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Conserved domains on  [gi|2192211525|gb|KAH9659508|]
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serine/threonine-protein phosphatase BSL3 [Citrus sinensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 651-953 0e+00

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 623.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 651 VIAHLLKPRGWKPPVRRQFFLDCNEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPST--AGD 728
Cdd:cd07419     1 IIAHLLKPRGWKPPVERRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTeeAGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 729 IAYIDYLFLGDYVDRGQHSLETITLLLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMGE--RDGIWAWHRINRL 806
Cdd:cd07419    81 IEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdiRDGDSVWQRINRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 807 FNWLPLAALIEKKIICMHGGIGRSINHVEQIENLQRPITMEAGSIVLMDLLWSDPTENDSVEGLRPNA---RGPGL-VTF 882
Cdd:cd07419   161 FNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSPVVMDLLWSDPTENDSVLGLRPNAidpRGTGLiVKF 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2192211525 883 GPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 953
Cdd:cd07419   241 GPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIHP 311
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
142-437 1.16e-22

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.07  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 142 GIRLAGATADVHCYDVLTNKWSRITPFgePPTPRAAHVATAVGTMVVIQGGIGPAGLSAE---DLHVLDLTQQrpRWHRV 218
Cdd:COG3055    30 GLSGGSASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTplnDVYVYDPATN--TWTKL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 219 vvqGPGPGPRYGHVMALVGQRYLmAIGGNDGKRPLADVWALDTAAKpyEWRKLEPegeGPPPCMYATASARSDGLLLLCG 298
Cdd:COG3055   106 ---APMPTPRGGATALLLDGKIY-VVGGWDDGGNVAWVEVYDPATG--TWTQLAP---LPTPRDHLAAAVLPDGKILVIG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 299 GRDASSvplasayglakhRDGRWEwaiAPGVSPSPRYQHAAVFVNARLHVSGGALGGgrmvedSSSVAVLDTAAGVWcdt 378
Cdd:COG3055   177 GRNGSG------------FSNTWT---TLAPLPTARAGHAAAVLGGKILVFGGESGF------SDEVEAYDPATNTW--- 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 379 kSVVTSPRTGRYSadaaggdaaveltrrcrHAAAAVGDLIFIYGG-LRGGVLLDDLLVAE 437
Cdd:COG3055   233 -TALGELPTPRHG-----------------HAAVLTDGKVYVIGGeTKPGVRTPLVTSAE 274
Kelch_4 pfam13418
Galactose oxidase, central domain;
91-167 4.87e-03

Galactose oxidase, central domain;


:

Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 4.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2192211525  91 PRCGHTLTavaavgeegtpgYIGP-RLILFGGATAlegnsaaSGTPSSagsagirlagataDVHCYDVLTNKWSRITP 167
Cdd:pfam13418   1 PRAYHTST------------SIPDdTIYLFGGEGE-------DGTLLS-------------DLWVFDLSTNEWTRLGS 46
 
Name Accession Description Interval E-value
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 651-953 0e+00

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 623.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 651 VIAHLLKPRGWKPPVRRQFFLDCNEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPST--AGD 728
Cdd:cd07419     1 IIAHLLKPRGWKPPVERRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTeeAGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 729 IAYIDYLFLGDYVDRGQHSLETITLLLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMGE--RDGIWAWHRINRL 806
Cdd:cd07419    81 IEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdiRDGDSVWQRINRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 807 FNWLPLAALIEKKIICMHGGIGRSINHVEQIENLQRPITMEAGSIVLMDLLWSDPTENDSVEGLRPNA---RGPGL-VTF 882
Cdd:cd07419   161 FNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSPVVMDLLWSDPTENDSVLGLRPNAidpRGTGLiVKF 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2192211525 883 GPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 953
Cdd:cd07419   241 GPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIHP 311
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 674-945 2.22e-105

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 329.17  E-value: 2.22e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525  674 NEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPstagdiAYIDYLFLGDYVDRGQHSLETITL 753
Cdd:smart00156   4 EEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQP------PETNYVFLGDYVDRGPFSIEVILL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525  754 LLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMGERdgiwAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINH 833
Cdd:smart00156  78 LFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGER----IYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTT 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525  834 VEQIENLQRPITMEAGSIvLMDLLWSDPTenDSVEGLRPNARGPGlVTFGPDRVMEFCNNNDLQLIVRAHECVMDGFERF 913
Cdd:smart00156 154 LDDIRKLKRPQEPPDDGL-LIDLLWSDPD--QPVNGFGPSIRGAS-YIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFF 229

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2192211525  914 AQGHLITLFSATNYCGTANNAGAILVLGRDLV 945
Cdd:smart00156 230 ADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 639-953 3.86e-77

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 255.35  E-value: 3.86e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 639 DRQMSINSvpKKVIAHLLKPRGWKPPvrRQFFLDCNEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFD 718
Cdd:PTZ00480    4 DKKGEIDV--DNIIERLLSVRGSKPG--KNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 719 EYGSPSTAgdiayiDYLFLGDYVDRGQHSLETITLLLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMgerdGIW 798
Cdd:PTZ00480   80 YGGYPPES------NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY----TIK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 799 AWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIENLQRPITMEAGSIvLMDLLWSDPTENdsVEGLRPNARGPG 878
Cdd:PTZ00480  150 LWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGL-LCDLLWSDPDKD--VQGWADNERGVS 226

