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Conserved domains on  [gi|2229888675|gb|UPI76623|]
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thiosulfate oxide protein subunit B, partial [uncultured Parasulfuritortus 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 ...
 1-171 4.21e-110

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: 324.18  E-value: 4.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTPIANPAYLIPDWSYGIRDDSMQRWVDEARAKGAKVVVVLSHNGMDVDLKMASRVNGIDAIFGGHTHDGVYQP 80
Cdd:TIGR04486 226 IGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKGADAVVLLSHNGMDVDLKLASRVKGIDVILGGHTHDAVPQP 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  81 VPVrrpdgGVCLVTNAGSNGKFLGVMDFDVKDGKIRSWKYRLLPVFSNFLPADPKMEAFIKQVRAPYEARLNEVLAVTDD 160
Cdd:TIGR04486 306 VRV-----GNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLLPADPEMAALIEKVRAPYEAKLSEVLAVTES 380

                         170
                  ....*....|.
gi 2229888675 161 LLYRRGNFNGT 171
Cdd:TIGR04486 381 LLYRRGNFNGT 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 ...
 1-171 4.21e-110

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: 324.18  E-value: 4.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTPIANPAYLIPDWSYGIRDDSMQRWVDEARAKGAKVVVVLSHNGMDVDLKMASRVNGIDAIFGGHTHDGVYQP 80
Cdd:TIGR04486 226 IGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKGADAVVLLSHNGMDVDLKLASRVKGIDVILGGHTHDAVPQP 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  81 VPVrrpdgGVCLVTNAGSNGKFLGVMDFDVKDGKIRSWKYRLLPVFSNFLPADPKMEAFIKQVRAPYEARLNEVLAVTDD 160
Cdd:TIGR04486 306 VRV-----GNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLLPADPEMAALIEKVRAPYEAKLSEVLAVTES 380

                         170
                  ....*....|.
gi 2229888675 161 LLYRRGNFNGT 171
Cdd:TIGR04486 381 LLYRRGNFNGT 391
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 1-169 3.64e-58

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: 188.14  E-value: 3.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTPIANPAYLIPDWSYGIRDDSMQRWVDEARAKGAKVVVVLSHNGMD-VDLKMASRVNGIDAIFGGHTHDGVYQ 79
Cdd:COG0737   141 IGLTTPDTPTWSSPGNIGGLTFTDPVEAAQKYVDELRAEGADVVVLLSHLGLDgEDRELAKEVPGIDVILGGHTHTLLPE 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  80 PVPVrrpdGGVCLVTNAGSNGKFLGVMDFDVKD--GKIRSWKYRLLPVFSNFLPADPKMEAFIKQVRAPYEARLNEVLAV 157
Cdd:COG0737   221 PVVV----NGGTLIVQAGSYGKYLGRLDLTLDDdgGKVVSVSAELIPVDDDLVPPDPEVAALVDEYRAKLEALLNEVVGT 296

                         170
                  ....*....|..
gi 2229888675 158 TDDLLYRRGNFN 169
Cdd:COG0737   297 TEVPLDGYRAFV 308
MPP_SoxB_N cd07411
Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB ...
 1-125 1.29e-52

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: 168.67  E-value: 1.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTPIANPAYLIPDWSYGIRDDSMQRWVDE-ARAKGAKVVVVLSHNGMDVDLKMASRVNGIDAIFGGHTHDGVYQ 79
Cdd:cd07411   153 IGQAFPYVPIANPPSFSPGWSFGIREEELQEHVVKlRRAEGVDAVVLLSHNGMPVDVALAERVEGIDVILSGHTHDRVPE 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2229888675  80 PVPvrrpdGGVCLVTNAGSNGKFLGVMDFDVKDGKIRSWKYRLLPV 125
Cdd:cd07411   233 PIR-----GGKTLVVAAGSHGKFVGRVDLKVRDGEIKSFRYELLPV 273
ushA PRK09558
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
 10-162 2.86e-16

