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Conserved domains on  [gi|1186157240|ref|WP_085359805|]
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MULTISPECIES: metallophosphoesterase family protein [Bradyrhizobium]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10065661)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to Saccharomyces cerevisiae zinc-dependent endopolyphosphatase that catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0042578|GO:0016311
PubMed:  25837850|8003970

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 22-227 3.39e-27

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: 104.38  E-value: 3.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  22 YAIGDVHGRADLLQSLLTVIDAdlarsaPERAIQVFLGDYVDRGPDSRAVIDLLIE--RSKSHETVCLKGNHEVFLlevl 99
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGF------PPEDKYLFLGDYVDRGPDSVEVIDLLLAlkILYPDNVFLLRGNHEFML---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 kdparleewrrygglltlvsygINPTMNPTPEQQIELIEGLRQALPREHLSFLQQLrPSFAC--GDFFFVHAGVKPGVAL 177
Cdd:cd00144    71 ----------------------LNFLYGFYDERTLRCLRKGGEELWREFNEVFNYL-PLAALvdGKILCVHGGLSPDLTL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 178 E-------------RQKEEDLLWIREEFLES----------------------ERRFGKYIVHGHTPVS---VPDIRSNR 219
Cdd:cd00144   128 LdqirnirpienpdDQLVEDLLWSDPDESVGdfesssrgggylfgedavdeflKKNGLKLIVRGHTPVEggyEFLHGGKL 207


                  ....*...
gi 1186157240 220 INIDTGAY 227
Cdd:cd00144   208 ITIFSAPN 215
 
Name Accession Description Interval E-value
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 22-227 3.39e-27

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: 104.38  E-value: 3.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  22 YAIGDVHGRADLLQSLLTVIDAdlarsaPERAIQVFLGDYVDRGPDSRAVIDLLIE--RSKSHETVCLKGNHEVFLlevl 99
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGF------PPEDKYLFLGDYVDRGPDSVEVIDLLLAlkILYPDNVFLLRGNHEFML---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 kdparleewrrygglltlvsygINPTMNPTPEQQIELIEGLRQALPREHLSFLQQLrPSFAC--GDFFFVHAGVKPGVAL 177
Cdd:cd00144    71 ----------------------LNFLYGFYDERTLRCLRKGGEELWREFNEVFNYL-PLAALvdGKILCVHGGLSPDLTL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 178 E-------------RQKEEDLLWIREEFLES----------------------ERRFGKYIVHGHTPVS---VPDIRSNR 219
Cdd:cd00144   128 LdqirnirpienpdDQLVEDLLWSDPDESVGdfesssrgggylfgedavdeflKKNGLKLIVRGHTPVEggyEFLHGGKL 207


                  ....*...
gi 1186157240 220 INIDTGAY 227
Cdd:cd00144   208 ITIFSAPN 215
PHA02239 PHA02239
putative protein phosphatase
 21-218 5.38e-16

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 74.65  E-value: 5.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  21 IYAIGDVHGRadlLQSLLTVIDADLARSAPERAIqVFLGDYVDRGPDSRAVIDLLIE-RSKSHETVCLKGNHEVFLLEVL 99
Cdd:PHA02239    3 IYVVPDIHGE---YQKLLTIMDKINNERKPEETI-VFLGDYVDRGKRSKDVVNYIFDlMSNDDNVVTLLGNHDDEFYNIM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 KDPARLE----EWRRYGGLLTLVSYGINP---TMNPTPE---QQIELIEGLRQALP-----REHLSFLQQLRPSFACGDF 164
Cdd:PHA02239   79 ENVDRLSiydiEWLSRYCIETLNSYGVSTvtlKYSSVEEnlrNNYDFIKSELKKLKesddyRKFKILMVNCRKYYKEDKY 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1186157240 165 FFVHAGVKPGVALERQKEEDLLWIREeflESERRFGKYIVHGHTPVSVPDIRSN 218
Cdd:PHA02239  159 IFSHSGGVSWKPVEEQTIDQLIWSRD---FQPRKDGFTYVCGHTPTDSGEVEIN 209
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
20-208 2.53e-11

