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Conserved domains on  [gi|2163862258|ref|WP_231523769|]
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bifunctional UDP-sugar hydrolase/5'-nucleotidase [Lactobacillus delbrueckii]

Protein Classification

bifunctional metallophosphatase/5'-nucleotidase( domain architecture ID 11432654)

bifunctional metallophosphatase/5'-nucleotidase contains an N-terminal metallophosphoesterase family domain that contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and a 5'-nucleotidase C-terminal domain

CATH:  3.60.21.10|3.90.780.10
EC:  3.1.3.5|3.1.-.-
Gene Ontology:  GO:0042578|GO:0046872|GO:0008253|GO:0009166|GO:0000166
PubMed:  25837850|8003970
SCOP:  3001067|4001892

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 1-507 6.38e-134

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: 396.53  E-value: 6.38e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   1 MKLVFLHSSDTHGYLLPTDYqSTGDYDAPYGLSRVASAIKAEKAKwgADHVIVTDAGDCLQGSPLAAYTHGSKNLDnlar 80
Cdd:COG0737     3 VTLTILHTNDLHGHLEPYDY-FDDKYGKAGGLARLATLIKQLRAE--NPNTLLLDAGDTIQGSPLSTLTKGEPMIE---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  81 ftaAYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQVPtLGRDYVILERSGVKVGVLGITTQYIPHW 160
Cdd:COG0737    76 ---AMNALGYDAATLGNHEFDYGLDVLLELLDGANFPVLSANVYDKDTGEP-LFKPYTIKEVGGVKVGVIGLTTPDTPTW 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 161 EAADRIKGLAFKSAYEQIAHFAKIIKPQ-VDVLAVLYHGGFEsdiasgeatephnGENEgyRILTEIPEVDVMLTGHQHR 239
Cdd:COG0737   152 SSPGNIGGLTFTDPVEAAQKYVDELRAEgADVVVLLSHLGLD-------------GEDR--ELAKEVPGIDVILGGHTHT 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 240 RLNMIS--PSGKPCVQPGYRGEAIAEVVLDLEKteAGYKVKEATSELIDTKD--FASDPEVEEIVKPLDLATQKWLDQPI 315
Cdd:COG0737   217 LLPEPVvvNGGTLIVQAGSYGKYLGRLDLTLDD--DGGKVVSVSAELIPVDDdlVPPDPEVAALVDEYRAKLEALLNEVV 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 316 AHLDQPAPIEDANkGRIEGAPFINLLQQMQLYFTHADLSAT---AVMNDVAKGfgkTVTMRDILLNYPYANQLVSVKLTG 392
Cdd:COG0737   295 GTTEVPLDGYRAF-VRGGESPLGNLIADAQLEATGADIALTnggGIRADLPAG---PITYGDVYTVLPFGNTLVVVELTG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 393 KQLRHIVEHTASFLEKDENGKihfidrylkpkpelYHFDVFYPLEYEADLSKPVGQRLTKLKFKGQDIQDDQVYHLAVNN 472
Cdd:COG0737   371 AQLKEALEQSASNIFPGDGFG--------------GNFLQVSGLTYTIDPSKPAGSRITDLTVNGKPLDPDKTYRVATND 436

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 2163862258 473 YRANGGGFYPEYSLDKIEFSLDKDYVQMFSEYLTQ 507
Cdd:COG0737   437 YLASGGDGYPMFKGGKDVPDTGPTLRDVLADYLKA 471
 
Name Accession Description Interval E-value
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 1-507 6.38e-134

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: 396.53  E-value: 6.38e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   1 MKLVFLHSSDTHGYLLPTDYqSTGDYDAPYGLSRVASAIKAEKAKwgADHVIVTDAGDCLQGSPLAAYTHGSKNLDnlar 80
Cdd:COG0737     3 VTLTILHTNDLHGHLEPYDY-FDDKYGKAGGLARLATLIKQLRAE--NPNTLLLDAGDTIQGSPLSTLTKGEPMIE---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  81 ftaAYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQVPtLGRDYVILERSGVKVGVLGITTQYIPHW 160
Cdd:COG0737    76 ---AMNALGYDAATLGNHEFDYGLDVLLELLDGANFPVLSANVYDKDTGEP-LFKPYTIKEVGGVKVGVIGLTTPDTPTW 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 161 EAADRIKGLAFKSAYEQIAHFAKIIKPQ-VDVLAVLYHGGFEsdiasgeatephnGENEgyRILTEIPEVDVMLTGHQHR 239
Cdd:COG0737   152 SSPGNIGGLTFTDPVEAAQKYVDELRAEgADVVVLLSHLGLD-------------GEDR--ELAKEVPGIDVILGGHTHT 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 240 RLNMIS--PSGKPCVQPGYRGEAIAEVVLDLEKteAGYKVKEATSELIDTKD--FASDPEVEEIVKPLDLATQKWLDQPI 315
Cdd:COG0737   217 LLPEPVvvNGGTLIVQAGSYGKYLGRLDLTLDD--DGGKVVSVSAELIPVDDdlVPPDPEVAALVDEYRAKLEALLNEVV 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 316 AHLDQPAPIEDANkGRIEGAPFINLLQQMQLYFTHADLSAT---AVMNDVAKGfgkTVTMRDILLNYPYANQLVSVKLTG 392
Cdd:COG0737   295 GTTEVPLDGYRAF-VRGGESPLGNLIADAQLEATGADIALTnggGIRADLPAG---PITYGDVYTVLPFGNTLVVVELTG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 393 KQLRHIVEHTASFLEKDENGKihfidrylkpkpelYHFDVFYPLEYEADLSKPVGQRLTKLKFKGQDIQDDQVYHLAVNN 472
Cdd:COG0737   371 AQLKEALEQSASNIFPGDGFG--------------GNFLQVSGLTYTIDPSKPAGSRITDLTVNGKPLDPDKTYRVATND 436

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 2163862258 473 YRANGGGFYPEYSLDKIEFSLDKDYVQMFSEYLTQ 507
Cdd:COG0737   437 YLASGGDGYPMFKGGKDVPDTGPTLRDVLADYLKA 471
MPP_CpdB_N cd07410
Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain; CpdB is a ...
 3-287 5.74e-81

