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Conserved domains on  [gi|19922446|ref|NP_611218|]
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Ecto-5'-nucleotidase 2, isoform A [Drosophila melanogaster]

Protein Classification

bifunctional metallophosphatase/5'-nucleotidase( domain architecture ID 10164740)

bifunctional metallophosphatase/5'-nucleotidase, similar to vertebrate 5'-nucleotidase that hydrolyzes extracellular nucleotides into membrane permeable nucleosides and to insect apyrase

CATH:  3.60.21.10|3.90.780.10
EC:  3.-.-.-
Gene Ontology:  GO:0042578|GO:0046872|GO:0008253|GO:0009166|GO:0000166
PubMed:  25837850|10331872
SCOP:  3001067|4001892

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_CD73_N cd07409
CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain; CD73 is ...
 33-320 5.88e-150

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: 432.38  E-value: 5.88e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  33 FIILHNNDMHARFDQTSVNSGTCppeDVHTNKCYGGFARVAHEVRKYRKEAQEggtsVLYLNAGDTYTGTSWFTIFKDKI 112
Cdd:cd07409   1 LTILHTNDVHARFEETSPSGGKK---CAAAKKCYGGVARVATKVKELRKEGPN----VLFLNAGDQFQGTLWYTVYKGNA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 113 ASAFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLKATWHlaNSAILETNGTKVGVIGYLTPDT 192
Cdd:cd07409  74 VAEFMNLLGYDAMTLGNHEFDDGPEGLAPFLENLKFPVLSANIDASNEPLLAGLLK--PSTILTVGGEKIGVIGYTTPDT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 193 KKLTLNMDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGYLKDLEIAKNCPEVDIVIGGHTNTFLYTGAQPDAEHIDGP 272
Cdd:cd07409 152 PTLSSPGKVKFLDEIEAIQEEAKKLKAQGVNKIIALGHSGYEVDKEIAKKVPGVDVIVGGHSHTFLYTGPPPSKEKPVGP 231

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 19922446 273 YPTMVKQNSGKEVPVVQAYAYTKYLGKLHVQFDADGNLIQWDGSPILL 320
Cdd:cd07409 232 YPTVVKNPDGRKVLVVQAYAFGKYLGYLDVTFDAKGNVLSWEGNPILL 279
5_nucleotid_C pfam02872
5'-nucleotidase, C-terminal domain;
348-519 2.84e-45

5'-nucleotidase, C-terminal domain;


:

Pssm-ID: 427027 [Multi-domain]  Cd Length: 155  Bit Score: 157.06  E-value: 2.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   348 VVGHTKVHLEGNKavCRAEECNLGNLIADAMvfsrlmeeqggDFWTDAAISIMQGGGIRSSIekrSDGAITDNDILSVLP 427
Cdd:pfam02872   1 VIGTTDVLLFDRR--CRTGETNLGNLIADAQ-----------RAAAGADIALTNGGGIRADI---PAGEITYGDLYTVLP 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   428 WGNKLYMVPMTGSTIRRALEHgAALRGKDSDGGFLQVSGIRVVFNSNKPEGQRVVSVqvrcaaCRVPTYSDLNDTAIYNV 507
Cdd:pfam02872  65 FGNTLVVVELTGSQIKDALEH-SVKTSSASPGGFLQVSGLRYTYDPSRPPGNRVTSI------CLVINGKPLDPDKTYTV 137

                         170
                  ....*....|..
gi 19922446   508 VLGEFLLDGGDG 519
Cdd:pfam02872 138 ATNDYLASGGDG 149
 
Name Accession Description Interval E-value
MPP_CD73_N cd07409
CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain; CD73 is ...
 33-320 5.88e-150

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: 432.38  E-value: 5.88e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  33 FIILHNNDMHARFDQTSVNSGTCppeDVHTNKCYGGFARVAHEVRKYRKEAQEggtsVLYLNAGDTYTGTSWFTIFKDKI 112
Cdd:cd07409   1 LTILHTNDVHARFEETSPSGGKK---CAAAKKCYGGVARVATKVKELRKEGPN----VLFLNAGDQFQGTLWYTVYKGNA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 113 ASAFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLKATWHlaNSAILETNGTKVGVIGYLTPDT 192
Cdd:cd07409  74 VAEFMNLLGYDAMTLGNHEFDDGPEGLAPFLENLKFPVLSANIDASNEPLLAGLLK--PSTILTVGGEKIGVIGYTTPDT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 193 KKLTLNMDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGYLKDLEIAKNCPEVDIVIGGHTNTFLYTGAQPDAEHIDGP 272
Cdd:cd07409 152 PTLSSPGKVKFLDEIEAIQEEAKKLKAQGVNKIIALGHSGYEVDKEIAKKVPGVDVIVGGHSHTFLYTGPPPSKEKPVGP 231

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 19922446 273 YPTMVKQNSGKEVPVVQAYAYTKYLGKLHVQFDADGNLIQWDGSPILL 320
Cdd:cd07409 232 YPTVVKNPDGRKVLVVQAYAFGKYLGYLDVTFDAKGNVLSWEGNPILL 279
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 30-544 7.66e-126

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: 378.04  E-value: 7.66e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  30 ATEFIILHNNDMHARFDQTSVNSGTcppedvhtNKCYGGFARVAHEVRKYRKEAQeggtSVLYLNAGDTYTGTSWFTIFK 109
Cdd:COG0737   2 TVTLTILHTNDLHGHLEPYDYFDDK--------YGKAGGLARLATLIKQLRAENP----NTLLLDAGDTIQGSPLSTLTK 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 110 DKIASAFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLkatwHLANSAILETNGTKVGVIGYLT 189
Cdd:COG0737  70 GEPMIEAMNALGYDAATLGNHEFDYGLDVLLELLDGANFPVLSANVYDKDTGEP----LFKPYTIKEVGGVKVGVIGLTT 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 190 PDTKKLT---LNMDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGY-LKDLEIAKNCPEVDIVIGGHTNTFLytgaqPD 265
Cdd:COG0737 146 PDTPTWSspgNIGGLTFTDPVEAAQKYVDELRAEGADVVVLLSHLGLdGEDRELAKEVPGIDVILGGHTHTLL-----PE 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 266 AEHIDGPyptmvkqnsgkeVPVVQAYAYTKYLGKLHVQFDADGN-LIQWDGSPILLNAS-VAQEQDLLDLLEVFRPNVTR 343
Cdd:COG0737 221 PVVVNGG------------TLIVQAGSYGKYLGRLDLTLDDDGGkVVSVSAELIPVDDDlVPPDPEVAALVDEYRAKLEA 288

