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Conserved domains on  [gi|12230412|sp|O35385|]
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RecName: Full=Serine/threonine-protein phosphatase with EF-hands 2; Short=PPEF-2

Protein Classification

MPP_RdgC and EFh domain-containing protein (domain architecture ID 13882284)

protein containing domains IQ, MPP_RdgC, and EFh

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
122-541 0e+00

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


:

Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 594.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 122 PLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPER 201
Cdd:cd07420   1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 202 AYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLA 281
Cdd:cd07420  81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 282 TLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVStmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhl 361
Cdd:cd07420 161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS----------------------------------------------- 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 362 gsgfkaykagrscsipcgspnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvlepTPEE 441
Cdd:cd07420 194 ----------------------------------------------------------------------------TKTE 197
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 442 WKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGS 521
Cdd:cd07420 198 WQQVVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGS 277
                       410       420
                ....*....|....*....|
gi 12230412 522 NRGAYVKLGPALTPHIVQYQ 541
Cdd:cd07420 278 NRGAYVKLGPQLTPHFVQYQ 297
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
661-726 5.04e-13

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 64.11  E-value: 5.04e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12230412 661 LETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDDGIcdlaRSIDFNKDGHIDINEFLEAFR 726
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI----REVDKDGDGKIDFEEFLELMA 63
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
581-725 1.09e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 48.84  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 581 FRKRDPDESGVITLSDWATavesvlhlglpwrMLRPQLVNSSADNVLEYRSWLDSlAKEQLSRENIQSSLLEKLYRN--R 658
Cdd:COG5126  26 FQLFDRDSDGLIDRNELGK-------------ILRSLGFNPSEAEINKLFEEIDA-GNETVDFPEFLTVMSVKLKRGdkE 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12230412 659 SNLETIFRIIDSDHSGFISLDEFRQTWKlfssHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAF 725
Cdd:COG5126  92 EELREAFKLFDKDHDGYISIGELRRVLK----SLGERLSDEEVEKLLKEYDEDGDGEIDYEEFKKLI 154
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
21-40 3.58e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470  Cd Length: 23  Bit Score: 34.99  E-value: 3.58e-03
                           10        20
                   ....*....|....*....|
gi 12230412     21 KAAALIQRWYRRYMARLEMR 40
Cdd:smart00015   4 RAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
122-541 0e+00

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 594.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 122 PLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPER 201
Cdd:cd07420   1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 202 AYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLA 281
Cdd:cd07420  81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 282 TLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVStmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhl 361
Cdd:cd07420 161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS----------------------------------------------- 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 362 gsgfkaykagrscsipcgspnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvlepTPEE 441
Cdd:cd07420 194 ----------------------------------------------------------------------------TKTE 197
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 442 WKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGS 521
Cdd:cd07420 198 WQQVVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGS 277
                       410       420
                ....*....|....*....|
gi 12230412 522 NRGAYVKLGPALTPHIVQYQ 541
Cdd:cd07420 278 NRGAYVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
141-544 1.09e-87

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


Pssm-ID: 197547  Cd Length: 271  Bit Score: 277.17  E-value: 1.09e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    141 LHARYVLNLLYETRKHLAQLPNINRVStcysEEVTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVL 220
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS----APVTVCGDIHGQFDDLLRLFDKNGQP-PETNYVFLGDYVDRGPFSIEVI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    221 MVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYkihGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDK-T 299
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDlT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    300 DLELLAKLDRHKIvstmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcg 379
Cdd:smart00156 153 TLDDIRKLKRPQE------------------------------------------------------------------- 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    380 spnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvleptPEEWKQVVDILWSDPAA-QEG 458
Cdd:smart00156 166 -----------------------------------------------------------PPDDGLLIDLLWSDPDQpVNG 186
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    459 CKANAvRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIV 538
Cdd:smart00156 187 FGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFE 265

                   ....*.
gi 12230412    539 QYQANK 544
Cdd:smart00156 266 QFKPGK 271
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
174-516 2.59e-33

