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Conserved domains on  [gi|1907117456|ref|XP_036015773|]
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serine/threonine-protein phosphatase CPPED1 isoform X2 [Mus musculus]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 2-172 7.73e-108

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.


The actual alignment was detected with superfamily member cd07395:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 263  Bit Score: 309.25  E-value: 7.73e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456   2 VSGNHDLGNAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQAQDHWLDQQLNIAEQKQCQHAIVF 81
Cdd:cd07395    93 VCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQLQIARESDAKHVVVF 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456  82 QHIPLFLQSIDEDDDYFNLTKTVRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQLGKDTHGLRVVAIT 161
Cdd:cd07395   173 QHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGCQLGNDTSGLRVVVVT 252

                         170
                  ....*....|.
gi 1907117456 162 AEKIVHRYYSL 172
Cdd:cd07395   253 ENKISHRYYSL 263
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 2-172 7.73e-108

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 309.25  E-value: 7.73e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456   2 VSGNHDLGNAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQAQDHWLDQQLNIAEQKQCQHAIVF 81
Cdd:cd07395    93 VCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQLQIARESDAKHVVVF 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456  82 QHIPLFLQSIDEDDDYFNLTKTVRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQLGKDTHGLRVVAIT 161
Cdd:cd07395   173 QHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGCQLGNDTSGLRVVVVT 252

                         170
                  ....*....|.
gi 1907117456 162 AEKIVHRYYSL 172
Cdd:cd07395   253 ENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
4-174 1.57e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 95.53  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456   4 GNHDLGNAPTAETVEEFCQTWGDD-YFSFWVGGVLFLVLNSQFLYDASRcpALKQAQDHWLDQQLniaEQKQCQHAIVFQ 82
Cdd:COG1409    72 GNHDIRAAMAEAYREYFGDLPPGGlYYSFDYGGVRFIGLDSNVPGRSSG--ELGPEQLAWLEEEL---AAAPAKPVIVFL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456  83 HIPLFLQSIDEDDDYFNLtktvRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQLgKDTHGLRVVAITA 162
Cdd:COG1409   147 HHPPYSTGSGSDRIGLRN----AEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV-RLPPGYRVIEVDG 221

                         170
                  ....*....|..
gi 1907117456 163 EKIVHRYYSLDE 174
Cdd:COG1409   222 DGLTVEVRRVDG 233
 
Name Accession Description Interval E-value
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 2-172 7.73e-108

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 309.25  E-value: 7.73e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456   2 VSGNHDLGNAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQAQDHWLDQQLNIAEQKQCQHAIVF 81
Cdd:cd07395    93 VCGNHDVGNTPTPETIQRYRDDFGDDYFSFWVGGVFFIVLNSQLFKDPSKVPELASAQDQWLEEQLQIARESDAKHVVVF 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456  82 QHIPLFLQSIDEDDDYFNLTKTVRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQLGKDTHGLRVVAIT 161
Cdd:cd07395   173 QHIPLFLEDPDEEDDYFNIPKSVRRELLDKFKKAGVKAVFSGHYHRNAGGRYRDLEMVVTSAVGCQLGNDTSGLRVVVVT 252

                         170
                  ....*....|.
gi 1907117456 162 AEKIVHRYYSL 172
Cdd:cd07395   253 ENKISHRYYSL 263
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
4-174 1.57e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 95.53  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456   4 GNHDLGNAPTAETVEEFCQTWGDD-YFSFWVGGVLFLVLNSQFLYDASRcpALKQAQDHWLDQQLniaEQKQCQHAIVFQ 82
Cdd:COG1409    72 GNHDIRAAMAEAYREYFGDLPPGGlYYSFDYGGVRFIGLDSNVPGRSSG--ELGPEQLAWLEEEL---AAAPAKPVIVFL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456  83 HIPLFLQSIDEDDDYFNLtktvRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQLgKDTHGLRVVAITA 162
Cdd:COG1409   147 HHPPYSTGSGSDRIGLRN----AEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQV-RLPPGYRVIEVDG 221

                         170
                  ....*....|..
gi 1907117456 163 EKIVHRYYSLDE 174
Cdd:COG1409   222 DGLTVEVRRVDG 233
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 2-133 1.11e-05

