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Conserved domains on  [gi|501135361|ref|WP_012183993|]
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metallophosphoesterase [Salinispora arenicola]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10005392)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0016787|GO:0046872|GO:0042578
PubMed:  25837850|8003970
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
4-239 7.71e-48

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


:

Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 157.48  E-value: 7.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   4 RIAAVGDVHLDEDvvgRFRPALEEVADY-ADVLLLAGDLTRHGTEAEARCVAREFGGLGVPVVTVLGNHEYqcdevPQVV 82
Cdd:COG2129    1 KILAVSDLHGNFD---LLEKLLELARAEdADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDD-----PEVL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  83 RVLEAAGITVLEGTGVVMDfpggRLGVAGVkgfGGGfagrCASDFGEPEMkafvrttaESADALEAALHSLDC-DLLVAL 161
Cdd:COG2129   73 DALEESGVHNLHGRVVEIG----GLRIAGL---GGS----RPTPFGTPYE--------YTEEEIEERLAKLREkDVDILL 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501135361 162 THYAPVPDTLagEPPEIYAFLGCYQLGQAIDSAPTALALHGHAHHGTERGTTpGGVRVRNVAHPVIKQaYSIFHLGDH 239
Cdd:COG2129  134 THAPPYGTTL--DRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRGVDKI-GGTRVVNPGSLAEGY-YALIDLEDR 207
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
4-239 7.71e-48

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 157.48  E-value: 7.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   4 RIAAVGDVHLDEDvvgRFRPALEEVADY-ADVLLLAGDLTRHGTEAEARCVAREFGGLGVPVVTVLGNHEYqcdevPQVV 82
Cdd:COG2129    1 KILAVSDLHGNFD---LLEKLLELARAEdADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDD-----PEVL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  83 RVLEAAGITVLEGTGVVMDfpggRLGVAGVkgfGGGfagrCASDFGEPEMkafvrttaESADALEAALHSLDC-DLLVAL 161
Cdd:COG2129   73 DALEESGVHNLHGRVVEIG----GLRIAGL---GGS----RPTPFGTPYE--------YTEEEIEERLAKLREkDVDILL 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501135361 162 THYAPVPDTLagEPPEIYAFLGCYQLGQAIDSAPTALALHGHAHHGTERGTTpGGVRVRNVAHPVIKQaYSIFHLGDH 239
Cdd:COG2129  134 THAPPYGTTL--DRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRGVDKI-GGTRVVNPGSLAEGY-YALIDLEDR 207
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 3-119 9.79e-11

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 59.99  E-value: 9.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   3 IRIAAVGDVHLDEDV-VGRFRPALEEVADYA-DVLLLAGDLTrHGTEAEARCVAREFGGL--GVPVVTVLGNHEYQCDEV 78
Cdd:cd07385    2 LRIVQLSDIHLGPFVgRTRLQKVVRKVNELNpDLIVITGDLV-DGDVSVLRLLASPLSKLkaPLGVYFVLGNHDYYSGDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501135361  79 PQVVRVLEAAGITVLEGTGVVMDFPGGRLGVAGVKGFGGGF 119
Cdd:cd07385   81 EVWIAALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGG 121
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 3-78 1.10e-06

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: 46.44  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361    3 IRIAAVGDVHLD------EDVVGRFRPALEevadyADVLLLAGDLTRHGTEAEARCVAREFGGLGVPVVTVLGNHEYQCD 76
Cdd:pfam00149   1 MRILVIGDLHLPgqlddlLELLKKLLEEGK-----PDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYG 75


                  ..
gi 501135361   77 EV 78
Cdd:pfam00149  76 EC 77
acc_ester TIGR03729
putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 ...
 4-206 3.07e-05

putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 (calcineurin-like phosphoesterase), a family largely defined by small motifs of metal-chelating residues. The subfamily in this model shows a good but imperfect co-occurrence in species with domain TIGR03715 that defines a novel class of signal peptide typical of the accessory secretory system.