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 130.03  E-value: 2.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  174 VTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFT 253
Cdd:PTZ00244  54 VRVCGDTHGQYYDLLRIFEKCGFP-PYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  254 KEVMHKYKIhgkKILRTLQDVFCWLPLATLVDEKVLVLHGGVS-DKTDLELLAKLDRhkivstmrcktrkesenreeqkr 332
Cdd:PTZ00244 133 DDVKRRYNI---KLFKAFTDVFNTMPVCCVISEKIICMHGGLSpDLTSLASVNEIER----------------------- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  333 kdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsiPCGSPNSkelsrrgqvrrsvdleleqcrqqagflgi 412
Cdd:PTZ00244 187 --------------------------------------------PCDVPDR----------------------------- 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  413 rekgeslplapdadcvadggGVLeptpeewkqvVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSH 492
Cdd:PTZ00244 194 --------------------GIL----------CDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAH 243
                        330       340
                 ....*....|....*....|....
gi 12230412  493 ECKPEGYEFCHNRKVLTIFSASNY 516
Cdd:PTZ00244 244 QVMERGYGFFASRQLVTVFSAPNY 267
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
661-726 5.04e-13

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 64.11  E-value: 5.04e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12230412 661 LETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDDGIcdlaRSIDFNKDGHIDINEFLEAFR 726
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI----REVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
658-726 8.14e-12

EF-hand domain pair;


Pssm-ID: 338778 [Multi-domain]  Cd Length: 68  Bit Score: 60.75  E-value: 8.14e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12230412   658 RSNLETIFRIIDSDHSGFISLDEFRQTWKLFSsHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAFR 726
Cdd:pfam13499   1 EEKLKEAFKLLDKDGDGYLDVEELKKLLRKLF-EEGEKLSDEEVEELFKEFDLDKDGRISFEEFLELYR 68
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
174-242 1.70e-09

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: 333878 [Multi-domain]  Cd Length: 79  Bit Score: 54.70  E-value: 1.70e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12230412   174 VTVCGDLH--GQLDDLIFIFykNGLPSPERAYVF--NGDFVDRGKDSVEVLmvLFAFMLVYPKEFHLNRGNHE 242
Cdd:pfam00149   3 ILVIGDLHgpGQLDDLLELL--KKLLEEEKPDLVlhAGDLVDRGPWETEVL--ELLERLIAYVPVYLVRGNHD 71
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
581-725 1.09e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 48.84  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 581 FRKRDPDESGVITLSDWATavesvlhlglpwrMLRPQLVNSSADNVLEYRSWLDSlAKEQLSRENIQSSLLEKLYRN--R 658
Cdd:COG5126  26 FQLFDRDSDGLIDRNELGK-------------ILRSLGFNPSEAEINKLFEEIDA-GNETVDFPEFLTVMSVKLKRGdkE 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12230412 659 SNLETIFRIIDSDHSGFISLDEFRQTWKlfssHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAF 725
Cdd:COG5126  92 EELREAFKLFDKDHDGYISIGELRRVLK----SLGERLSDEEVEKLLKEYDEDGDGEIDYEEFKKLI 154
PTZ00184 PTZ00184
calmodulin; Provisional
661-721 1.17e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.83  E-value: 1.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12230412  661 LETIFRIIDSDHSGFISLDEFRQTWklfsSHMSIDITDDGICDLARSIDFNKDGHIDINEF 721
Cdd:PTZ00184  86 IKEAFKVFDRDGNGFISAAELRHVM----TNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
447-517 1.87e-04

Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal transduction mechanisms];


Pssm-ID: 223712  Cd Length: 155  Bit Score: 42.34  E-value: 1.87e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12230412 447 DILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYY 517
Cdd:COG0639  84 DLLWSDPDGGDRRIWNPGPRGVPRDGGDVTAVFGIVHTPKLIERAHVLYDIDTGAVFGGGLLTAFSAPNYC 154
bacter_Pnkp TIGR04075
polynucleotide kinase-phosphatase; Members of this protein family are the bacterial ...
163-246 3.24e-04

polynucleotide kinase-phosphatase; Members of this protein family are the bacterial polynucleotide kinase-phosphatase (Pnkp) whose genes occur paired with genes for the 3' terminal RNA ribose 2'-O-methyltransferase Hen1. All members of the seed alignment belong to a cassette with the Hen1. The pair acts in bacterial RNA repair. This enzyme performs end-healing reactions on broken RNA, preparing from the RNA ligase to close the break. The working hypothesis is that the combination of Pnkp (RNA repair) and Hen1 (RNA modification) serves to first repair RNA damage from ribotoxins and then perform a modification that prevents the damage from recurring. [Transcription, RNA processing]