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: 253.79  E-value: 5.74e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   3 LVFLHSSDTHGYLLPTDYqSTGDYDAPYGLSRVASAIKAEKAKWGadHVIVTDAGDCLQGSPLAAYTHGSKNLDnLARFT 82
Cdd:cd07410     1 LRILETSDLHGNVLPYDY-AKDKPTLPFGLARTATLIKKARAENP--NTVLVDNGDLIQGNPLAYYYATIKDGP-IHPLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  83 AAYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQvPTLGRDYVILERS-GVKVGVLGITTQYIPHWE 161
Cdd:cd07410    77 AAMNALKYDAGVLGNHEFNYGLDYLDRAIKQAKFPVLSANIIDAKTG-EPFLPPYVIKEREvGVKIGILGLTTPQIPVWE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 162 AADRIKGLAFKSAYEQIAHFAKIIKP-QVDVLAVLYHGGFESDIASGEatephnGENEGYRILTEIPEVDVMLTGHQHRR 240
Cdd:cd07410   156 KANLIGDLTFQDIVETAKKYVPELRAeGADVVVVLAHGGIEADLEQLT------GENGAYDLAKKVPGIDAIVTGHQHRE 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2163862258 241 LNMIS----PSGKPCVQPGYRGEAIAEVVLDLEKTEAGYKVKEATSELIDT 287
Cdd:cd07410   230 FPGKVfngtVNGVPVIEPGSRGNHLGVIDLTLEKTDGKWKVKDSKAELRPT 280
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
6-516 6.44e-59

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 211.22  E-value: 6.44e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258    6 LHSSDTHGYLLPTDYQSTGDYDApYGLSRVASAIKaeKAKWGADHVIVTDAGDCLQGSPLAAYTHGSKNL--DNLARFTA 83
Cdd:PRK09419    45 LATTDLHGNFMDYDYASDKETTG-FGLAQTATLIK--KARKENPNTLLVDNGDLIQGNPLGEYAVKDNILfkNKTHPMIK 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   84 AYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQ---VPtlgrdYVILERS---------GVKVGVLG 151
Cdd:PRK09419   122 AMNALGYDAGTLGNHEFNYGLDFLDGTIKGANFPVLNANVKYKNGKnvyTP-----YKIKEKTvtdengkkqGVKVGYIG 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  152 ITTQYIPHWEAadriKGLAFKSAYEQIAHFAKIIKPQV-----DVLAVLYHGGFESDiasgeaTEPHNGENEGYRILTEI 226
Cdd:PRK09419   197 FVPPQIMTWDK----KNLKGKVEVKNIVEEANKTIPEMkkggaDVIVALAHSGIESE------YQSSGAEDSVYDLAEKT 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  227 PEVDVMLTGHQHR-------------RLNMISPSGKPCVQPGYRGEAIAEVVLDLEKTEAGYKVKEATS--ELIDTKDFA 291
Cdd:PRK09419   267 KGIDAIVAGHQHGlfpgadykgvpqfDNAKGTINGIPVVMPKSWGKYLGKIDLTLEKDGGKWKVVDKKSslESISGKVVS 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  292 SDPEVEEIVKPLDLATQKWLDQPIAHldqpaPIEDANK--GRIEGAPFINLLQQMQLYFTHAD-----------LSATAV 358
Cdd:PRK09419   347 RDETVVDALKDTHEATIAYVRAPVGK-----TEDDIKSifASVKDDPSIQIVTDAQKYYAEKYmkgteyknlpiLSAGAP 421

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  359 MNDVAKGFGKT-------VTMRDILLNYPYANQLVSVKLTGKQLRHIVEHTASFLE--KDENGKIHFIdryLKPKPELYH 429
Cdd:PRK09419   422 FKAGRNGVDYYtnikegdLAIKDIGDLYLYDNTLYIVKLNGSQVKDWMEMSAGQFNqiKPNDGDLQAL---LNENFRSYN 498

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  430 FDVFYPLEYEADLSKPV------------GQRLTKLKFKGQDIQDDQVYHLAVNNYRANGGGFYPEYSLDKIEFSLDKDY 497
Cdd:PRK09419   499 FDVIDGVTYQIDVTKPAkynengnvinadGSRIVNLKYDGKPVEDSQEFLVVTNNYRASGGGGFPHLKEDEIVYDSADEN 578

                          570
                   ....*....|....*....
gi 2163862258  498 VQMFSEYLTqgEVKVDTKK 516
Cdd:PRK09419   579 RQLLMDYII--EQKTINPN 595
5_nucleotid_C pfam02872
5'-nucleotidase, C-terminal domain;
314-482 6.29e-30

5'-nucleotidase, C-terminal domain;


Pssm-ID: 427027 [Multi-domain]  Cd Length: 155  Bit Score: 114.69  E-value: 6.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 314 PIAHLDQPAPiedANKGRIEGAPFINLLQQMQLYFTHADLSATAVMN---DVAKGfgkTVTMRDILLNYPYANQLVSVKL 390
Cdd:pfam02872   1 VIGTTDVLLF---DRRCRTGETNLGNLIADAQRAAAGADIALTNGGGiraDIPAG---EITYGDLYTVLPFGNTLVVVEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 391 TGKQLRHIVEHTASflekdenGKIHFIDRYLKpkpelyhfdvFYPLEYEADLSKPVGQRLTKLKF--KGQDIQDDQVYHL 468
Cdd:pfam02872  75 TGSQIKDALEHSVK-------TSSASPGGFLQ----------VSGLRYTYDPSRPPGNRVTSICLviNGKPLDPDKTYTV 137

                         170
                  ....*....|....
gi 2163862258 469 AVNNYRANGGGFYP 482
Cdd:pfam02872 138 ATNDYLASGGDGFP 151
PGA_cap smart00854
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 26-201 3.12e-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: 42.58  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   26 YDAPYGLSRVASAIKAekakwgADHVIV------TDAGDCLQGSPLAAYTHGSKNLDNLArftaaynAVGYDVRCLG-NH 98
Cdd:smart00854  17 ADFSPPFAGVKPLLRA------ADLAIGnletpiTTSGSPASGKKYPNFRAPPENAAALK-------AAGFDVVSLAnNH 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   99 DFNFGQEYMAYYVDN-NKAPFVNCNILDTETQVptlgRDYVILERSGVKVGVLGITTQYIPHWEAADRIKGLA--FKSAY 175
Cdd:smart00854  84 SLDYGEEGLLDTLAAlDAAGIAHVGAGRNLAEA----RKPAIVEVKGIKIALLAYTYGTNNGWAASRDRPGVAllPDLDA 159

                          170       180
                   ....*....|....*....|....*.
gi 2163862258  176 EQIAHFAKIIKPQVDVLAVLYHGGFE 201
Cdd:smart00854 160 EKILADIARARKEADVVIVSLHWGVE 185
 
Name Accession Description Interval E-value
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 1-507 6.38e-134