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 344 LEKSVVGHTKVHLEGNKAVCRAEECNLGNLIADAMvfsrlMEeqggdfWTDAAISIMQGGGIRSSIEKrsdGAITDNDIL 423
Cdd:COG0737 289 LLNEVVGTTEVPLDGYRAFVRGGESPLGNLIADAQ-----LE------ATGADIALTNGGGIRADLPA---GPITYGDVY 354

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 424 SVLPWGNKLYMVPMTGSTIRRALEHGAA--LRGKDSDGGFLQVSGIRVVFNSNKPEGQRVVSVQVRCAAcrvptysdLND 501
Cdd:COG0737 355 TVLPFGNTLVVVELTGAQLKEALEQSASniFPGDGFGGNFLQVSGLTYTIDPSKPAGSRITDLTVNGKP--------LDP 426

                       490       500       510       520
                ....*....|....*....|....*....|....*....|...
gi 19922446 502 TAIYNVVLGEFLLDGGDGHVMRDSAHQPQRLQNNDLEAVSQYL 544
Cdd:COG0737 427 DKTYRVATNDYLASGGDGYPMFKGGKDVPDTGPTLRDVLADYL 469
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
31-558 4.85e-79

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 270.54  E-value: 4.85e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446    31 TEFIILHNNDMHARFDqtsvnsgtcppedvhtnkcygGFARVAHEVRKYRKEAQEggtSVLyLNAGDTYTGTSWFTIFKD 110
Cdd:PRK09419  659 WELTILHTNDFHGHLD---------------------GAAKRVTKIKEVKEENPN---TIL-VDAGDVYQGSLYSNLLKG 713

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   111 KIASAFLNKLKPDAISLGNHEFDERVEGLIPFL------------NEVTFPVLACNLDLSKVPQLKATWHlaNSAILETN 178
Cdd:PRK09419  714 LPVLKMMKEMGYDASTFGNHEFDWGPDVLPDWLkgggdpknrhqfEKPDFPFVASNIYVKKTGKLVSWAK--PYILVEVN 791

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   179 GTKVGVIGYLTPDTKKLT---LNMDVEFNEEVESINVEAKKLKA-QGIKIIIALGHSGYLKD--------LEIAKNCPEV 246
Cdd:PRK09419  792 GKKVGFIGLTTPETAYKTspgNVKNLEFKDPAEAAKKWVKELKEkEKVDAIIALTHLGSNQDrttgeitgLELAKKVKGV 871

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   247 DIVIGGHTNTFLytgaqpdaEHIDGPyptmvkqnsgkeVPVVQAYAYTKYLGKLHVQFDADGNLI----QWDGSPIllNA 322
Cdd:PRK09419  872 DAIISAHTHTLV--------DKVVNG------------TPVVQAYKYGRALGRVDVKFDKKGVVVvktsRIDLSKI--DD 929

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   323 SVAQEQDLLDLLEVFRPNVTRLEKSVVGHTKVHLEGNKAVCRAEECNLGNLIADAMVFSrlmeeqggdfwTDAAISIMQG 402
Cdd:PRK09419  930 DLPEDPEMKEILDKYEKELAPIKNEKVGYTSVDLDGQPEHVRTGVSNLGNFIADGMKKI-----------VGADIAITNG 998

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   403 GGIRSSIEKrsdGAITDNDILSVLPWGNKLYMVPMTGSTIRRALEHGaaLRGKDSDGG-FLQVSGIRVVFNSNKPEGQRV 481
Cdd:PRK09419  999 GGVRAPIDK---GDITVGDLYTVMPFGNTLYTMDLTGADIKKALEHG--ISPVEFGGGaFPQVAGLKYTFTLSAEPGNRI 1073

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922446   482 VSVqvrcaacRVPTYSDLNDTAIYNVVLGEFLLDGGDGHVMRDSAHQpQRLQNNDLEAVSQYL-NQRDYVYPEIEGRI 558
Cdd:PRK09419 1074 TDV-------RLEDGSKLDKDKTYTVATNNFMGAGGDGYSFSAASNG-VDTGLVDREIFTEYLkKLGNPVSPKIEGRI 1143
nadN TIGR01530
NAD pyrophosphatase/5'-nucleotidase NadN; This model describes NadN of Haemophilus influenzae ...
 35-520 3.16e-57

NAD pyrophosphatase/5'-nucleotidase NadN; This model describes NadN of Haemophilus influenzae and a small number of close homologs in pathogenic, Gram-negative bacteria. NadN is a periplasmic enzyme that cleaves NAD (nicotinamide adenine dinucleotide) to NMN (nicotinamide mononucleotide) and AMP. The NMN must be converted by a 5'-nucleotidase to nicotinamide riboside for import. NadN belongs a large family of 5'-nucleotidases and has NMN 5'-nucleotidase activity for NMN, AMP, etc. [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 211667 [Multi-domain]  Cd Length: 545  Bit Score: 200.97  E-value: 3.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446    35 ILHNNDMHARFD--QTSVN-SGTCPPEDVhtnkcyGGFARVAHEVRKYRKEAQeggtSVLYLNAGDTYTGTSWFTIFKDK 111
Cdd:TIGR01530   3 ILHINDHHSYLEphETRINlNGQQTKVDI------GGFSAVNAKLNKLRKKYK----NPLVLHAGDAITGTLYFTLFGGS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   112 IASAFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLKATWHlaNSAILETNGTKVGVIGYltpD 191
Cdd:TIGR01530  73 ADAAVMNAGNFHYFTLGNHEFDAGNEGLLKLLEPLKIPVLSANVIPDKASILYNKWK--PYDIFTVDGEKIAIIGL---D 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   192 TKKLTLN-----MDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGYLKDLEIAKNCPEVDIVIGGHTNtFLYTGAQPDA 266
Cdd:TIGR01530 148 TVNKTVNssspgKDVKFYDEIATAQIMANALKQQGINKIILLSHAGSEKNIEIAQKVNDIDVIVTGDSH-YLYGNDELRS 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   267 EHID--GPYPTMVKQNSGKEVPVVQAYAYTKYLGKLHVQFDADG---------------NLIQWDGS-----PI------ 318
Cdd:TIGR01530 227 LKLPviYEYPLEFKNPNGEPVFVMEGWAYSAVVGDLGVKFSPEGiasitrkiphvlmssHKLQVKNAegkwyELtgderk 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   319 -LLNA-------SVAQEQDLLD-LLEVFRPNVTRLEKSVVG--------HTKVHLEGNKAVCRAEECNLGNLIADAMvfs 381
Cdd:TIGR01530 307 kALDTlksmksiSLDDHDAKTDsLIEKYKSEKDRLAQEIVGvitgsampGGSANRIPNKAGSNPEGSIATRFIAETM--- 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   382 rLMEEQGGDfwtdaaISIMQGGGIRSSIEKrsdGAITDNDILSVLPWGNKLYMVPMTGSTIRRALEHGAALR-GKDSDGG 460
Cdd:TIGR01530 384 -YNELKTVD------LTIQNAGGVRADILP---GNVTFNDAYTFLPFGNTLYTYKMEGSLVKQVLEDAMQFAlVDGSTGA 453