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


Pssm-ID: 236566 [Multi-domain]  Cd Length: 551  Bit Score: 75.32  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  10 IANPAYlIPDWSYgiRD--DSMQRWVDEAR-AKGAKVVVVLSHNGM------------DVDLKMASRVNGIDAIFGGHTH 74
Cdd:PRK09558  179 IGNPEY-FTDIEF--RDpaEEAKKVIPELKqTEKPDVIIALTHMGHyddgehgsnapgDVEMARSLPAGGLDMIVGGHSQ 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  75 DGV-----------YQPVPVRRPD--GGVCLVtNAGSNGKFLGVMDFDVKDGKIRSWKYRLLPV---------------- 125
Cdd:PRK09558  256 DPVcmaaenkkqvdYVPGTPCKPDqqNGTWIV-QAHEWGKYVGRADFEFRNGELKLVSYQLIPVnlkkkvkwedgkserv 334

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2229888675 126 -FSNFLPADPKMEAFIKQVRAPYEARLNEVLAVTDDLL 162
Cdd:PRK09558  335 lYTEEIAEDPQVLELLTPFQEKGQAQLDVKIGETNGKL 372
PGA_cap pfam09587
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 9-85 4.11e-03

Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.


Pssm-ID: 430701 [Multi-domain]  Cd Length: 246  Bit Score: 36.44  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   9 PIANPAYLIPDWSYGIRDDSMQRWVDEARAKGAkVVVVLSHNGM-------DVDLKMASRV--NGIDAIFGGHTHdgVYQ 79
Cdd:pfam09587 149 GRGAGAPPERPGVAPIDLERILADIREARQPAD-VVIVSLHWGVeygyeppDEQRELARALidAGADVVIGHHPH--VLQ 225


                  ....*.
gi 2229888675  80 PVPVRR 85
Cdd:pfam09587 226 GIEIYR 231
 
Name Accession Description Interval E-value
thiosulf_SoxB TIGR04486
thiosulfohydrolase SoxB; SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type ...
 1-171 4.21e-110

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: 324.18  E-value: 4.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTPIANPAYLIPDWSYGIRDDSMQRWVDEARAKGAKVVVVLSHNGMDVDLKMASRVNGIDAIFGGHTHDGVYQP 80
Cdd:TIGR04486 226 IGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKGADAVVLLSHNGMDVDLKLASRVKGIDVILGGHTHDAVPQP 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  81 VPVrrpdgGVCLVTNAGSNGKFLGVMDFDVKDGKIRSWKYRLLPVFSNFLPADPKMEAFIKQVRAPYEARLNEVLAVTDD 160
Cdd:TIGR04486 306 VRV-----GNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLLPADPEMAALIEKVRAPYEAKLSEVLAVTES 380

                         170
                  ....*....|.
gi 2229888675 161 LLYRRGNFNGT 171
Cdd:TIGR04486 381 LLYRRGNFNGT 391
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 1-169 3.64e-58

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: 188.14  E-value: 3.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTPIANPAYLIPDWSYGIRDDSMQRWVDEARAKGAKVVVVLSHNGMD-VDLKMASRVNGIDAIFGGHTHDGVYQ 79
Cdd:COG0737   141 IGLTTPDTPTWSSPGNIGGLTFTDPVEAAQKYVDELRAEGADVVVLLSHLGLDgEDRELAKEVPGIDVILGGHTHTLLPE 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  80 PVPVrrpdGGVCLVTNAGSNGKFLGVMDFDVKD--GKIRSWKYRLLPVFSNFLPADPKMEAFIKQVRAPYEARLNEVLAV 157
Cdd:COG0737   221 PVVV----NGGTLIVQAGSYGKYLGRLDLTLDDdgGKVVSVSAELIPVDDDLVPPDPEVAALVDEYRAKLEALLNEVVGT 296

                         170
                  ....*....|..
gi 2229888675 158 TDDLLYRRGNFN 169
Cdd:COG0737   297 TEVPLDGYRAFV 308
MPP_SoxB_N cd07411
Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB ...
 1-125 1.29e-52