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: 396.53  E-value: 6.38e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   1 MKLVFLHSSDTHGYLLPTDYqSTGDYDAPYGLSRVASAIKAEKAKwgADHVIVTDAGDCLQGSPLAAYTHGSKNLDnlar 80
Cdd:COG0737     3 VTLTILHTNDLHGHLEPYDY-FDDKYGKAGGLARLATLIKQLRAE--NPNTLLLDAGDTIQGSPLSTLTKGEPMIE---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  81 ftaAYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQVPtLGRDYVILERSGVKVGVLGITTQYIPHW 160
Cdd:COG0737    76 ---AMNALGYDAATLGNHEFDYGLDVLLELLDGANFPVLSANVYDKDTGEP-LFKPYTIKEVGGVKVGVIGLTTPDTPTW 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 161 EAADRIKGLAFKSAYEQIAHFAKIIKPQ-VDVLAVLYHGGFEsdiasgeatephnGENEgyRILTEIPEVDVMLTGHQHR 239
Cdd:COG0737   152 SSPGNIGGLTFTDPVEAAQKYVDELRAEgADVVVLLSHLGLD-------------GEDR--ELAKEVPGIDVILGGHTHT 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 240 RLNMIS--PSGKPCVQPGYRGEAIAEVVLDLEKteAGYKVKEATSELIDTKD--FASDPEVEEIVKPLDLATQKWLDQPI 315
Cdd:COG0737   217 LLPEPVvvNGGTLIVQAGSYGKYLGRLDLTLDD--DGGKVVSVSAELIPVDDdlVPPDPEVAALVDEYRAKLEALLNEVV 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 316 AHLDQPAPIEDANkGRIEGAPFINLLQQMQLYFTHADLSAT---AVMNDVAKGfgkTVTMRDILLNYPYANQLVSVKLTG 392
Cdd:COG0737   295 GTTEVPLDGYRAF-VRGGESPLGNLIADAQLEATGADIALTnggGIRADLPAG---PITYGDVYTVLPFGNTLVVVELTG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 393 KQLRHIVEHTASFLEKDENGKihfidrylkpkpelYHFDVFYPLEYEADLSKPVGQRLTKLKFKGQDIQDDQVYHLAVNN 472
Cdd:COG0737   371 AQLKEALEQSASNIFPGDGFG--------------GNFLQVSGLTYTIDPSKPAGSRITDLTVNGKPLDPDKTYRVATND 436

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 2163862258 473 YRANGGGFYPEYSLDKIEFSLDKDYVQMFSEYLTQ 507
Cdd:COG0737   437 YLASGGDGYPMFKGGKDVPDTGPTLRDVLADYLKA 471
MPP_CpdB_N cd07410
Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain; CpdB is a ...
 3-287 5.74e-81

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: 253.79  E-value: 5.74e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   3 LVFLHSSDTHGYLLPTDYqSTGDYDAPYGLSRVASAIKAEKAKWGadHVIVTDAGDCLQGSPLAAYTHGSKNLDnLARFT 82
Cdd:cd07410     1 LRILETSDLHGNVLPYDY-AKDKPTLPFGLARTATLIKKARAENP--NTVLVDNGDLIQGNPLAYYYATIKDGP-IHPLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  83 AAYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQvPTLGRDYVILERS-GVKVGVLGITTQYIPHWE 161
Cdd:cd07410    77 AAMNALKYDAGVLGNHEFNYGLDYLDRAIKQAKFPVLSANIIDAKTG-EPFLPPYVIKEREvGVKIGILGLTTPQIPVWE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 162 AADRIKGLAFKSAYEQIAHFAKIIKP-QVDVLAVLYHGGFESDIASGEatephnGENEGYRILTEIPEVDVMLTGHQHRR 240
Cdd:cd07410   156 KANLIGDLTFQDIVETAKKYVPELRAeGADVVVVLAHGGIEADLEQLT------GENGAYDLAKKVPGIDAIVTGHQHRE 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2163862258 241 LNMIS----PSGKPCVQPGYRGEAIAEVVLDLEKTEAGYKVKEATSELIDT 287
Cdd:cd07410   230 FPGKVfngtVNGVPVIEPGSRGNHLGVIDLTLEKTDGKWKVKDSKAELRPT 280
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
6-516 6.44e-59

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 211.22  E-value: 6.44e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258    6 LHSSDTHGYLLPTDYQSTGDYDApYGLSRVASAIKaeKAKWGADHVIVTDAGDCLQGSPLAAYTHGSKNL--DNLARFTA 83
Cdd:PRK09419    45 LATTDLHGNFMDYDYASDKETTG-FGLAQTATLIK--KARKENPNTLLVDNGDLIQGNPLGEYAVKDNILfkNKTHPMIK 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   84 AYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQ---VPtlgrdYVILERS---------GVKVGVLG 151
Cdd:PRK09419   122 AMNALGYDAGTLGNHEFNYGLDFLDGTIKGANFPVLNANVKYKNGKnvyTP-----YKIKEKTvtdengkkqGVKVGYIG 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  152 ITTQYIPHWEAadriKGLAFKSAYEQIAHFAKIIKPQV-----DVLAVLYHGGFESDiasgeaTEPHNGENEGYRILTEI 226
Cdd:PRK09419   197 FVPPQIMTWDK----KNLKGKVEVKNIVEEANKTIPEMkkggaDVIVALAHSGIESE------YQSSGAEDSVYDLAEKT 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  227 PEVDVMLTGHQHR-------------RLNMISPSGKPCVQPGYRGEAIAEVVLDLEKTEAGYKVKEATS--ELIDTKDFA 291
Cdd:PRK09419   267 KGIDAIVAGHQHGlfpgadykgvpqfDNAKGTINGIPVVMPKSWGKYLGKIDLTLEKDGGKWKVVDKKSslESISGKVVS 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  292 SDPEVEEIVKPLDLATQKWLDQPIAHldqpaPIEDANK--GRIEGAPFINLLQQMQLYFTHAD-----------LSATAV 358
Cdd:PRK09419   347 RDETVVDALKDTHEATIAYVRAPVGK-----TEDDIKSifASVKDDPSIQIVTDAQKYYAEKYmkgteyknlpiLSAGAP 421

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  359 MNDVAKGFGKT-------VTMRDILLNYPYANQLVSVKLTGKQLRHIVEHTASFLE--KDENGKIHFIdryLKPKPELYH 429
Cdd:PRK09419   422 FKAGRNGVDYYtnikegdLAIKDIGDLYLYDNTLYIVKLNGSQVKDWMEMSAGQFNqiKPNDGDLQAL---LNENFRSYN 498

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  430 FDVFYPLEYEADLSKPV------------GQRLTKLKFKGQDIQDDQVYHLAVNNYRANGGGFYPEYSLDKIEFSLDKDY 497
Cdd:PRK09419   499 FDVIDGVTYQIDVTKPAkynengnvinadGSRIVNLKYDGKPVEDSQEFLVVTNNYRASGGGGFPHLKEDEIVYDSADEN 578

                          570
                   ....*....|....*....
gi 2163862258  498 VQMFSEYLTqgEVKVDTKK 516
Cdd:PRK09419   579 RQLLMDYII--EQKTINPN 595
MPP_UshA_N_like cd00845
Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes ...
 3-287 8.64e-46