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922446   461 FLQVSGIRVVFNSN-KPEGQRVVSVQVRCAacRVPTYSDLNDTAIYNVVLGEFLLDGGDGH 520
Cdd:TIGR01530 454 FPYGAGIRYEANETpNAEGKRLVSVEVLNK--QTQQWEPIDDNKRYLVGTNAYVAGGKDGY 512
5_nucleotid_C pfam02872
5'-nucleotidase, C-terminal domain;
348-519 2.84e-45

5'-nucleotidase, C-terminal domain;


Pssm-ID: 427027 [Multi-domain]  Cd Length: 155  Bit Score: 157.06  E-value: 2.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   348 VVGHTKVHLEGNKavCRAEECNLGNLIADAMvfsrlmeeqggDFWTDAAISIMQGGGIRSSIekrSDGAITDNDILSVLP 427
Cdd:pfam02872   1 VIGTTDVLLFDRR--CRTGETNLGNLIADAQ-----------RAAAGADIALTNGGGIRADI---PAGEITYGDLYTVLP 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   428 WGNKLYMVPMTGSTIRRALEHgAALRGKDSDGGFLQVSGIRVVFNSNKPEGQRVVSVqvrcaaCRVPTYSDLNDTAIYNV 507
Cdd:pfam02872  65 FGNTLVVVELTGSQIKDALEH-SVKTSSASPGGFLQVSGLRYTYDPSRPPGNRVTSI------CLVINGKPLDPDKTYTV 137

                         170
                  ....*....|..
gi 19922446   508 VLGEFLLDGGDG 519
Cdd:pfam02872 138 ATNDYLASGGDG 149
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 59-161 1.05e-04

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 41.82  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446    59 DVHtnkCYGGFARVAHEVRKYRKEAQEggtsVLYLNAGDTYTGTSWFTIFKDKIASafLNKLKPDAISLGNHEFDE-RVE 137
Cdd:pfam00149   8 DLH---LPGQLDDLLELLKKLLEEGKP----DLVLHAGDLVDRGPPSEEVLELLER--LIKYVPVYLVRGNHDFDYgECL 78

                          90       100
                  ....*....|....*....|....
gi 19922446   138 GLIPFLNEVTFPVLACNLDLSKVP 161
Cdd:pfam00149  79 RLYPYLGLLARPWKRFLEVFNFLP 102
 
Name Accession Description Interval E-value
MPP_CD73_N cd07409
CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain; CD73 is ...
 33-320 5.88e-150

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: 432.38  E-value: 5.88e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  33 FIILHNNDMHARFDQTSVNSGTCppeDVHTNKCYGGFARVAHEVRKYRKEAQEggtsVLYLNAGDTYTGTSWFTIFKDKI 112
Cdd:cd07409   1 LTILHTNDVHARFEETSPSGGKK---CAAAKKCYGGVARVATKVKELRKEGPN----VLFLNAGDQFQGTLWYTVYKGNA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 113 ASAFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLKATWHlaNSAILETNGTKVGVIGYLTPDT 192
Cdd:cd07409  74 VAEFMNLLGYDAMTLGNHEFDDGPEGLAPFLENLKFPVLSANIDASNEPLLAGLLK--PSTILTVGGEKIGVIGYTTPDT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 193 KKLTLNMDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGYLKDLEIAKNCPEVDIVIGGHTNTFLYTGAQPDAEHIDGP 272
Cdd:cd07409 152 PTLSSPGKVKFLDEIEAIQEEAKKLKAQGVNKIIALGHSGYEVDKEIAKKVPGVDVIVGGHSHTFLYTGPPPSKEKPVGP 231

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 19922446 273 YPTMVKQNSGKEVPVVQAYAYTKYLGKLHVQFDADGNLIQWDGSPILL 320
Cdd:cd07409 232 YPTVVKNPDGRKVLVVQAYAFGKYLGYLDVTFDAKGNVLSWEGNPILL 279
UshA COG0737
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family ...
 30-544 7.66e-126

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: 378.04  E-value: 7.66e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  30 ATEFIILHNNDMHARFDQTSVNSGTcppedvhtNKCYGGFARVAHEVRKYRKEAQeggtSVLYLNAGDTYTGTSWFTIFK 109
Cdd:COG0737   2 TVTLTILHTNDLHGHLEPYDYFDDK--------YGKAGGLARLATLIKQLRAENP----NTLLLDAGDTIQGSPLSTLTK 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 110 DKIASAFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLkatwHLANSAILETNGTKVGVIGYLT 189
Cdd:COG0737  70 GEPMIEAMNALGYDAATLGNHEFDYGLDVLLELLDGANFPVLSANVYDKDTGEP----LFKPYTIKEVGGVKVGVIGLTT 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 190 PDTKKLT---LNMDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGY-LKDLEIAKNCPEVDIVIGGHTNTFLytgaqPD 265
Cdd:COG0737 146 PDTPTWSspgNIGGLTFTDPVEAAQKYVDELRAEGADVVVLLSHLGLdGEDRELAKEVPGIDVILGGHTHTLL-----PE 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 266 AEHIDGPyptmvkqnsgkeVPVVQAYAYTKYLGKLHVQFDADGN-LIQWDGSPILLNAS-VAQEQDLLDLLEVFRPNVTR 343
Cdd:COG0737 221 PVVVNGG------------TLIVQAGSYGKYLGRLDLTLDDDGGkVVSVSAELIPVDDDlVPPDPEVAALVDEYRAKLEA 288

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 344 LEKSVVGHTKVHLEGNKAVCRAEECNLGNLIADAMvfsrlMEeqggdfWTDAAISIMQGGGIRSSIEKrsdGAITDNDIL 423
Cdd:COG0737 289 LLNEVVGTTEVPLDGYRAFVRGGESPLGNLIADAQ-----LE------ATGADIALTNGGGIRADLPA---GPITYGDVY 354