Pssm-ID: 163441 [Multi-domain]  Cd Length: 239  Bit Score: 43.83  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361    4 RIAAVGDVHLDEDVVGRFRpALEEVADY-----ADVLLLAGDLTRHGTEAEArcVAREFGGL-GVPVVTVLGNHeyqcDE 77
Cdd:TIGR03729   1 KIAFSSDLHIDLNHFDTEE-MLETLAQYlkkqkIDHLHIAGDISNDFQRSLP--FIEKLQELkGIKVTFNAGNH----DM 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   78 VPQVVRVLEAAGITVLEGTGVVMDFPGGRlgvAGVKGFGGGFAGRCASDFGEPEMKAFVRT----------------TAE 141
Cdd:TIGR03729  74 LKDLTYEEIESNDSPLYLHNRFIDIPNTQ---WRIIGNNGWYDYSFSNDKTSKEILRWKKSfwfdrrikrpmsdperTAI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  142 SADALEAALHSLDCDLLVALTHYAPVPDTLA-GEPPEIY----AFLGCYQLGQAIDSAPTALALHGHAHH 206
Cdd:TIGR03729 151 VLKQLKKQLNQLDNKQVIFVTHFVPHRDFIYvPMDHRRFdmfnAFLGSQHFGQLLVKYEIKDVIFGHLHR 220
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
7-72 4.82e-03

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 37.45  E-value: 4.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501135361   7 AVGDVH--LDE-----DVVgRFRPAleevadyADVLLLAGDLTRHGTEAEArcVAREFGGLGVPVVTVLGNHE 72
Cdd:PRK00166   5 AIGDIQgcYDElqrllEKI-DFDPA-------KDTLWLVGDLVNRGPDSLE--VLRFVKSLGDSAVTVLGNHD 67
PGA_cap smart00854
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 4-151 9.22e-03

Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.


Pssm-ID: 214858 [Multi-domain]  Cd Length: 239  Bit Score: 36.42  E-value: 9.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361     4 RIAAVGDVHLDEDVV-GRFRPALEEVADY---ADVLL--LAGDLTRHGTEAEARC---------VAREFGGLGVPVVTVL 68
Cdd:smart00854   1 TLSFVGDVMLGRGVYkADFSPPFAGVKPLlraADLAIgnLETPITTSGSPASGKKypnfrappeNAAALKAAGFDVVSLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361    69 GNHEYQCDEVPQV--VRVLEAAGITVLeGTG---------VVMDFPGGRLGVAGV-KGFGGGFAGR-------CASDFGE 129
Cdd:smart00854  81 NNHSLDYGEEGLLdtLAALDAAGIAHV-GAGrnlaearkpAIVEVKGIKIALLAYtYGTNNGWAASrdrpgvaLLPDLDA 159

                          170       180
                   ....*....|....*....|..
gi 501135361   130 PEMKAFVRTTAESADALEAALH 151
Cdd:smart00854 160 EKILADIARARKEADVVIVSLH 181
 
Name Accession Description Interval E-value
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
4-239 7.71e-48

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 157.48  E-value: 7.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   4 RIAAVGDVHLDEDvvgRFRPALEEVADY-ADVLLLAGDLTRHGTEAEARCVAREFGGLGVPVVTVLGNHEYqcdevPQVV 82
Cdd:COG2129    1 KILAVSDLHGNFD---LLEKLLELARAEdADLVILAGDLTDFGTAEEAREVLEELAALGVPVLAVPGNHDD-----PEVL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  83 RVLEAAGITVLEGTGVVMDfpggRLGVAGVkgfGGGfagrCASDFGEPEMkafvrttaESADALEAALHSLDC-DLLVAL 161
Cdd:COG2129   73 DALEESGVHNLHGRVVEIG----GLRIAGL---GGS----RPTPFGTPYE--------YTEEEIEERLAKLREkDVDILL 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501135361 162 THYAPVPDTLagEPPEIYAFLGCYQLGQAIDSAPTALALHGHAHHGTERGTTpGGVRVRNVAHPVIKQaYSIFHLGDH 239
Cdd:COG2129  134 THAPPYGTTL--DRVEDGPHVGSKALRELIEEFQPKLVLHGHIHESRGVDKI-GGTRVVNPGSLAEGY-YALIDLEDR 207
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
3-219 1.03e-15