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 60.70  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  20 RIYAIGDVHGRADLLQSLLtvidADLARSAPERAIqvFLGDYVDRGPDSRAVIDLLiersKSHETVCLKGNHevfllevl 99
Cdd:COG0622     1 KIAVISDTHGNLPALEAVL----EDLEREGVDLIV--HLGDLVGYGPDPPEVLDLL----RELPIVAVRGNH-------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 kDPARLEEWRRYgglltlvsyginptmnptPEQQIELIEGLRqalprehlsflqqlrpsfacgdFFFVHAGVKPGVALER 179
Cdd:COG0622    63 -DGAVLRGLRSL------------------PETLRLELEGVR----------------------ILLVHGSPNEYLLPDT 101

                         170       180
                  ....*....|....*....|....*....
gi 1186157240 180 QKEEdllwIREEFLESErrfGKYIVHGHT 208
Cdd:COG0622   102 PAER----LRALAAEGD---ADVVVCGHT 123
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 20-110 6.92e-11

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: 57.99  E-value: 6.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  20 RIYAIGDVHGRaDLLQSLLTVIDAdlARSAPERAIQVFLGDYVDRGPDSRAVIDLLIERSKSHETVCLKGNHEVFLLEVL 99
Cdd:pfam00149   2 RILVIGDLHLP-GQLDDLLELLKK--LLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGECL 78

                          90
                  ....*....|.
gi 1186157240 100 KDPARLEEWRR 110
Cdd:pfam00149  79 RLYPYLGLLAR 89
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 21-93 4.70e-07

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: 49.52  E-value: 4.70e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186157240   21 IYAIGDVHGRADLLQSLLtvidaDLARSAPERAIqVFLGDYVDRGPDSRAVIDLLIERSKSHET--VCLKGNHEV 93
Cdd:smart00156  30 VTVCGDIHGQFDDLLRLF-----DKNGQPPETNY-VFLGDYVDRGPFSIEVILLLFALKILYPNriVLLRGNHES 98
 
Name Accession Description Interval E-value
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 22-227 3.39e-27

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: 104.38  E-value: 3.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  22 YAIGDVHGRADLLQSLLTVIDAdlarsaPERAIQVFLGDYVDRGPDSRAVIDLLIE--RSKSHETVCLKGNHEVFLlevl 99
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGF------PPEDKYLFLGDYVDRGPDSVEVIDLLLAlkILYPDNVFLLRGNHEFML---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 kdparleewrrygglltlvsygINPTMNPTPEQQIELIEGLRQALPREHLSFLQQLrPSFAC--GDFFFVHAGVKPGVAL 177
Cdd:cd00144    71 ----------------------LNFLYGFYDERTLRCLRKGGEELWREFNEVFNYL-PLAALvdGKILCVHGGLSPDLTL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 178 E-------------RQKEEDLLWIREEFLES----------------------ERRFGKYIVHGHTPVS---VPDIRSNR 219
Cdd:cd00144   128 LdqirnirpienpdDQLVEDLLWSDPDESVGdfesssrgggylfgedavdeflKKNGLKLIVRGHTPVEggyEFLHGGKL 207


                  ....*...
gi 1186157240 220 INIDTGAY 227
Cdd:cd00144   208 ITIFSAPN 215
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 20-238 3.41e-22

