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Conserved domains on  [gi|321399594|emb|CBJ49371|]
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sulfate thioesterase/sulfate thiohydrolase, partial [Phaeochromatium fluminis]

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 ...
 1-251 1.31e-141

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: 408.16  E-value: 1.31e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594    1 GACNLLGVDVMTGHWEFTYRDVEVIRNIGAFKGDFVAQNVkvreealFDYKFEDfagfdedmgLAFRPYSIKEIGGVKVA 80
Cdd:TIGR04486 161 DAMNLLGVDVMTGHWEFTYGQERVKELVEKLKGEFLAQNV-------FDADFGD---------PVFKPYVIKERGGVKVA 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   81 VVGQAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVREEEkPALVVVLSHNGMDVDLKMASRVTGIDVIFGGHTHDGVP 160
Cdd:TIGR04486 225 VIGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKG-ADAVVLLSHNGMDVDLKLASRVKGIDVILGGHTHDAVP 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  161 TPTIVanasGKTLVTNAGSNGKFVGVMDLDVKDGRLHDYRYRLLPVFSNLLKPDPAMADYIAGVRAPYKAKLEEKLAVAE 240
Cdd:TIGR04486 304 QPVRV----GNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLLPADPEMAALIEKVRAPYEAKLSEVLAVTE 379

                         250
                  ....*....|.
gi 321399594  241 KTLYRRGNFNG 251
Cdd:TIGR04486 380 SLLYRRGNFNG 390
 
Name Accession Description Interval E-value
thiosulf_SoxB TIGR04486
thiosulfohydrolase SoxB; SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type ...
 1-251 1.31e-141

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: 408.16  E-value: 1.31e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594    1 GACNLLGVDVMTGHWEFTYRDVEVIRNIGAFKGDFVAQNVkvreealFDYKFEDfagfdedmgLAFRPYSIKEIGGVKVA 80
Cdd:TIGR04486 161 DAMNLLGVDVMTGHWEFTYGQERVKELVEKLKGEFLAQNV-------FDADFGD---------PVFKPYVIKERGGVKVA 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   81 VVGQAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVREEEkPALVVVLSHNGMDVDLKMASRVTGIDVIFGGHTHDGVP 160
Cdd:TIGR04486 225 VIGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKG-ADAVVLLSHNGMDVDLKLASRVKGIDVILGGHTHDAVP 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  161 TPTIVanasGKTLVTNAGSNGKFVGVMDLDVKDGRLHDYRYRLLPVFSNLLKPDPAMADYIAGVRAPYKAKLEEKLAVAE 240
Cdd:TIGR04486 304 QPVRV----GNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLLPADPEMAALIEKVRAPYEAKLSEVLAVTE 379

                         250
                  ....*....|.
gi 321399594  241 KTLYRRGNFNG 251
Cdd:TIGR04486 380 SLLYRRGNFNG 390
MPP_SoxB_N cd07411
Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB ...
 2-206 2.25e-90

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: 268.05  E-value: 2.25e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   2 ACNLLGVDVMTGHWEFTYRDVEVIRNIGAFKGDFVAQNVKVREEAlfdykfedfagfdedmGLAFRPYSIKEIGGVKVAV 81
Cdd:cd07411   89 IMNLLGVDAMVGHWEFTYGKDRVLELLELLDGPFLAQNIFDEETG----------------DLLFPPYRIKEVGGLKIGV 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  82 VGQAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVREEEKPALVVVLSHNGMDVDLKMASRVTGIDVIFGGHTHDGVPT 161
Cdd:cd07411  153 IGQAFPYVPIANPPSFSPGWSFGIREEELQEHVVKLRRAEGVDAVVLLSHNGMPVDVALAERVEGIDVILSGHTHDRVPE 232

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 321399594 162 PtivaNASGKTLVTNAGSNGKFVGVMDLDVKDGRLHDYRYRLLPV 206
Cdd:cd07411  233 P----IRGGKTLVVAAGSHGKFVGRVDLKVRDGEIKSFRYELLPV 273
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 2-250 7.95e-75