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2192211525 879 LVtFGPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 953
Cdd:PTZ00480  227 YV-FSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKP 300
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
142-437 1.16e-22

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.07  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 142 GIRLAGATADVHCYDVLTNKWSRITPFgePPTPRAAHVATAVGTMVVIQGGIGPAGLSAE---DLHVLDLTQQrpRWHRV 218
Cdd:COG3055    30 GLSGGSASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTplnDVYVYDPATN--TWTKL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 219 vvqGPGPGPRYGHVMALVGQRYLmAIGGNDGKRPLADVWALDTAAKpyEWRKLEPegeGPPPCMYATASARSDGLLLLCG 298
Cdd:COG3055   106 ---APMPTPRGGATALLLDGKIY-VVGGWDDGGNVAWVEVYDPATG--TWTQLAP---LPTPRDHLAAAVLPDGKILVIG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 299 GRDASSvplasayglakhRDGRWEwaiAPGVSPSPRYQHAAVFVNARLHVSGGALGGgrmvedSSSVAVLDTAAGVWcdt 378
Cdd:COG3055   177 GRNGSG------------FSNTWT---TLAPLPTARAGHAAAVLGGKILVFGGESGF------SDEVEAYDPATNTW--- 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 379 kSVVTSPRTGRYSadaaggdaaveltrrcrHAAAAVGDLIFIYGG-LRGGVLLDDLLVAE 437
Cdd:COG3055   233 -TALGELPTPRHG-----------------HAAVLTDGKVYVIGGeTKPGVRTPLVTSAE 274
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 699-816 1.63e-16

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: 76.48  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 699 PIKIFGDLH--GQFGDLMRLFDEYGSPSTAgDIayidYLFLGDYVDRGQHSlETITLLLALKVEYpNNVHLIRGNHEAAd 776
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKP-DL----VLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2192211525 777 inalfgfRIECIERMGERDG-IWAWHRINRLFNWLPLAALI 816
Cdd:pfam00149  74 -------YGECLRLYPYLGLlARPWKRFLEVFNFLPLAGIL 107
PLN02193 PLN02193
nitrile-specifier protein
 82-300 3.32e-11

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 66.90  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525  82 IEKKEDGPGPRCGHTLTAVA----AVGEEGTPGY-IGPRLILFGGATALEGNSAASGTPSSAGSAGIRLA--GATADV-- 152
Cdd:PLN02193  156 VEQKGEGPGLRCSHGIAQVGnkiySFGGEFTPNQpIDKHLYVFDLETRTWSISPATGDVPHLSCLGVRMVsiGSTLYVfg 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 153 -----------HCYDVLTNKWSRITPFGEPPTPRAAHVATAVGTMVVIQGGI---------------------------- 193
Cdd:PLN02193  236 grdasrqyngfYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVsatarlktldsynivdkkwfhcstpgds 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 194 ----GPAGLSA----------------EDLHVLDLTQQrpRWHRVVVQGPGPGPRYGHVMALVGqRYLMAIGGNDGKRPL 253
Cdd:PLN02193  316 fsirGGAGLEVvqgkvwvvygfngcevDDVHYYDPVQD--KWTQVETFGVRPSERSVFASAAVG-KHIVIFGGEIAMDPL 392

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2192211525 254 ADV---------WALDTaaKPYEWRKLEPEG--EGPPPCMYATASARS--DGL--LLLCGGR 300
Cdd:PLN02193  393 AHVgpgqltdgtFALDT--ETLQWERLDKFGeeEETPSSRGWTASTTGtiDGKkgLVMHGGK 452
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 333-381 9.43e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 40.78  E-value: 9.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2192211525 333 PRYQHAAVFVNARLHVSGGAlgGGRMVEDSSSVAVLDTAAGVWCDTKSV 381
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGS--DGLGDLSSSDVLVYDPETNVWTEVPRL 47
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
702-780 3.83e-04

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 42.60  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 702 IFGDLHGQFGDLMRLFDEYGSpstagdiAYID-YLFLGDYVDRGQHSLETITLLLALkveypnNVHLIRGNHEAADINAL 780
Cdd:COG0622     4 VISDTHGNLPALEAVLEDLER-------EGVDlIVHLGDLVGYGPDPPEVLDLLREL------PIVAVRGNHDGAVLRGL 70
Kelch_4 pfam13418
Galactose oxidase, central domain;
91-167 4.87e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 4.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2192211525  91 PRCGHTLTavaavgeegtpgYIGP-RLILFGGATAlegnsaaSGTPSSagsagirlagataDVHCYDVLTNKWSRITP 167
Cdd:pfam13418   1 PRAYHTST------------SIPDdTIYLFGGEGE-------DGTLLS-------------DLWVFDLSTNEWTRLGS 46
 
Name Accession Description Interval E-value
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 651-953 0e+00

