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Conserved domains on  [gi|2229888665|gb|UPI76618|]
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thiosulfate oxide protein subunit B, partial [uncultured Rhodoferax sp.]

Protein Classification

thiosulfohydrolase SoxB family protein( domain architecture ID 1003979)

thiosulfohydrolase SoxB is a di-manganese(II) enzyme that works with SoxYZ and the c-type cytochrome SoxXA in oxidation of thiosulfate to sulfat

Gene Ontology:  GO:0016787|GO:0009166|GO:0030145
PubMed:  26655737|19535341

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
thiosulf_SoxB super family cl37453
thiosulfohydrolase SoxB; SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type ...
 1-170 1.01e-111

thiosulfohydrolase SoxB; SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type cytochrome SoxXA in oxidation of thiosulfate to sulfate.


The actual alignment was detected with superfamily member TIGR04486:

Pssm-ID: 275279 [Multi-domain]  Cd Length: 556  Bit Score: 328.42  E-value: 1.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDEARGKGAQVVVVLSHNGMDVDLKMASRVSGIDAIMGGHTHDGMPVA 80
Cdd:TIGR04486 226 IGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKGADAVVLLSHNGMDVDLKLASRVKGIDVILGGHTHDAVPQP 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  81 SIIsnkgGKTLVTNAGSNSKFLAVLDFEVKDKKVTDFRYKLLPVFANMLPADAEMDALITKVRAPYEAKLAEKLAITEGT 160
Cdd:TIGR04486 306 VRV----GNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLLPADPEMAALIEKVRAPYEAKLSEVLAVTESL 381

                         170
                  ....*....|
gi 2229888665 161 LYRRGNFNGT 170
Cdd:TIGR04486 382 LYRRGNFNGT 391
 
Name Accession Description Interval E-value
thiosulf_SoxB TIGR04486
thiosulfohydrolase SoxB; SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type ...
 1-170 1.01e-111

thiosulfohydrolase SoxB; SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type cytochrome SoxXA in oxidation of thiosulfate to sulfate.


Pssm-ID: 275279 [Multi-domain]  Cd Length: 556  Bit Score: 328.42  E-value: 1.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDEARGKGAQVVVVLSHNGMDVDLKMASRVSGIDAIMGGHTHDGMPVA 80
Cdd:TIGR04486 226 IGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKGADAVVLLSHNGMDVDLKLASRVKGIDVILGGHTHDAVPQP 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  81 SIIsnkgGKTLVTNAGSNSKFLAVLDFEVKDKKVTDFRYKLLPVFANMLPADAEMDALITKVRAPYEAKLAEKLAITEGT 160
Cdd:TIGR04486 306 VRV----GNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLLPADPEMAALIEKVRAPYEAKLSEVLAVTESL 381

                         170
                  ....*....|
gi 2229888665 161 LYRRGNFNGT 170
Cdd:TIGR04486 382 LYRRGNFNGT 391
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 1-168 1.94e-56

2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms];


Pssm-ID: 440500 [Multi-domain]  Cd Length: 471  Bit Score: 183.52  E-value: 1.94e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDEARGKGAQVVVVLSHNGMD-VDLKMASRVSGIDAIMGGHTHDGMPV 79
Cdd:COG0737   141 IGLTTPDTPTWSSPGNIGGLTFTDPVEAAQKYVDELRAEGADVVVLLSHLGLDgEDRELAKEVPGIDVILGGHTHTLLPE 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  80 ASIIsnkGGKTLVTNAGSNSKFLAVLDFEVKD--KKVTDFRYKLLPVFANMLPADAEMDALITKVRAPYEAKLAEKLAIT 157
Cdd:COG0737   221 PVVV---NGGTLIVQAGSYGKYLGRLDLTLDDdgGKVVSVSAELIPVDDDLVPPDPEVAALVDEYRAKLEALLNEVVGTT 297