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: 90.45  E-value: 3.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  20 RIYAIGDVHGRADLLQSLLTVIDADLARsapERAIQVflGDYVDRGPDSRAVIDLLiersKSHETVCLKGNHEVFLLEVL 99
Cdd:cd07424     2 RDFVVGDIHGHFQRLQRALDAVGFDPAR---DRLISV--GDLVDRGPESLEVLELL----KQPWFHAVQGNHEQMAIDAL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 KDpARLEEWRRYGG--LLTLvsyginptmnpTPEQQIELIEGLRqalpreHLSFLQQLRPsfACGDFFFVHAGVKPGV-- 175
Cdd:cd07424    73 RG-GDDVMWRANGGgwFFDL-----------PDEEAKVLLEKLH------HLPIAIEVES--RNGKVGIVHADYPFDEys 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1186157240 176 ALERQKEED---LLWIREEFLESER---RFGKYIVHGHTPVSVPDIRSNRINIDTGAYATGNLTLLTIQ 238
Cdd:cd07424   133 FGFVEKPEDeeeALWSRDRLQKSQTqpvAGADAFIFGHTPVPEPLDLGNVYYIDTGGVFDGNLTLVKLQ 201
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 24-235 2.88e-20

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: 86.03  E-value: 2.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  24 IGDVHGRADLLQSLLT----VIDADLARSAPERAIQVFLGDYVDRGPDSRAVIDLLIERSKSHETVCLKGNHEVFLLEVL 99
Cdd:cd07423     3 IGDVHGCYDELVELLEklgyQKKEEGLYVHPEGRKLVFLGDLVDRGPDSIDVLRLVMNMVKAGKALYVPGNHCNKLYRYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 K-DPARLEEwrrygGLLTLVsyginptmnptpEQQIELIEGLRQALPREHLSFLQQLrPSFAC---GDFFFVHAGVKP-- 173
Cdd:cd07423    83 KgRNVQLAH-----GLETTV------------EELEALSKEERPEFRERFAEFLESL-PSHLVldgGRLVVAHAGIKEem 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1186157240 174 -GVALER------------QKEEDLLWIREEFLESERrfGK-YIVHGHTPVSVPDIRSNRINIDTGAYATGNLTLL 235
Cdd:cd07423   145 iGRGSKRvrdfclygdttgETDEDGLPVRRDWAKDYR--GKaLVVYGHTPVPEPRWLNNTINIDTGCVFGGKLTAL 218
PHA02239 PHA02239
putative protein phosphatase
 21-218 5.38e-16

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 74.65  E-value: 5.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  21 IYAIGDVHGRadlLQSLLTVIDADLARSAPERAIqVFLGDYVDRGPDSRAVIDLLIE-RSKSHETVCLKGNHEVFLLEVL 99
Cdd:PHA02239    3 IYVVPDIHGE---YQKLLTIMDKINNERKPEETI-VFLGDYVDRGKRSKDVVNYIFDlMSNDDNVVTLLGNHDDEFYNIM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 KDPARLE----EWRRYGGLLTLVSYGINP---TMNPTPE---QQIELIEGLRQALP-----REHLSFLQQLRPSFACGDF 164
Cdd:PHA02239   79 ENVDRLSiydiEWLSRYCIETLNSYGVSTvtlKYSSVEEnlrNNYDFIKSELKKLKesddyRKFKILMVNCRKYYKEDKY 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1186157240 165 FFVHAGVKPGVALERQKEEDLLWIREeflESERRFGKYIVHGHTPVSVPDIRSN 218
Cdd:PHA02239  159 IFSHSGGVSWKPVEEQTIDQLIWSRD---FQPRKDGFTYVCGHTPTDSGEVEIN 209
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 24-92 4.12e-13

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: 67.53  E-value: 4.12e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1186157240  24 IGDVHGRADLLQSLLTVIDADLARSAPERAIQVFLGDYVDRGPDSRAVIDLLI---ERSKSHETVCLKGNHE 92
Cdd:cd07421     7 VGDIHGYISKLNNLWLNLQSALGPSDFASALVIFLGDYCDRGPETRKVIDFLIslpEKHPKQRHVFLCGNHD 78
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
21-173 2.36e-11

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 62.11  E-value: 2.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  21 IYAIGDVHGRADLLQSLLTVIDADlarsaPERAIQVFLGDYVDRGPDSRAVIDLLIERSKSHETVcLkGNHEVFLLevlk 100
Cdd:PRK00166    3 TYAIGDIQGCYDELQRLLEKIDFD-----PAKDTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTV-L-GNHDLHLL---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 101 dparleewrrygglltLVSYGI-----NPTMNPtpeqqI-------ELIEGLRqalpreHLSFLQQLRPsfacGDFFFVH 168
Cdd:PRK00166   72 ----------------AVAAGIkrnkkKDTLDP-----IleapdrdELLDWLR------HQPLLHVDEE----LGLVMVH 120