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 623.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 651 VIAHLLKPRGWKPPVRRQFFLDCNEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPST--AGD 728
Cdd:cd07419     1 IIAHLLKPRGWKPPVERRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTeeAGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 729 IAYIDYLFLGDYVDRGQHSLETITLLLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMGE--RDGIWAWHRINRL 806
Cdd:cd07419    81 IEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdiRDGDSVWQRINRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 807 FNWLPLAALIEKKIICMHGGIGRSINHVEQIENLQRPITMEAGSIVLMDLLWSDPTENDSVEGLRPNA---RGPGL-VTF 882
Cdd:cd07419   161 FNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSPVVMDLLWSDPTENDSVLGLRPNAidpRGTGLiVKF 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2192211525 883 GPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 953
Cdd:cd07419   241 GPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIHP 311
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 674-945 2.22e-105

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 329.17  E-value: 2.22e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525  674 NEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPstagdiAYIDYLFLGDYVDRGQHSLETITL 753
Cdd:smart00156   4 EEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQP------PETNYVFLGDYVDRGPFSIEVILL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525  754 LLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMGERdgiwAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINH 833
Cdd:smart00156  78 LFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGER----IYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTT 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525  834 VEQIENLQRPITMEAGSIvLMDLLWSDPTenDSVEGLRPNARGPGlVTFGPDRVMEFCNNNDLQLIVRAHECVMDGFERF 913
Cdd:smart00156 154 LDDIRKLKRPQEPPDDGL-LIDLLWSDPD--QPVNGFGPSIRGAS-YIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFF 229

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2192211525  914 AQGHLITLFSATNYCGTANNAGAILVLGRDLV 945
Cdd:smart00156 230 ADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 651-953 9.54e-99

PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 (protein phosphatase type 1) is a serine/threonine phosphatase that regulates many cellular processes including: cell-cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling, through its interaction with at least 180 known targeting proteins. PP1 occurs in all tissues and regulates many pathways, ranging from cell-cycle progression to carbohydrate metabolism. Also included here are the PPKL (PP1 and kelch-like) enzymes including the PPQ, PPZ1, and PPZ2 fungal phosphatases. These PPKLs have a large N-terminal kelch repeat in addition to a C-terminal phosphoesterase domain. The PPP (phosphoprotein phosphatase) family, to which PP1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 312.35  E-value: 9.54e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 651 VIAHLLKPRGWKPpvRRQFFLDCNEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPSTAgdia 730
Cdd:cd07414     5 IIERLLEVRGSRP--GKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPES---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 731 yiDYLFLGDYVDRGQHSLETITLLLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMgerdGIWAWHRINRLFNWL 810
Cdd:cd07414    79 --NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY----NIKLWKTFTDCFNCL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 811 PLAALIEKKIICMHGGIGRSINHVEQIENLQRPITM-EAGsiVLMDLLWSDPTENdsVEGLRPNARGPGlVTFGPDRVME 889
Cdd:cd07414   153 PVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVpDQG--LLCDLLWSDPDKD--VQGWGENDRGVS-FTFGADVVAK 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2192211525 890 FCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 953
Cdd:cd07414   228 FLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 702-940 2.10e-94

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 298.52  E-value: 2.10e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 702 IFGDLHGQFGDLMRLFDEYGSPSTAgdiayiDYLFLGDYVDRGQHSLETITLLLALKVEYPNNVHLIRGNHEAADINALF 781
Cdd:cd00144     2 VVGDIHGCFDDLLRLLEKLGFPPED------KYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 782 GFRIECIERMGERDGIWAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIENLQRPITMEAGsiVLMDLLWSDP 861
Cdd:cd00144    76 GFYDERTLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNIRPIENPDDQ--LVEDLLWSDP 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2192211525 862 TENDSVEGLRPNARGPglvTFGPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVL 940
Cdd:cd00144   154 DESVGDFESSSRGGGY---LFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 674-944 4.27e-87

PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of phosphoprotein phosphatases (PPP's) including PP4 and PP6. PP2A (Protein phosphatase 2A) is a critical regulator of many cellular activities. PP2A comprises about 1% of total cellular proteins. PP2A, together with protein phosphatase 1 (PP1), accounts for more than 90% of all serine/threonine phosphatase activities in most cells and tissues. The PP2A subunit in addition to having a catalytic domain homologous to PP1, has a unique C-terminal tail, containing a motif that is conserved in the catalytic subunits of all PP2A-like phosphatases including PP4 and PP6, and has an important role in PP2A regulation. The PP2A-like family of phosphatases all share a similar heterotrimeric architecture, that includes: a 65kDa scaffolding subunit (A), a 36kDa catalytic subunit (C), and one of 18 regulatory subunits (B). The PPP (phosphoprotein phosphatase) family, to which PP2A belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277360 [Multi-domain]  Cd Length: 285  Bit Score: 281.01  E-value: 4.27e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 674 NEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFdeygspSTAGDIAYIDYLFLGDYVDRGQHSLETITL 753
Cdd:cd07415    18 SEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELF------RIGGDVPDTNYLFLGDYVDRGYYSVETFLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 754 LLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMGerdGIWAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINH 833
Cdd:cd07415    92 LLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYG---NANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 834 VEQIENLQRpiTMEAGSIVLM-DLLWSDPtenDSVEGLRPNARGPGlVTFGPDRVMEFCNNNDLQLIVRAHECVMDGFER 912
Cdd:cd07415   169 LDQIRALDR--FQEVPHEGPMcDLLWSDP---DDREGWGISPRGAG-YLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQW 242