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 424 SVLPWGNKLYMVPMTGSTIRRALEHGAA--LRGKDSDGGFLQVSGIRVVFNSNKPEGQRVVSVQVRCAAcrvptysdLND 501
Cdd:COG0737 355 TVLPFGNTLVVVELTGAQLKEALEQSASniFPGDGFGGNFLQVSGLTYTIDPSKPAGSRITDLTVNGKP--------LDP 426

                       490       500       510       520
                ....*....|....*....|....*....|....*....|...
gi 19922446 502 TAIYNVVLGEFLLDGGDGHVMRDSAHQPQRLQNNDLEAVSQYL 544
Cdd:COG0737 427 DKTYRVATNDYLASGGDGYPMFKGGKDVPDTGPTLRDVLADYL 469
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
31-558 4.85e-79

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 270.54  E-value: 4.85e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446    31 TEFIILHNNDMHARFDqtsvnsgtcppedvhtnkcygGFARVAHEVRKYRKEAQEggtSVLyLNAGDTYTGTSWFTIFKD 110
Cdd:PRK09419  659 WELTILHTNDFHGHLD---------------------GAAKRVTKIKEVKEENPN---TIL-VDAGDVYQGSLYSNLLKG 713

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   111 KIASAFLNKLKPDAISLGNHEFDERVEGLIPFL------------NEVTFPVLACNLDLSKVPQLKATWHlaNSAILETN 178
Cdd:PRK09419  714 LPVLKMMKEMGYDASTFGNHEFDWGPDVLPDWLkgggdpknrhqfEKPDFPFVASNIYVKKTGKLVSWAK--PYILVEVN 791

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   179 GTKVGVIGYLTPDTKKLT---LNMDVEFNEEVESINVEAKKLKA-QGIKIIIALGHSGYLKD--------LEIAKNCPEV 246
Cdd:PRK09419  792 GKKVGFIGLTTPETAYKTspgNVKNLEFKDPAEAAKKWVKELKEkEKVDAIIALTHLGSNQDrttgeitgLELAKKVKGV 871

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   247 DIVIGGHTNTFLytgaqpdaEHIDGPyptmvkqnsgkeVPVVQAYAYTKYLGKLHVQFDADGNLI----QWDGSPIllNA 322
Cdd:PRK09419  872 DAIISAHTHTLV--------DKVVNG------------TPVVQAYKYGRALGRVDVKFDKKGVVVvktsRIDLSKI--DD 929

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   323 SVAQEQDLLDLLEVFRPNVTRLEKSVVGHTKVHLEGNKAVCRAEECNLGNLIADAMVFSrlmeeqggdfwTDAAISIMQG 402
Cdd:PRK09419  930 DLPEDPEMKEILDKYEKELAPIKNEKVGYTSVDLDGQPEHVRTGVSNLGNFIADGMKKI-----------VGADIAITNG 998

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   403 GGIRSSIEKrsdGAITDNDILSVLPWGNKLYMVPMTGSTIRRALEHGaaLRGKDSDGG-FLQVSGIRVVFNSNKPEGQRV 481
Cdd:PRK09419  999 GGVRAPIDK---GDITVGDLYTVMPFGNTLYTMDLTGADIKKALEHG--ISPVEFGGGaFPQVAGLKYTFTLSAEPGNRI 1073

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922446   482 VSVqvrcaacRVPTYSDLNDTAIYNVVLGEFLLDGGDGHVMRDSAHQpQRLQNNDLEAVSQYL-NQRDYVYPEIEGRI 558
Cdd:PRK09419 1074 TDV-------RLEDGSKLDKDKTYTVATNNFMGAGGDGYSFSAASNG-VDTGLVDREIFTEYLkKLGNPVSPKIEGRI 1143
ushA PRK09558
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
 31-522 7.84e-59

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


Pssm-ID: 236566 [Multi-domain]  Cd Length: 551  Bit Score: 205.52  E-value: 7.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   31 TEFIILHNNDMHARFDQTSvnsgtcppedvhtnkcYG--GFARVAHEVRKYRKEAQEGGTSVLYLNAGDTYTGT--Swft 106
Cdd:PRK09558  33 YKITILHTNDHHGHFWRNE----------------YGeyGLAAQKTLVDQIRKEVAAEGGSVLLLSGGDINTGVpeS--- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  107 IFKDKIASAF-LNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNL--DLSKVPQLKATwhlansAILETNGTKVG 183
Cdd:PRK09558  94 DLQDAEPDFRgMNLIGYDAMAVGNHEFDNPLSVLRKQEKWAKFPFLSANIyqKSTGERLFKPY------AIFDRQGLKIA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  184 VIGYLTPDTKKLT--LNM-DVEFNEEVEsinvEAKKLKAQgIK------IIIALGHSGYLKDLEIAKNCPE--------- 245
Cdd:PRK09558 168 VIGLTTEDTAKIGnpEYFtDIEFRDPAE----EAKKVIPE-LKqtekpdVIIALTHMGHYDDGEHGSNAPGdvemarslp 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  246 ---VDIVIGGHTNT--FLYTGAQPDAEHIDGPYPTMVKQNsgkEVPVVQAYAYTKYLGKLHVQFDaDGNLIQWDGSPILL 320
Cdd:PRK09558 243 aggLDMIVGGHSQDpvCMAAENKKQVDYVPGTPCKPDQQN---GTWIVQAHEWGKYVGRADFEFR-NGELKLVSYQLIPV 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  321 NASV------------------AQEQDLLDLLEVFRPNVTRLEKSVVGHTKVHLEGNKAVCRAEECNLGNLIADAMvfsr 382
Cdd:PRK09558 319 NLKKkvkwedgkservlyteeiAEDPQVLELLTPFQEKGQAQLDVKIGETNGKLEGDRSKVRFVQTNLGRLIAAAQ---- 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  383 lMEeqggdfWTDAAISIMQGGGIRSSIEkrsDGAITDNDILSVLPWGNKLYMVPMTGSTIRRALEHgAALRGKDSdGGFL 462
Cdd:PRK09558 395 -ME------RTGADFAVMNGGGIRDSIE---AGDITYKDVLTVQPFGNTVVYVDMTGKEVMDYLNV-VATKPPDS-GAYA 462

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  463 QVSGIRVVFNSNKpegqrVVSVQVRCaacrvptySDLNDTAIYNVVLGEFLLDGGDGHVM 522
Cdd:PRK09558 463 QFAGVSMVVDCGK-----VVDVKING--------KPLDPAKTYRMATPSFNAAGGDGYPK 509
nadN TIGR01530
NAD pyrophosphatase/5'-nucleotidase NadN; This model describes NadN of Haemophilus influenzae ...
 35-520 3.16e-57