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: 160.93  E-value: 8.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   3 LVFLHSSDTHGYLLPTDYQstgdydAPYGLSRVASAIKAEKAKwgADHVIVTDAGDCLQGSPLAAYTHGSKNLDnlarft 82
Cdd:cd00845     1 LTILHTNDLHGHLDPHSNG------GIGGAARLAGLVKQIRAE--NPNTLLLDAGDNFQGSPLSTLTDGEAVID------ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  83 aAYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQV-PTLGRDYVILERSGVKVGVLGITTQYIPHWE 161
Cdd:cd00845    67 -LMNALGYDAATVGNHEFDYGLDQLEELLKQAKFPWLSANVYEDGTGTgEPGAKPYTIITVDGVKVGVIGLTTPDTPTVT 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 162 AADRIKGLAF-KSAYEQIAHFAKIIKPQVDVLAVLYHGGFESDIasgeatephngenegyRILTEIPEVDVMLTGHQHRR 240
Cdd:cd00845   146 PPEGNRGVEFpDPAEAIAEAAEELKAEGVDVIIALSHLGIDTDE----------------RLAAAVKGIDVILGGHSHTL 209

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2163862258 241 LNM-ISPSGKPCVQPGYRGEAIAEVVLDLEKteAGYKVKEATSELIDT 287
Cdd:cd00845   210 LEEpEVVNGTLIVQAGAYGKYVGRVDLEFDK--ATKNVATTSGELVDV 255
cpdB PRK09420
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
2-493 9.64e-46

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


Pssm-ID: 236506 [Multi-domain]  Cd Length: 649  Bit Score: 169.73  E-value: 9.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   2 KLVFLHSSDTHGYLLPTDYQStgdyDAP---YGLSRVASAIKAEKAKwgADHVIVTDAGDCLQGSPLAAY--THGSKNLD 76
Cdd:PRK09420   25 DLRIMETTDLHSNMMDFDYYK----DKPtekFGLVRTASLIKAARAE--AKNSVLVDNGDLIQGSPLGDYmaAKGLKAGD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  77 nLARFTAAYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQVPtLGRDYVILERS---------GVKV 147
Cdd:PRK09420   99 -VHPVYKAMNTLDYDVGNLGNHEFNYGLDYLKKALAGAKFPYVNANVIDAKTGKP-LFTPYLIKEKEvkdkdgkehTIKI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 148 GVLGITTQYIPHWEAADrikgLAFKSAYEQIAHFAKIIKPQV-----DVLAVLYHGGFESDiasgeatePH--NGENEGY 220
Cdd:PRK09420  177 GYIGFVPPQIMVWDKAN----LEGKVTVRDITETARKYVPEMkekgaDIVVAIPHSGISAD--------PYkaMAENSVY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 221 RiLTEIPEVDVMLTGHQHRrlnmISPS-----------------GKPCVQPGYRGEAIAEVVLDLEKTEAGYKVKEATSE 283
Cdd:PRK09420  245 Y-LSEVPGIDAIMFGHSHA----VFPGkdfadipgadiakgtlnGVPAVMPGRWGDHLGVVDLVLENDSGKWQVTDAKAE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 284 L--IDTKD-----FASDPEVEEIVKPLDLATQKWLDQPIAHLDQP-----APIED---------ANKGRIEgapfinllQ 342
Cdd:PRK09420  320 ArpIYDKAnkkslAAEDPKLVAALKADHQATRAFVSQPIGKAADNmysylALVQDdptvqivnnAQKAYVE--------H 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 343 QMQLYFTHAD---LSATAVMN------------DVAKGfgkTVTMRDILLNYPYANQLVSVKLTGKQLRHIVEHTAS-FL 406
Cdd:PRK09420  392 FIQGDPDLADlpvLSAAAPFKaggrkndpasyvEVEKG---QLTFRNAADLYLYPNTLVVVKATGAEVKEWLECSAGqFN 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 407 EKDENGKihfidrylKPKPEL-------YHFDVFYPLEYEADLSKPV------------GQRLTKLKFKGQDIQDDQVYH 467
Cdd:PRK09420  469 QIDPNST--------KPQSLInwdgfrtYNFDVIDGVNYQIDVTQPArydgecklinpnANRIKNLTFNGKPIDPKATFL 540

                         570       580
                  ....*....|....*....|....*.
gi 2163862258 468 LAVNNYRANGGGFyPEYSLDKIEFSL 493
Cdd:PRK09420  541 VATNNYRAYGGKF-AGTGDDHIAFAS 565
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
2-505 2.75e-43

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 164.99  E-value: 2.75e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258    2 KLVFLHSSDTHGYLLptdyqstgdydapyGLSRVASAIKAEKAKwgADHVIVTDAGDCLQGSPLAAYTHGSKNLDNLarf 81
Cdd:PRK09419   660 ELTILHTNDFHGHLD--------------GAAKRVTKIKEVKEE--NPNTILVDAGDVYQGSLYSNLLKGLPVLKMM--- 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   82 taayNAVGYDVRCLGNHDFNFGQEYMA------------YYVDNNKAPFVNCNILDTETQVP-TLGRDYVILERSGVKVG 148
Cdd:PRK09419   721 ----KEMGYDASTFGNHEFDWGPDVLPdwlkgggdpknrHQFEKPDFPFVASNIYVKKTGKLvSWAKPYILVEVNGKKVG 796

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  149 VLGITTQYIPHWEAADRIKGLAFKSAYEQIAHFAKIIKPQ--VDVLAVLYHGGFESDIASGEAtephngenEGYRILTEI 226
Cdd:PRK09419   797 FIGLTTPETAYKTSPGNVKNLEFKDPAEAAKKWVKELKEKekVDAIIALTHLGSNQDRTTGEI--------TGLELAKKV 868

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  227 PEVDVMLTGHQHRRLNMISpSGKPCVQPGYRGEAIAEVVLDLEKTEAGYKVKEATSELIDTKDFASDPEVEEIVKPLDLA 306
Cdd:PRK09419   869 KGVDAIISAHTHTLVDKVV-NGTPVVQAYKYGRALGRVDVKFDKKGVVVVKTSRIDLSKIDDDLPEDPEMKEILDKYEKE 947

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  307 TQKWLDQPIAHLDQPAPIEdANKGRIEGAPFINLLQQMQLYFTHADLSAT---AVMNDVAKGfgkTVTMRDILLNYPYAN 383
Cdd:PRK09419   948 LAPIKNEKVGYTSVDLDGQ-PEHVRTGVSNLGNFIADGMKKIVGADIAITnggGVRAPIDKG---DITVGDLYTVMPFGN 1023

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  384 QLVSVKLTGKQLRHIVEHTasfLEKDENGKIHFIDrylkpkpelyhfdvFYPLEYEADLSKPVGQRLTKLKFK-GQDIQD 462
Cdd:PRK09419  1024 TLYTMDLTGADIKKALEHG---ISPVEFGGGAFPQ--------------VAGLKYTFTLSAEPGNRITDVRLEdGSKLDK 1086