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2192211525 913 FAQGHLITLFSATNYCGTANNAGAILVLGRDL 944
Cdd:cd07415   243 MFNNKLVTVWSAPNYCYRCGNVASILELDEHL 274
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 639-953 3.86e-77

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 255.35  E-value: 3.86e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 639 DRQMSINSvpKKVIAHLLKPRGWKPPvrRQFFLDCNEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFD 718
Cdd:PTZ00480    4 DKKGEIDV--DNIIERLLSVRGSKPG--KNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 719 EYGSPSTAgdiayiDYLFLGDYVDRGQHSLETITLLLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMgerdGIW 798
Cdd:PTZ00480   80 YGGYPPES------NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY----TIK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 799 AWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIENLQRPITMEAGSIvLMDLLWSDPTENdsVEGLRPNARGPG 878
Cdd:PTZ00480  150 LWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGL-LCDLLWSDPDKD--VQGWADNERGVS 226

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2192211525 879 LVtFGPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 953
Cdd:PTZ00480  227 YV-FSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKP 300
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 646-938 1.62e-67

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 228.25  E-value: 1.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 646 SVPKKVIAHLLKPRGWKPPvrRQFFLDCNEIADLCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPSt 725
Cdd:PTZ00244    2 SLVQTLIEKMLTVKGNRTQ--RQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPP- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 726 agdiaYIDYLFLGDYVDRGQHSLETITLLLALKVEYPNNVHLIRGNHEAADINALFGFriecIERMGERDGIWAWHRINR 805
Cdd:PTZ00244   79 -----YSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGF----FDDVKRRYNIKLFKAFTD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 806 LFNWLPLAALIEKKIICMHGGIGRSINHVEQIENLQRPITMEAGSIvLMDLLWSDPteNDSVEGLRPNARGPGLVtFGPD 885
Cdd:PTZ00244  150 VFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPDRGI-LCDLLWADP--EDEVRGFLESDRGVSYL-FGED 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2192211525 886 RVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAIL 938
Cdd:PTZ00244  226 IVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVM 278
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 686-938 6.04e-66

PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands. The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277361 [Multi-domain]  Cd Length: 305  Bit Score: 224.11  E-value: 6.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 686 IFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPSTAgdiayiDYLFLGDYVDRGQHSLETITLLLALKVEYPNNV 765
Cdd:cd07416    31 ILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANT------RYLFLGDYVDRGYFSIECVLYLWALKILYPKTL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 766 HLIRGNHEAADINALFGFRIECIERMGERdgiwAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIENLQRpiT 845
Cdd:cd07416   105 FLLRGNHECRHLTEYFTFKQECKIKYSER----VYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDR--F 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 846 MEAGSIVLM-DLLWSDPTENDSVEGLR----PNA-RGPGLVtFGPDRVMEFCNNNDLQLIVRAHECVMDGFE--RFAQG- 916
Cdd:cd07416   179 REPPSYGPMcDLLWSDPLEDFGNEKTQehfvHNTvRGCSYF-YSYRAVCEFLQKNNLLSIIRAHEAQDAGYRmyRKSQTt 257

                         250       260
                  ....*....|....*....|....*
gi 2192211525 917 ---HLITLFSATNYCGTANNAGAIL 938
Cdd:cd07416   258 gfpSLITIFSAPNYLDVYNNKAAVL 282
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 679-944 3.23e-65

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 222.00  E-value: 3.23e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 679 LCDSAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEygspstAGDIAYIDYLFLGDYVDRGQHSLETITLLLALK 758
Cdd:PTZ00239   24 ICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKE------GGDIPNANYIFIGDFVDRGYNSVETMEYLLCLK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 759 VEYPNNVHLIRGNHEAADINALFGFRIECIERMGERDgiwAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIE 838
Cdd:PTZ00239   98 VKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSN---PWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIR 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 839 NLQRPITMEAGSiVLMDLLWSDPTEndsVEGLRPNARGPGLVtFGPDRVMEFCNNNDLQLIVRAHECVMDGFER-FAQGH 917
Cdd:PTZ00239  175 TIDRKIEIPHEG-PFCDLMWSDPEE---VEYWAVNSRGAGYL-FGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQN 249

                         250       260
                  ....*....|....*....|....*..
gi 2192211525 918 LITLFSATNYCGTANNAGAILVLGRDL 944
Cdd:PTZ00239  250 LVTVWSAPNYCYRCGNIASILCLDENL 276
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 683-944 1.50e-63

PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 217.89  E-value: 1.50e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 683 AERIFSSEPSVLQLKAP----IKIFGDLHGQFGDLMRLFDEYGSPSTAGDiayidYLFLGDYVDRGQHSLETITLLLALK 758
Cdd:cd07417    41 VKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNP-----YLFNGDFVDRGSFSVEVILTLFAFK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 759 VEYPNNVHLIRGNHEAADINALFGFRIECIERMGErdgiwawhRINRLF----NWLPLAALIEKKIICMHGGI----GRS 830
Cdd:cd07417   116 LLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNE--------QMFNLFsevfNWLPLAHLINGKVLVVHGGLfsddGVT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 831 INHVEQIENLQRPitMEAGsiVLMDLLWSDPTENDsveGLRPNARGPGLvTFGPDRVMEFCNNNDLQLIVRAHECVMDGF 910
Cdd:cd07417   188 LDDIRKIDRFRQP--PDSG--LMCELLWSDPQPQP---GRGPSKRGVGC-QFGPDVTKRFLEENNLDYIIRSHEVKDEGY 259