NAD pyrophosphatase/5'-nucleotidase NadN; This model describes NadN of Haemophilus influenzae and a small number of close homologs in pathogenic, Gram-negative bacteria. NadN is a periplasmic enzyme that cleaves NAD (nicotinamide adenine dinucleotide) to NMN (nicotinamide mononucleotide) and AMP. The NMN must be converted by a 5'-nucleotidase to nicotinamide riboside for import. NadN belongs a large family of 5'-nucleotidases and has NMN 5'-nucleotidase activity for NMN, AMP, etc. [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 211667 [Multi-domain]  Cd Length: 545  Bit Score: 200.97  E-value: 3.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446    35 ILHNNDMHARFD--QTSVN-SGTCPPEDVhtnkcyGGFARVAHEVRKYRKEAQeggtSVLYLNAGDTYTGTSWFTIFKDK 111
Cdd:TIGR01530   3 ILHINDHHSYLEphETRINlNGQQTKVDI------GGFSAVNAKLNKLRKKYK----NPLVLHAGDAITGTLYFTLFGGS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   112 IASAFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLKATWHlaNSAILETNGTKVGVIGYltpD 191
Cdd:TIGR01530  73 ADAAVMNAGNFHYFTLGNHEFDAGNEGLLKLLEPLKIPVLSANVIPDKASILYNKWK--PYDIFTVDGEKIAIIGL---D 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   192 TKKLTLN-----MDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGYLKDLEIAKNCPEVDIVIGGHTNtFLYTGAQPDA 266
Cdd:TIGR01530 148 TVNKTVNssspgKDVKFYDEIATAQIMANALKQQGINKIILLSHAGSEKNIEIAQKVNDIDVIVTGDSH-YLYGNDELRS 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   267 EHID--GPYPTMVKQNSGKEVPVVQAYAYTKYLGKLHVQFDADG---------------NLIQWDGS-----PI------ 318
Cdd:TIGR01530 227 LKLPviYEYPLEFKNPNGEPVFVMEGWAYSAVVGDLGVKFSPEGiasitrkiphvlmssHKLQVKNAegkwyELtgderk 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   319 -LLNA-------SVAQEQDLLD-LLEVFRPNVTRLEKSVVG--------HTKVHLEGNKAVCRAEECNLGNLIADAMvfs 381
Cdd:TIGR01530 307 kALDTlksmksiSLDDHDAKTDsLIEKYKSEKDRLAQEIVGvitgsampGGSANRIPNKAGSNPEGSIATRFIAETM--- 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   382 rLMEEQGGDfwtdaaISIMQGGGIRSSIEKrsdGAITDNDILSVLPWGNKLYMVPMTGSTIRRALEHGAALR-GKDSDGG 460
Cdd:TIGR01530 384 -YNELKTVD------LTIQNAGGVRADILP---GNVTFNDAYTFLPFGNTLYTYKMEGSLVKQVLEDAMQFAlVDGSTGA 453

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922446   461 FLQVSGIRVVFNSN-KPEGQRVVSVQVRCAacRVPTYSDLNDTAIYNVVLGEFLLDGGDGH 520
Cdd:TIGR01530 454 FPYGAGIRYEANETpNAEGKRLVSVEVLNK--QTQQWEPIDDNKRYLVGTNAYVAGGKDGY 512
MPP_UshA_N_like cd00845
Escherichia coli UshA-like family, N-terminal metallophosphatase domain; This family includes ...
 35-320 5.84e-55

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: 186.74  E-value: 5.84e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  35 ILHNNDMHARFDQtsvnsgtcppedvHTNKCYGGFARVAHEVRKYRKEAQEggtsVLYLNAGDTYTGTSWFTIFKDKIAS 114
Cdd:cd00845   3 ILHTNDLHGHLDP-------------HSNGGIGGAARLAGLVKQIRAENPN----TLLLDAGDNFQGSPLSTLTDGEAVI 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 115 AFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKvPQLKATWHLAnSAILETNGTKVGVIGYLTPDTKK 194
Cdd:cd00845  66 DLMNALGYDAATVGNHEFDYGLDQLEELLKQAKFPWLSANVYEDG-TGTGEPGAKP-YTIITVDGVKVGVIGLTTPDTPT 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 195 LTL---NMDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGYLKDLEIAKNCPEVDIVIGGHTNTFLytgaqPDAEHIDG 271
Cdd:cd00845 144 VTPpegNRGVEFPDPAEAIAEAAEELKAEGVDVIIALSHLGIDTDERLAAAVKGIDVILGGHSHTLL-----EEPEVVNG 218

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 19922446 272 pyptmvkqnsgkeVPVVQAYAYTKYLGKLHVQFDADGNLIQ-WDGSPILL 320
Cdd:cd00845 219 -------------TLIVQAGAYGKYVGRVDLEFDKATKNVAtTSGELVDV 255
5_nucleotid_C pfam02872
5'-nucleotidase, C-terminal domain;
348-519 2.84e-45

5'-nucleotidase, C-terminal domain;


Pssm-ID: 427027 [Multi-domain]  Cd Length: 155  Bit Score: 157.06  E-value: 2.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   348 VVGHTKVHLEGNKavCRAEECNLGNLIADAMvfsrlmeeqggDFWTDAAISIMQGGGIRSSIekrSDGAITDNDILSVLP 427
Cdd:pfam02872   1 VIGTTDVLLFDRR--CRTGETNLGNLIADAQ-----------RAAAGADIALTNGGGIRADI---PAGEITYGDLYTVLP 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   428 WGNKLYMVPMTGSTIRRALEHgAALRGKDSDGGFLQVSGIRVVFNSNKPEGQRVVSVqvrcaaCRVPTYSDLNDTAIYNV 507
Cdd:pfam02872  65 FGNTLVVVELTGSQIKDALEH-SVKTSSASPGGFLQVSGLRYTYDPSRPPGNRVTSI------CLVINGKPLDPDKTYTV 137

                         170
                  ....*....|..
gi 19922446   508 VLGEFLLDGGDG 519
Cdd:pfam02872 138 ATNDYLASGGDG 149
MPP_CpdB_N cd07410
Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain; CpdB is a ...
 35-307 2.64e-29