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: 234.75  E-value: 7.95e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   2 ACNLLGVDVMT-GHWEFTYRDVEVIRNIGAFKGDFVAQNVKvreealfdykfedfagFDEDMGLAFRPYSIKEIGGVKVA 80
Cdd:COG0737   76 AMNALGYDAATlGNHEFDYGLDVLLELLDGANFPVLSANVY----------------DKDTGEPLFKPYTIKEVGGVKVG 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  81 VVGQAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVReEEKPALVVVLSHNGMD-VDLKMASRVTGIDVIFGGHTHDGV 159
Cdd:COG0737  140 VIGLTTPDTPTWSSPGNIGGLTFTDPVEAAQKYVDELR-AEGADVVVLLSHLGLDgEDRELAKEVPGIDVILGGHTHTLL 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594 160 PTPTIVANasgKTLVTNAGSNGKFVGVMDLDVKD--GRLHDYRYRLLPVFSNLLKPDPAMADYIAGVRAPYKAKLEEKLA 237
Cdd:COG0737  219 PEPVVVNG---GTLIVQAGSYGKYLGRLDLTLDDdgGKVVSVSAELIPVDDDLVPPDPEVAALVDEYRAKLEALLNEVVG 295

                        250
                 ....*....|...
gi 321399594 238 VAEKTLYRRGNFN 250
Cdd:COG0737  296 TTEVPLDGYRAFV 308
ushA PRK09558
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
 66-238 3.50e-24

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


Pssm-ID: 236566 [Multi-domain]  Cd Length: 551  Bit Score: 100.74  E-value: 3.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  66 FRPYSIKEIGGVKVAVVGQAFPYTP-IANPQrFIPDWTFGIQDGRMQEIVDQVREEEKPALVVVLSHNGM---------- 134
Cdd:PRK09558 153 FKPYAIFDRQGLKIAVIGLTTEDTAkIGNPE-YFTDIEFRDPAEEAKKVIPELKQTEKPDVIIALTHMGHyddgehgsna 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594 135 --DVDLKMASRVTGIDVIFGGHTHDGV----PTPTIVANASGK---------TLVTNAGSNGKFVGVMDLDVKDGRLHDY 199
Cdd:PRK09558 232 pgDVEMARSLPAGGLDMIVGGHSQDPVcmaaENKKQVDYVPGTpckpdqqngTWIVQAHEWGKYVGRADFEFRNGELKLV 311

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 321399594 200 RYRLLPVfsNL-------------------LKPDPAMADYIagvrAPYKAKLEEKLAV 238
Cdd:PRK09558 312 SYQLIPV--NLkkkvkwedgkservlyteeIAEDPQVLELL----TPFQEKGQAQLDV 363
PGA_cap pfam09587
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 45-156 2.24e-06

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: 47.22  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   45 EALFDYKFeDFAGFDEDMGLAFRPYsIKEIGGVKVAVVG--QAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVREEEK 122
Cdd:pfam09587 101 DALDRAGI-AHVGAGRDLAEARRPA-ILEVNGIRVAFLAytYGTNALASSGRGAGAPPERPGVAPIDLERILADIREARQ 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 321399594  123 PA-LVVVLSHNGM-------DVDLKMASRVT--GIDVIFGGHTH 156
Cdd:pfam09587 179 PAdVVIVSLHWGVeygyeppDEQRELARALIdaGADVVIGHHPH 222
PGA_cap smart00854
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 45-156 2.11e-04

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: 214858 [Multi-domain]  Cd Length: 239  Bit Score: 41.43  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594    45 EALFDYKFeDFAGFDEDMGLAFRPYsIKEIGGVKVAVVGqafpYTPIANPQRFIPD---WTFGIQDGRMQEIVDQVREEE 121
Cdd:smart00854  97 AALDAAGI-AHVGAGRNLAEARKPA-IVEVKGIKIALLA----YTYGTNNGWAASRdrpGVALLPDLDAEKILADIARAR 170

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 321399594   122 KPA-LVVVLSHNGM-------DVDLKMASRVT--GIDVIFGGHTH 156
Cdd:smart00854 171 KEAdVVIVSLHWGVeyqyeptPEQRELAHALIdaGADVVIGHHPH 215
 
Name Accession Description Interval E-value
thiosulf_SoxB TIGR04486
thiosulfohydrolase SoxB; SoxB, a di-manganese(II) enzyme, works with SoxYZ and the c-type ...
 1-251 1.31e-141