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2192211525 911 ERFAQGHLITLFSATNYCGTANNAGA-ILVLGRDL 944
Cdd:cd07417   260 EVEHDGKCITVFSAPNYCDQMGNKGAfIRFKGSDL 294
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 683-945 2.94e-50

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 179.53  E-value: 2.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 683 AERIFSSEPSVLQLKA----PIKIFGDLHGQFGDLMRLFDEYGSPSTAGDiayidYLFLGDYVDRGQHSLETITLLLALK 758
Cdd:cd07420    32 ARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGLPSPENP-----YVFNGDFVDRGKRSIEILMILFAFV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 759 VEYPNNVHLIRGNHEAADINALFGFRIEcIERMGERDGiwawHRINRL----FNWLPLAALIEKKIICMHGGIGRS--IN 832
Cdd:cd07420   107 LVYPNAVHLNRGNHEDHIMNLRYGFTKE-VMQKYKDHG----KKILRLledvFSWLPLATIIDNKVLVVHGGISDStdLD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 833 HVEQIENLQRPITMEAGSIVLmDLLWSDPTENdsvEGLRPNA-RGPGlVTFGPDRVMEFCNNNDLQLIVRAHECVMDGFE 911
Cdd:cd07420   182 LLDKIDRHKYVSTKTEWQQVV-DILWSDPKAT---KGCKPNTfRGGG-CYFGPDVTSQFLQKHGLSLLIRSHECKPEGYE 256

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2192211525 912 RFAQGHLITLFSATNYCGTANNAGAILVLGRDLV 945
Cdd:cd07420   257 FCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLT 290
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 663-940 1.41e-40

PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 163661 [Multi-domain]  Cd Length: 377  Bit Score: 154.19  E-value: 1.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 663 PPVRRQFFLDCNEIADLCDSAERIFSSEPSVLQL----KAPIKIFGDLHGQFGDLMRLFDEYGSPStagdiAYIDYLFLG 738
Cdd:cd07418    27 PPSELPSVLPVNVFDSLVLTAHKILHREPNCVRIdvedVCEVVVVGDVHGQLHDVLFLLEDAGFPD-----QNRFYVFNG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 739 DYVDRGQHSLETITLLLALKVEYPNNVHLIRGNHEAADINALFGFRIECIERMGERdGIWAWHRINRLFNWLPLAALIEK 818
Cdd:cd07418   102 DYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDK-GKHVYRKCLGCFEGLPLASIIAG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 819 KIICMHGGIGRSI----------NHVEQIENLQRPITMEAGSI--------------------VLMDLLWSDPTENDsve 868
Cdd:cd07418   181 RVYTAHGGLFRSPslpkrkkqkgKNRRVLLLEPESESLKLGTLddlmkarrsvldppgegsnlIPGDVLWSDPSLTP--- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 869 GLRPNA-RGPGLVtFGPDRVMEFCNNNDLQLIVRAHE------------CVMDGF---ERFAQGHLITLFSATNYCG--- 929
Cdd:cd07418   258 GLSPNKqRGIGLL-WGPDCTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYtvdHDVESGKLITLFSAPDYPQfqa 336

                         330
                  ....*....|....
gi 2192211525 930 ---TANNAGAILVL 940
Cdd:cd07418   337 teeRYNNKGAYIIL 350
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
142-437 1.16e-22

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.07  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 142 GIRLAGATADVHCYDVLTNKWSRITPFgePPTPRAAHVATAVGTMVVIQGGIGPAGLSAE---DLHVLDLTQQrpRWHRV 218
Cdd:COG3055    30 GLSGGSASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTplnDVYVYDPATN--TWTKL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 219 vvqGPGPGPRYGHVMALVGQRYLmAIGGNDGKRPLADVWALDTAAKpyEWRKLEPegeGPPPCMYATASARSDGLLLLCG 298
Cdd:COG3055   106 ---APMPTPRGGATALLLDGKIY-VVGGWDDGGNVAWVEVYDPATG--TWTQLAP---LPTPRDHLAAAVLPDGKILVIG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 299 GRDASSvplasayglakhRDGRWEwaiAPGVSPSPRYQHAAVFVNARLHVSGGALGGgrmvedSSSVAVLDTAAGVWcdt 378
Cdd:COG3055   177 GRNGSG------------FSNTWT---TLAPLPTARAGHAAAVLGGKILVFGGESGF------SDEVEAYDPATNTW--- 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 379 kSVVTSPRTGRYSadaaggdaaveltrrcrHAAAAVGDLIFIYGG-LRGGVLLDDLLVAE 437
Cdd:COG3055   233 -TALGELPTPRHG-----------------HAAVLTDGKVYVIGGeTKPGVRTPLVTSAE 274
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 699-816 1.63e-16