                         170
                  ....*....|.
gi 2229888665 158 EGTLYRRGNFN 168
Cdd:COG0737   298 EVPLDGYRAFV 308
MPP_SoxB_N cd07411
Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB ...
 1-124 7.84e-50

Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB (sulfur oxidation protein B) is a periplasmic thiosulfohydrolase and an essential component of the sulfur oxidation pathway in archaea and bacteria. SoxB has a dinuclear manganese cluster and is thought to catalyze the release of sulfate from a protein-bound cysteine S-thiosulfonate. SoxB is expressed from the sox (sulfur oxidation) gene cluster, which encodes 15 other sox genes, and has two domains, an N-terminal metallophosphatase domain and a C-terminal 5'-nucleotidase domain. SoxB binds the SoxYZ complex and is thought to function as a sulfate-thiohydrolase. SoxB is closely related to the UshA, YchR, and CpdB proteins, all of which have the same two-domain architecture. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that 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). 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 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: 277356 [Multi-domain]  Cd Length: 273  Bit Score: 161.35  E-value: 7.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDE-ARGKGAQVVVVLSHNGMDVDLKMASRVSGIDAIMGGHTHDGMPV 79
Cdd:cd07411   153 IGQAFPYVPIANPPSFSPGWSFGIREEELQEHVVKlRRAEGVDAVVLLSHNGMPVDVALAERVEGIDVILSGHTHDRVPE 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2229888665  80 AsiisNKGGKTLVTNAGSNSKFLAVLDFEVKDKKVTDFRYKLLPV 124
Cdd:cd07411   233 P----IRGGKTLVVAAGSHGKFVGRVDLKVRDGEIKSFRYELLPV 273
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
1-157 6.90e-12

multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 62.53  E-value: 6.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665    1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDEAR-GKGAQVVVVLSHNGMDVD--------LKMASRVSGIDAIMGG 71
Cdd:PRK09419   798 IGLTTPETAYKTSPGNVKNLEFKDPAEAAKKWVKELKeKEKVDAIIALTHLGSNQDrttgeitgLELAKKVKGVDAIISA 877

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   72 HTHdgMPVASIISNkggkTLVTNAGSNSKFLAVLDFEVkDKK----VTDFRYKLLPVFANmLPADAEMDALITKVRAPYE 147
Cdd:PRK09419   878 HTH--TLVDKVVNG----TPVVQAYKYGRALGRVDVKF-DKKgvvvVKTSRIDLSKIDDD-LPEDPEMKEILDKYEKELA 949

                          170
                   ....*....|
gi 2229888665  148 AKLAEKLAIT 157
Cdd:PRK09419   950 PIKNEKVGYT 959
 
Name Accession Description Interval E-value
thiosulf_SoxB TIGR04486
thiosulfohydrolase SoxB; SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type ...
 1-170 1.01e-111

thiosulfohydrolase SoxB; SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type cytochrome SoxXA in oxidation of thiosulfate to sulfate.


Pssm-ID: 275279 [Multi-domain]  Cd Length: 556  Bit Score: 328.42  E-value: 1.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDEARGKGAQVVVVLSHNGMDVDLKMASRVSGIDAIMGGHTHDGMPVA 80
Cdd:TIGR04486 226 IGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKGADAVVLLSHNGMDVDLKLASRVKGIDVILGGHTHDAVPQP 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  81 SIIsnkgGKTLVTNAGSNSKFLAVLDFEVKDKKVTDFRYKLLPVFANMLPADAEMDALITKVRAPYEAKLAEKLAITEGT 160
Cdd:TIGR04486 306 VRV----GNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLLPADPEMAALIEKVRAPYEAKLSEVLAVTESL 381

                         170
                  ....*....|
gi 2229888665 161 LYRRGNFNGT 170
Cdd:TIGR04486 382 LYRRGNFNGT 391
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 1-168 1.94e-56

2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms];