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 73.96  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   3 IRIAAVGDVHLDEDVVGRFRPALEEVADYA-----DVLLLAGDLTRHGTEAEARCVAREFGGLGVPVVTVLGNHEYqcdE 77
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEVLAAALADInaprpDFVVVTGDLTDDGEPEEYAAAREILARLGVPVYVVPGNHDI---R 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  78 VPQVVRVLEAAGITVLEGTGVVMDFPGGRL-GV-AGVKGFGGGfagrcasdfgepemkafvRTTAESADALEAALHSLDC 155
Cdd:COG1409   78 AAMAEAYREYFGDLPPGGLYYSFDYGGVRFiGLdSNVPGRSSG------------------ELGPEQLAWLEEELAAAPA 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501135361 156 DLLVALTHYAPVPdtlAGEPPEIYAFLGCYQLGQAIDSAPTALALHGHAHHgtERGTTPGGVRV 219
Cdd:COG1409  140 KPVIVFLHHPPYS---TGSGSDRIGLRNAEELLALLARYGVDLVLSGHVHR--YERTRRDGVPY 198
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
3-112 4.29e-12

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 64.43  E-value: 4.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   3 IRIAAVGDVHLDEDVVGRF-RPALEEVADY-ADVLLLAGDLTRHGTEAEARcVAREFGGL--GVPVVTVLGNHEYQcDEV 78
Cdd:COG1408   43 LRIVQLSDLHLGPFIGGERlERLVEKINALkPDLVVLTGDLVDGSVAELEA-LLELLKKLkaPLGVYAVLGNHDYY-AGL 120

                         90       100       110
                 ....*....|....*....|....*....|....
gi 501135361  79 PQVVRVLEAAGITVLEGTGVVMDFPGGRLGVAGV 112
Cdd:COG1408  121 EELRAALEEAGVRVLRNEAVTLERGGDRLNLAGV 154
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 3-119 9.79e-11

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 59.99  E-value: 9.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   3 IRIAAVGDVHLDEDV-VGRFRPALEEVADYA-DVLLLAGDLTrHGTEAEARCVAREFGGL--GVPVVTVLGNHEYQCDEV 78
Cdd:cd07385    2 LRIVQLSDIHLGPFVgRTRLQKVVRKVNELNpDLIVITGDLV-DGDVSVLRLLASPLSKLkaPLGVYFVLGNHDYYSGDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501135361  79 PQVVRVLEAAGITVLEGTGVVMDFPGGRLGVAGVKGFGGGF 119
Cdd:cd07385   81 EVWIAALEKAGITVLRNESVELSRDGATIGLAGSGVDDIGG 121
MPP_MS158 cd07404
Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized ...
 3-219 1.34e-07

Microscilla MS158 and related proteins, metallophosphatase domain; MS158 is an uncharacterized Microscilla protein with a metallophosphatase domain. Microscilla proteins MS152, and MS153 are also included in this family. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277349 [Multi-domain]  Cd Length: 201  Bit Score: 50.41  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   3 IRIAAvgDVHLdedvvgRFRPALEEVADY-----ADVLLLAGDLTRhGTEAEARCV-----AREFgglgVPVVTVLGNHE 72
Cdd:cd07404    1 LQIAS--DLHL------EVEQNLAKLKFFpkvpdADILILAGDIGR-LTDAEAWDNfldlqSFQF----EPVYYVPGNHE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  73 Y--QCDEVPQVVRVLEA---AGITVLEGTGVVMDfpGGR-LGV---AGVKGFGGGFAGRCASDFGepemkafvRTTaesa 143
Cdd:cd07404   68 FygGSLDITLDALRMAAqdlSNVHYLNNQEVVLD--DVRiLGCtlwSDFDPDGEDIVQRKLNDFR--------GAT---- 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501135361 144 daleaalhsldcdllVALTHYAPVPDTLAGEPPEIYAFLGCYQLGQA--IDSAPTALALHGHAHHGTErgTTPGGVRV 219
Cdd:cd07404  134 ---------------VVVTHHAPSPRSTSDNYADGLPKNAAFHVDLKdlILAPPIDLWIHGHTHFNTD--YSVGGTRV 194
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 6-72 3.14e-07