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: 117.43  E-value: 2.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  35 ILHNNDMHARFdqtsvnsgtcPPEDVHTNKCY--GGFARVAHEVRKYRKEaqegGTSVLYLNAGDTYTGTS----WFTIF 108
Cdd:cd07410   3 ILETSDLHGNV----------LPYDYAKDKPTlpFGLARTATLIKKARAE----NPNTVLVDNGDLIQGNPlayyYATIK 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 109 KDKIA--SAFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKvpqlKATWHLANSAILE-TNGTKVGVI 185
Cdd:cd07410  69 DGPIHplIAAMNALKYDAGVLGNHEFNYGLDYLDRAIKQAKFPVLSANIIDAK----TGEPFLPPYVIKErEVGVKIGIL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 186 GYLTPDT---KKLTLNMDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGYLKDLE----------IAKNCPEVDIVIGG 252
Cdd:cd07410 145 GLTTPQIpvwEKANLIGDLTFQDIVETAKKYVPELRAEGADVVVVLAHGGIEADLEqltgengaydLAKKVPGIDAIVTG 224

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19922446 253 HtntflytgaqpdaEHidGPYPTMVKQNSGKEVPVVQAYAYTKYLGKLHVQFDAD 307
Cdd:cd07410 225 H-------------QH--REFPGKVFNGTVNGVPVIEPGSRGNHLGVIDLTLEKT 264
PRK09419 PRK09419
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase;
35-465 2.29e-27

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


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 117.61  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446    35 ILHNNDMHARFdqtsvnsgtcPPEDVHTNKCY--GGFARVAHEVRKYRKEaqegGTSVLYLNAGDTYTGTSWFT-IFKDK 111
Cdd:PRK09419   44 ILATTDLHGNF----------MDYDYASDKETtgFGLAQTATLIKKARKE----NPNTLLVDNGDLIQGNPLGEyAVKDN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   112 IASA--------FLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLKATWHLANSAILETNGT--- 180
Cdd:PRK09419  110 ILFKnkthpmikAMNALGYDAGTLGNHEFNYGLDFLDGTIKGANFPVLNANVKYKNGKNVYTPYKIKEKTVTDENGKkqg 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   181 -KVGVIGYLTP---DTKKLTLNMDVEFNEEVESINVEAKKLKAQGIKIIIALGHSGYLKD----------LEIAKNCPEV 246
Cdd:PRK09419  190 vKVGYIGFVPPqimTWDKKNLKGKVEVKNIVEEANKTIPEMKKGGADVIVALAHSGIESEyqssgaedsvYDLAEKTKGI 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   247 DIVIGGHTNTFLytgaqPDAEhidgpYPTMVKQNSGKE----VPVVQAYAYTKYLGKLHVQFDADGNLI-----QWDGSP 317
Cdd:PRK09419  270 DAIVAGHQHGLF-----PGAD-----YKGVPQFDNAKGtingIPVVMPKSWGKYLGKIDLTLEKDGGKWkvvdkKSSLES 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   318 ILLNaSVAQEQDLLDLLEVFRPNVTRLEKSVVGHTKVHLEGnkavcraeecnlgnliadamVFSRLMEEQGGDFWTDAA- 396
Cdd:PRK09419  340 ISGK-VVSRDETVVDALKDTHEATIAYVRAPVGKTEDDIKS--------------------IFASVKDDPSIQIVTDAQk 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   397 --------------ISIMQGGGIRSSIEKRSD-------GAITDNDILSVLPWGNKLYMVPMTGSTIRRALEHGAAL--R 453
Cdd:PRK09419  399 yyaekymkgteyknLPILSAGAPFKAGRNGVDyytnikeGDLAIKDIGDLYLYDNTLYIVKLNGSQVKDWMEMSAGQfnQ 478

                         490
                  ....*....|..
gi 19922446   454 GKDSDGGfLQVS 465
Cdd:PRK09419  479 IKPNDGD-LQAL 489
MPP_UshA_N cd07405
Escherichia coli UshA and related proteins, N-terminal metallophosphatase domain; UshA is a ...
 34-321 3.79e-25

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: 105.41  E-value: 3.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  34 IILHNNDMHARFdqtsvnSGTCPPEdvhtnkcyGGFARVAHEVRKYRKEAQEGGTSVLYLNAGDTYTGTSWFTIFKDKIA 113
Cdd:cd07405   2 TVLHTNDHHGHF------WRNEYGE--------YGLAAQKTLVDGIRKEVAAEGGSVLLLSGGDINTGVPESDLQDAEPD 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 114 SAFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNldlskVPQLKATWHLANSAILETNGT-KVGVIGYLTPDT 192
Cdd:cd07405  68 FRGMNLVGYDAMAIGNHEFDNPLTVLRQQEKWAKFPLLSAN-----IYQKSTGERLFKPWALFKRQDlKIAVIGLTTDDT 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 193 KKLtLN----MDVEFNEEVESINVEAKKLK-AQGIKIIIALGHSGYLKDLEIAKNCPE------------VDIVIGGHTN 255
Cdd:cd07405 143 AKI-GNpeyfTDIEFRKPADEAKLVIQELQqTEKPDIIIAATHMGHYDNGEHGSNAPGdvemaralpagsLAMIVGGHSQ 221

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922446 256 TFLYTGAQpDAEHIDGPYPTMVKQNSGKEVPVVQAYAYTKYLGKLHVQFDaDGNLIQWDGSPILLN 321
Cdd:cd07405 222 DPVCMAAE-NKKQVDYVPGTPCKPDQQNGIWIVQAHEWGKYVGRADFEFR-NGEMKMVNYQLIPVN 285
MPP_YhcR_N cd07412
Bacillus subtilis YhcR endonuclease and related proteins, N-terminal metallophosphatase domain; ...
 35-311 1.61e-24

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: 103.99  E-value: 1.61e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  35 ILHNNDMHARFDQTS-----VNSGTCPPedvhtnkcYGGFARVAhevrKYRKEAQEGGTSVLYLNAGDTyTGTSWFT--I 107
Cdd:cd07412   3 ILGINDFHGNLEPTGgayigVQGKKYST--------AGGIAVLA----AYLDEARDGTGNSIIVGAGDM-VGASPANsaL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 108 FKDKIASAFLNKLKPDAISLGNHEFDERVEGLIPFLN-----------------EVTFPVLACNLDLSKV--PQLKATWh 168
Cdd:cd07412  70 LQDEPTVEALNKMGFEVGTLGNHEFDEGLAELLRIINggchpteptkacqypypGAGFPYIAANVVDKKTgkPLLPPYL- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 169 lansaILETNGTKVGVIGYLTPDTKKLTLN---MDVEFNEEVESINVEAKKLKAQGIKIIIALGH--------------- 230
Cdd:cd07412 149 -----IKEIHGVPIAFIGAVTKSTPDIVSPenvEGLKFLDEAETINKYAPELKAKGVNAIVVLIHeggsqapyfgttacs 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 231 --SGYLKDleIAKNC-PEVDIVIGGHTNTFLytgaqpdaehidgpyptmvkQNSGKEVPVVQAYAYTKYLGKLHVQFDAD 307
Cdd:cd07412 224 alSGPIVD--IVKKLdPAVDVVISGHTHQYY--------------------NCTVGGRLVTQADSYGKAYADVTLTIDPT 281


