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Conserved domains on  [gi|1109279082|ref|XP_019163803|]
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PREDICTED: serine/threonine-protein phosphatase BSL3 isoform X2 [Ipomoea nil]

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 ...
 652-954 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 1109279082  652 VIAHLLKPRGWKPPVRRQFFLDCNEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPST--AGD 729
Cdd:cd07419      1 IIAHLLKPRGWKPPVERRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTeeAGD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  730 IAYIDYLFLGDYVDRGQHSLETITLLLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMGE--RDGIWAWHRINRL 807
Cdd:cd07419     81 IEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdiRDGDSVWQRINRL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  808 FNWLPLAALIEKKIICMHGGIGRSINHVEQIENIQRPITMEAGSIVLMDLLWSDPTENDSVEGLRPNA---RGPGL-VTF 883
Cdd:cd07419    161 FNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSPVVMDLLWSDPTENDSVLGLRPNAidpRGTGLiVKF 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109279082  884 GPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 954
Cdd:cd07419    241 GPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIHP 311
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
140-435 2.15e-21

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 95.22  E-value: 2.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  140 GIRLAGATADVHCYDVLTNKWSRITPIgePPTPRAAHVATAVGTMVVLQGGIGPAGLSAE---DLHVLDLTQQrpRWHRV 216
Cdd:COG3055     30 GLSGGSASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTplnDVYVYDPATN--TWTKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  217 vvqGPGPGPRYGHVMALVGQRYLmAIGGNDGKRPLADVWALDTAAKpyEWRKLEPegeGPPPCMYATASARSDGLLLLCG 296
Cdd:COG3055    106 ---APMPTPRGGATALLLDGKIY-VVGGWDDGGNVAWVEVYDPATG--TWTQLAP---LPTPRDHLAAAVLPDGKILVIG 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  297 GRDANSvplasayglakhRDGRWEwaiAPGVSPSPRYQHAAVFVNARLHVSGGALGGgrmvedSSSVAVLDTAAGVWcdt 376
Cdd:COG3055    177 GRNGSG------------FSNTWT---TLAPLPTARAGHAAAVLGGKILVFGGESGF------SDEVEAYDPATNTW--- 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  377 KSVVTSPRPgrysadaaggdaaveltrRCRHAAAAVGDLIFIYGG-LRGGVLLDDLLVAE 435
Cdd:COG3055    233 TALGELPTP------------------RHGHAAVLTDGKVYVIGGeTKPGVRTPLVTSAE 274
PLN02193 super family cl31837
nitrile-specifier protein
 73-197 3.30e-06

nitrile-specifier protein


The actual alignment was detected with superfamily member PLN02193:

Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 50.72  E-value: 3.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   73 YSVLQPIiektEDGPGPRCGHTLTAvppvGEEGMpgYIgprlilFGGATALE----------------GNSAASGTPSSA 136
Cdd:PLN02193   256 WKLLTPV----EEGPTPRSFHSMAA----DEENV--YV------FGGVSATArlktldsynivdkkwfHCSTPGDSFSIR 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  137 GSAGIRLAGATA------------DVHCYDVLTNKWSRITPIGEPPTPRAAHVATAVGTMVVLQGG---------IGPAG 195
Cdd:PLN02193   320 GGAGLEVVQGKVwvvygfngcevdDVHYYDPVQDKWTQVETFGVRPSERSVFASAAVGKHIVIFGGeiamdplahVGPGQ 399


                   ..
gi 1109279082  196 LS 197
Cdd:PLN02193   400 LT 401
 
Name Accession Description Interval E-value
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 652-954 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 1109279082  652 VIAHLLKPRGWKPPVRRQFFLDCNEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPST--AGD 729
Cdd:cd07419      1 IIAHLLKPRGWKPPVERRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTeeAGD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  730 IAYIDYLFLGDYVDRGQHSLETITLLLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMGE--RDGIWAWHRINRL 807
Cdd:cd07419     81 IEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdiRDGDSVWQRINRL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  808 FNWLPLAALIEKKIICMHGGIGRSINHVEQIENIQRPITMEAGSIVLMDLLWSDPTENDSVEGLRPNA---RGPGL-VTF 883
Cdd:cd07419    161 FNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSPVVMDLLWSDPTENDSVLGLRPNAidpRGTGLiVKF 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109279082  884 GPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 954
Cdd:cd07419    241 GPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIHP 311
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 675-946 2.07e-104

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: 326.86  E-value: 2.07e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   675 NEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPstagdiAYIDYLFLGDYVDRGQHSLETITL 754
Cdd:smart00156    4 EEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQP------PETNYVFLGDYVDRGPFSIEVILL 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   755 LLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMGERdgiwAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINH 834
Cdd:smart00156   78 LFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGER----IYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTT 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   835 VEQIENIQRPITMEAGSIvLMDLLWSDPTenDSVEGLRPNARGPGlVTFGPDRVMEFCNNNDLQLIVRAHECVMDGFERF 914
Cdd:smart00156  154 LDDIRKLKRPQEPPDDGL-LIDLLWSDPD--QPVNGFGPSIRGAS-YIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFF 229

                           250       260       270
                    ....*....|....*....|....*....|..
gi 1109279082   915 AQGHLITLFSATNYCGTANNAGAILVLGRDLV 946
Cdd:smart00156  230 ADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 640-954 1.55e-77