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: 44.24  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456   2 VSGNHDLGNAPTAETVEEFCQTwGDD--YFSFWVG-GVLFLVLNSQFLydasrCPALKQAQDHWLDQQLNIAEQKQcQHA 78
Cdd:cd07396    87 VLGNHEFYNFPREYLNHLKTLN-GEDayYYSFSPGpGFRFLVLDFVKF-----NGGIGEEQLAWLRNELTSADANG-EKV 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456  79 IVFQHIPLflQSIDEDD-----DYFNLTKTVRKelaekltRAGIRAVFSGHYHRnagGTY 133
Cdd:cd07396   160 IVLSHLPI--YPEAADPqcllwNYEEVLAILES-------YPCVKACFSGHNHE---GGY 207
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 1-147 3.14e-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: 43.04  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456   1 MVSGNHDLGNAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFlyDASRCPALKQAQDHWLDQQLNIAEQKqcqHAIV 80
Cdd:cd07402    74 WIPGNHDDRAAMREALPEPPYDDNGPVQYVVDFGGWRLILLDTSV--PGVHHGELSDEQLDWLEAALAEAPDR---PTLI 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907117456  81 FQHIPLFLQSIDEDDDYfNLTKTvrKELAEKLTR-AGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQ 147
Cdd:cd07402   149 FLHHPPFPLGIPWMDAI-RLRNS--QALFAVLARhPQVKAILCGHIHRPISGSFRGIPFSTAPSTCHQ 213
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 1-154 8.61e-05

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: 41.90  E-value: 8.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456   1 MVS-GNHDLG----------NAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRcpaLKQAQDHWLDQQLNI 69
Cdd:cd00839    72 MVApGNHEADyngstskikfFMPGRGMPPSPSGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456  70 AEQKQCQHAIVFQHIPLFLQSIDEDDDYFNltKTVRKELAEKLTRAGIRAVFSGHYH------RNAGGTYQNLDM----- 138
Cdd:cd00839   149 VDRSRTPWIIVMGHRPMYCSNDDDADCIEG--EKMREALEDLFYKYGVDLVLSGHVHayertcPVYNNTVANSKDniytn 226

                         170       180
                  ....*....|....*....|..
gi 1907117456 139 ------VVSSAIGCQLGKDTHG 154
Cdd:cd00839   227 pkgpvhIVIGAAGNDEGLDDAF 248
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 28-127 9.09e-04

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase 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: 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: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 38.82  E-value: 9.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456  28 YFSFWVGGVLFLVLNSQFLYDASRcPALKQAQD-----HWLDQQLNIAEQKQcQHAIVFQHIPLflqSIDEDDDYFN--L 100
Cdd:cd00842   163 YSVDVKDGLRVISLNTNLYYKKNF-WLYSNNTDpcgqlQWLEDELEDAEQKG-EKVWIIGHIPP---GLNSYDADWSerF 237

                          90       100
                  ....*....|....*....|....*..
gi 1907117456 101 TKTVRKelaeklTRAGIRAVFSGHYHR 127
Cdd:cd00842   238 YQIINR------YSDTIAGQFFGHTHR 258
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 77-132 3.41e-03

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: 36.09  E-value: 3.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907117456  77 HAIVFQHIPLFlqsiDEDDDYFNLTKTVRKELAEKLTRAGIRAVFSGHYHRNAGGT 132
Cdd:cd00838    67 HDILVTHGPPY----DPLDEGSPGEDPGSEALLELLDKYGPDLVLSGHTHVPGRRE 118
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 49-171 7.12e-03

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: 36.15  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907117456  49 ASRCPALKQAQDHWLDQQLNIAEQkqcQHAIVFQHIPLFlqSIDEDDDyfnlTKTVRKELAEKLTRAGIRAVFSGHYH-- 126
Cdd:cd07378   149 GPPNKKLAETQLAWLEKQLAASKA---DYKIVVGHYPIY--SSGEHGP----TKCLVDILLPLLKKYKVDAYLSGHDHnl 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907117456 127 ---RNAGGTYqnldMVVSSAIGCQLGKDTH--------------------GLRVVAITAEKIVHRYYS 171
Cdd:cd07378   220 qhiVDESGTY----YVISGAGSKADPSDIHrdkvpqgyllffsgfyssggGFAYLEITSSELVIRFVD 283
 
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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