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 2163862258  463 DQVYHLAVNNYRANGGgfyPEYSLDKIEFSLDKDYV--QMFSEYL 505
Cdd:PRK09419  1087 DKTYTVATNNFMGAGG---DGYSFSAASNGVDTGLVdrEIFTEYL 1128
PRK09418 PRK09418
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
1-510 4.62e-43

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


Pssm-ID: 236504 [Multi-domain]  Cd Length: 780  Bit Score: 163.34  E-value: 4.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   1 MKLVFLHSSDTHGYLLPTDYQSTgDYDAPYGLSRVASAIKaeKAKWGADHVIVTDAGDCLQGSPLAAYThGSKNLDNLAR 80
Cdd:PRK09418   38 VNLRILETSDIHVNLMNYDYYQT-KTDNKVGLVQTATLVN--KAREEAKNSVLFDDGDALQGTPLGDYV-ANKINDPKKP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  81 FTAAY--------NAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNIL-----DTETQVPTLGRDYVILER----- 142
Cdd:PRK09418  114 VDPSYthplyrlmNLMKYDVISLGNHEFNYGLDYLNKVISKTEFPVINSNVYkddkdNNEENDQNYFKPYHVFEKevede 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 143 SG----VKVGVLGITTQYIPHWEAADrikgLAFKSAYEQIAHFAKIIKPQ-----VDVLAVLYHGGFESdiaSGEATeph 213
Cdd:PRK09418  194 SGqkqkVKIGVMGFVPPQVMNWDKAN----LEGKVKAKDIVETAKKMVPKmkaegADVIVALAHSGVDK---SGYNV--- 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 214 NGENEGYRiLTEIPEVDVMLTGHQHRRLNMISpSGKPCVQPGYRGEAIAEVVLDLEKTEAGYKVKEATSE-----LIDTK 288
Cdd:PRK09418  264 GMENASYY-LTEVPGVDAVLMGHSHTEVKDVF-NGVPVVMPGVFGSNLGIIDMQLKKVNGKWEVQKEQSKpqlrpIADSK 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 289 DFA---SDPEVEEIVKPLDLATQKWLDQPIAhlDQPAPIeDANKGRIEGAPFINLLQQMQLYFTHAD------------- 352
Cdd:PRK09418  342 GNPlvqSDQNLVNEIKDDHQATIDYVNTAVG--KTTAPI-NSYFSLVQDDPSVQLVTNAQKWYVEKLfaengqyskykgi 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 353 --LSATA-----------VMNDVAKGfgkTVTMRDILLNYPYANQLVSVKLTGKQLRHIVEHTAsflekdenGKIHFIDR 419
Cdd:PRK09418  419 pvLSAGApfkaggrngatYYTDIPAG---TLAIKNVADLYVYPNTLYAVKVNGAQVKEWLEMSA--------GQFNQIDP 487

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 420 YLKPKPEL-------YHFDVFYPLEYEADLSKPV------------GQRLTKLKFKGQDIQDDQVYHLAVNNYRANGGGF 480
Cdd:PRK09418  488 KKTEEQPLvnigyptYNFDILDGLKYEIDVTQPAkydkdgkvvnanTNRIINMTYEGKPVADNQEFIVATNNYRGSSQTF 567

                         570       580       590
                  ....*....|....*....|....*....|
gi 2163862258 481 yPEYSLDKIEFSLDKDYVQMFSEYLTQGEV 510
Cdd:PRK09418  568 -PGVSKGEVVYQSQDETRQIIVKYMQETPV 596
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
6-477 3.64e-42

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 161.17  E-value: 3.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   6 LHSSDTHGYLLPTDYQStgdyDAP---YGLSRVASAIkaEKAKWGADHVIVTDAGDCLQGSPLAAYthgsKNL-DNLAR- 80
Cdd:PRK11907  119 LSTTDLHTNLVNYDYYQ----DKPsqtLGLAKTAVLI--EEAKKENPNVVLVDNGDTIQGTPLGTY----KAIvDPVEEg 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  81 ----FTAAYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQVPtLGRDYVILERS---------GVKV 147
Cdd:PRK11907  189 eqhpMYAALEALGFDAGTLGNHEFNYGLDYLEKVIATANMPIVNANVLDPTTGDF-LYTPYTIVTKTftdtegkkvTLNI 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 148 GVLGITTQYIPHWEAADRIKGLAFKSAYEQIahfaKIIKPQV-----DVLAVLYHGGFESDI-ASGEatephngENEGYR 221
Cdd:PRK11907  268 GITGIVPPQILNWDKANLEGKVIVRDAVEAV----RDIIPTMraagaDIVLVLSHSGIGDDQyEVGE-------ENVGYQ 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 222 IlTEIPEVDVMLTGHQHRRLnmisPS---------------------GKPCVQPGYRGEAIAEVVLDLEKTEAGYKVKEA 280
Cdd:PRK11907  337 I-ASLSGVDAVVTGHSHAEF----PSgngtsfyakysgvddingkinGTPVTMAGKYGDHLGIIDLNLSYTDGKWTVTSS 411

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 281 TSEL--IDTKDFASDPEVEEIVKPLDLATQKWLDQPIAhlDQPAPIeDANKGRIEGAPFINLLQQMQLYFTHADLSATAV 358
Cdd:PRK11907  412 KAKIrkIDTKSTVADGRIIDLAKEAHNGTINYVRQQVG--ETTAPI-TSYFALVQDDPSVQIVNNAQLWYAKQQLAGTPE 488

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 359 MN----------------------DVAKGfgkTVTMRDILLNYPYANQLVSVKLTGKQLRHIVEHTAsflekdenGKIHF 416
Cdd:PRK11907  489 ANlpilsaaapfkagtrgdasaytDIPAG---PIAIKNVADLYLYDNVTAILKVTGAQLKEWLEMSA--------GQFNQ 557

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 417 IDRYLKPKPEL-------YHFDVFYPLEYEADLSKP------------VGQRLTKLKFKGQDIQDDQVYHLAVNNYRANG 477
Cdd:PRK11907  558 IDPNSKEPQNLvntdyrtYNFDVIDGVTYKFDITQPnkydrdgklvnpTASRVRNLQYNGQPVDANQEFIVVTNNYRANG 637
5_nucleotid_C pfam02872
5'-nucleotidase, C-terminal domain;
314-482 6.29e-30

5'-nucleotidase, C-terminal domain;


Pssm-ID: 427027 [Multi-domain]  Cd Length: 155  Bit Score: 114.69  E-value: 6.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 314 PIAHLDQPAPiedANKGRIEGAPFINLLQQMQLYFTHADLSATAVMN---DVAKGfgkTVTMRDILLNYPYANQLVSVKL 390
Cdd:pfam02872   1 VIGTTDVLLF---DRRCRTGETNLGNLIADAQRAAAGADIALTNGGGiraDIPAG---EITYGDLYTVLPFGNTLVVVEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 391 TGKQLRHIVEHTASflekdenGKIHFIDRYLKpkpelyhfdvFYPLEYEADLSKPVGQRLTKLKF--KGQDIQDDQVYHL 468
Cdd:pfam02872  75 TGSQIKDALEHSVK-------TSSASPGGFLQ----------VSGLRYTYDPSRPPGNRVTSICLviNGKPLDPDKTYTV 137