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: 408.16  E-value: 1.31e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594    1 GACNLLGVDVMTGHWEFTYRDVEVIRNIGAFKGDFVAQNVkvreealFDYKFEDfagfdedmgLAFRPYSIKEIGGVKVA 80
Cdd:TIGR04486 161 DAMNLLGVDVMTGHWEFTYGQERVKELVEKLKGEFLAQNV-------FDADFGD---------PVFKPYVIKERGGVKVA 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   81 VVGQAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVREEEkPALVVVLSHNGMDVDLKMASRVTGIDVIFGGHTHDGVP 160
Cdd:TIGR04486 225 VIGQAFPYTPIANPRRFTPDWSFGIREEELQKLVDELRAKG-ADAVVLLSHNGMDVDLKLASRVKGIDVILGGHTHDAVP 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  161 TPTIVanasGKTLVTNAGSNGKFVGVMDLDVKDGRLHDYRYRLLPVFSNLLKPDPAMADYIAGVRAPYKAKLEEKLAVAE 240
Cdd:TIGR04486 304 QPVRV----GNTLVTNAGSNGKFLGRLDLDVKKGKVKDFRYRLLPVFSNLLPADPEMAALIEKVRAPYEAKLSEVLAVTE 379

                         250
                  ....*....|.
gi 321399594  241 KTLYRRGNFNG 251
Cdd:TIGR04486 380 SLLYRRGNFNG 390
MPP_SoxB_N cd07411
Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB ...
 2-206 2.25e-90

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: 268.05  E-value: 2.25e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   2 ACNLLGVDVMTGHWEFTYRDVEVIRNIGAFKGDFVAQNVKVREEAlfdykfedfagfdedmGLAFRPYSIKEIGGVKVAV 81
Cdd:cd07411   89 IMNLLGVDAMVGHWEFTYGKDRVLELLELLDGPFLAQNIFDEETG----------------DLLFPPYRIKEVGGLKIGV 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  82 VGQAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVREEEKPALVVVLSHNGMDVDLKMASRVTGIDVIFGGHTHDGVPT 161
Cdd:cd07411  153 IGQAFPYVPIANPPSFSPGWSFGIREEELQEHVVKLRRAEGVDAVVLLSHNGMPVDVALAERVEGIDVILSGHTHDRVPE 232

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 321399594 162 PtivaNASGKTLVTNAGSNGKFVGVMDLDVKDGRLHDYRYRLLPV 206
Cdd:cd07411  233 P----IRGGKTLVVAAGSHGKFVGRVDLKVRDGEIKSFRYELLPV 273
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 2-250 7.95e-75

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: 234.75  E-value: 7.95e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   2 ACNLLGVDVMT-GHWEFTYRDVEVIRNIGAFKGDFVAQNVKvreealfdykfedfagFDEDMGLAFRPYSIKEIGGVKVA 80
Cdd:COG0737   76 AMNALGYDAATlGNHEFDYGLDVLLELLDGANFPVLSANVY----------------DKDTGEPLFKPYTIKEVGGVKVG 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  81 VVGQAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVReEEKPALVVVLSHNGMD-VDLKMASRVTGIDVIFGGHTHDGV 159
Cdd:COG0737  140 VIGLTTPDTPTWSSPGNIGGLTFTDPVEAAQKYVDELR-AEGADVVVLLSHLGLDgEDRELAKEVPGIDVILGGHTHTLL 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594 160 PTPTIVANasgKTLVTNAGSNGKFVGVMDLDVKD--GRLHDYRYRLLPVFSNLLKPDPAMADYIAGVRAPYKAKLEEKLA 237
Cdd:COG0737  219 PEPVVVNG---GTLIVQAGSYGKYLGRLDLTLDDdgGKVVSVSAELIPVDDDLVPPDPEVAALVDEYRAKLEALLNEVVG 295

                        250
                 ....*....|...
gi 321399594 238 VAEKTLYRRGNFN 250
Cdd:COG0737  296 TTEVPLDGYRAFV 308
MPP_UshA_N_like cd00845
Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes ...
 4-194 1.79e-33