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 256.51  E-value: 1.55e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  640 DRQMSINSvpKKVIAHLLKPRGWKPPvrRQFFLDCNEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFD 719
Cdd:PTZ00480     4 DKKGEIDV--DNIIERLLSVRGSKPG--KNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  720 EYGSPSTAgdiayiDYLFLGDYVDRGQHSLETITLLLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMgerdGIW 799
Cdd:PTZ00480    80 YGGYPPES------NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY----TIK 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  800 AWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIENIQRPITMEAGSIvLMDLLWSDPTENdsVEGLRPNARGPG 879
Cdd:PTZ00480   150 LWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGL-LCDLLWSDPDKD--VQGWADNERGVS 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109279082  880 LVtFGPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 954
Cdd:PTZ00480   227 YV-FSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKP 300
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
140-435 2.15e-21

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 95.22  E-value: 2.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  140 GIRLAGATADVHCYDVLTNKWSRITPIgePPTPRAAHVATAVGTMVVLQGGIGPAGLSAE---DLHVLDLTQQrpRWHRV 216
Cdd:COG3055     30 GLSGGSASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTplnDVYVYDPATN--TWTKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  217 vvqGPGPGPRYGHVMALVGQRYLmAIGGNDGKRPLADVWALDTAAKpyEWRKLEPegeGPPPCMYATASARSDGLLLLCG 296
Cdd:COG3055    106 ---APMPTPRGGATALLLDGKIY-VVGGWDDGGNVAWVEVYDPATG--TWTQLAP---LPTPRDHLAAAVLPDGKILVIG 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  297 GRDANSvplasayglakhRDGRWEwaiAPGVSPSPRYQHAAVFVNARLHVSGGALGGgrmvedSSSVAVLDTAAGVWcdt 376
Cdd:COG3055    177 GRNGSG------------FSNTWT---TLAPLPTARAGHAAAVLGGKILVFGGESGF------SDEVEAYDPATNTW--- 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  377 KSVVTSPRPgrysadaaggdaaveltrRCRHAAAAVGDLIFIYGG-LRGGVLLDDLLVAE 435
Cdd:COG3055    233 TALGELPTP------------------RHGHAAVLTDGKVYVIGGeTKPGVRTPLVTSAE 274
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 700-817 2.56e-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: 75.71  E-value: 2.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  700 PIKIFGDLH--GQFGDLMRLFDEYGSPSTAgDIayidYLFLGDYVDRGQHSlETITLLLALKVEYpHNVHLIRGNHEAAd 777
Cdd:pfam00149    2 RILVIGDLHlpGQLDDLLELLKKLLEEGKP-DL----VLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD- 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1109279082  778 inalfgfRIECIERMGERDG-IWAWHRINRLFNWLPLAALI 817
Cdd:pfam00149   74 -------YGECLRLYPYLGLlARPWKRFLEVFNFLPLAGIL 107
PLN02153 PLN02153
epithiospecifier protein
 167-421 4.65e-10

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 62.31  E-value: 4.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  167 GEPPTPRAAHVATAVGTMVVLQGG-IGPAGLSAEDLHVLDLTQQRprWHrvVVQGPGPGPR---YGHVMALVGQRyLMAI 242
Cdd:PLN02153    17 GKGPGPRCSHGIAVVGDKLYSFGGeLKPNEHIDKDLYVFDFNTHT--WS--IAPANGDVPRiscLGVRMVAVGTK-LYIF 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  243 GGNDGKRPLADVWALDTAAKpyEWR---KLEPEGeGPPPCMYATASARSDGLLLLCGGRDANSVPLAS------AYGLAk 313
Cdd:PLN02153    92 GGRDEKREFSDFYSYDTVKN--EWTfltKLDEEG-GPEARTFHSMASDENHVYVFGGVSKGGLMKTPErfrtieAYNIA- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  314 hrDGRWEWAIAPGVSPSPRYQHAAVFVNARLHVSGG----ALGGGRMVEDSSSVAVLDTAAGVWCDTKSVVTSPrpgrys 389
Cdd:PLN02153   168 --DGKWVQLPDPGENFEKRGGAGFAVVQGKIWVVYGfatsILPGGKSDYESNAVQFFDPASGKWTEVETTGAKP------ 239

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1109279082  390 adaaggdaavelTRRCRHAAAAVGDLIFIYGG 421
Cdd:PLN02153   240 ------------SARSVFAHAVVGKYIIIFGG 259
PLN02193 PLN02193
nitrile-specifier protein
 73-197 3.30e-06

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 50.72  E-value: 3.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   73 YSVLQPIiektEDGPGPRCGHTLTAvppvGEEGMpgYIgprlilFGGATALE----------------GNSAASGTPSSA 136
Cdd:PLN02193   256 WKLLTPV----EEGPTPRSFHSMAA----DEENV--YV------FGGVSATArlktldsynivdkkwfHCSTPGDSFSIR 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  137 GSAGIRLAGATA------------DVHCYDVLTNKWSRITPIGEPPTPRAAHVATAVGTMVVLQGG---------IGPAG 195
Cdd:PLN02193   320 GGAGLEVVQGKVwvvygfngcevdDVHYYDPVQDKWTQVETFGVRPSERSVFASAAVGKHIVIFGGeiamdplahVGPGQ 399