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: 168.67  E-value: 1.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTPIANPAYLIPDWSYGIRDDSMQRWVDE-ARAKGAKVVVVLSHNGMDVDLKMASRVNGIDAIFGGHTHDGVYQ 79
Cdd:cd07411   153 IGQAFPYVPIANPPSFSPGWSFGIREEELQEHVVKlRRAEGVDAVVLLSHNGMPVDVALAERVEGIDVILSGHTHDRVPE 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2229888675  80 PVPvrrpdGGVCLVTNAGSNGKFLGVMDFDVKDGKIRSWKYRLLPV 125
Cdd:cd07411   233 PIR-----GGKTLVVAAGSHGKFVGRVDLKVRDGEIKSFRYELLPV 273
MPP_UshA_N_like cd00845
Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes ...
 1-125 3.55e-24

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: 94.68  E-value: 3.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTPIANPayliPDWSYGIRDDSM----QRWVDEARAKGAKVVVVLSHNGMDVDLKMASRVNGIDAIFGGHTHDG 76
Cdd:cd00845   134 IGLTTPDTPTVTP----PEGNRGVEFPDPaeaiAEAAEELKAEGVDVIIALSHLGIDTDERLAAAVKGIDVILGGHSHTL 209

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2229888675  77 VYQPVPVrrpdGGVcLVTNAGSNGKFLGVMDFDV--KDGKIRSWKYRLLPV 125
Cdd:cd00845   210 LEEPEVV----NGT-LIVQAGAYGKYVGRVDLEFdkATKNVATTSGELVDV 255
MPP_CD73_N cd07409
CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain; CD73 is ...
 1-119 6.52e-18

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: 78.39  E-value: 6.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTP-IANPAYLIpdwsygIRD--DSMQRWVDEARAKGAKVVVVLSHNGMDVDLKMASRVNGIDAIFGGHTH--- 74
Cdd:cd07409   144 IGYTTPDTPtLSSPGKVK------FLDeiEAIQEEAKKLKAQGVNKIIALGHSGYEVDKEIAKKVPGVDVIVGGHSHtfl 217

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2229888675  75 -----------DGVYqPVPVRRPDGGVCLVTNAGSNGKFLGVMD--FDvKDGKIRSWK 119
Cdd:cd07409   218 ytgpppskekpVGPY-PTVVKNPDGRKVLVVQAYAFGKYLGYLDvtFD-AKGNVLSWE 273
ushA PRK09558
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
 10-162 2.86e-16

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


Pssm-ID: 236566 [Multi-domain]  Cd Length: 551  Bit Score: 75.32  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  10 IANPAYlIPDWSYgiRD--DSMQRWVDEAR-AKGAKVVVVLSHNGM------------DVDLKMASRVNGIDAIFGGHTH 74
Cdd:PRK09558  179 IGNPEY-FTDIEF--RDpaEEAKKVIPELKqTEKPDVIIALTHMGHyddgehgsnapgDVEMARSLPAGGLDMIVGGHSQ 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  75 DGV-----------YQPVPVRRPD--GGVCLVtNAGSNGKFLGVMDFDVKDGKIRSWKYRLLPV---------------- 125
Cdd:PRK09558  256 DPVcmaaenkkqvdYVPGTPCKPDqqNGTWIV-QAHEWGKYVGRADFEFRNGELKLVSYQLIPVnlkkkvkwedgkserv 334

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2229888675 126 -FSNFLPADPKMEAFIKQVRAPYEARLNEVLAVTDDLL 162
Cdd:PRK09558  335 lYTEEIAEDPQVLELLTPFQEKGQAQLDVKIGETNGKL 372
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
28-162 8.38e-15

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 71.00  E-value: 8.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   28 SMQRWVDEARAK-GAKVVVVLSHNGMDVD--------LKMASRVNGIDAIFGGHTH---DGVYQPVPvrrpdggvclVTN 95
Cdd:PRK09419   825 AAKKWVKELKEKeKVDAIIALTHLGSNQDrttgeitgLELAKKVKGVDAIISAHTHtlvDKVVNGTP----------VVQ 894