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: 121.64  E-value: 1.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   4 NLLGVDVMT-GHWEFTYrDVEVIRNI-GAFKGDFVAQNVKvreealfdykfEDFAGFDEDmglAFRPYSIKEIGGVKVAV 81
Cdd:cd00845   69 NALGYDAATvGNHEFDY-GLDQLEELlKQAKFPWLSANVY-----------EDGTGTGEP---GAKPYTIITVDGVKVGV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  82 VGQAFPYTPIANPqrfiPDWTFGIQDGRMQEIVDQVREE---EKPALVVVLSHNGMDVDLKMASRVTGIDVIFGGHTHDG 158
Cdd:cd00845  134 IGLTTPDTPTVTP----PEGNRGVEFPDPAEAIAEAAEElkaEGVDVIIALSHLGIDTDERLAAAVKGIDVILGGHSHTL 209

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 321399594 159 VPTPTIVanasGKTLVTNAGSNGKFVGVMDLDVKDG 194
Cdd:cd00845  210 LEEPEVV----NGTLIVQAGAYGKYVGRVDLEFDKA 241
ushA PRK09558
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
 66-238 3.50e-24

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


Pssm-ID: 236566 [Multi-domain]  Cd Length: 551  Bit Score: 100.74  E-value: 3.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  66 FRPYSIKEIGGVKVAVVGQAFPYTP-IANPQrFIPDWTFGIQDGRMQEIVDQVREEEKPALVVVLSHNGM---------- 134
Cdd:PRK09558 153 FKPYAIFDRQGLKIAVIGLTTEDTAkIGNPE-YFTDIEFRDPAEEAKKVIPELKQTEKPDVIIALTHMGHyddgehgsna 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594 135 --DVDLKMASRVTGIDVIFGGHTHDGV----PTPTIVANASGK---------TLVTNAGSNGKFVGVMDLDVKDGRLHDY 199
Cdd:PRK09558 232 pgDVEMARSLPAGGLDMIVGGHSQDPVcmaaENKKQVDYVPGTpckpdqqngTWIVQAHEWGKYVGRADFEFRNGELKLV 311

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 321399594 200 RYRLLPVfsNL-------------------LKPDPAMADYIagvrAPYKAKLEEKLAV 238
Cdd:PRK09558 312 SYQLIPV--NLkkkvkwedgkservlyteeIAEDPQVLELL----TPFQEKGQAQLDV 363
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
4-238 2.62e-20

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 89.88  E-value: 2.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594    4 NLLGVDVMT-GHWEFTY---------RDVEVIRNIGAFKG---DFVAQNVKVREEAlfdyKFEDFAgfdedmglafRPYS 70
Cdd:PRK09419  721 KEMGYDASTfGNHEFDWgpdvlpdwlKGGGDPKNRHQFEKpdfPFVASNIYVKKTG----KLVSWA----------KPYI 786

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   71 IKEIGGVKVAVVGQAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVREEEKPALVVVLSHNGMDVD--------LKMAS 142
Cdd:PRK09419  787 LVEVNGKKVGFIGLTTPETAYKTSPGNVKNLEFKDPAEAAKKWVKELKEKEKVDAIIALTHLGSNQDrttgeitgLELAK 866

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  143 RVTGIDVIFGGHTH---DGVPTPTIVANASgktlvtnagSNGKFVGvmDLDVKdgrlHDYRYRLLPVFSNL--------L 211
Cdd:PRK09419  867 KVKGVDAIISAHTHtlvDKVVNGTPVVQAY---------KYGRALG--RVDVK----FDKKGVVVVKTSRIdlskidddL 931

                         250       260
                  ....*....|....*....|....*..
gi 321399594  212 KPDPAMADyiagVRAPYKAKLEEKLAV 238
Cdd:PRK09419  932 PEDPEMKE----ILDKYEKELAPIKNE 954
MPP_CD73_N cd07409
CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain; CD73 is ...
 4-199 9.70e-20