                         170
                  ....*....|....
gi 2163862258 469 AVNNYRANGGGFYP 482
Cdd:pfam02872 138 ATNDYLASGGDGFP 151
MPP_CD73_N cd07409
CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain; CD73 is ...
 3-238 1.03e-28

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: 114.98  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   3 LVFLHSSDTHGYLLPTDyQSTGDYDAPY-----GLSRVASAIKAEKAKwgADHVIVTDAGDCLQGSPLaaYTHGSKNLDn 77
Cdd:cd07409     1 LTILHTNDVHARFEETS-PSGGKKCAAAkkcygGVARVATKVKELRKE--GPNVLFLNAGDQFQGTLW--YTVYKGNAV- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  78 lARFtaaYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNI-LDTETQVPTLGRDYVILERSGVKVGVLGITTQY 156
Cdd:cd07409    75 -AEF---MNLLGYDAMTLGNHEFDDGPEGLAPFLENLKFPVLSANIdASNEPLLAGLLKPSTILTVGGEKIGVIGYTTPD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 157 IPhweAADRIKGLAFKSAYEQIAHFAKIIKPQ-VDVLAVLYHGGFESDIasgeatephngenegyRILTEIPEVDVMLTG 235
Cdd:cd07409   151 TP---TLSSPGKVKFLDEIEAIQEEAKKLKAQgVNKIIALGHSGYEVDK----------------EIAKKVPGVDVIVGG 211


                  ...
gi 2163862258 236 HQH 238
Cdd:cd07409   212 HSH 214
ushA PRK09558
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
 2-482 2.73e-27

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


Pssm-ID: 236566 [Multi-domain]  Cd Length: 551  Bit Score: 115.38  E-value: 2.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   2 KLVFLHSSDTHGYLLPTDYqstGDYdapyGLSRVAS---AIKAEKAKWGAdHVIVTDAGDCLQGSPlaaythGSKNLDNL 78
Cdd:PRK09558   34 KITILHTNDHHGHFWRNEY---GEY----GLAAQKTlvdQIRKEVAAEGG-SVLLLSGGDINTGVP------ESDLQDAE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  79 ARFTAaYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQVPtLGRDYVILERSGVKVGVLGITTQYIP 158
Cdd:PRK09558  100 PDFRG-MNLIGYDAMAVGNHEFDNPLSVLRKQEKWAKFPFLSANIYQKSTGER-LFKPYAIFDRQGLKIAVIGLTTEDTA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 159 HWEAADRIKGLAFKSAYEQIAHFAKIIKP--QVDVLAVLYHGGFESDIASGEaTEPhnGENEGYRILtEIPEVDVMLTGH 236
Cdd:PRK09558  178 KIGNPEYFTDIEFRDPAEEAKKVIPELKQteKPDVIIALTHMGHYDDGEHGS-NAP--GDVEMARSL-PAGGLDMIVGGH 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 237 QHRRLNMISPS--------GKPC----------VQPG----YRGEAIAEVVlDLEKTEAGY---------KVK---EATS 282
Cdd:PRK09558  254 SQDPVCMAAENkkqvdyvpGTPCkpdqqngtwiVQAHewgkYVGRADFEFR-NGELKLVSYqlipvnlkkKVKwedGKSE 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 283 ELIDTKDFASDPEVEEIVKPLDLATQKWLDQPIAHLDqpAPIE-DANKGRIEGAPFINLLQQMQLYFTHADLsatAVMN- 360
Cdd:PRK09558  333 RVLYTEEIAEDPQVLELLTPFQEKGQAQLDVKIGETN--GKLEgDRSKVRFVQTNLGRLIAAAQMERTGADF---AVMNg 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 361 -----DVAKGfgkTVTMRDILLNYPYANQLVSVKLTGKQLRHIVEHTASFlEKDENGKIHfidrylkpkpelyhfdvFYP 435
Cdd:PRK09558  408 ggirdSIEAG---DITYKDVLTVQPFGNTVVYVDMTGKEVMDYLNVVATK-PPDSGAYAQ-----------------FAG 466

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 2163862258 436 LEYEADlskpvGQRLTKLKFKGQDIQDDQVYHLAVNNYRANGGGFYP 482
Cdd:PRK09558  467 VSMVVD-----CGKVVDVKINGKPLDPAKTYRMATPSFNAAGGDGYP 508
MPP_SoxB_N cd07411
Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB ...
 3-278 1.69e-26

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: 108.58  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   3 LVFLHSSDTHGYLLPTDY------QSTGDYDAPY---------GLSRVASAIKAEKAKWGaDHVIVTDAGDCLQGSPLAA 67
Cdd:cd07411     1 LTLLHITDTHAQLNPHYFrepsnnLGIGSVDFGAlarvfgkagGFAHIATLVDRLRAEVG-GKTLLLDGGDTWQGSGVAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  68 YTHGSKNLDnlarftaAYNAVGYDVrCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQVPtLGRDYVILERSGVKV 147
Cdd:cd07411    80 LTRGKAMVD-------IMNLLGVDA-MVGHWEFTYGKDRVLELLELLDGPFLAQNIFDEETGDL-LFPPYRIKEVGGLKI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 148 GVLGITTQYIPHWEAADRIKGLAFKSAYEQIA-HFAKIIKPQ-VDVLAVLYHGGFESDIASGEATEPhngenegyrilte 225
Cdd:cd07411   151 GVIGQAFPYVPIANPPSFSPGWSFGIREEELQeHVVKLRRAEgVDAVVLLSHNGMPVDVALAERVEG------------- 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2163862258 226 ipeVDVMLTGHQHRRLNMISPSGKP-CVQPGYRGEAIAEVVLDLEKTE-AGYKVK 278
Cdd:cd07411   218 ---IDVILSGHTHDRVPEPIRGGKTlVVAAGSHGKFVGRVDLKVRDGEiKSFRYE 269
MPP_YhcR_N cd07412
Bacillus subtilis YhcR endonuclease and related proteins, N-terminal metallophosphatase domain; ...
 5-282 5.29e-22