Pssm-ID: 274963 [Multi-domain]  Cd Length: 851  Bit Score: 43.83  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412   163 INRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPERAYVFNGDFVDRGKDSVEVL-----MVLFAFMLVYPkefhln 237
Cdd:TIGR04075 185 IGDVHGCRDELETLLEELGYQIERDEGGRGVDVTHPEGRKAVFVGDLVDRGPDSPGVLrlvmgMVAAGTALCVP------ 258

                  ....*....
gi 12230412   238 rGNHEDHLV 246
Cdd:TIGR04075 259 -GNHDVKLL 266
PTZ00183 PTZ00183
centrin; Provisional
585-722 7.21e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.83  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  585 DPDESGVITLSDWATAVESvlhLGLPWRmlRPQL------VNSSADNVLEYRSWLDSLAKEQLSRENiqsslleklyrnR 658
Cdd:PTZ00183  27 DTDGSGTIDPKELKVAMRS---LGFEPK--KEEIkqmiadVDKDGSGKIDFEEFLDIMTKKLGERDP------------R 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12230412  659 SNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMsidiTDDGICDLARSIDFNKDGHIDINEFL 722
Cdd:PTZ00183  90 EEILKAFRLFDDDKTGKISLKNLKRVAKELGETI----TDEELQEMIDEADRNGDGEISEEEFY 149
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
21-40 3.58e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470  Cd Length: 23  Bit Score: 34.99  E-value: 3.58e-03
                           10        20
                   ....*....|....*....|
gi 12230412     21 KAAALIQRWYRRYMARLEMR 40
Cdd:smart00015   4 RAAIIIQAAWRGYLARKRYK 23
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
664-683 4.25e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.05  E-value: 4.25e-03
                           10        20
                   ....*....|....*....|
gi 12230412    664 IFRIIDSDHSGFISLDEFRQ 683
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKD 24
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
122-541 0e+00

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 594.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 122 PLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPER 201
Cdd:cd07420   1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 202 AYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLA 281
Cdd:cd07420  81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 282 TLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVStmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhl 361
Cdd:cd07420 161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS----------------------------------------------- 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 362 gsgfkaykagrscsipcgspnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvlepTPEE 441
Cdd:cd07420 194 ----------------------------------------------------------------------------TKTE 197
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 442 WKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGS 521
Cdd:cd07420 198 WQQVVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGS 277
                       410       420
                ....*....|....*....|
gi 12230412 522 NRGAYVKLGPALTPHIVQYQ 541
Cdd:cd07420 278 NRGAYVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
141-544 1.09e-87

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


Pssm-ID: 197547  Cd Length: 271  Bit Score: 277.17  E-value: 1.09e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    141 LHARYVLNLLYETRKHLAQLPNINRVStcysEEVTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVL 220
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS----APVTVCGDIHGQFDDLLRLFDKNGQP-PETNYVFLGDYVDRGPFSIEVI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    221 MVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYkihGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDK-T 299
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDlT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    300 DLELLAKLDRHKIvstmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcg 379
Cdd:smart00156 153 TLDDIRKLKRPQE------------------------------------------------------------------- 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    380 spnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvleptPEEWKQVVDILWSDPAA-QEG 458
Cdd:smart00156 166 -----------------------------------------------------------PPDDGLLIDLLWSDPDQpVNG 186
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    459 CKANAvRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIV 538
Cdd:smart00156 187 FGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFE 265

                   ....*.
gi 12230412    539 QYQANK 544
Cdd:smart00156 266 QFKPGK 271
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
114-542 6.03e-86

PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277362  Cd Length: 316  Bit Score: 274.13  E-value: 6.03e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 114 YTGPRLSFPLLP-DHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFY 192
Cdd:cd07417   1 YSGPKLEDGKVTlEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 193 KNGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYkihGKKILRTLQ 272
Cdd:cd07417  81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKY---NEQMFNLFS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 273 DVFCWLPLATLVDEKVLVLHGGV--SDKTDLELLAKLDRHkivstmrcktrkesenreeqkrkdnqtssgqkptpwflpq 350
Cdd:cd07417 158 EVFNWLPLAHLINGKVLVVHGGLfsDDGVTLDDIRKIDRF---------------------------------------- 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 351 srslpsspfhlgsgfkaykagrscsipcgspnskelsrrgqvrrsvdleleqcrqqagflgiREKGESLPLapdadCvad 430
Cdd:cd07417 198 --------------------------------------------------------------RQPPDSGLM-----C--- 207
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 431 gggvleptpeewkqvvDILWSDPAAQEGcKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTI 510
Cdd:cd07417 208 ----------------ELLWSDPQPQPG-RGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITV 270
                       410       420       430
                ....*....|....*....|....*....|...
gi 12230412 511 FSASNYYEVGSNRGAYVKL-GPALTPHIVQYQA 542
Cdd:cd07417 271 FSAPNYCDQMGNKGAFIRFkGSDLKPKFTQFEA 303
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
175-529 3.46e-65

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: 216.08  E-value: 3.46e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 175 TVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTK 254
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFP-PEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 255 EVMHKYKI-HGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDktdlellakldrhkivstmrcktrkesenreeqkrk 333
Cdd:cd00144  80 ERTLRCLRkGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSP------------------------------------ 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 334 dnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcgspnskelsrrgqvrrsvDLELEQCRQQagflgir 413
Cdd:cd00144 124 ---------------------------------------------------------------DLTLLDQIRN------- 133
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 414 ekgeslplapdadcvadgggvLEPTPEEWKQVV-DILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSH 492
Cdd:cd00144 134 ---------------------IRPIENPDDQLVeDLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGH 192
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 12230412 493 ECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKL 529
Cdd:cd00144 193 TPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
149-531 1.85e-52

PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 163661 [Multi-domain]  Cd Length: 377  Bit Score: 186.54  E-value: 1.85e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 149 LLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFML 228
Cdd:cd07418  43 LVLTAHKILHREPNCVRIDVEDVCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKV 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 229 VYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTDLELlakld 308
Cdd:cd07418 123 LLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPK----- 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 309 rhkivstmrcktrkesenREEQKRKDNQTSSGQkptpwflPQSRSLPsspfhLGSgfkaykagrscsipcgspnSKELSr 388
Cdd:cd07418 198 ------------------RKKQKGKNRRVLLLE-------PESESLK-----LGT-------------------LDDLM- 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 389 rgQVRRSVdleleqcrqqagflgIREKGESLPLAPDadcvadgggvleptpeewkqvvDILWSDPAAQEGCKANAVRGGG 468
Cdd:cd07418 228 --KARRSV---------------LDPPGEGSNLIPG----------------------DVLWSDPSLTPGLSPNKQRGIG 268
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 469 CYFGPDVTERLMEKYKLQLLIRSHEC------KPE------GYEFCHN---RKVLTIFSASNY------YEVGSNRGAYV 527
Cdd:cd07418 269 LLWGPDCTEEFLEKNNLKLIIRSHEGpdarekRPGlagmnkGYTVDHDvesGKLITLFSAPDYpqfqatEERYNNKGAYI 348

                ....
gi 12230412 528 KLGP 531
Cdd:cd07418 349 ILQP 352
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
157-542 3.86e-46

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: 165.84  E-value: 3.86e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 157 LAQLPNINRVSTcyseEVTVCGDLHGQLDDLIFIFyKNGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHL 236
Cdd:cd07415  31 LVKESNVQRVRS----PVTVCGDIHGQFYDLLELF-RIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 237 NRGNHEDHLVNLRYGFTKEVMHKYKihGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTD-LELLAKLDRHkivst 315
Cdd:cd07415 106 LRGNHESRQITQVYGFYDECLRKYG--NANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQtLDQIRALDRF----- 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 316 mrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcgspnsKELSRRGqvrrs 395
Cdd:cd07415 179 --------------------------------------------------------------------QEVPHEG----- 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 396 vdleleqcrqqagflgirekgeslPLApdadcvadgggvleptpeewkqvvDILWSDPAAQEGCKANAvRGGGCYFGPDV 475
Cdd:cd07415 186 ------------------------PMC------------------------DLLWSDPDDREGWGISP-RGAGYLFGQDV 216
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12230412 476 TERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQA 542
Cdd:cd07415 217 VEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEA 283
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
140-525 1.08e-39