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: 85.71  E-value: 9.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   4 NLLGVDVMT-GHWEFTyRDVEVIRN-IGAFKGDFVAQNVKVREEALFDYKFedfagfdedmglafRPYSIKEIGGVKVAV 81
Cdd:cd07409   79 NLLGYDAMTlGNHEFD-DGPEGLAPfLENLKFPVLSANIDASNEPLLAGLL--------------KPSTILTVGGEKIGV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  82 VGQAFPYTP-IANPqrfiPDWTFGIQDGRMQEIVDQVREEeKPALVVVLSHNGMDVDLKMASRVTGIDVIFGGHTH---- 156
Cdd:cd07409  144 IGYTTPDTPtLSSP----GKVKFLDEIEAIQEEAKKLKAQ-GVNKIIALGHSGYEVDKEIAKKVPGVDVIVGGHSHtfly 218

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 321399594 157 DGVPT---------PTIVANASG-KTLVTNAGSNGKFVGvmDLDV---KDGRLHDY 199
Cdd:cd07409  219 TGPPPskekpvgpyPTVVKNPDGrKVLVVQAYAFGKYLG--YLDVtfdAKGNVLSW 272
MPP_CpdB_N cd07410
Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain; CpdB is a ...
 2-192 1.21e-17

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: 80.06  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   2 ACNLLGVDVMT-GHWEFTYRDVEVIRNIGAFKGDFVAQNVKvreealfdykfedfagfDEDMGLAF-RPYSIKEIG-GVK 78
Cdd:cd07410   78 AMNALKYDAGVlGNHEFNYGLDYLDRAIKQAKFPVLSANII-----------------DAKTGEPFlPPYVIKEREvGVK 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  79 VAVVGQAFPYTPIANPQRFIPDWTFgiqdgrmQEIVDQVRE------EEKPALVVVLSHNGMDVDLK----------MAS 142
Cdd:cd07410  141 IGILGLTTPQIPVWEKANLIGDLTF-------QDIVETAKKyvpelrAEGADVVVVLAHGGIEADLEqltgengaydLAK 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 321399594 143 RVTGIDVIFGGHTHDGVPTPTIVANASGKTlVTNAGSNGKFVGVMDLDVK 192
Cdd:cd07410  214 KVPGIDAIVTGHQHREFPGKVFNGTVNGVP-VIEPGSRGNHLGVIDLTLE 262
MPP_UshA_N cd07405
Escherichia coli UshA and related proteins, N-terminal metallophosphatase domain; UshA is a ...
 50-206 2.06e-16

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: 76.52  E-value: 2.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  50 YKFEDF----AGF-DEDMG-LAFRPYSIKEIGGVKVAVVGQAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVREEEKP 123
Cdd:cd07405   97 EKWAKFpllsANIyQKSTGeRLFKPWALFKRQDLKIAVIGLTTDDTAKIGNPEYFTDIEFRKPADEAKLVIQELQQTEKP 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594 124 ALVVVLSHNG----------MDVDLKMASR--VTGIDVIFGGHTH-------------DGVPTPTIVANASGKTLVTNAG 178
Cdd:cd07405  177 DIIIAATHMGhydngehgsnAPGDVEMARAlpAGSLAMIVGGHSQdpvcmaaenkkqvDYVPGTPCKPDQQNGIWIVQAH 256

                        170       180
                 ....*....|....*....|....*...
gi 321399594 179 SNGKFVGVMDLDVKDGRLHDYRYRLLPV 206
Cdd:cd07405  257 EWGKYVGRADFEFRNGEMKMVNYQLIPV 284
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
66-192 3.04e-09

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 57.14  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   66 FRPYSIKEIG---------GVKVAVVGqafpytpIANPQrfIPDWTFGIQDGR--MQEIVDQVRE------EEKPALVVV 128
Cdd:PRK09419  170 YTPYKIKEKTvtdengkkqGVKVGYIG-------FVPPQ--IMTWDKKNLKGKveVKNIVEEANKtipemkKGGADVIVA 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  129 LSHNGM----------DVDLKMASRVTGIDVIFGGHTHDGVPTP-----TIVANASGK---TLVTNAGSNGKFVGVMDLD 190
Cdd:PRK09419  241 LAHSGIeseyqssgaeDSVYDLAEKTKGIDAIVAGHQHGLFPGAdykgvPQFDNAKGTingIPVVMPKSWGKYLGKIDLT 320