                   ..
gi 1109279082  196 LS 197
Cdd:PLN02193   400 LT 401
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 331-379 1.02e-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: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 40.78  E-value: 1.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1109279082  331 PRYQHAAVFVNARLHVSGGAlgGGRMVEDSSSVAVLDTAAGVWCDTKSV 379
Cdd:pfam07646    1 PRYPHASSVPGGKLYVVGGS--DGLGDLSSSDVLVYDPETNVWTEVPRL 47
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
703-781 3.50e-04

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 42.60  E-value: 3.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  703 IFGDLHGQFGDLMRLFDEYGSpstagdiAYID-YLFLGDYVDRGQHSLETITLLLAlkveypHNVHLIRGNHEAADINAL 781
Cdd:COG0622      4 VISDTHGNLPALEAVLEDLER-------EGVDlIVHLGDLVGYGPDPPEVLDLLRE------LPIVAVRGNHDGAVLRGL 70
Kelch_4 pfam13418
Galactose oxidase, central domain;
89-165 3.17e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.44  E-value: 3.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109279082   89 PRCGHTLTAVPPvgeegmpGYIgprlILFGGATAlegnsaaSGTPSSagsagirlagataDVHCYDVLTNKWSRITP 165
Cdd:pfam13418    1 PRAYHTSTSIPD-------DTI----YLFGGEGE-------DGTLLS-------------DLWVFDLSTNEWTRLGS 46
 
Name Accession Description Interval E-value
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 652-954 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 1109279082  652 VIAHLLKPRGWKPPVRRQFFLDCNEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPST--AGD 729
Cdd:cd07419      1 IIAHLLKPRGWKPPVERRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTeeAGD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  730 IAYIDYLFLGDYVDRGQHSLETITLLLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMGE--RDGIWAWHRINRL 807
Cdd:cd07419     81 IEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEdiRDGDSVWQRINRL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  808 FNWLPLAALIEKKIICMHGGIGRSINHVEQIENIQRPITMEAGSIVLMDLLWSDPTENDSVEGLRPNA---RGPGL-VTF 883
Cdd:cd07419    161 FNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSPVVMDLLWSDPTENDSVLGLRPNAidpRGTGLiVKF 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109279082  884 GPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 954
Cdd:cd07419    241 GPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIHP 311
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 675-946 2.07e-104

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: 326.86  E-value: 2.07e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   675 NEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPstagdiAYIDYLFLGDYVDRGQHSLETITL 754
Cdd:smart00156    4 EEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQP------PETNYVFLGDYVDRGPFSIEVILL 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   755 LLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMGERdgiwAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINH 834
Cdd:smart00156   78 LFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGER----IYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTT 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   835 VEQIENIQRPITMEAGSIvLMDLLWSDPTenDSVEGLRPNARGPGlVTFGPDRVMEFCNNNDLQLIVRAHECVMDGFERF 914
Cdd:smart00156  154 LDDIRKLKRPQEPPDDGL-LIDLLWSDPD--QPVNGFGPSIRGAS-YIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFF 229

                           250       260       270
                    ....*....|....*....|....*....|..
gi 1109279082   915 AQGHLITLFSATNYCGTANNAGAILVLGRDLV 946
Cdd:smart00156  230 ADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLK 261
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 652-954 5.09e-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: 313.12  E-value: 5.09e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  652 VIAHLLKPRGWKPpvRRQFFLDCNEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPSTAgdia 731
Cdd:cd07414      5 IIERLLEVRGSRP--GKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPES---- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  732 yiDYLFLGDYVDRGQHSLETITLLLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMgerdGIWAWHRINRLFNWL 811
Cdd:cd07414     79 --NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY----NIKLWKTFTDCFNCL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  812 PLAALIEKKIICMHGGIGRSINHVEQIENIQRPITM-EAGsiVLMDLLWSDPTENdsVEGLRPNARGPGlVTFGPDRVME 890
Cdd:cd07414    153 PVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVpDQG--LLCDLLWSDPDKD--VQGWGENDRGVS-FTFGADVVAK 227

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109279082  891 FCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 954
Cdd:cd07414    228 FLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 703-941 6.12e-95

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: 300.06  E-value: 6.12e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  703 IFGDLHGQFGDLMRLFDEYGSPSTAgdiayiDYLFLGDYVDRGQHSLETITLLLALKVEYPHNVHLIRGNHEAADINALF 782
Cdd:cd00144      2 VVGDIHGCFDDLLRLLEKLGFPPED------KYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLY 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  783 GFRIECIERMGERDGIWAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIENIQRPITMEAGsiVLMDLLWSDP 862
Cdd:cd00144     76 GFYDERTLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNIRPIENPDDQ--LVEDLLWSDP 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109279082  863 TENDSVEGLRPNARGPglvTFGPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVL 941
Cdd:cd00144    154 DESVGDFESSSRGGGY---LFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 675-945 3.70e-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: 281.40  E-value: 3.70e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  675 NEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFdeygspSTAGDIAYIDYLFLGDYVDRGQHSLETITL 754
Cdd:cd07415     18 SEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELF------RIGGDVPDTNYLFLGDYVDRGYYSVETFLL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  755 LLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMGerdGIWAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINH 834
Cdd:cd07415     92 LLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYG---NANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQT 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  835 VEQIENIQRpiTMEAGSIVLM-DLLWSDPtenDSVEGLRPNARGPGlVTFGPDRVMEFCNNNDLQLIVRAHECVMDGFER 913
Cdd:cd07415    169 LDQIRALDR--FQEVPHEGPMcDLLWSDP---DDREGWGISPRGAG-YLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQW 242