                ....
gi 19922446 308 GNLI 311
Cdd:cd07412 282 THDI 285
MPP_CG11883_N cd07406
Drosophila melanogaster CG11883 and related proteins, N-terminal metallophosphatase domain; ...
 60-327 3.24e-24

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: 101.97  E-value: 3.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  60 VHTNKCY----------GGFARVAHEVRKYRKEAQEGgtsvLYLNAGDTYTGTSWFTIFKDKIASAFLNKLKPDAISLGN 129
Cdd:cd07406   4 LHFNDVYeiapqdnepvGGAARFATLRKQFEAENPNP----LVLFSGDVFNPSALSTATKGKHMVPVLNALGVDVACVGN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 130 HEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLKAtwHLANSAILETNGTKVGVIGYLTPD-TKKLTLNM-DVEFNEEV 207
Cdd:cd07406  80 HDFDFGLDQFQKLIEESNFPWLLSNVFDAETGGPLG--NGKEHHIIERNGVKIGLLGLVEEEwLETLTINPpNVEYRDYI 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 208 ESINVEAKKLKAQGIKIIIALGHSGYLKDLEIAKNCPEVDIVIGGHtntflytgaqpDAEHIDgpyptmVKQNsgkEVPV 287
Cdd:cd07406 158 ETARELVVELREKGADVIIALTHMRLPNDIRLAQEVPEIDLILGGH-----------DHEYYI------EEIN---GTLI 217

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 19922446 288 VQAYAYTKYLGKLHVQFDADGNLIQWDGSPILLNASVAQE 327
Cdd:cd07406 218 VKSGTDFRNLSIIDLEVDTGGRKWKVNIRRVDITSSIEED 257
MPP_SoxB_N cd07411
Thermus thermophilus SoxB and related proteins, N-terminal metallophosphatase domain; SoxB ...
 35-314 1.28e-21

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: 95.10  E-value: 1.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  35 ILHNNDMHARFD-----QTSVNSGTCPPEDVHTNKCY---GGFARVAHEVRKYRKEAqegGTSVLYLNAGDTYTGTSWFT 106
Cdd:cd07411   3 LLHITDTHAQLNphyfrEPSNNLGIGSVDFGALARVFgkaGGFAHIATLVDRLRAEV---GGKTLLLDGGDTWQGSGVAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 107 IFKDKIASAFLNKLKPDAIsLGNHEF---DERVEGLIPFLNevtFPVLACNL--DLSKVPQLKATWhlansaILETNGTK 181
Cdd:cd07411  80 LTRGKAMVDIMNLLGVDAM-VGHWEFtygKDRVLELLELLD---GPFLAQNIfdEETGDLLFPPYR------IKEVGGLK 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 182 VGVIGYLTPDTKKL---TLNMDVEFNEEVESI-NVEAKKLKAQGIKIIIALGHSGYLKDLEIAKNCPEVDIVIGGHTNTF 257
Cdd:cd07411 150 IGVIGQAFPYVPIAnppSFSPGWSFGIREEELqEHVVKLRRAEGVDAVVLLSHNGMPVDVALAERVEGIDVILSGHTHDR 229

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19922446 258 LYtgaQPdaehidgpyptmvkqNSGKEVPVVQAYAYTKYLGKLHVQFDaDGNLIQWD 314
Cdd:cd07411 230 VP---EP---------------IRGGKTLVVAAGSHGKFVGRVDLKVR-DGEIKSFR 267
MPP_SA0022_N cd07408
Staphylococcus aureus SA0022 and related proteins, N-terminal metallophosphatase domain; ...
 35-263 1.63e-19

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: 88.40  E-value: 1.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  35 ILHNNDMHARFDQtsvnsgtcppEDVHTNkcYGGFARVAHEVRkyrkeaqeggtSVLYLNAGDTYTGTSWFTIFKDKIAS 114
Cdd:cd07408   3 ILHTNDIHGRYAE----------EDDVIG--MAKLATIKEEER-----------NTILVDAGDAFQGLPISNMSKGEDAA 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 115 AFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNLDLSKVPQLKAtwhlanSAILETNGTKVGVIGYLTPDTKK 194
Cdd:cd07408  60 ELMNAVGYDAMTVGNHEFDFGKDQLKKLSKSLNFPFLSSNIYVNGKRVFDA------STIVDKNGIEYGVIGVTTPETKT 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 195 LT--LNMD-VEFNEEVESINVEAKKLKAQGIKIIIALGHSG------------YL-KDLEIAKNCPEVDIVIGGHTNTFL 258
Cdd:cd07408 134 KThpKNVEgVEFTDPITSVTEVVAELKGKGYKNYVIICHLGvdsttqeewrgdDLaNALSNSPLAGKRVIVIDGHSHTVF 213


                ....*
gi 19922446 259 YTGAQ 263
Cdd:cd07408 214 ENGKQ 218
MPP_PhoA_N cd08162
Synechococcus sp. strain PCC 7942 PhoA and related proteins, N-terminal metallophosphatase ...
 80-311 5.77e-17

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: 82.20  E-value: 5.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  80 RKEAQEGGTSVLYLNAGDTYTGTSWFTIFKDKIA--------SAFLNKLKPDAISLGNHEFD---ERVEGLIPF-----L 143
Cdd:cd08162  30 YEEAKADNANSLHVSAGDNTIPGPFFDASAEVPSlgaqgradISIQNELGVQAIALGNHEFDlgtDLLAGLIAYsargnT 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 144 NEVTFPVLACNLDLSKVPQL-------------KATWHLANSAILETNGTKVGVIGYLTPDTKKLTLNMDVEFN------ 204
Cdd:cd08162 110 LGAAFPSLSVNLDFSNDANLaglvitadgqeasTIAGKVAKSCIVDVNGEKVGIVGATTPGLRSISSPGAEKLPgldfvs 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446 205 --EEVESINVEAKKLKAQ---------GIKIIIALGHSGYLK-DLEIAKNCPEVDIVIGGHTNTFLYtGAQP---DAEHI 269
Cdd:cd08162 190 grDEAENLPLESAIIQALvdvlaanapDCNKVVLLSHMQQISiEQELADRLSGVDVIVAGGSNTRLV-DTNDmlrAGDSS 268