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: 96.29  E-value: 5.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   5 FLHSSDTHGYLLPTDYQSTGDYDAPY----GLSRVASAIKAEKAkwGADHVIVTDAGDCLQGSPLaaythgSKNLDNLAR 80
Cdd:cd07412     3 ILGINDFHGNLEPTGGAYIGVQGKKYstagGIAVLAAYLDEARD--GTGNSIIVGAGDMVGASPA------NSALLQDEP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  81 FTAAYNAVGYDVRCLGNHDFNFGQ-EYM----------------AYYVDNNKAPFVNCNILDTETQVPTLgRDYVILERS 143
Cdd:cd07412    75 TVEALNKMGFEVGTLGNHEFDEGLaELLriinggchpteptkacQYPYPGAGFPYIAANVVDKKTGKPLL-PPYLIKEIH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 144 GVKVGVLGITTQYIPHWEAADRIKGLAFKSAYEQIAHFAKIIKPQ-VDVLAVLYH-GGFESDIASGEATEPHNGENEGYR 221
Cdd:cd07412   154 GVPIAFIGAVTKSTPDIVSPENVEGLKFLDEAETINKYAPELKAKgVNAIVVLIHeGGSQAPYFGTTACSALSGPIVDIV 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163862258 222 ILTEiPEVDVMLTGHQHRRLNMiSPSGKPCVQPGYRGEAIAEVVLDLEKTEAGYKVKEATS 282
Cdd:cd07412   234 KKLD-PAVDVVISGHTHQYYNC-TVGGRLVTQADSYGKAYADVTLTIDPTTHDIVNKSAEN 292
MPP_CG11883_N cd07406
Drosophila melanogaster CG11883 and related proteins, N-terminal metallophosphatase domain; ...
 31-238 5.40e-18

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: 83.86  E-value: 5.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  31 GLSRVASAIKAEKAKwgADHVIVTDAGDCLQGSPLAAYTHGSKNLDNLarftaayNAVGYDVRCLGNHDFNFGQEYMAYY 110
Cdd:cd07406    22 GAARFATLRKQFEAE--NPNPLVLFSGDVFNPSALSTATKGKHMVPVL-------NALGVDVACVGNHDFDFGLDQFQKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 111 VDNNKAPFVNCNILDTETQVPTL-GRDYVILERSGVKVGVLGITtqyIPHWEAADRIK--GLAFKSAYEQIAHFAKIIKP 187
Cdd:cd07406    93 IEESNFPWLLSNVFDAETGGPLGnGKEHHIIERNGVKIGLLGLV---EEEWLETLTINppNVEYRDYIETARELVVELRE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2163862258 188 -QVDVLAVLYHggfesdiasgeATEPHNgenegYRILTEIPEVDVMLTGHQH 238
Cdd:cd07406   170 kGADVIIALTH-----------MRLPND-----IRLAQEVPEIDLILGGHDH 205
MPP_SA0022_N cd07408
Staphylococcus aureus SA0022 and related proteins, N-terminal metallophosphatase domain; ...
 4-272 2.80e-17

Staphylococcus aureus SA0022 and related proteins, N-terminal metallophosphatase domain; SA0022 is an uncharacterized Staphylococcus aureus UshA-like protein with two putative domains, an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. SA0022 also contains a putative C-terminal cell wall anchor 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: 277353 [Multi-domain]  Cd Length: 255  Bit Score: 81.46  E-value: 2.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   4 VFLHSSDTHGYLLptdyqstgDYDAPYGLSRVASAIKAEKakwgadHVIVTDAGDCLQGSPLAAYTHGSKNLdnlarftA 83
Cdd:cd07408     2 TILHTNDIHGRYA--------EEDDVIGMAKLATIKEEER------NTILVDAGDAFQGLPISNMSKGEDAA-------E 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  84 AYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQVptlGRDYVILERSGVKVGVLGITTQYIPHWEAA 163
Cdd:cd07408    61 LMNAVGYDAMTVGNHEFDFGKDQLKKLSKSLNFPFLSSNIYVNGKRV---FDASTIVDKNGIEYGVIGVTTPETKTKTHP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 164 DRIKGLAFKSAYEQI-AHFAKIIKPQVDVLAVLYHGGFES---------DIASGEATEPHNGENegyrilteipevDVML 233
Cdd:cd07408   138 KNVEGVEFTDPITSVtEVVAELKGKGYKNYVIICHLGVDSttqeewrgdDLANALSNSPLAGKR------------VIVI 205

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2163862258 234 TGHQHRRLNMISPSGKPC-VQPGYRGEAIAEVVLDLEKTE 272
Cdd:cd07408   206 DGHSHTVFENGKQYGNVTyNQTGSYLNNIGKIKLNSDTNL 245
MPP_UshA_N cd07405
Escherichia coli UshA and related proteins, N-terminal metallophosphatase domain; UshA is a ...
 3-249 2.11e-14

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: 73.82  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   3 LVFLHSSDTHGYLLPTDYQStgdydapYGLSRVAS---AIKAEKAKWGAdHVIVTDAGDCLQGSPlaaythGSKNLDNLA 79
Cdd:cd07405     1 ITVLHTNDHHGHFWRNEYGE-------YGLAAQKTlvdGIRKEVAAEGG-SVLLLSGGDINTGVP------ESDLQDAEP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  80 RFTAaYNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKAPFVNCNILDTETQVPtLGRDYVILERSGVKVGVLGITTQYIPH 159
Cdd:cd07405    67 DFRG-MNLVGYDAMAIGNHEFDNPLTVLRQQEKWAKFPLLSANIYQKSTGER-LFKPWALFKRQDLKIAVIGLTTDDTAK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 160 WEAADRIKGLAFKSAYEQIAHFAKIIK--PQVDVLAVLYHGGFESDiasGEATEPHNGENEGYRILTeIPEVDVMLTGHQ 237
Cdd:cd07405   145 IGNPEYFTDIEFRKPADEAKLVIQELQqtEKPDIIIAATHMGHYDN---GEHGSNAPGDVEMARALP-AGSLAMIVGGHS 220

                         250
                  ....*....|..
gi 2163862258 238 HRRLNMISPSGK 249
Cdd:cd07405   221 QDPVCMAAENKK 232
CapA COG2843
Poly-gamma-glutamate biosynthesis protein CapA/YwtB (capsule formation), metallophosphatase ...
 135-201 1.31e-05

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: 47.21  E-value: 1.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163862258 135 RDYVILERSGVKVGVLGITtQYIPHWEAADRIKGLAFKSAYEQIAHFAKIIKPQVDVLAVLYHGGFE 201
Cdd:COG2843   126 RRPLILEVNGVRVAFLAYT-YGTNEWAAGEDKPGVANLDDLERIKEDIAAARAGADLVIVSLHWGVE 191
PGA_cap smart00854
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 26-201 3.12e-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: 42.58  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   26 YDAPYGLSRVASAIKAekakwgADHVIV------TDAGDCLQGSPLAAYTHGSKNLDNLArftaaynAVGYDVRCLG-NH 98
Cdd:smart00854  17 ADFSPPFAGVKPLLRA------ADLAIGnletpiTTSGSPASGKKYPNFRAPPENAAALK-------AAGFDVVSLAnNH 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   99 DFNFGQEYMAYYVDN-NKAPFVNCNILDTETQVptlgRDYVILERSGVKVGVLGITTQYIPHWEAADRIKGLA--FKSAY 175
Cdd:smart00854  84 SLDYGEEGLLDTLAAlDAAGIAHVGAGRNLAEA----RKPAIVEVKGIKIALLAYTYGTNNGWAASRDRPGVAllPDLDA 159