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1109279082  914 FAQGHLITLFSATNYCGTANNAGAILVLGRDL 945
Cdd:cd07415    243 MFNNKLVTVWSAPNYCYRCGNVASILELDEHL 274
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 640-954 1.55e-77

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 256.51  E-value: 1.55e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  640 DRQMSINSvpKKVIAHLLKPRGWKPPvrRQFFLDCNEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFD 719
Cdd:PTZ00480     4 DKKGEIDV--DNIIERLLSVRGSKPG--KNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  720 EYGSPSTAgdiayiDYLFLGDYVDRGQHSLETITLLLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMgerdGIW 799
Cdd:PTZ00480    80 YGGYPPES------NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY----TIK 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  800 AWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIENIQRPITMEAGSIvLMDLLWSDPTENdsVEGLRPNARGPG 879
Cdd:PTZ00480   150 LWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGL-LCDLLWSDPDKD--VQGWADNERGVS 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109279082  880 LVtFGPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHP 954
Cdd:PTZ00480   227 YV-FSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKP 300
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 647-939 9.03e-68

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 229.02  E-value: 9.03e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  647 SVPKKVIAHLLKPRGWKPPvrRQFFLDCNEIADLCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPSt 726
Cdd:PTZ00244     2 SLVQTLIEKMLTVKGNRTQ--RQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPP- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  727 agdiaYIDYLFLGDYVDRGQHSLETITLLLALKVEYPHNVHLIRGNHEAADINALFGFriecIERMGERDGIWAWHRINR 806
Cdd:PTZ00244    79 -----YSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGF----FDDVKRRYNIKLFKAFTD 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  807 LFNWLPLAALIEKKIICMHGGIGRSINHVEQIENIQRPITMEAGSIvLMDLLWSDPteNDSVEGLRPNARGPGLVtFGPD 886
Cdd:PTZ00244   150 VFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPDRGI-LCDLLWADP--EDEVRGFLESDRGVSYL-FGED 225

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1109279082  887 RVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAIL 939
Cdd:PTZ00244   226 IVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVM 278
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 680-945 1.07e-65

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 223.54  E-value: 1.07e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  680 LCDNAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEygspstAGDIAYIDYLFLGDYVDRGQHSLETITLLLALK 759
Cdd:PTZ00239    24 ICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKE------GGDIPNANYIFIGDFVDRGYNSVETMEYLLCLK 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  760 VEYPHNVHLIRGNHEAADINALFGFRIECIERMGERDgiwAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIE 839
Cdd:PTZ00239    98 VKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSN---PWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIR 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  840 NIQRPITMEAGSiVLMDLLWSDPTEndsVEGLRPNARGPGLVtFGPDRVMEFCNNNDLQLIVRAHECVMDGFER-FAQGH 918
Cdd:PTZ00239   175 TIDRKIEIPHEG-PFCDLMWSDPEE---VEYWAVNSRGAGYL-FGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQN 249

                          250       260
                   ....*....|....*....|....*..
gi 1109279082  919 LITLFSATNYCGTANNAGAILVLGRDL 945
Cdd:PTZ00239   250 LVTVWSAPNYCYRCGNIASILCLDENL 276
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 683-939 1.29e-65

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: 223.34  E-value: 1.29e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  683 NAERIFSSEPSVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPSTAgdiayiDYLFLGDYVDRGQHSLETITLLLALKVEY 762
Cdd:cd07416     27 EGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANT------RYLFLGDYVDRGYFSIECVLYLWALKILY 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  763 PHNVHLIRGNHEAADINALFGFRIECIERMGERdgiwAWHRINRLFNWLPLAALIEKKIICMHGGIGRSINHVEQIENIQ 842
Cdd:cd07416    101 PKTLFLLRGNHECRHLTEYFTFKQECKIKYSER----VYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLD 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  843 RpiTMEAGSIVLM-DLLWSDPTENDSVEGLR----PNA-RGPGLVtFGPDRVMEFCNNNDLQLIVRAHECVMDGFE--RF 914
Cdd:cd07416    177 R--FREPPSYGPMcDLLWSDPLEDFGNEKTQehfvHNTvRGCSYF-YSYRAVCEFLQKNNLLSIIRAHEAQDAGYRmyRK 253