                  ....*
gi 1186157240 169 AGVKP 173
Cdd:PRK00166  121 AGIPP 125
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
20-208 2.53e-11

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 60.70  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  20 RIYAIGDVHGRADLLQSLLtvidADLARSAPERAIqvFLGDYVDRGPDSRAVIDLLiersKSHETVCLKGNHevfllevl 99
Cdd:COG0622     1 KIAVISDTHGNLPALEAVL----EDLEREGVDLIV--HLGDLVGYGPDPPEVLDLL----RELPIVAVRGNH-------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 kDPARLEEWRRYgglltlvsyginptmnptPEQQIELIEGLRqalprehlsflqqlrpsfacgdFFFVHAGVKPGVALER 179
Cdd:COG0622    63 -DGAVLRGLRSL------------------PETLRLELEGVR----------------------ILLVHGSPNEYLLPDT 101

                         170       180
                  ....*....|....*....|....*....
gi 1186157240 180 QKEEdllwIREEFLESErrfGKYIVHGHT 208
Cdd:COG0622   102 PAER----LRALAAEGD---ADVVVCGHT 123
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 20-110 6.92e-11

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: 57.99  E-value: 6.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  20 RIYAIGDVHGRaDLLQSLLTVIDAdlARSAPERAIQVFLGDYVDRGPDSRAVIDLLIERSKSHETVCLKGNHEVFLLEVL 99
Cdd:pfam00149   2 RILVIGDLHLP-GQLDDLLELLKK--LLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYGECL 78

                          90
                  ....*....|.
gi 1186157240 100 KDPARLEEWRR 110
Cdd:pfam00149  79 RLYPYLGLLAR 89
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 21-182 1.05e-10

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: 59.86  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  21 IYAIGDVHGRADLLQSLLTVIDADlarsaPERAIQVFLGDYVDRGPDSRAVIDLLIERSKSHETVClkGNHEVFLLevlk 100
Cdd:cd07422     1 TYAIGDIQGCYDELQRLLEKINFD-----PAKDRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVL--GNHDLHLL---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 101 dparleewrrygglltLVSYGI---NPTMNPTP----EQQIELIEGLR-QALPREHlsflqqlrpsfACGDFFFVHAGVK 172
Cdd:cd07422    70 ----------------AVAAGIkklKKKDTLDEileaPDRDELLDWLRhQPLLHRD-----------DELGIVMVHAGIP 122

                         170
                  ....*....|....
gi 1186157240 173 PG----VALERQKE 182
Cdd:cd07422   123 PQwdieKALALARE 136
pphA PRK11439
protein-serine/threonine phosphatase;
21-238 1.41e-10

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 59.01  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  21 IYAIGDVHGRADLLQSLLTVIDADlarsaPERAIQVFLGDYVDRGPDSRAVIDLLIERSksheTVCLKGNHEVFLLEVLK 100
Cdd:PRK11439   19 IWLVGDIHGCFEQLMRKLRHCRFD-----PWRDLLISVGDLIDRGPQSLRCLQLLEEHW----VRAVRGNHEQMALDALA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 101 DpARLEEWRRYGGlltlvsygiNPTMNPTPEQQIELIEGLRQAlprEHLSFLQQLRpsfaCGDFFFV--HAGVkPGVALE 178
Cdd:PRK11439   90 S-QQMSLWLMNGG---------DWFIALTDNQQKQAKTLLEKC---QRLPFILEVH----CRTGKHViaHADY-PADVYE 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1186157240 179 RQKEEDL---LWIREEFleSERRFGKYIV---H---GHTPVSVPDIRSNRINIDTGAYATGNLTLLTIQ 238
Cdd:PRK11439  152 WQKDVDLhqvLWSRSRL--GERQKGQGITgadHfwfGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ 218
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 24-235 1.06e-09