Pssm-ID: 440500 [Multi-domain]  Cd Length: 471  Bit Score: 183.52  E-value: 1.94e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDEARGKGAQVVVVLSHNGMD-VDLKMASRVSGIDAIMGGHTHDGMPV 79
Cdd:COG0737   141 IGLTTPDTPTWSSPGNIGGLTFTDPVEAAQKYVDELRAEGADVVVLLSHLGLDgEDRELAKEVPGIDVILGGHTHTLLPE 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  80 ASIIsnkGGKTLVTNAGSNSKFLAVLDFEVKD--KKVTDFRYKLLPVFANMLPADAEMDALITKVRAPYEAKLAEKLAIT 157
Cdd:COG0737   221 PVVV---NGGTLIVQAGSYGKYLGRLDLTLDDdgGKVVSVSAELIPVDDDLVPPDPEVAALVDEYRAKLEALLNEVVGTT 297

                         170
                  ....*....|.
gi 2229888665 158 EGTLYRRGNFN 168
Cdd:COG0737   298 EVPLDGYRAFV 308
MPP_SoxB_N cd07411
Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB ...
 1-124 7.84e-50

Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB (sulfur oxidation protein B) is a periplasmic thiosulfohydrolase and an essential component of the sulfur oxidation pathway in archaea and bacteria. SoxB has a dinuclear manganese cluster and is thought to catalyze the release of sulfate from a protein-bound cysteine S-thiosulfonate. SoxB is expressed from the sox (sulfur oxidation) gene cluster, which encodes 15 other sox genes, and has two domains, an N-terminal metallophosphatase domain and a C-terminal 5'-nucleotidase domain. SoxB binds the SoxYZ complex and is thought to function as a sulfate-thiohydrolase. SoxB is closely related to the UshA, YchR, and CpdB proteins, all of which have the same two-domain architecture. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that 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). 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 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: 277356 [Multi-domain]  Cd Length: 273  Bit Score: 161.35  E-value: 7.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDE-ARGKGAQVVVVLSHNGMDVDLKMASRVSGIDAIMGGHTHDGMPV 79
Cdd:cd07411   153 IGQAFPYVPIANPPSFSPGWSFGIREEELQEHVVKlRRAEGVDAVVLLSHNGMPVDVALAERVEGIDVILSGHTHDRVPE 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2229888665  80 AsiisNKGGKTLVTNAGSNSKFLAVLDFEVKDKKVTDFRYKLLPV 124
Cdd:cd07411   233 P----IRGGKTLVVAAGSHGKFVGRVDLKVRDGEIKSFRYELLPV 273
MPP_UshA_N_like cd00845
Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes ...
 1-124 4.09e-20

Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes the bacterial enzyme UshA, and related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that 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). 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 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: 277323 [Multi-domain]  Cd Length: 255  Bit Score: 83.89  E-value: 4.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   1 IGQAFPYTPIANPrymvADWAFGIQDENM----QKMVDEARGKGAQVVVVLSHNGMDVDLKMASRVSGIDAIMGGHTHDG 76
Cdd:cd00845   134 IGLTTPDTPTVTP----PEGNRGVEFPDPaeaiAEAAEELKAEGVDVIIALSHLGIDTDERLAAAVKGIDVILGGHSHTL 209

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2229888665  77 MPVASiisnKGGKTLVTNAGSNSKFLAVLDFEV--KDKKVTDFRYKLLPV 124
Cdd:cd00845   210 LEEPE----VVNGTLIVQAGAYGKYVGRVDLEFdkATKNVATTSGELVDV 255
MPP_CD73_N cd07409
CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain; CD73 is ...
 30-117 2.39e-12

CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain; CD73 is a mammalian ecto-5'-nucleotidase expressed in endothelial cells and lymphocytes that catalyzes the conversion of 5'-AMP to adenosine in the final step of a pathway that generates adenosine from ATP. This pathway also includes a CD39 nucleoside triphosphate dephosphorylase that mediates the dephosphorylation of ATP to ADP and then to 5'-AMP. These enzymes all have an N-terminal metallophosphatase domain and a C-terminal 5'nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that 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). 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 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: 277354 [Multi-domain]  Cd Length: 279  Bit Score: 62.98  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  30 QKMVDEARGKGAQVVVVLSHNGMDVDLKMASRVSGIDAIMGGHTH---------DGMPVA----SIISNKGG-KTLVTNA 95
Cdd:cd07409   170 QEEAKKLKAQGVNKIIALGHSGYEVDKEIAKKVPGVDVIVGGHSHtflytgpppSKEKPVgpypTVVKNPDGrKVLVVQA 249