                          250       260
                   ....*....|....*....|....*....
gi 1109279082  915 AQG----HLITLFSATNYCGTANNAGAIL 939
Cdd:cd07416    254 SQTtgfpSLITIFSAPNYLDVYNNKAAVL 282
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 684-945 6.75e-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: 215.97  E-value: 6.75e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  684 AERIFSSEPSVLQLKAP----IKIFGDLHGQFGDLMRLFDEYGSPSTAGDiayidYLFLGDYVDRGQHSLETITLLLALK 759
Cdd:cd07417     41 VKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNP-----YLFNGDFVDRGSFSVEVILTLFAFK 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  760 VEYPHNVHLIRGNHEAADINALFGFRIECIERMGErdgiwawhRINRLF----NWLPLAALIEKKIICMHGGI----GRS 831
Cdd:cd07417    116 LLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNE--------QMFNLFsevfNWLPLAHLINGKVLVVHGGLfsddGVT 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  832 INHVEQIENIQRPitMEAGsiVLMDLLWSDPTENDsveGLRPNARGPGLvTFGPDRVMEFCNNNDLQLIVRAHECVMDGF 911
Cdd:cd07417    188 LDDIRKIDRFRQP--PDSG--LMCELLWSDPQPQP---GRGPSKRGVGC-QFGPDVTKRFLEENNLDYIIRSHEVKDEGY 259

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1109279082  912 ERFAQGHLITLFSATNYCGTANNAGA-ILVLGRDL 945
Cdd:cd07417    260 EVEHDGKCITVFSAPNYCDQMGNKGAfIRFKGSDL 294
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 684-946 9.29e-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: 178.37  E-value: 9.29e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  684 AERIFSSEPSVLQLKA----PIKIFGDLHGQFGDLMRLFDEYGSPSTAGDiayidYLFLGDYVDRGQHSLETITLLLALK 759
Cdd:cd07420     32 ARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGLPSPENP-----YVFNGDFVDRGKRSIEILMILFAFV 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  760 VEYPHNVHLIRGNHEAADINALFGFRIEcIERMGERDGiwawHRINRL----FNWLPLAALIEKKIICMHGGIGRSINhV 835
Cdd:cd07420    107 LVYPNAVHLNRGNHEDHIMNLRYGFTKE-VMQKYKDHG----KKILRLledvFSWLPLATIIDNKVLVVHGGISDSTD-L 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  836 EQIENIQRpitmeaGSIV--------LMDLLWSDPTENdsvEGLRPNA-RGPGlVTFGPDRVMEFCNNNDLQLIVRAHEC 906
Cdd:cd07420    181 DLLDKIDR------HKYVstktewqqVVDILWSDPKAT---KGCKPNTfRGGG-CYFGPDVTSQFLQKHGLSLLIRSHEC 250

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1109279082  907 VMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLV 946
Cdd:cd07420    251 KPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLT 290
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 664-941 2.29e-41

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: 156.50  E-value: 2.29e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  664 PPVRRQFFLDCNEIADLCDNAERIFSSEPSVLQL----KAPIKIFGDLHGQFGDLMRLFDEYGSPStagdiAYIDYLFLG 739
Cdd:cd07418     27 PPSELPSVLPVNVFDSLVLTAHKILHREPNCVRIdvedVCEVVVVGDVHGQLHDVLFLLEDAGFPD-----QNRFYVFNG 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  740 DYVDRGQHSLETITLLLALKVEYPHNVHLIRGNHEAADINALFGFRIECIERMGERdGIWAWHRINRLFNWLPLAALIEK 819
Cdd:cd07418    102 DYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDK-GKHVYRKCLGCFEGLPLASIIAG 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  820 KIICMHGGIGRSI----------NHVEQIENIQRPITMEAGSI--------------------VLMDLLWSDPTENDsve 869
Cdd:cd07418    181 RVYTAHGGLFRSPslpkrkkqkgKNRRVLLLEPESESLKLGTLddlmkarrsvldppgegsnlIPGDVLWSDPSLTP--- 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  870 GLRPNA-RGPGLVtFGPDRVMEFCNNNDLQLIVRAHE------------CVMDGF---ERFAQGHLITLFSATNYCG--- 930
Cdd:cd07418    258 GLSPNKqRGIGLL-WGPDCTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYtvdHDVESGKLITLFSAPDYPQfqa 336

                          330
                   ....*....|....
gi 1109279082  931 ---TANNAGAILVL 941
Cdd:cd07418    337 teeRYNNKGAYIIL 350
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
140-435 2.15e-21

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 95.22  E-value: 2.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  140 GIRLAGATADVHCYDVLTNKWSRITPIgePPTPRAAHVATAVGTMVVLQGGIGPAGLSAE---DLHVLDLTQQrpRWHRV 216
Cdd:COG3055     30 GLSGGSASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTplnDVYVYDPATN--TWTKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  217 vvqGPGPGPRYGHVMALVGQRYLmAIGGNDGKRPLADVWALDTAAKpyEWRKLEPegeGPPPCMYATASARSDGLLLLCG 296
Cdd:COG3055    106 ---APMPTPRGGATALLLDGKIY-VVGGWDDGGNVAWVEVYDPATG--TWTQLAP---LPTPRDHLAAAVLPDGKILVIG 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  297 GRDANSvplasayglakhRDGRWEwaiAPGVSPSPRYQHAAVFVNARLHVSGGALGGgrmvedSSSVAVLDTAAGVWcdt 376
Cdd:COG3055    177 GRNGSG------------FSNTWT---TLAPLPTARAGHAAAVLGGKILVFGGESGF------SDEVEAYDPATNTW--- 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  377 KSVVTSPRPgrysadaaggdaaveltrRCRHAAAAVGDLIFIYGG-LRGGVLLDDLLVAE 435
Cdd:COG3055    233 TALGELPTP------------------RHGHAAVLTDGKVYVIGGeTKPGVRTPLVTSAE 274
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 700-817 2.56e-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: 75.71  E-value: 2.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  700 PIKIFGDLH--GQFGDLMRLFDEYGSPSTAgDIayidYLFLGDYVDRGQHSlETITLLLALKVEYpHNVHLIRGNHEAAd 777
Cdd:pfam00149    2 RILVIGDLHlpGQLDDLLELLKKLLEEGKP-DL----VLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD- 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1109279082  778 inalfgfRIECIERMGERDG-IWAWHRINRLFNWLPLAALI 817
Cdd:pfam00149   74 -------YGECLRLYPYLGLlARPWKRFLEVFNFLPLAGIL 107
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
220-424 2.25e-13