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 57.02  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  24 IGDVHGRADLLQSLLT----VIDADLARSaPERAIQVFLGDYVDRGPDSRAVIDLLIERSKSHETVCLKGNHEVFLlevl 99
Cdd:PRK13625    6 IGDIHGCYQEFQALTEklgyNWSSGLPVH-PDQRKLAFVGDLTDRGPHSLRMIEIVWELVEKKAAYYVPGNHCNKL---- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 100 kdparleeWRRYGGLLTLVSYGINPTMNptpeqQIELIEGLRQALPREHLSFLQQLRPSFAC---GDFFFVHAG------ 170
Cdd:PRK13625   81 --------YRFFLGRNVTIAHGLETTVA-----EYEALPSHKQNMIKEKFITLYEQAPLYHIldeGRLVVAHAGirqdyi 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186157240 171 ------VKPGV---ALERQKEEDLLWIREEFLESERrfGK-YIVHGHTPVSVPDIRSNRINIDTGAYATGNLTLL 235
Cdd:PRK13625  148 grqdkkVQTFVlygDITGEKHPDGSPVRRDWAKEYK--GTaWIVYGHTPVKEPRFVNHTVNIDTGCVFGGRLTAL 220
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 22-225 1.98e-09

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: 55.77  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  22 YAIGDVHGRADLLQSLL---TVIDADLARSApERAIQVFLGDYVDRGPDSRAVIDLLIE-----RSKSHETVCLKGNHEV 93
Cdd:cd07425     1 VAIGDLHGDLDRLRTILklaGVIDSNDRWIG-GDTVVVQTGDILDRGDDEIEILKLLEKlkrqaRKAGGKVILLLGNHEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  94 FLLEvlkdparleewrrygglltlvsyGINPTMNPTPEQQIELIEGLRQAL--PREHL-SFLQQLRPSFACGDFFFVHAG 170
Cdd:cd07425    80 MNLC-----------------------GDFRYVHPRGLNEFGGVAKRRYALlsDGGYIgRYLRTHPVVLVVNDILFVHGG 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1186157240 171 VKP----GVALERQKEEDLLWIREEFLEserRFG-KYIVHGHTPVsvpdiRSNRIN---------IDTG 225
Cdd:cd07425   137 LGPlwsrGYSLETKNGACERSALDKALA---KLGvKRMVVGHTPQ-----EGGVVNtlcggklirIDVG 197
PRK09968 PRK09968
protein-serine/threonine phosphatase;
21-238 3.00e-09

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 55.28  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  21 IYAIGDVHGRADLLQSLLTVIDAdlarsAPERAIQVFLGDYVDRGPDSRAVIDLLiersKSHETVCLKGNHEVFLLEVLK 100
Cdd:PRK09968   17 IWVVGDIHGEYQLLQSRLHQLSF-----CPETDLLISVGDNIDRGPESLNVLRLL----NQPWFISVKGNHEAMALDAFE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240 101 DParleewrryGGLLTLVSYGiNPTMNPTPEQQIELIEGLrqaLPREHLSFLQQLRPSFAcgDFFFVHAGVkPGVALERQ 180
Cdd:PRK09968   88 TG---------DGNMWLASGG-DWFFDLNDSEQQEATDLL---LKFHHLPHIIEITNDNI--KYVIAHADY-PGDEYDFG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1186157240 181 KE---EDLLWIREEFLES------ERRFGKYIVHGHTPVSVPDIRSNRINIDTGAYATGNLTLLTIQ 238
Cdd:PRK09968  152 KEiaeSELLWPVDRVQKSlngelqQINGADYFIFGHMMFDNIQTFANQIYIDTGSPKSGRLSFYKIK 218
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 23-95 5.33e-08