                  ..
gi 321399594  191 VK 192
Cdd:PRK09419  321 LE 322
MPP_YhcR_N cd07412
Bacillus subtilis YhcR endonuclease and related proteins, N-terminal metallophosphatase domain; ...
 64-198 1.00e-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: 51.60  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  64 LAFRPYSIKEIGGVKVAVVGQAFPYTPIANPQRFIPDWTFgiQDgRMQEIVDQVREEEKPAL--VVVLSHNGM----DVD 137
Cdd:cd07412  142 PLLPPYLIKEIHGVPIAFIGAVTKSTPDIVSPENVEGLKF--LD-EAETINKYAPELKAKGVnaIVVLIHEGGsqapYFG 218

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 321399594 138 LKMASRVTG------------IDVIFGGHTHDGVptptivaNAS-GKTLVTNAGSNGKFVGVMDLDVkDGRLHD 198
Cdd:cd07412  219 TTACSALSGpivdivkkldpaVDVVISGHTHQYY-------NCTvGGRLVTQADSYGKAYADVTLTI-DPTTHD 284
MPP_CG11883_N cd07406
Drosophila melanogaster CG11883 and related proteins, N-terminal metallophosphatase domain; ...
 66-210 4.03e-07

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: 49.58  E-value: 4.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  66 FRPYSIKEIGGVKVAVVGQAfpytpianpqrfIPDWTFGIQDG----RMQEIVDQVRE------EEKPALVVVLSHNGMD 135
Cdd:cd07406  117 GKEHHIIERNGVKIGLLGLV------------EEEWLETLTINppnvEYRDYIETARElvvelrEKGADVIIALTHMRLP 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321399594 136 VDLKMASRVTGIDVIFGGHTHDGVPTPTivanasGKTLVTNAGSNGKFVGVMDLDVKDGRLH-DYRYRLLPVFSNL 210
Cdd:cd07406  185 NDIRLAQEVPEIDLILGGHDHEYYIEEI------NGTLIVKSGTDFRNLSIIDLEVDTGGRKwKVNIRRVDITSSI 254
PGA_cap pfam09587
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 45-156 2.24e-06

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: 47.22  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   45 EALFDYKFeDFAGFDEDMGLAFRPYsIKEIGGVKVAVVG--QAFPYTPIANPQRFIPDWTFGIQDGRMQEIVDQVREEEK 122
Cdd:pfam09587 101 DALDRAGI-AHVGAGRDLAEARRPA-ILEVNGIRVAFLAytYGTNALASSGRGAGAPPERPGVAPIDLERILADIREARQ 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 321399594  123 PA-LVVVLSHNGM-------DVDLKMASRVT--GIDVIFGGHTH 156
Cdd:pfam09587 179 PAdVVIVSLHWGVeygyeppDEQRELARALIdaGADVVIGHHPH 222
PRK09418 PRK09418
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
4-192 2.64e-06

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


Pssm-ID: 236504 [Multi-domain]  Cd Length: 780  Bit Score: 48.17  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   4 NLLGVDVMT-GHWEFTYrDVEVIRNIGAfKGDFVAQNVKVreealfdYKfEDFAGFDEDMGLAFRPYSI--KEI---GG- 76
Cdd:PRK09418 127 NLMKYDVISlGNHEFNY-GLDYLNKVIS-KTEFPVINSNV-------YK-DDKDNNEENDQNYFKPYHVfeKEVedeSGq 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  77 ---VKVAVVGqafpYTPianPQrfIPDWTFGIQDGRMQ--EIVDQVR------EEEKPALVVVLSHNGMD-----VDLKM 140
Cdd:PRK09418 197 kqkVKIGVMG----FVP---PQ--VMNWDKANLEGKVKakDIVETAKkmvpkmKAEGADVIVALAHSGVDksgynVGMEN 267

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 321399594 141 AS----RVTGIDVIFGGHTHdgvptpTIVANASGKTLVTNAGSNGKFVGVMDLDVK 192
Cdd:PRK09418 268 ASyyltEVPGVDAVLMGHSH------TEVKDVFNGVPVVMPGVFGSNLGIIDMQLK 317
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
2-195 4.58e-06