                          90       100
                  ....*....|....*....|...
gi 2229888665  96 GSNSKFLAVLDFEVKDK-KVTDF 117
Cdd:cd07409   250 YAFGKYLGYLDVTFDAKgNVLSW 272
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
1-157 6.90e-12

multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 62.53  E-value: 6.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665    1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDEAR-GKGAQVVVVLSHNGMDVD--------LKMASRVSGIDAIMGG 71
Cdd:PRK09419   798 IGLTTPETAYKTSPGNVKNLEFKDPAEAAKKWVKELKeKEKVDAIIALTHLGSNQDrttgeitgLELAKKVKGVDAIISA 877

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   72 HTHdgMPVASIISNkggkTLVTNAGSNSKFLAVLDFEVkDKK----VTDFRYKLLPVFANmLPADAEMDALITKVRAPYE 147
Cdd:PRK09419   878 HTH--TLVDKVVNG----TPVVQAYKYGRALGRVDVKF-DKKgvvvVKTSRIDLSKIDDD-LPEDPEMKEILDKYEKELA 949

                          170
                   ....*....|
gi 2229888665  148 AKLAEKLAIT 157
Cdd:PRK09419   950 PIKNEKVGYT 959
MPP_CpdB_N cd07410
Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain; CpdB is a ...
 1-124 6.36e-11

Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain; CpdB is a bacterial periplasmic protein with an N-terminal metallophosphatase domain and a C-terminal 3'-nucleotidase domain. This alignment model represents the N-terminal metallophosphatase domain, which has 2',3'-cyclic phosphodiesterase activity, hydrolyzing the 2',3'-cyclic phosphates of adenosine, guanosine, cytosine and uridine to yield nucleoside and phosphate. CpdB also hydrolyzes the chromogenic substrates p-nitrophenyl phosphate (PNPP), bis(PNPP) and p-nitrophenyl phosphorylcholine (NPPC). CpdB is thought to play a scavenging role during RNA hydrolysis by converting the non-transportable nucleotides produced by RNaseI to nucleosides which can easily enter a cell for use as a carbon source. This family also includes YfkN, a Bacillus subtilis nucleotide phosphoesterase with two copies of each of the metallophosphatase and 3'-nucleotidase domains. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that 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). 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 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: 277355 [Multi-domain]  Cd Length: 280  Bit Score: 59.26  E-value: 6.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   1 IGQAFPYTPIANPRYMVADWAFGIQDENMQKMVDEARGKGAQVVVVLSHNGMDVDLK----------MASRVSGIDAIMG 70
Cdd:cd07410   144 LGLTTPQIPVWEKANLIGDLTFQDIVETAKKYVPELRAEGADVVVVLAHGGIEADLEqltgengaydLAKKVPGIDAIVT 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2229888665  71 GHTHDGMPvASIISNKGGKTLVTNAGSNSKFLAVLDFEVKDK----KVTDFRYKLLPV 124
Cdd:cd07410   224 GHQHREFP-GKVFNGTVNGVPVIEPGSRGNHLGVIDLTLEKTdgkwKVKDSKAELRPT 280
ushA PRK09558
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
 10-161 2.19e-10

bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed


Pssm-ID: 236566 [Multi-domain]  Cd Length: 551  Bit Score: 57.98  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  10 IANPRYmVADWAFGIQDENMQKMVDEAR-GKGAQVVVVLSHNGM------------DVDLKMASRVSGIDAIMGGHTHDg 76
Cdd:PRK09558  179 IGNPEY-FTDIEFRDPAEEAKKVIPELKqTEKPDVIIALTHMGHyddgehgsnapgDVEMARSLPAGGLDMIVGGHSQD- 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  77 mPVASIISNKGGK---------------TLVTNAGSNSKFLAVLDFEVKDKKVTDFRYKLLPV----------------- 124
Cdd:PRK09558  257 -PVCMAAENKKQVdyvpgtpckpdqqngTWIVQAHEWGKYVGRADFEFRNGELKLVSYQLIPVnlkkkvkwedgkservl 335