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: 76.48  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 699 PIKIFGDLH--GQFGDLMRLFDEYGSPSTAgDIayidYLFLGDYVDRGQHSlETITLLLALKVEYpNNVHLIRGNHEAAd 776
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKP-DL----VLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2192211525 777 inalfgfRIECIERMGERDG-IWAWHRINRLFNWLPLAALI 816
Cdd:pfam00149  74 -------YGECLRLYPYLGLlARPWKRFLEVFNFLPLAGIL 107
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
222-426 6.35e-14

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 73.27  E-value: 6.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 222 GPGPGPRYGHVMALVGQRyLMAIGGNDGKRPLADVWALDTAAKpyEWRKLEPegeGPPPCMYATASARSDGLLLLCGGRD 301
Cdd:COG3055     7 PDLPTPRSEAAAALLDGK-VYVAGGLSGGSASNSFEVYDPATN--TWSELAP---LPGPPRHHAAAVAQDGKLYVFGGFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 302 A---SSVPLASA--YGLAKhrdGRWEwAIAPgvSPSPRYQHAAVFVNARLHVSGGALGGGrmveDSSSVAVLDTAAGVWc 376
Cdd:COG3055    81 GanpSSTPLNDVyvYDPAT---NTWT-KLAP--MPTPRGGATALLLDGKIYVVGGWDDGG----NVAWVEVYDPATGTW- 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2192211525 377 DTKSVVTSPRT----------------GRYSADAAGGDAAVE--LTRRCRHAAAAVGDLIFIYGGLRG 426
Cdd:COG3055   150 TQLAPLPTPRDhlaaavlpdgkilvigGRNGSGFSNTWTTLAplPTARAGHAAAVLGGKILVFGGESG 217
PLN02193 PLN02193
nitrile-specifier protein
 82-300 3.32e-11

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 66.90  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525  82 IEKKEDGPGPRCGHTLTAVA----AVGEEGTPGY-IGPRLILFGGATALEGNSAASGTPSSAGSAGIRLA--GATADV-- 152
Cdd:PLN02193  156 VEQKGEGPGLRCSHGIAQVGnkiySFGGEFTPNQpIDKHLYVFDLETRTWSISPATGDVPHLSCLGVRMVsiGSTLYVfg 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 153 -----------HCYDVLTNKWSRITPFGEPPTPRAAHVATAVGTMVVIQGGI---------------------------- 193
Cdd:PLN02193  236 grdasrqyngfYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVsatarlktldsynivdkkwfhcstpgds 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 194 ----GPAGLSA----------------EDLHVLDLTQQrpRWHRVVVQGPGPGPRYGHVMALVGqRYLMAIGGNDGKRPL 253
Cdd:PLN02193  316 fsirGGAGLEVvqgkvwvvygfngcevDDVHYYDPVQD--KWTQVETFGVRPSERSVFASAAVG-KHIVIFGGEIAMDPL 392

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2192211525 254 ADV---------WALDTaaKPYEWRKLEPEG--EGPPPCMYATASARS--DGL--LLLCGGR 300
Cdd:PLN02193  393 AHVgpgqltdgtFALDT--ETLQWERLDKFGeeEETPSSRGWTASTTGtiDGKkgLVMHGGK 452
PLN02153 PLN02153
epithiospecifier protein
 169-423 4.35e-10

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 62.31  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 169 GEPPTPRAAHVATAVGTMVVIQGG-IGPAGLSAEDLHVLDLTQQRprWHrvVVQGPGPGPR---YGHVMALVGQRyLMAI 244
Cdd:PLN02153   17 GKGPGPRCSHGIAVVGDKLYSFGGeLKPNEHIDKDLYVFDFNTHT--WS--IAPANGDVPRiscLGVRMVAVGTK-LYIF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 245 GGNDGKRPLADVWALDTAAKpyEWR---KLEPEGeGPPPCMYATASARSDGLLLLCGGRDASSVPLAS------AYGLAk 315
Cdd:PLN02153   92 GGRDEKREFSDFYSYDTVKN--EWTfltKLDEEG-GPEARTFHSMASDENHVYVFGGVSKGGLMKTPErfrtieAYNIA- 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 316 hrDGRWEWAIAPGVSPSPRYQHAAVFVNARLHVSGG----ALGGGRMVEDSSSVAVLDTAAGVWCDTKSVVTSPrtgrys 391
Cdd:PLN02153  168 --DGKWVQLPDPGENFEKRGGAGFAVVQGKIWVVYGfatsILPGGKSDYESNAVQFFDPASGKWTEVETTGAKP------ 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2192211525 392 adaaggdaavelTRRCRHAAAAVGDLIFIYGG 423
Cdd:PLN02153  240 ------------SARSVFAHAVVGKYIIIFGG 259
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 704-780 4.13e-08

PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine and tyrosine phosphatases thought to modulate the expression of proteins that protect the cell upon accumulation of misfolded proteins in the periplasm. The PPP (phosphoprotein phosphatase) family, to which PrpA and PrpB belong, is one of two known protein phosphatase families specific for serine and threonine. This family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 54.63  E-value: 4.13e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2192211525 704 GDLHGQFGDLMRLFDEYG-SPstagdiaYIDYLF-LGDYVDRGQHSLETITLLlalkvEYPnNVHLIRGNHEAADINAL 780
Cdd:cd07424     7 GDIHGHFQRLQRALDAVGfDP-------ARDRLIsVGDLVDRGPESLEVLELL-----KQP-WFHAVQGNHEQMAIDAL 72
PLN02193 PLN02193
nitrile-specifier protein
 158-423 1.85e-07