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 47.16  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594   2 ACNLLGVDVMT-GHWEFTYrDVEVIRNIGAFKG-DFVAQNVkvreealFDYKFEDFAgfdedmglaFRPYSI-----KEI 74
Cdd:PRK11907 196 ALEALGFDAGTlGNHEFNY-GLDYLEKVIATANmPIVNANV-------LDPTTGDFL---------YTPYTIvtktfTDT 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  75 GGVKVAV-VGqafpYTPIANPQrfIPDWTFGIQDGR---------MQEIVDQVREEeKPALVVVLSHNGM---------- 134
Cdd:PRK11907 259 EGKKVTLnIG----ITGIVPPQ--ILNWDKANLEGKvivrdaveaVRDIIPTMRAA-GADIVLVLSHSGIgddqyevgee 331

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 321399594 135 DVDLKMASrVTGIDVIFGGHTHDGVPTP---------TIVANASGK---TLVTNAGSNGKFVGVMDLDV--KDGR 195
Cdd:PRK11907 332 NVGYQIAS-LSGVDAVVTGHSHAEFPSGngtsfyakySGVDDINGKingTPVTMAGKYGDHLGIIDLNLsyTDGK 405
PGA_cap smart00854
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 45-156 2.11e-04

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: 214858 [Multi-domain]  Cd Length: 239  Bit Score: 41.43  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594    45 EALFDYKFeDFAGFDEDMGLAFRPYsIKEIGGVKVAVVGqafpYTPIANPQRFIPD---WTFGIQDGRMQEIVDQVREEE 121
Cdd:smart00854  97 AALDAAGI-AHVGAGRNLAEARKPA-IVEVKGIKIALLA----YTYGTNNGWAASRdrpGVALLPDLDAEKILADIARAR 170

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 321399594   122 KPA-LVVVLSHNGM-------DVDLKMASRVT--GIDVIFGGHTH 156
Cdd:smart00854 171 KEAdVVIVSLHWGVeyqyeptPEQRELAHALIdaGADVVIGHHPH 215
MPP_CapA cd07381
CapA and related proteins, metallophosphatase domain; CapA is one of three membrane-associated ...
 45-156 2.99e-04

CapA and related proteins, metallophosphatase domain; CapA is one of three membrane-associated enzymes in Bacillus anthracis that is required for synthesis of gamma-polyglutamic acid (PGA), a major component of the bacterial capsule. The YwtB and PgsA proteins of Bacillus subtilis are closely related to CapA and are also included in this alignment model. CapA 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: 277327 [Multi-domain]  Cd Length: 239  Bit Score: 41.12  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  45 EALFDYKFeDFAGFDEDMGLAFRPySIKEIGGVKVAVVGqafpYTPIANPQRFIPD--WTFGIQDGRMQEIVDQVREEEK 122
Cdd:cd07381  100 EALDRAGI-DHAGAGRNLAEAGRP-AYLEVKGVRVAFLG----YTTGTNGGPEAADaaPGALVNDADEAAILADVAEAKK 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 321399594 123 PA-LVVVLSHNGM-------DVDLKMASRVT--GIDVIFGGHTH 156
Cdd:cd07381  174 KAdIVIVSLHWGGeygyepaPEQRQLARALIdaGADLVVGHHPH 217
CapA COG2843
Poly-gamma-glutamate biosynthesis protein CapA/YwtB (capsule formation), metallophosphatase ...
 65-156 4.61e-04

Poly-gamma-glutamate biosynthesis protein CapA/YwtB (capsule formation), metallophosphatase superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442091 [Multi-domain]  Cd Length: 310  Bit Score: 40.66  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321399594  65 AFRPYsIKEIGGVKVAVVGqafpYTPIANPQRFIPD--WTFGIQDgrMQEIVDQVREEEKPA-LVVVLSHNGM------- 134
Cdd:COG2843  125 ARRPL-ILEVNGVRVAFLA----YTYGTNEWAAGEDkpGVANLDD--LERIKEDIAAARAGAdLVIVSLHWGVeyerepn 197

                         90       100
                 ....*....|....*....|....
gi 321399594 135 DVDLKMASRVT--GIDVIFGGHTH 156
Cdd:COG2843  198 PEQRELARALIdaGADLVIGHHPH 221
 
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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