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 71.73  E-value: 2.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  220 GPGPGPRYGHVMALVGQRyLMAIGGNDGKRPLADVWALDTAAKpyEWRKLEPegeGPPPCMYATASARSDGLLLLCGGRD 299
Cdd:COG3055      7 PDLPTPRSEAAAALLDGK-VYVAGGLSGGSASNSFEVYDPATN--TWSELAP---LPGPPRHHAAAVAQDGKLYVFGGFT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  300 AN---SVPLASA--YGLAKhrdGRWEwAIAPgvSPSPRYQHAAVFVNARLHVSGGALGGGrmveDSSSVAVLDTAAGVWc 374
Cdd:COG3055     81 GAnpsSTPLNDVyvYDPAT---NTWT-KLAP--MPTPRGGATALLLDGKIYVVGGWDDGG----NVAWVEVYDPATGTW- 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109279082  375 DTKSVVTSPRP----------------GRYSADAAGGDAAVE--LTRRCRHAAAAVGDLIFIYGGLRG 424
Cdd:COG3055    150 TQLAPLPTPRDhlaaavlpdgkilvigGRNGSGFSNTWTTLAplPTARAGHAAAVLGGKILVFGGESG 217
PLN02153 PLN02153
epithiospecifier protein
 167-421 4.65e-10

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 62.31  E-value: 4.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  167 GEPPTPRAAHVATAVGTMVVLQGG-IGPAGLSAEDLHVLDLTQQRprWHrvVVQGPGPGPR---YGHVMALVGQRyLMAI 242
Cdd:PLN02153    17 GKGPGPRCSHGIAVVGDKLYSFGGeLKPNEHIDKDLYVFDFNTHT--WS--IAPANGDVPRiscLGVRMVAVGTK-LYIF 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  243 GGNDGKRPLADVWALDTAAKpyEWR---KLEPEGeGPPPCMYATASARSDGLLLLCGGRDANSVPLAS------AYGLAk 313
Cdd:PLN02153    92 GGRDEKREFSDFYSYDTVKN--EWTfltKLDEEG-GPEARTFHSMASDENHVYVFGGVSKGGLMKTPErfrtieAYNIA- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  314 hrDGRWEWAIAPGVSPSPRYQHAAVFVNARLHVSGG----ALGGGRMVEDSSSVAVLDTAAGVWCDTKSVVTSPrpgrys 389
Cdd:PLN02153   168 --DGKWVQLPDPGENFEKRGGAGFAVVQGKIWVVYGfatsILPGGKSDYESNAVQFFDPASGKWTEVETTGAKP------ 239

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1109279082  390 adaaggdaavelTRRCRHAAAAVGDLIFIYGG 421
Cdd:PLN02153   240 ------------SARSVFAHAVVGKYIIIFGG 259
PLN02193 PLN02193
nitrile-specifier protein
 80-298 1.33e-09

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 61.51  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   80 IEKTEDGPGPRCGHTLTAVP----PVGEEGMPGY-IGPRLILFGGATALEGNSAASGTPSSAGSAGIRLA--GATADV-- 150
Cdd:PLN02193   156 VEQKGEGPGLRCSHGIAQVGnkiySFGGEFTPNQpIDKHLYVFDLETRTWSISPATGDVPHLSCLGVRMVsiGSTLYVfg 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  151 -----------HCYDVLTNKWSRITPIGEPPTPRAAHVATAVGTMVVLQGGI---------------------------- 191
Cdd:PLN02193   236 grdasrqyngfYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVsatarlktldsynivdkkwfhcstpgds 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  192 ----GPAGLSA----------------EDLHVLDLTQQrpRWHRVVVQGPGPGPRYGHVMALVGqRYLMAIGGNDGKRPL 251
Cdd:PLN02193   316 fsirGGAGLEVvqgkvwvvygfngcevDDVHYYDPVQD--KWTQVETFGVRPSERSVFASAAVG-KHIVIFGGEIAMDPL 392