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: 50.34  E-value: 5.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1186157240  23 AIGDVHGRADLLQSLLtviDADLARSAPERAIqVFLGDYVDRGPDSRAVIDLLIERSKSHETV-CLKGNHEVFL 95
Cdd:cd00838     2 VISDIHGNLEALEAVL---EAALAKAEKPDLV-ICLGDLVDYGPDPEEVELKALRLLLAGIPVyVVPGNHDILV 71
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 24-92 3.33e-07

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. 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: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 49.47  E-value: 3.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1186157240  24 IGDVHGRADLLQSLLTVIDADLARSA---PERAIqVFLGDYVDRGPDSRAVIDLLIERSKSHETVCLKGNHE 92
Cdd:cd07413     4 IGDVHGCAHTLDRLLDLLGYRLQGGVwrhPRRQA-LFVGDLIDRGPRIREVLHRVHAMVDAGEALCVMGNHE 74
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 21-93 4.70e-07

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: 49.52  E-value: 4.70e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186157240   21 IYAIGDVHGRADLLQSLLtvidaDLARSAPERAIqVFLGDYVDRGPDSRAVIDLLIERSKSHET--VCLKGNHEV 93
Cdd:smart00156  30 VTVCGDIHGQFDDLLRLF-----DKNGQPPETNY-VFLGDYVDRGPFSIEVILLLFALKILYPNriVLLRGNHES 98
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
20-135 4.71e-05

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 43.08  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  20 RIYAIGDVHGRADLLQSLLTVI---DADLArsaperaiqVFLGDYVDRGPDSRA--VIDLLIERSKshETVCLKGNHEVF 94
Cdd:COG2129     1 KILAVSDLHGNFDLLEKLLELAraeDADLV---------ILAGDLTDFGTAEEAreVLEELAALGV--PVLAVPGNHDDP 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1186157240  95 -LLEVLKDPARL---EEWRRYGGLLTLVSYGINPTMNPTPEQQIE 135
Cdd:COG2129    70 eVLDALEESGVHnlhGRVVEIGGLRIAGLGGSRPTPFGTPYEYTE 114
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 25-92 2.18e-04

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: 41.56  E-value: 2.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1186157240  25 GDVHGR-ADLLQsLLTvidadlARSAPERAIQVFLGDYVDRGPDSRAVIDLLIE-RSKSHET-VCLKGNHE 92
Cdd:cd07414    56 GDIHGQyYDLLR-LFE------YGGFPPESNYLFLGDYVDRGKQSLETICLLLAyKIKYPENfFLLRGNHE 119
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 10-92 1.33e-03

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: 39.11  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  10 NVKP-RLPdgvrIYAIGDVHGRADLLQSLLTVidadlARSAPERAIqVFLGDYVDRGPDSRAVIDLLIE---RSKSHETV 85
Cdd:cd07415    36 NVQRvRSP----VTVCGDIHGQFYDLLELFRI-----GGDVPDTNY-LFLGDYVDRGYYSVETFLLLLAlkvRYPDRITL 105


                  ....*..
gi 1186157240  86 cLKGNHE 92
Cdd:cd07415   106 -LRGNHE 111
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 25-92 1.36e-03

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: 39.21  E-value: 1.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1186157240  25 GDVHGR-ADLLQsLLTVidadlaRSAPERAIQVFLGDYVDRGPDSRAVIDLLIERSKSHET--VCLKGNHE 92
Cdd:cd07416    49 GDIHGQfYDLLK-LFEV------GGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKtlFLLRGNHE 112
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 14-92 6.73e-03

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: 37.03  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186157240  14 RLPdgVRIYaiGDVHGR-ADLLQ------SLLTVIDADLarsapERAIQVFLGDYVDRGPDSRAVIDLLIE-RSKSHETV 85
Cdd:cd07419    47 RAP--IKIF--GDIHGQfGDLMRlfdeygSPVTEEAGDI-----EYIDYLFLGDYVDRGSHSLETICLLLAlKVKYPNQI 117


                  ....*...
gi 1186157240  86 CL-KGNHE 92
Cdd:cd07419   118 HLiRGNHE 125
 
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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