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 19922446 270 DGPYPTMVKQNSGKEVPVVQAYAYTKYLGKLHVQFDADGNLI 311
Cdd:cd08162 269 QGVYPLFTTDADGNTTLIVNTDGNYKYVGRLVVDFDEEGNVI 310
PRK09418 PRK09418
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
36-528 8.32e-17

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


Pssm-ID: 236504 [Multi-domain]  Cd Length: 780  Bit Score: 83.99  E-value: 8.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   36 LHNNDMHARFDQTSVNsgtcppedvhtNKCygGFARVAHEVRKYRKEAQeggTSVLYlNAGDTYTGTSWFTIFKDKIASA 115
Cdd:PRK09418  48 IHVNLMNYDYYQTKTD-----------NKV--GLVQTATLVNKAREEAK---NSVLF-DDGDALQGTPLGDYVANKINDP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  116 --------------FLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPVLACNL--------DLSKVPQLKAtWHLANSA 173
Cdd:PRK09418 111 kkpvdpsythplyrLMNLMKYDVISLGNHEFNYGLDYLNKVISKTEFPVINSNVykddkdnnEENDQNYFKP-YHVFEKE 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  174 ILETNG----TKVGVIGYLTPDT---KKLTLNMDVEFNEEVESINVEAKKLKAQGIKIIIALGHSG-----YLKDLEIAK 241
Cdd:PRK09418 190 VEDESGqkqkVKIGVMGFVPPQVmnwDKANLEGKVKAKDIVETAKKMVPKMKAEGADVIVALAHSGvdksgYNVGMENAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  242 ----NCPEVDIVIGGHTNTflytgaqpdaehidgpyptmVKQNSGKEVPVVQAYAYTKYLGKLHVQF-DADGNL-IQWDG 315
Cdd:PRK09418 270 yyltEVPGVDAVLMGHSHT--------------------EVKDVFNGVPVVMPGVFGSNLGIIDMQLkKVNGKWeVQKEQ 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  316 SPILL--------NASVAQEQDLLDLLEVFRPNVTRLEKSVVGHTKVHLegNKAVCRAEECNLGNLIADAMVF--SRLME 385
Cdd:PRK09418 330 SKPQLrpiadskgNPLVQSDQNLVNEIKDDHQATIDYVNTAVGKTTAPI--NSYFSLVQDDPSVQLVTNAQKWyvEKLFA 407

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  386 EQgGDFWTDAAISIMQGG-----GIRSSIEKRSD---GAITDNDILSVLPWGNKLYMVPMTGSTIRRALEHGAalrgkds 457
Cdd:PRK09418 408 EN-GQYSKYKGIPVLSAGapfkaGGRNGATYYTDipaGTLAIKNVADLYVYPNTLYAVKVNGAQVKEWLEMSA------- 479

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922446  458 dGGFLQVsgirvvfNSNKPEGQRVVSVQvrcaacrVPTYS-DLNDTAIYNVVLGEFLLDGGDGHVMRDSAHQ 528
Cdd:PRK09418 480 -GQFNQI-------DPKKTEEQPLVNIG-------YPTYNfDILDGLKYEIDVTQPAKYDKDGKVVNANTNR 536
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
81-298 6.63e-09

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 58.71  E-value: 6.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   81 KEAQEGGTSVLYLNAGDTYTGTSWFTiFK---DKIAS-------AFLNKLKPDAISLGNHEFDERVEGLIPFLNEVTFPV 150
Cdd:PRK11907 152 EEAKKENPNVVLVDNGDTIQGTPLGT-YKaivDPVEEgeqhpmyAALEALGFDAGTLGNHEFNYGLDYLEKVIATANMPI 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  151 LACN-LDLSKVPQLKATWHLANSAILETNGT----KVGVIGYLTPDT---KKLTLNMDVEFNEEVESINVEAKKLKAQGI 222
Cdd:PRK11907 231 VNANvLDPTTGDFLYTPYTIVTKTFTDTEGKkvtlNIGITGIVPPQIlnwDKANLEGKVIVRDAVEAVRDIIPTMRAAGA 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  223 KIIIALGHSG-----YLKDLE-----IAkNCPEVDIVIGGHTNTFLYTGaqpdaehiDGP-----YPTmVKQNSGK--EV 285
Cdd:PRK11907 311 DIVLVLSHSGigddqYEVGEEnvgyqIA-SLSGVDAVVTGHSHAEFPSG--------NGTsfyakYSG-VDDINGKinGT 380

                        250
                 ....*....|...
gi 19922446  286 PVVQAYAYTKYLG 298
Cdd:PRK11907 381 PVTMAGKYGDHLG 393
cpdB PRK09420
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
68-253 5.98e-08

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


Pssm-ID: 236506 [Multi-domain]  Cd Length: 649  Bit Score: 55.71  E-value: 5.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446   68 GFARVAHEVRKYRKEAqegGTSVLYLNaGDTYTGTSwftiFKDKIAS------------AFLNKLKPDAISLGNHEFDEr 135
Cdd:PRK09420  53 GLVRTASLIKAARAEA---KNSVLVDN-GDLIQGSP----LGDYMAAkglkagdvhpvyKAMNTLDYDVGNLGNHEFNY- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446  136 veGLiPFLNEV----TFPVLACNL-DLSKVPQLKATWHLANSAILETNGT----KVGVIGYLTP-----DTKKLTLNMdv 201
Cdd:PRK09420 124 --GL-DYLKKAlagaKFPYVNANViDAKTGKPLFTPYLIKEKEVKDKDGKehtiKIGYIGFVPPqimvwDKANLEGKV-- 198

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922446  202 efneEVESINVEAKK----LKAQGIKIIIALGHSGYLKD--LEIAKNC-------PEVDIVIGGH 253
Cdd:PRK09420 199 ----TVRDITETARKyvpeMKEKGADIVVAIPHSGISADpyKAMAENSvyylsevPGIDAIMFGH 259
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 59-161 1.05e-04

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 41.82  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922446    59 DVHtnkCYGGFARVAHEVRKYRKEAQEggtsVLYLNAGDTYTGTSWFTIFKDKIASafLNKLKPDAISLGNHEFDE-RVE 137
Cdd:pfam00149   8 DLH---LPGQLDDLLELLKKLLEEGKP----DLVLHAGDLVDRGPPSEEVLELLER--LIKYVPVYLVRGNHDFDYgECL 78

                          90       100
                  ....*....|....*....|....
gi 19922446   138 GLIPFLNEVTFPVLACNLDLSKVP 161
Cdd:pfam00149  79 RLYPYLGLLARPWKRFLEVFNFLP 102
 
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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