHTKKYAYGILE 182
Cdd:cd00839   231 VHIVIGAAGNDEGLddafsyPQPEWSAFRSSDFGFGRLT 269
PLN02533 PLN02533
probable purple acid phosphatase
 25-158 2.60e-11

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 62.39  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  25 GNH--EKNSKIYYEAFDlpkgggNYNKQW--------------YSFSYGKCHFIILDSI--ISTKSEIFKnetiWMINEF 86
Cdd:PLN02533  206 GNHelEKIPILHPEKFT------AYNARWrmpfeesgstsnlyYSFNVYGVHIIMLGSYtdFEPGSEQYQ----WLENNL 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  87 KNNKGKN---FFVFFHYPFWN-NSSISWRKQFDKLEKAWRPIFERYNVKIVFNGHVHAYERF--------EKNGIIYITT 154
Cdd:PLN02533  276 KKIDRKTtpwVVAVVHAPWYNsNEAHQGEKESVGMKESMETLLYKARVDLVFAGHVHAYERFdrvyqgktDKCGPVYITI 355


                  ....
gi 1176198877 155 GGGG 158
Cdd:PLN02533  356 GDGG 359
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 95-155 6.24e-08

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 49.96  E-value: 6.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176198877  95 FVFFHYPFWNnSSISWRKQFDKLEKAWRPIFERYNVKIVFNGHVHAYERFE--KNGIIYITTG 155
Cdd:cd00838    69 ILVTHGPPYD-PLDEGSPGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREvdKGGTLVVNPG 130
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 21-195 1.88e-06

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 47.32  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  21 YPILGNH----------EKNSKIYYEAFDLPkgggNYnkqWYSFSYG------KCHFIILDSII--------------ST 70
Cdd:cd07378    78 YLVLGNHdhrgnvsaqiAYTQRPNSKRWNFP----NY---YYDISFKfpssdvTVAFIMIDTVLlcgntddeasgqprGP 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  71 KSEIFKNETI-WMINEFKNNKGKNFFVFFHYPFWnnsSISWRKQFDKLEKAWRPIFERYNVKIVFNGHVHAYERFEKNGI 149
Cdd:cd07378   151 PNKKLAETQLaWLEKQLAASKADYKIVVGHYPIY---SSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESG 227

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1176198877 150 I-YITTGGGGAPFDHGAKKEILPHTKKYAYGILEY-----ILVEVTNEKIKI 195
Cdd:cd07378   228 TyYVISGAGSKADPSDIHRDKVPQGYLLFFSGFYSsgggfAYLEITSSELVI 279
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 20-156 1.40e-05

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 44.58  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  20 YYPILGNHEKNSKiYYEAF-DLPKGGGNYNKQWYSFsyGKCHFIILDSIISTKSE-IFKNETI-WMINEFKNNKGKNFFV 96
Cdd:cd07402    72 VYWIPGNHDDRAA-MREALpEPPYDDNGPVQYVVDF--GGWRLILLDTSVPGVHHgELSDEQLdWLEAALAEAPDRPTLI 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176198877  97 FFHY-PFwnNSSISWrkqFDKL-----EKAWRPIFERYNVKIVFNGHVHAYERFEKNGIIYITTGG 156
Cdd:cd07402   149 FLHHpPF--PLGIPW---MDAIrlrnsQALFAVLARHPQVKAILCGHIHRPISGSFRGIPFSTAPS 209
COG5555 COG5555
Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and ...
 52-155 2.12e-05

Cytolysin, a secreted calcineurin-like phosphatase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444298 [Multi-domain]  Cd Length: 325  Bit Score: 44.47  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  52 YSFSYGKCHFIILDSIISTKSEIFKNETIWMINEFKN--NKGKNFFVFFHYPfWNNSSISWRKQFDKLEKAWRPIFERYN 129
Cdd:COG5555   182 YSWDWGDLHLVQLHRAPGDEVKGDVSSLDWLKKDLAAaaADGRPVILFFHYG-LEGFSTEYWFASGPDRQALLDILKGYN 260

                          90       100
                  ....*....|....*....|....*.
gi 1176198877 130 VKIVFNGHVHAYERFEKNGIIYITTG 155
Cdd:COG5555   261 VLGIFHGHYHTTGIYRWHGIDVYKPG 286
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 13-156 2.39e-03

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 38.08  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176198877  13 FKGLNSFYYPILGNHE--KNSKIYYEAFDLPKGGGNYnkqWYSFSYG-KCHFIILDsIISTKSEIFKNETIWMINEFK-- 87
Cdd:cd07396    77 LDRLKGPVHHVLGNHEfyNFPREYLNHLKTLNGEDAY---YYSFSPGpGFRFLVLD-FVKFNGGIGEEQLAWLRNELTsa 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1176198877  88 NNKGKNFFVFFHYPFWNNSSiswrkqfDKLEKAW------RPIFERYNVKIVFNGHVH--AYERfEKNGIIYITTGG 156
Cdd:cd07396   153 DANGEKVIVLSHLPIYPEAA-------DPQCLLWnyeevlAILESYPCVKACFSGHNHegGYEQ-DSHGVHHVTLEG 221
DR1119 COG1768
Predicted phosphohydrolase, DR1119 family, metallophosphatase superfamily [General function ...
 87-151 6.56e-03

Predicted phosphohydrolase, DR1119 family, metallophosphatase superfamily [General function prediction only];


Pssm-ID: 441374 [Multi-domain]  Cd Length: 230  Bit Score: 36.72  E-value: 6.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176198877  87 KNNKGKNFFVFFHYPFWNnssiswrkqfDKLEK-AWRPIFERYNVKIVFNGHVHAYERF-----EKNGIIY 151
Cdd:COG1768   153 KKLGGKKIIVMLHYPPFN----------DKGEPsEFTELLEEYGVDKCVYGHLHGEGHKnalegEINGIRY 213
 
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.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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