                          170       180
                   ....*....|....*....|....*.
gi 2163862258  176 EQIAHFAKIIKPQVDVLAVLYHGGFE 201
Cdd:smart00854 160 EKILADIARARKEADVVIVSLHWGVE 185
MPP_YHR202W_N cd07407
Saccharomyces cerevisiae YHR202W and related proteins, N-terminal metallophosphatase domain; ...
 5-272 3.61e-04

Saccharomyces cerevisiae YHR202W and related proteins, N-terminal metallophosphatase domain; YHR202W is an uncharacterized Saccharomyces cerevisiae 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: 277352 [Multi-domain]  Cd Length: 286  Bit Score: 42.71  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   5 FLHSSDTHGYLLptDYQSTGDYDAPYGlsRVASAIK--AEKAKWGADHVIVTDAGDCLQGSPLAAYTH--GSKNLDnlar 80
Cdd:cd07407     8 FLHTTDTHGWLG--GHLRDPNYSADYG--DFLSFVQhmREIADGKGVDLLLVDTGDLHDGTGLSDASDppGSYTSP---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  81 ftaAYNAVGYDVRCLGNHDF----NFGQEYmAYYVDNNKAPFVNCNI---LDTETQVPtLGRDYVILERS-GVKV---GV 149
Cdd:cd07407    80 ---IFRMMPYDALTIGNHELylaeVALLEY-EGFVPSWGGRYLASNVditDDSGLLVP-FGSRYAIFTTKhGVRVlafGF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 150 L--------GITTQyiphwEAADRIKGLAFKSAyeqiahfakIIKPQVDVLAVLYHggfesdiasgeatEPHNGENEGYR 221
Cdd:cd07407   155 LfdfkgnanNVTVT-----PVQDVVQQPWFQNA---------IKNEDVDLIIVLGH-------------MPVRDPSEFKV 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2163862258 222 ILTEIPEVD-----VMLTGHQHRRLNMISPSGKPCVQPGYRGEAIAEVVLDLEKTE 272
Cdd:cd07407   208 LHDAIRKIFpntpiQFFGGHSHIRDFTQYDSSSTSLESGRYLETVGWVSFDGPKAS 263
MPP_CapA cd07381
CapA and related proteins, metallophosphatase domain; CapA is one of three membrane-associated ...
 19-201 8.75e-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: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  19 DYQSTGDYDAPYGLSRVASAIKaekakwGADHVIV------TDAGDclqgSPLAAYTHGSKNLDNLARFTAAynavGYDV 92
Cdd:cd07381    14 REPILRRYDYSPPFGDVKPLLR------NADLAFGnletpiTTRGE----EAPKKGFHFRAPPENADALKAA----GFDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  93 RCLG-NHDFNFGQEYMAY---YVDNNKAPFVNCNILDTETQVPTlgrdyvILERSGVKVGVLGITTQYIPHWEAADRIKG 168
Cdd:cd07381    80 VSLAnNHALDYGEDGLRDtleALDRAGIDHAGAGRNLAEAGRPA------YLEVKGVRVAFLGYTTGTNGGPEAADAAPG 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2163862258 169 LAFKSAYEQI--AHFAKiIKPQVDVLAVLYHGGFE 201
Cdd:cd07381   154 ALVNDADEAAilADVAE-AKKKADIVIVSLHWGGE 187
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
3-257 1.53e-03

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 40.44  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   3 LVFLHSSDTHgyllptdYQSTGDYDAPYGLSRVASAIKAEKAkwgaDHVIVTdaGDCLQGSPLAAYTHGSKNLDNLARFT 82
Cdd:COG1409     1 FRFAHISDLH-------LGAPDGSDTAEVLAAALADINAPRP----DFVVVT--GDLTDDGEPEEYAAAREILARLGVPV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  83 AAynavgydvrCLGNHDFN--FGQEYMAYYvdnnkapfvncnildteTQVPTLGRDYVIlERSGVKvgVLGITTQYIPHW 160
Cdd:COG1409    68 YV---------VPGNHDIRaaMAEAYREYF-----------------GDLPPGGLYYSF-DYGGVR--FIGLDSNVPGRS 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258 161 EAADRIkglafksayEQIAHFAKIIK--PQVDVLAVLYHGGFESDIASgEATEPHNGEnEGYRILTEIPeVDVMLTGHQH 238
Cdd:COG1409   119 SGELGP---------EQLAWLEEELAaaPAKPVIVFLHHPPYSTGSGS-DRIGLRNAE-ELLALLARYG-VDLVLSGHVH 186

                         250       260
                  ....*....|....*....|....*....
gi 2163862258 239 RR----------LNMISPSGKPCVQPGYR 257
Cdd:COG1409   187 RYertrrdgvpyIVAGSTGGQVRLPPGYR 215
MPP_PhoA_N cd08162
Synechococcus sp. strain PCC 7942 PhoA and related proteins, N-terminal metallophosphatase ...
 3-193 1.65e-03

Synechococcus sp. strain PCC 7942 PhoA and related proteins, N-terminal metallophosphatase domain; Synechococcus sp. strain PCC 7942 PhoA is a large atypical alkaline phosphatase. It is known to be transported across the inner cytoplasmic membrane and into the periplasmic space. In vivo inactivation of the gene encoding PhoA leads to a loss of extracellular, phosphate-regulated phosphatase activity, but does not appear to affect the cells capacity for phosphate uptake. PhoA may play a role in scavenging phosphate during growth of Synechococcus sp. strain PCC 7942 in its natural environment. PhoA belongs to a domain family which includes the bacterial enzyme UshA and several other 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: 277369 [Multi-domain]  Cd Length: 325  Bit Score: 40.59  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258   3 LVFLHSSDTHGyllptDYQSTGDYDApygLSRVASAIKAEKAKWGADHVIVTdAGDCLQGSPL-----AAYTHGSKNLDN 77
Cdd:cd08162     1 LQLLHFSDQEA-----GFQAIEDIPN---LSAVLSALYEEAKADNANSLHVS-AGDNTIPGPFfdasaEVPSLGAQGRAD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163862258  78 LARFtaayNAVGYDVRCLGNHDFNFGQEYMAYYVDNNKA--------PFVNCNI-----------------LDTETQVPT 132
Cdd:cd08162    72 ISIQ----NELGVQAIALGNHEFDLGTDLLAGLIAYSARgntlgaafPSLSVNLdfsndanlaglvitadgQEASTIAGK 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163862258 133 LGRDyVILERSGVKVGVLGITTQYIPHWEA--ADRIKGLAF---KSAYEQIAHFAKIIKPQVDVLA 193
Cdd:cd08162   148 VAKS-CIVDVNGEKVGIVGATTPGLRSISSpgAEKLPGLDFvsgRDEAENLPLESAIIQALVDVLA 212
 
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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