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: 48.42  E-value: 3.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501135361   6 AAVGDVHLDEDVVGRFRPALEEVADYADVLLLAGDLT-RHGTEAEARCVAREFGGLGVPVVTVLGNHE 72
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAKAEKPDLVICLGDLVdYGPDPEEVELKALRLLLAGIPVYVVPGNHD 68
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 3-78 1.10e-06

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: 46.44  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361    3 IRIAAVGDVHLD------EDVVGRFRPALEevadyADVLLLAGDLTRHGTEAEARCVAREFGGLGVPVVTVLGNHEYQCD 76
Cdd:pfam00149   1 MRILVIGDLHLPgqlddlLELLKKLLEEGK-----PDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYG 75


                  ..
gi 501135361   77 EV 78
Cdd:pfam00149  76 EC 77
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 5-210 1.53e-06

Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277338 [Multi-domain]  Cd Length: 190  Bit Score: 47.31  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   5 IAAVGDVHldedvvGRFRP--ALEEVADYADVLLLAGDLTRHGTEAEARCVAREFGGLGVPVVTVLGNheyqCDEvPQVV 82
Cdd:cd07392    1 ILAISDVH------GDVPKlkKIKLKAEEADAVIVAGDITHFGPGEEAIEALNLLLAIGAPVLAVPGN----CDT-PEVL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  83 RVLEAAGITVlegTGVVMDFpgGRLGVAGVKGfGGGFAGRCASDFGEPEMKAFVRttaesadaleaALHSLDCDLLVALT 162
Cdd:cd07392   70 GELNSAGLNI---HGKVVEV--GGYIFVGVGG-SNPTPFNTPFEYSEEEIYSKLG-----------LLNVKLPGRLILVT 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501135361 163 HyAPVPDTLAGE-PPEIYAflGCYQLGQAIDSAPTALALHGHAH--HGTER 210
Cdd:cd07392  133 H-APPYGTAVDRvSSGVHV--GSKAIRKFIEEFQPLLCICGHIHesRGIDK 180
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 5-107 4.16e-06

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 46.50  E-value: 4.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   5 IAAVGDVHLD---------EDVVGRFRPALEEVADY---ADVLLLAGDLTRHGTEAEARCVAREFGGLGVPVVTVLGNHe 72
Cdd:cd07402    1 IAQISDTHLFapgegallgVDTAARLAAAVAQVNALhprPDLVVVTGDLSDDGSPESYERLRELLAPLPAPVYWIPGNH- 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501135361  73 yqcDEVPQVVRVLEAAGITVLEGTGVVMDFPGGRL 107
Cdd:cd07402   80 ---DDRAAMREALPEPPYDDNGPVQYVVDFGGWRL 111
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
4-93 1.51e-05

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 44.52  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   4 RIAAVGDVHldedvvgRFRPALEEVADY-----ADVLLLAGDLTRHGTEAEArcVAREFGGLgvPVVTVLGNHEYQCD-- 76
Cdd:COG0622    1 KIAVISDTH-------GNLPALEAVLEDleregVDLIVHLGDLVGYGPDPPE--VLDLLREL--PIVAVRGNHDGAVLrg 69

                         90
                 ....*....|....*....
gi 501135361  77 --EVPQvVRVLEAAGITVL 93
Cdd:COG0622   70 lrSLPE-TLRLELEGVRIL 87
acc_ester TIGR03729
putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 ...
 4-206 3.07e-05

putative phosphoesterase; Members of this protein family belong to the larger family pfam00149 (calcineurin-like phosphoesterase), a family largely defined by small motifs of metal-chelating residues. The subfamily in this model shows a good but imperfect co-occurrence in species with domain TIGR03715 that defines a novel class of signal peptide typical of the accessory secretory system.