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   96 AGSNGKFLGVMD--FDvKDGKIRSWKYRL-LPVFSNFLPADPKMEAFIKQVRAPYEARLNEVLAVTDDLL 162
Cdd:PRK09419   895 AYKYGRALGRVDvkFD-KKGVVVVKTSRIdLSKIDDDLPEDPEMKEILDKYEKELAPIKNEKVGYTSVDL 963
MPP_CpdB_N cd07410
Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain; CpdB is a ...
 1-119 6.07e-13

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: 64.66  E-value: 6.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   1 IGQAFPYTPIANPAYLIPDWSYGIRDDSMQRWVDEARAKGAKVVVVLSHNGMDVDLK----------MASRVNGIDAIFG 70
Cdd:cd07410   144 LGLTTPQIPVWEKANLIGDLTFQDIVETAKKYVPELRAEGADVVVVLAHGGIEADLEqltgengaydLAKKVPGIDAIVT 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2229888675  71 GHTHDGVYQPVPVRRPDGgvCLVTNAGSNGKFLGVMDFDVK--DGKirsWK 119
Cdd:cd07410   224 GHQHREFPGKVFNGTVNG--VPVIEPGSRGNHLGVIDLTLEktDGK---WK 269
MPP_CG11883_N cd07406
Drosophila melanogaster CG11883 and related proteins, N-terminal metallophosphatase domain; ...
 31-129 9.68e-11

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: 58.44  E-value: 9.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  31 RWVDEARAKGAKVVVVLSHNGMDVDLKMASRVNGIDAIFGGHTHdgVYQPVPVrrpdgGVCLVTNAGSNGKFLGVMDFDV 110
Cdd:cd07406   162 ELVVELREKGADVIIALTHMRLPNDIRLAQEVPEIDLILGGHDH--EYYIEEI-----NGTLIVKSGTDFRNLSIIDLEV 234

                          90       100
                  ....*....|....*....|.
gi 2229888675 111 KDGKiRSWKY--RLLPVFSNF 129
Cdd:cd07406   235 DTGG-RKWKVniRRVDITSSI 254
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
27-160 1.33e-10

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 59.06  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   27 DSMQRWVDEARAKGAKVVVVLSHNGM----------DVDLKMASRVNGIDAIFGGHTHDGV----YQPVPVRRPDGGV-- 90
Cdd:PRK09419   221 EEANKTIPEMKKGGADVIVALAHSGIeseyqssgaeDSVYDLAEKTKGIDAIVAGHQHGLFpgadYKGVPQFDNAKGTin 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   91 -CLVTNAGSNGKFLGVMDFDVK--DGKIR--SWKYRLLPVFSNFLPADPKMEAFIKQ--------VRAPY---EARLNEV 154
Cdd:PRK09419   301 gIPVVMPKSWGKYLGKIDLTLEkdGGKWKvvDKKSSLESISGKVVSRDETVVDALKDtheatiayVRAPVgktEDDIKSI 380


                   ....*..
gi 2229888675  155 LA-VTDD 160
Cdd:PRK09419   381 FAsVKDD 387
MPP_UshA_N cd07405
Escherichia coli UshA and related proteins, N-terminal metallophosphatase domain; UshA is a ...
 41-125 2.98e-10

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: 57.26  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  41 AKVVVVLSHNG----------MDVDLKMASR--VNGIDAIFGGHTHDGV-----------YQPVPVRRPD--GGVcLVTN 95
Cdd:cd07405   176 PDIIIAATHMGhydngehgsnAPGDVEMARAlpAGSLAMIVGGHSQDPVcmaaenkkqvdYVPGTPCKPDqqNGI-WIVQ 254

                          90       100       110
                  ....*....|....*....|....*....|
gi 2229888675  96 AGSNGKFLGVMDFDVKDGKIRSWKYRLLPV 125
Cdd:cd07405   255 AHEWGKYVGRADFEFRNGEMKMVNYQLIPV 284
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
26-119 2.82e-07