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109279082  252 ADV---------WALDTaaKPYEWRKLEPEG--EGPPPCMYATASARS--DGL--LLLCGGR 298
Cdd:PLN02193   393 AHVgpgqltdgtFALDT--ETLQWERLDKFGeeEETPSSRGWTASTTGtiDGKkgLVMHGGK 452
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 705-781 1.60e-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: 55.79  E-value: 1.60e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109279082  705 GDLHGQFGDLMRLFDEYG-SPstagdiaYIDYLF-LGDYVDRGQHSLETITLLLAlkveypHNVHLIRGNHEAADINAL 781
Cdd:cd07424      7 GDIHGHFQRLQRALDAVGfDP-------ARDRLIsVGDLVDRGPESLEVLELLKQ------PWFHAVQGNHEQMAIDAL 72
PLN02193 PLN02193
nitrile-specifier protein
 156-421 2.60e-07

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 54.19  E-value: 2.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  156 LTNKWSRITPIGEPPTPRAAHVATAVGTMVVLQGG-IGPAGLSAEDLHVLDLTQQrpRWHRVVVQGPGPGPR-YGHVMAL 233
Cdd:PLN02193   149 LLGKWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGeFTPNQPIDKHLYVFDLETR--TWSISPATGDVPHLScLGVRMVS 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  234 VGQRyLMAIGGNDGKRPLADVWALDTAAKpyEWRKLEPEGEGPPPCMYATASARSDGLLLLCGGRDANSVPLASAYGLAk 313
Cdd:PLN02193   227 IGST-LYVFGGRDASRQYNGFYSFDTTTN--EWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLKTLDSYNIV- 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  314 hrDGRWEWAIAPGVSPSPRYQHAAVFVNARLHVSGGAlgGGRMVEDsssVAVLDTAAGVWCDTKSVVTSPrpgrysadaa 393
Cdd:PLN02193   303 --DKKWFHCSTPGDSFSIRGGAGLEVVQGKVWVVYGF--NGCEVDD---VHYYDPVQDKWTQVETFGVRP---------- 365

                          250       260
                   ....*....|....*....|....*...
gi 1109279082  394 ggdaavelTRRCRHAAAAVGDLIFIYGG 421
Cdd:PLN02193   366 --------SERSVFASAAVGKHIVIFGG 385
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
703-828 7.21e-07

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 51.71  E-value: 7.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  703 IFGDLHGQFGDLMRLFDEYG-SPSTagdiayiDYL-FLGDYVDRGQHSLETITLLLALKveypHNVHLIRGNHeaaDINA 780
Cdd:PRK00166     5 AIGDIQGCYDELQRLLEKIDfDPAK-------DTLwLVGDLVNRGPDSLEVLRFVKSLG----DSAVTVLGNH---DLHL 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1109279082  781 LFGFRieCIERMGERD---GIWAWHRINRLFNWL---PLAA-LIEKKIICMHGGI 828
Cdd:PRK00166    71 LAVAA--GIKRNKKKDtldPILEAPDRDELLDWLrhqPLLHvDEELGLVMVHAGI 123
PLN02193 PLN02193
nitrile-specifier protein
 73-197 3.30e-06

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 50.72  E-value: 3.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082   73 YSVLQPIiektEDGPGPRCGHTLTAvppvGEEGMpgYIgprlilFGGATALE----------------GNSAASGTPSSA 136
Cdd:PLN02193   256 WKLLTPV----EEGPTPRSFHSMAA----DEENV--YV------FGGVSATArlktldsynivdkkwfHCSTPGDSFSIR 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  137 GSAGIRLAGATA------------DVHCYDVLTNKWSRITPIGEPPTPRAAHVATAVGTMVVLQGG---------IGPAG 195
Cdd:PLN02193   320 GGAGLEVVQGKVwvvygfngcevdDVHYYDPVQDKWTQVETFGVRPSERSVFASAAVGKHIVIFGGeiamdplahVGPGQ 399


                   ..
gi 1109279082  196 LS 197
Cdd:PLN02193   400 LT 401
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 703-774 1.03e-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: 46.11  E-value: 1.03e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109279082  703 IFGDLHGQFGDLMRLFDEYgspstAGDIAYIDYL-FLGDYVDRGQHSLETITLLLALKvEYPHNVHLIRGNHE 774
Cdd:cd00838      2 VISDIHGNLEALEAVLEAA-----LAKAEKPDLViCLGDLVDYGPDPEEVELKALRLL-LAGIPVYVVPGNHD 68
PHA02239 PHA02239
putative protein phosphatase
 701-799 1.37e-05

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 47.68  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  701 IKIFGDLHGQFGDLMRLFDEYGSPSTAGDIAyidyLFLGDYVDRGQHSLETITLLLALKVEyPHNVHLIRGNHEAADINA 780
Cdd:PHA02239     3 IYVVPDIHGEYQKLLTIMDKINNERKPEETI----VFLGDYVDRGKRSKDVVNYIFDLMSN-DDNVVTLLGNHDDEFYNI 77

                           90
                   ....*....|....*....
gi 1109279082  781 lfgfrIECIERMGERDGIW 799
Cdd:PHA02239    78 -----MENVDRLSIYDIEW 91
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 705-776 1.49e-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: 48.27  E-value: 1.49e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109279082  705 GDLHGQFGDLMRLFDEYGSPSTAGDIAYIDYLFLGDYVDRGQHSLETITLLLALKVEYPHNVH-LIRGNHEAA 776
Cdd:cd07421      8 GDIHGYISKLNNLWLNLQSALGPSDFASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHvFLCGNHDFA 80
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 703-828 2.57e-05