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2229888665 125 FANMLPADAEMDALITKVRAPYEAKLAEKLAITEGTL 161
Cdd:PRK09558  336 YTEEIAEDPQVLELLTPFQEKGQAQLDVKIGETNGKL 372
MPP_CG11883_N cd07406
Drosophila melanogaster CG11883 and related proteins, N-terminal metallophosphatase domain; ...
 31-128 1.12e-09

Drosophila melanogaster CG11883 and related proteins, N-terminal metallophosphatase domain; CG11883 is an uncharacterized Drosophila melanogaster UshA-like protein with two domains, an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that 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). 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 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: 277351 [Multi-domain]  Cd Length: 257  Bit Score: 55.36  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  31 KMVDEARGKGAQVVVVLSHNGMDVDLKMASRVSGIDAIMGGHTHDgmpvasIISNKGGKTLVTNAGSNSKFLAVLDFEVK 110
Cdd:cd07406   162 ELVVELREKGADVIIALTHMRLPNDIRLAQEVPEIDLILGGHDHE------YYIEEINGTLIVKSGTDFRNLSIIDLEVD 235

                          90
                  ....*....|....*....
gi 2229888665 111 DK-KVTDFRYKLLPVFANM 128
Cdd:cd07406   236 TGgRKWKVNIRRVDITSSI 254
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
27-145 1.21e-09

multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 55.98  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665   27 ENMQKMVDEARGKGAQVVVVLSHNGM----------DVDLKMASRVSGIDAIMGGHTHDGMP------VASIISNKG--G 88
Cdd:PRK09419   221 EEANKTIPEMKKGGADVIVALAHSGIeseyqssgaeDSVYDLAEKTKGIDAIVAGHQHGLFPgadykgVPQFDNAKGtiN 300

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2229888665   89 KTLVTNAGSNSKFLAVLDFEVKDK----KVTDFRYKLLPVFANMLPADAEMDALITK--------VRAP 145
Cdd:PRK09419   301 GIPVVMPKSWGKYLGKIDLTLEKDggkwKVVDKKSSLESISGKVVSRDETVVDALKDtheatiayVRAP 369
cpdB PRK09420
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
27-151 1.64e-07

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 236506 [Multi-domain]  Cd Length: 649  Bit Score: 49.93  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  27 ENMQKMVDEARGKGAQVVVVLSHNGMDVD--LKMA-------SRVSGIDAIMGGHTH--------DGMPVASIisNKG-- 87
Cdd:PRK09420  205 ETARKYVPEMKEKGADIVVAIPHSGISADpyKAMAensvyylSEVPGIDAIMFGHSHavfpgkdfADIPGADI--AKGtl 282

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2229888665  88 -GKTLVTNA--GSNskfLAVLDFEVKDK----KVTDFRYKLLPVF--ANMLPADAEMDALITKVRAPYEAKLA 151
Cdd:PRK09420  283 nGVPAVMPGrwGDH---LGVVDLVLENDsgkwQVTDAKAEARPIYdkANKKSLAAEDPKLVAALKADHQATRA 352
MPP_YhcR_N cd07412
Bacillus subtilis YhcR endonuclease and related proteins, N-terminal metallophosphatase domain; ...
 17-117 3.91e-07