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 54.96  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 158 LTNKWSRITPFGEPPTPRAAHVATAVGTMVVIQGG-IGPAGLSAEDLHVLDLTQQrpRWHRVVVQGPGPGPR-YGHVMAL 235
Cdd:PLN02193  149 LLGKWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGeFTPNQPIDKHLYVFDLETR--TWSISPATGDVPHLScLGVRMVS 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 236 VGQRyLMAIGGNDGKRPLADVWALDTAAKpyEWRKLEPEGEGPPPCMYATASARSDGLLLLCGGRDASSVPLASAYGLAk 315
Cdd:PLN02193  227 IGST-LYVFGGRDASRQYNGFYSFDTTTN--EWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLKTLDSYNIV- 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 316 hrDGRWEWAIAPGVSPSPRYQHAAVFVNARLHVSGGAlgGGRMVEDsssVAVLDTAAGVWCDTKSVVTSPrtgrysadaa 395
Cdd:PLN02193  303 --DKKWFHCSTPGDSFSIRGGAGLEVVQGKVWVVYGF--NGCEVDD---VHYYDPVQDKWTQVETFGVRP---------- 365

                         250       260
                  ....*....|....*....|....*...
gi 2192211525 396 ggdaavelTRRCRHAAAAVGDLIFIYGG 423
Cdd:PLN02193  366 --------SERSVFASAAVGKHIVIFGG 385
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
702-827 2.36e-07

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 53.25  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 702 IFGDLHGQFGDLMRLFDEYG-SPSTagdiayiDYL-FLGDYVDRGQHSLETITLLLALKveypNNVHLIRGNHeaaDINA 779
Cdd:PRK00166    5 AIGDIQGCYDELQRLLEKIDfDPAK-------DTLwLVGDLVNRGPDSLEVLRFVKSLG----DSAVTVLGNH---DLHL 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2192211525 780 LFGFRieCIERMGERD---GIWAWHRINRLFNWL---PLAA-LIEKKIICMHGGI 827
Cdd:PRK00166   71 LAVAA--GIKRNKKKDtldPILEAPDRDELLDWLrhqPLLHvDEELGLVMVHAGI 123
PHA02239 PHA02239
putative protein phosphatase
 700-798 3.55e-06

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 49.22  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 700 IKIFGDLHGQFGDLMRLFDEYGSPSTAGDIAyidyLFLGDYVDRGQHSLETITLLLALKVEYPNNVHLIrGNHEAADINA 779
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIMDKINNERKPEETI----VFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL-GNHDDEFYNI 77

                          90
                  ....*....|....*....
gi 2192211525 780 lfgfrIECIERMGERDGIW 798
Cdd:PHA02239   78 -----MENVDRLSIYDIEW 91
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 702-827 4.31e-06

Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as symmetrically cleaving Ap4A hydrolase and bis(5'nucleosyl)-tetraphosphatase) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases that hydrolyzes the nucleotide-signaling molecule diadenosine tetraphosphate (Ap(4)A) into two ADP and also hydrolyzes Ap(5)A, Gp(4)G, and other extending compounds. Null mutations in apaH result in high intracellular levels of Ap(4)A which correlate with multiple phenotypes, including a decreased expression of catabolite-repressible genes, a reduction in the expression of flagellar operons, and an increased sensitivity to UV and heat. Ap4A hydrolase is important in responding to heat shock and oxidative stress via regulating the concentration of Ap4A in bacteria. Ap4A hydrolase is also thought to play a role in siderophore production, but the mechanism by which ApaH interacts with siderophore pathways in unknown. The PPP (phosphoprotein phosphatase) family, to which ApaH belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, and PrpA/PrpB. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 49.46  E-value: 4.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 702 IFGDLHGQFGDLMRLFDEYG-SPSTagdiayiDYL-FLGDYVDRGQHSLETITLLLALKveypNNVHLIRGNHeaaDINA 779
Cdd:cd07422     3 AIGDIQGCYDELQRLLEKINfDPAK-------DRLwLVGDLVNRGPDSLETLRFVKSLG----DSAVVVLGNH---DLHL 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2192211525 780 L---FGfriecIERMGERD---GIWAWHRINRLFNWL---PLAALIEKKIICM-HGGI 827
Cdd:cd07422    69 LavaAG-----IKKLKKKDtldEILEAPDRDELLDWLrhqPLLHRDDELGIVMvHAGI 121
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 704-775 1.03e-05

Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 163664  Cd Length: 304  Bit Score: 48.65  E-value: 1.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2192211525 704 GDLHGQFGDLMRLFDEYGSPSTAGDIAYIDYLFLGDYVDRGQHSLETITLLLALKVEYPNNVH-LIRGNHEAA 775
Cdd:cd07421     8 GDIHGYISKLNNLWLNLQSALGPSDFASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHvFLCGNHDFA 80
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 702-773 1.30e-05