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: 46.77  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  703 IFGDLHGQFGDLMRLFDEYG-SPSTagdiayiDYL-FLGDYVDRGQHSLETITLLLALKVeyphNVHLIRGNHeaaDINA 780
Cdd:cd07422      3 AIGDIQGCYDELQRLLEKINfDPAK-------DRLwLVGDLVNRGPDSLETLRFVKSLGD----SAVVVLGNH---DLHL 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1109279082  781 L---FGfriecIERMGERD---GIWAWHRINRLFNWL---PLAALIEKKIICM-HGGI 828
Cdd:cd07422     69 LavaAG-----IKKLKKKDtldEILEAPDRDELLDWLrhqPLLHRDDELGIVMvHAGI 121
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 331-379 1.02e-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: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 40.78  E-value: 1.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1109279082  331 PRYQHAAVFVNARLHVSGGAlgGGRMVEDSSSVAVLDTAAGVWCDTKSV 379
Cdd:pfam07646    1 PRYPHASSVPGGKLYVVGGS--DGLGDLSSSDVLVYDPETNVWTEVPRL 47
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 704-853 1.77e-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: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  704 FGDLHGQFGDLMRLFDEYGSPSTAGDIAYIDYLF--LGDYVDRGQHSLETITLLLALKVEYPH---NVHLIRGNHEaadI 778
Cdd:cd07425      3 IGDLHGDLDRLRTILKLAGVIDSNDRWIGGDTVVvqTGDILDRGDDEIEILKLLEKLKRQARKaggKVILLLGNHE---L 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  779 NALFG-FRIECIERMGERdGIWAwHRINRLFNWLPLAA--LIEKK-------IICMHGGIG----RSINHVEQIENIQRP 844
Cdd:cd07425     80 MNLCGdFRYVHPRGLNEF-GGVA-KRRYALLSDGGYIGryLRTHPvvlvvndILFVHGGLGplwsRGYSLETKNGACERS 157


                   ....*....
gi 1109279082  845 ITMEAGSIV 853
Cdd:cd07425    158 ALDKALAKL 166
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
703-781 3.50e-04

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 42.60  E-value: 3.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  703 IFGDLHGQFGDLMRLFDEYGSpstagdiAYID-YLFLGDYVDRGQHSLETITLLLAlkveypHNVHLIRGNHEAADINAL 781
Cdd:COG0622      4 VISDTHGNLPALEAVLEDLER-------EGVDlIVHLGDLVGYGPDPPEVLDLLRE------LPIVAVRGNHDGAVLRGL 70
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 225-271 1.10e-03

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: 37.59  E-value: 1.10e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1109279082  225 PRYGHVMALVGQRyLMAIGGNDGKRPLADVWALDTAAKpyEWRKLEP 271
Cdd:pfam01344    1 RRSGAGVVVVGGK-IYVIGGFDGNQSLNSVEVYDPETN--TWSKLPS 44
pphA PRK11439
protein-serine/threonine phosphatase;
701-781 2.61e-03

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 40.52  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  701 IKIFGDLHGQFGDLMRLFDEYG-SPstagdiaYIDYLF-LGDYVDRGQHSLETITLLlalkveYPHNVHLIRGNHEAADI 778
Cdd:PRK11439    19 IWLVGDIHGCFEQLMRKLRHCRfDP-------WRDLLIsVGDLIDRGPQSLRCLQLL------EEHWVRAVRGNHEQMAL 85


                   ...
gi 1109279082  779 NAL 781
Cdd:PRK11439    86 DAL 88
Kelch_4 pfam13418
Galactose oxidase, central domain;
89-165 3.17e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.44  E-value: 3.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109279082   89 PRCGHTLTAVPPvgeegmpGYIgprlILFGGATAlegnsaaSGTPSSagsagirlagataDVHCYDVLTNKWSRITP 165
Cdd:pfam13418    1 PRAYHTSTSIPD-------DTI----YLFGGEGE-------DGTLLS-------------DLWVFDLSTNEWTRLGS 46
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 701-828 4.06e-03

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 40.07  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109279082  701 IKIFGDLHGQFGDLMRLFDEYGSPSTAGDIAYID---YLFLGDYVDRGQHSLETITLLLALkveYPHN-VHLIRGNHeaa 776
Cdd:PRK13625     3 YDIIGDIHGCYQEFQALTEKLGYNWSSGLPVHPDqrkLAFVGDLTDRGPHSLRMIEIVWEL---VEKKaAYYVPGNH--- 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109279082  777 dINALFGF--------------RIECIERMGERDGIWAWHRINRLFNWLPL-AALIEKKIICMHGGI 828
Cdd:PRK13625    77 -CNKLYRFflgrnvtiahgletTVAEYEALPSHKQNMIKEKFITLYEQAPLyHILDEGRLVVAHAGI 142
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 703-774 7.60e-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: 7.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109279082  703 IFGDLHGQFGDLMRLFDEYG-SPSTAGDIAYID---YLFLGDYVDRGQHSLETITLLLAL-KVEYPHNVHlirGNHE 774
Cdd:cd07423      2 IIGDVHGCYDELVELLEKLGyQKKEEGLYVHPEgrkLVFLGDLVDRGPDSIDVLRLVMNMvKAGKALYVP---GNHC 75
 
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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