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 49.08  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  26 DDSMQ---RWVDEARAKGAKVVVVLSHNGM----------DVDLKMASrVNGIDAIFGGHTH--------DGVYQPVP-V 83
Cdd:PRK11907  292 RDAVEavrDIIPTMRAAGADIVLVLSHSGIgddqyevgeeNVGYQIAS-LSGVDAVVTGHSHaefpsgngTSFYAKYSgV 370

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2229888675  84 RRPDGGV--CLVTNAGSNGKFLGVMDFDV--KDGKirsWK 119
Cdd:PRK11907  371 DDINGKIngTPVTMAGKYGDHLGIIDLNLsyTDGK---WT 407
PRK09418 PRK09418
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
27-114 4.55e-07

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


Pssm-ID: 236504 [Multi-domain]  Cd Length: 780  Bit Score: 48.55  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  27 DSMQRWVDEARAKGAKVVVVLSHNGMD-----VDLKMAS----RVNGIDAIFGGHTH---DGVYQPVPVRRPdgGVclvt 94
Cdd:PRK09418  231 ETAKKMVPKMKAEGADVIVALAHSGVDksgynVGMENASyyltEVPGVDAVLMGHSHtevKDVFNGVPVVMP--GV---- 304

                          90       100
                  ....*....|....*....|..
gi 2229888675  95 nAGSNgkfLGVMDFDVK--DGK 114
Cdd:PRK09418  305 -FGSN---LGIIDMQLKkvNGK 322
cpdB PRK09420
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
30-74 5.45e-07

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


Pssm-ID: 236506 [Multi-domain]  Cd Length: 649  Bit Score: 48.39  E-value: 5.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2229888675  30 QRWVDEARAKGAKVVVVLSHNGMDVD--LKMA-------SRVNGIDAIFGGHTH 74
Cdd:PRK09420  208 RKYVPEMKEKGADIVVAIPHSGISADpyKAMAensvyylSEVPGIDAIMFGHSH 261
MPP_YhcR_N cd07412
Bacillus subtilis YhcR endonuclease and related proteins, N-terminal metallophosphatase domain; ...
 27-107 1.92e-05

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: 43.51  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  27 DSMQRWVDEARAKGAKVVVVLSHNGM----DVDLKMASRVNG------------IDAIFGGHTHDGVYQPVpvrrpdGGV 90
Cdd:cd07412   186 ETINKYAPELKAKGVNAIVVLIHEGGsqapYFGTTACSALSGpivdivkkldpaVDVVISGHTHQYYNCTV------GGR 259

                          90
                  ....*....|....*..
gi 2229888675  91 cLVTNAGSNGKFLGVMD 107
Cdd:cd07412   260 -LVTQADSYGKAYADVT 275
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
17-122 3.90e-05

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 42.37  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675  17 IPDWSYGIRDDSMQRWVDEA-RAKGAKVVVVLSH-------NGMD-VDLKMASRV------NGIDAIFGGHTHdgvyqpV 81
Cdd:COG1409   114 VPGRSSGELGPEQLAWLEEElAAAPAKPVIVFLHhppystgSGSDrIGLRNAEELlallarYGVDLVLSGHVH------R 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2229888675  82 PVRRPDGGVCLVTNAGSNGKFL---GVMDFDVKDGKIRSWKYRL 122
Cdd:COG1409   188 YERTRRDGVPYIVAGSTGGQVRlppGYRVIEVDGDGLTVEVRRV 231
PGA_cap pfam09587
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 9-85 4.11e-03

Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.


Pssm-ID: 430701 [Multi-domain]  Cd Length: 246  Bit Score: 36.44  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2229888675   9 PIANPAYLIPDWSYGIRDDSMQRWVDEARAKGAkVVVVLSHNGM-------DVDLKMASRV--NGIDAIFGGHTHdgVYQ 79
Cdd:pfam09587 149 GRGAGAPPERPGVAPIDLERILADIREARQPAD-VVIVSLHWGVeygyeppDEQRELARALidAGADVVIGHHPH--VLQ 225


                  ....*.
gi 2229888675  80 PVPVRR 85
Cdd:pfam09587 226 GIEIYR 231
 
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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