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing 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. This superfamily includes: the phosphoprotein phosphatases (PPPs), 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: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 45.72  E-value: 1.30e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2192211525 702 IFGDLHGQFGDLMRLFDEYgspstAGDIAYIDYL-FLGDYVDRGQHSLETITLLLALKvEYPNNVHLIRGNHE 773
Cdd:cd00838     2 VISDIHGNLEALEAVLEAA-----LAKAEKPDLViCLGDLVDYGPDPEEVELKALRLL-LAGIPVYVVPGNHD 68
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 333-381 9.43e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 40.78  E-value: 9.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2192211525 333 PRYQHAAVFVNARLHVSGGAlgGGRMVEDSSSVAVLDTAAGVWCDTKSV 381
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGS--DGLGDLSSSDVLVYDPETNVWTEVPRL 47
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 703-835 1.79e-04

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 43.83  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 703 FGDLHGQFGDLMRLFDEYGSPSTAGDIAYIDYLF--LGDYVDRGQHSLETITLLLALKVEYP---NNVHLIRGNHEaadI 777
Cdd:cd07425     3 IGDLHGDLDRLRTILKLAGVIDSNDRWIGGDTVVvqTGDILDRGDDEIEILKLLEKLKRQARkagGKVILLLGNHE---L 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2192211525 778 NALFG-FRIECIERMGERdGIWAwHRINRLFNWLPLAA--LIEKK-------IICMHGGIG----RSINHVE 835
Cdd:cd07425    80 MNLCGdFRYVHPRGLNEF-GGVA-KRRYALLSDGGYIGryLRTHPvvlvvndILFVHGGLGplwsRGYSLET 149
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
702-780 3.83e-04

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 42.60  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 702 IFGDLHGQFGDLMRLFDEYGSpstagdiAYID-YLFLGDYVDRGQHSLETITLLLALkveypnNVHLIRGNHEAADINAL 780
Cdd:COG0622     4 VISDTHGNLPALEAVLEDLER-------EGVDlIVHLGDLVGYGPDPPEVLDLLREL------PIVAVRGNHDGAVLRGL 70
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 227-273 9.55e-04

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 37.98  E-value: 9.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2192211525 227 PRYGHVMALVGQRyLMAIGGNDGKRPLADVWALDTAAKpyEWRKLEP 273
Cdd:pfam01344   1 RRSGAGVVVVGGK-IYVIGGFDGNQSLNSVEVYDPETN--TWSKLPS 44
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 700-827 3.12e-03

bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 40.46  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 700 IKIFGDLHGQFGDLMRLFDEYGSPSTAGDIAYID---YLFLGDYVDRGQHSLETITLLLALkVEYpNNVHLIRGNHeaad 776
Cdd:PRK13625    3 YDIIGDIHGCYQEFQALTEKLGYNWSSGLPVHPDqrkLAFVGDLTDRGPHSLRMIEIVWEL-VEK-KAAYYVPGNH---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2192211525 777 INALFGF--------------RIECIERMGERDGIWAWHRINRLFNWLPL-AALIEKKIICMHGGI 827
Cdd:PRK13625   77 CNKLYRFflgrnvtiahgletTVAEYEALPSHKQNMIKEKFITLYEQAPLyHILDEGRLVVAHAGI 142
Kelch_4 pfam13418
Galactose oxidase, central domain;
91-167 4.87e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 4.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2192211525  91 PRCGHTLTavaavgeegtpgYIGP-RLILFGGATAlegnsaaSGTPSSagsagirlagataDVHCYDVLTNKWSRITP 167
Cdd:pfam13418   1 PRAYHTST------------SIPDdTIYLFGGEGE-------DGTLLS-------------DLWVFDLSTNEWTRLGS 46
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
331-427 6.14e-03

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 39.75  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 331 PSPRYQHAAVFVNARLHVSGGALGGGrmveDSSSVAVLDTAAGVWCDTKSVVTSPRTGrysadaaggdaaveltrrcrHA 410
Cdd:COG3055    10 PTPRSEAAAALLDGKVYVAGGLSGGS----ASNSFEVYDPATNTWSELAPLPGPPRHH--------------------AA 65

                          90
                  ....*....|....*..
gi 2192211525 411 AAAVGDLIFIYGGLRGG 427
Cdd:COG3055    66 AVAQDGKLYVFGGFTGA 82
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 702-773 7.99e-03

Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong 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: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 39.04  E-value: 7.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2192211525 702 IFGDLHGQFGDLMRLFDEYG-SPSTAGDIAYID---YLFLGDYVDRGQHSLETITLLLALkVEYpNNVHLIRGNHE 773
Cdd:cd07423     2 IIGDVHGCYDELVELLEKLGyQKKEEGLYVHPEgrkLVFLGDLVDRGPDSIDVLRLVMNM-VKA-GKALYVPGNHC 75
pphA PRK11439
protein-serine/threonine phosphatase;
700-780 8.62e-03

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 38.98  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192211525 700 IKIFGDLHGQFGDLMRLFDEYG-SPstagdiaYIDYLF-LGDYVDRGQHSLETITLLlalkveYPNNVHLIRGNHEAADI 777
Cdd:PRK11439   19 IWLVGDIHGCFEQLMRKLRHCRfDP-------WRDLLIsVGDLIDRGPQSLRCLQLL------EEHWVRAVRGNHEQMAL 85


                  ...
gi 2192211525 778 NAL 780
Cdd:PRK11439   86 DAL 88
 
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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