Bacillus subtilis YhcR endonuclease and related proteins, N-terminal metallophosphatase domain; YhcR is a Bacillus subtilis sugar-nonspecific endonuclease. It cleaves endonucleolytically to yield nucleotide 3'-monophosphate products, similar to Staphylococcus aureus micrococcal nuclease. YhcR appears to be located in the cell wall, and is thought to be a substrate for a Bacillus subtilis sortase. YhcR is the major calcium-activated nuclease of B. subtilis. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that 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). 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 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: 277357 [Multi-domain]  Cd Length: 295  Bit Score: 48.52  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  17 VADWAFGIQDENMQKMVDEARGKGAQVVVVLSHNGM----DVDLKMASRVSG------------IDAIMGGHTHDGmpva 80
Cdd:cd07412   176 VEGLKFLDEAETINKYAPELKAKGVNAIVVLIHEGGsqapYFGTTACSALSGpivdivkkldpaVDVVISGHTHQY---- 251

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2229888665  81 siISNKGGKTLVTNAGSNSKFLAVLDFEVkDKKVTDF 117
Cdd:cd07412   252 --YNCTVGGRLVTQADSYGKAYADVTLTI-DPTTHDI 285
MPP_UshA_N cd07405
Escherichia coli UshA and related proteins, N-terminal metallophosphatase domain; UshA is a ...
 10-124 7.40e-07

Escherichia coli UshA and related proteins, N-terminal metallophosphatase domain; UshA is a bacterial periplasmic enzyme with UDP-sugar hydrolase and dinucleoside-polyphosphate hydrolase activities associated with its N-terminal metallophosphatase domain, and 5'-nucleotidase activity associated with its C-terminal domain. UshA has been studied in Escherichia coli where it is expressed from the ushA gene as an immature precursor and proteolytically cleaved to form a mature product upon export to the periplasm. UshA hydrolyzes many different nucleotides and nucleotide derivatives and has been shown to degrade external UDP-glucose to uridine, glucose 1-phosphate and phosphate for utilization by the cell. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that 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). 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 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: 277350 [Multi-domain]  Cd Length: 287  Bit Score: 47.63  E-value: 7.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  10 IANPRYMvADWAFGIQDENMQKMVDEAR-GKGAQVVVVLSHNG----------MDVDLKMASR--VSGIDAIMGGHTH-- 74
Cdd:cd07405   145 IGNPEYF-TDIEFRKPADEAKLVIQELQqTEKPDIIIAATHMGhydngehgsnAPGDVEMARAlpAGSLAMIVGGHSQdp 223

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2229888665  75 -----------DGMPVASIISNKGGKTLVTNAGSNSKFLAVLDFEVKDKKVTDFRYKLLPV 124
Cdd:cd07405   224 vcmaaenkkqvDYVPGTPCKPDQQNGIWIVQAHEWGKYVGRADFEFRNGEMKMVNYQLIPV 284
PRK09418 PRK09418
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
27-79 6.47e-06

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 236504 [Multi-domain]  Cd Length: 780  Bit Score: 45.09  E-value: 6.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2229888665  27 ENMQKMVDEARGKGAQVVVVLSHNGMD-----VDLKMAS----RVSGIDAIMGGHTH-------DGMPV 79
Cdd:PRK09418  231 ETAKKMVPKMKAEGADVIVALAHSGVDksgynVGMENASyyltEVPGVDAVLMGHSHtevkdvfNGVPV 299
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
27-138 3.55e-05

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 42.92  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888665  27 ENMQKMVDEARGKGAQVVVVLSHNGM----------DVDLKMASrVSGIDAIMGGHTHDGMPVASI------------IS 84
Cdd:PRK11907  296 EAVRDIIPTMRAAGADIVLVLSHSGIgddqyevgeeNVGYQIAS-LSGVDAVVTGHSHAEFPSGNGtsfyakysgvddIN 374

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2229888665  85 NKGGKTLVTNAGSNSKFLAVLDFEV--KDKK--VTDFRYKLLPVFANMLPADAEMDAL 138
Cdd:PRK11907  375 GKINGTPVTMAGKYGDHLGIIDLNLsyTDGKwtVTSSKAKIRKIDTKSTVADGRIIDL 432
 
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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