Pssm-ID: 163441 [Multi-domain]  Cd Length: 239  Bit Score: 43.83  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361    4 RIAAVGDVHLDEDVVGRFRpALEEVADY-----ADVLLLAGDLTRHGTEAEArcVAREFGGL-GVPVVTVLGNHeyqcDE 77
Cdd:TIGR03729   1 KIAFSSDLHIDLNHFDTEE-MLETLAQYlkkqkIDHLHIAGDISNDFQRSLP--FIEKLQELkGIKVTFNAGNH----DM 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   78 VPQVVRVLEAAGITVLEGTGVVMDFPGGRlgvAGVKGFGGGFAGRCASDFGEPEMKAFVRT----------------TAE 141
Cdd:TIGR03729  74 LKDLTYEEIESNDSPLYLHNRFIDIPNTQ---WRIIGNNGWYDYSFSNDKTSKEILRWKKSfwfdrrikrpmsdperTAI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  142 SADALEAALHSLDCDLLVALTHYAPVPDTLA-GEPPEIY----AFLGCYQLGQAIDSAPTALALHGHAHH 206
Cdd:TIGR03729 151 VLKQLKKQLNQLDNKQVIFVTHFVPHRDFIYvPMDHRRFdmfnAFLGSQHFGQLLVKYEIKDVIFGHLHR 220
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 4-73 1.28e-04

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 41.49  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   4 RIAAVGDVHLD---EDVVGR---FRPALEEVADYA-----DVLLLAGDL---TRHGTEAEARCVA--REFGGLGVPVVTV 67
Cdd:cd00840    1 RFLHTADWHLGyplYGLSRReedFFKAFEEIVDLAieekvDFVLIAGDLfdsNNPSPEALKLAIEglRRLCEAGIPVFVI 80


                 ....*.
gi 501135361  68 LGNHEY 73
Cdd:cd00840   81 AGNHDS 86
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
3-93 1.75e-04

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 41.82  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   3 IRIAAVGDVHLDEDVVGRFRP-----ALEEVADYA-----DVLLLAGDLTRHGT---EAEARCVA--REFGGLGVPVVTV 67
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRRedqlaALDRLVDLAieekvDAVLIAGDLFDSANpspEAVRLLAEalRRLSEAGIPVVLI 80

                         90       100
                 ....*....|....*....|....*.
gi 501135361  68 LGNHEYQcDEVPQVVRVLEAAGITVL 93
Cdd:COG0420   81 AGNHDSP-SRLSAGSPLLENLGVHVF 105
CapA COG2843
Poly-gamma-glutamate biosynthesis protein CapA/YwtB (capsule formation), metallophosphatase ...
 1-151 1.99e-04

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


Pssm-ID: 442091 [Multi-domain]  Cd Length: 310  Bit Score: 41.82  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   1 MVIRIAAVGDVHLDEDVVGR-----FRPALEEVADY---ADVLL--LAGDLTRHGTEAEARC--------VAREFGGLGV 62
Cdd:COG2843    4 DTITLAAVGDVMLGRGVDQAlprydFDYPFGDVKPLlraADLAIgnLETPLTDSGTPYPSKGyhfrappeYADALKAAGF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  63 PVVTVLGNHEYQCDE--VPQVVRVLEAAGITVLeGTG---------VVMDFPGGRLGVAGVKGFGGGFAGR-----CASD 126
Cdd:COG2843   84 DVVSLANNHSLDYGEegLLDTLDALDAAGIAHV-GAGrnlaearrpLILEVNGVRVAFLAYTYGTNEWAAGedkpgVANL 162

                        170       180
                 ....*....|....*....|....*
gi 501135361 127 FGEPEMKAFVRTTAESADALEAALH 151
Cdd:COG2843  163 DDLERIKEDIAAARAGADLVIVSLH 187
MPP_NostocDevT-like cd07397
Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative ...
 3-166 2.60e-04

Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative protein phosphatase from Nostoc PCC 7120 (Anabaena PCC 7120). DevT mutants form mature heterocysts, but they are unable to fix N(2) and must be supplied with a source of combined nitrogen in order to survive. Anabaena DevT shows homology to phosphatases of the PPP family and displays a Mn(2+)-dependent phosphatase activity. DevT is constitutively expressed in both vegetative cells and heterocysts, and is not regulated by NtcA. The heterocyst regulator HetR may exert a certain inhibition on the expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. The role that DevT plays in a late essential step of heterocyst differentiation is still unknown. 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: 277342 [Multi-domain]  Cd Length: 245  Bit Score: 41.12  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   3 IRIAAVGDVHLDEDVvgRFRPALEEVAdyADVLLLAGDLtrhGTEAEArcVAREFGGLGVPVVTVLGNH----------- 71
Cdd:cd07397    1 VRIAIVGDVHGQWDA--EDERALRLLQ--PDLVLFVGDF---GNENVQ--LVRRIASLDLPKAVILGNHdawytatrwgr 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361  72 -EYQCDEVPQVVRVLEAAGiTVLEGTGvVMDFPGGRLGVAGVKGF--GGGFAgrcasdFGEPEMKAF--VRTTAESADAL 146
Cdd:cd07397   72 cPYDRSKGDRVQQQLEILG-DEHVGYG-RLDFPSLKLSVVGGRPFskGGGRW------LSKRFLSAVygVISLEESAQRI 143

                        170       180
                 ....*....|....*....|.
gi 501135361 147 -EAALHSLDCDLLVALTHYAP 166
Cdd:cd07397  144 aDAAKAAPEDHPLIFLAHNGP 164
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 4-94 8.65e-04

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 38.79  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   4 RIAAVGDVHLDEDVVGRfrpALEEVADYADVLLLAGDLTRHGTEaearcvaREFGGLGVPVVTVLGNheyqCD-EVPQVV 82
Cdd:cd00841    1 KIGVISDTHGNLEAIEK---ALELFEDGVDAVIHAGDFVSPFVL-------NALLELKAPLIAVRGN----NDgEVDQLL 66

                         90
                 ....*....|..
gi 501135361  83 RVLEAAGITVLE 94
Cdd:cd00841   67 GRPILPEFLTLE 78
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 7-72 1.14e-03

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: 39.45  E-value: 1.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361   7 AVGDVH--LDEdvvgrFRPALEEVA--DYADVLLLAGDLTRHGTEAEArcVAREFGGLGVPVVTVLGNHE 72
Cdd:cd07422    3 AIGDIQgcYDE-----LQRLLEKINfdPAKDRLWLVGDLVNRGPDSLE--TLRFVKSLGDSAVVVLGNHD 65
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
7-72 4.82e-03

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 37.45  E-value: 4.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501135361   7 AVGDVH--LDE-----DVVgRFRPAleevadyADVLLLAGDLTRHGTEAEArcVAREFGGLGVPVVTVLGNHE 72
Cdd:PRK00166   5 AIGDIQgcYDElqrllEKI-DFDPA-------KDTLWLVGDLVNRGPDSLE--VLRFVKSLGDSAVTVLGNHD 67
PGA_cap smart00854
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ...
 4-151 9.22e-03

Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.


Pssm-ID: 214858 [Multi-domain]  Cd Length: 239  Bit Score: 36.42  E-value: 9.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361     4 RIAAVGDVHLDEDVV-GRFRPALEEVADY---ADVLL--LAGDLTRHGTEAEARC---------VAREFGGLGVPVVTVL 68
Cdd:smart00854   1 TLSFVGDVMLGRGVYkADFSPPFAGVKPLlraADLAIgnLETPITTSGSPASGKKypnfrappeNAAALKAAGFDVVSLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501135361    69 GNHEYQCDEVPQV--VRVLEAAGITVLeGTG---------VVMDFPGGRLGVAGV-KGFGGGFAGR-------CASDFGE 129
Cdd:smart00854  81 NNHSLDYGEEGLLdtLAALDAAGIAHV-GAGrnlaearkpAIVEVKGIKIALLAYtYGTNNGWAASrdrpgvaLLPDLDA 159

                          170       180
                   ....*....|....*....|..
gi 501135361   130 PEMKAFVRTTAESADALEAALH 151
Cdd:smart00854 160 EKILADIARARKEADVVIVSLH 181
 
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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