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: 147.87  E-value: 1.08e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 140 QLHARYVLNLLYETRKHLAQLPNINRVSTcyseEVTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEV 219
Cdd:cd07414  22 QLTEAEIRGLCLKSREIFLSQPILLELEA----PLKICGDIHGQYYDLLRLFEYGGFP-PESNYLFLGDYVDRGKQSLET 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 220 LMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIhgkKILRTLQDVFCWLPLATLVDEKVLVLHGGVsdkt 299
Cdd:cd07414  97 ICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNI---KLWKTFTDCFNCLPVAAIVDEKIFCCHGGL---- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 300 dlellakldrhkivstmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcg 379
Cdd:cd07414     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 380 spnSKELSRRGQVRRsvdleleqcrqqagflgirekgeslplapdadcvadgggVLEPT--PEEwKQVVDILWSDPAAQE 457
Cdd:cd07414 170 ---SPDLQSMEQIRR---------------------------------------IMRPTdvPDQ-GLLCDLLWSDPDKDV 206
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12230412 458 GCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGA 525
Cdd:cd07414 207 QGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGA 274
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
125-529 1.23e-35

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: 136.67  E-value: 1.23e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 125 PDHaTALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVStcysEEVTVCGDLHGQLDDLIFIFYKNGLPSPERaYV 204
Cdd:cd07416   1 PRV-DILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIE----APVTVCGDIHGQFYDLLKLFEVGGSPANTR-YL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 205 FNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIhgkKILRTLQDVFCWLPLATLV 284
Cdd:cd07416  75 FLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSE---RVYDACMEAFDCLPLAALM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 285 DEKVLVLHGGVS-DKTDLELLAKLDRHkivstmrcktrkesenreeqkrkdnqtssgqkptpwflpqsRSLPSSpfhlgs 363
Cdd:cd07416 152 NQQFLCVHGGLSpELKTLDDIRKLDRF-----------------------------------------REPPSY------ 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 364 gfkaykaGRSCsipcgspnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvleptpeewk 443
Cdd:cd07416 185 -------GPMC--------------------------------------------------------------------- 188
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 444 qvvDILWSDPAAQEGCKA-------NAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRK------VLTI 510
Cdd:cd07416 189 ---DLLWSDPLEDFGNEKtqehfvhNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITI 265
                       410
                ....*....|....*....
gi 12230412 511 FSASNYYEVGSNRGAYVKL 529
Cdd:cd07416 266 FSAPNYLDVYNNKAAVLKY 284
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
178-534 4.87e-35

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: 135.26  E-value: 4.87e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 178 GDLHGQLDDLIFIFYKNGLPSPERA-------YVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRY 250
Cdd:cd07419  54 GDIHGQFGDLMRLFDEYGSPVTEEAgdieyidYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALF 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 251 GFTKEVMHKYKIH---GKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTdlellakldrHKIvstmrcktrkesenr 327
Cdd:cd07419 134 GFREECIERLGEDirdGDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRSI----------NHI--------------- 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 328 eeqkrkdNQTSSGQKPTPwflpqsrslpsspfhlgsgfkaykagrscsIPCGSPnskelsrrgqvrrsvdleleqcrqqa 407
Cdd:cd07419 189 -------HQIENLKRPIT------------------------------MEAGSP-------------------------- 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 408 gflgirekgeslplapdadcvadgggvleptpeewkQVVDILWSDPA---AQEGCKANAV--RGGGCY--FGPDVTERLM 480
Cdd:cd07419 206 ------------------------------------VVMDLLWSDPTendSVLGLRPNAIdpRGTGLIvkFGPDRVMEFL 249
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 12230412 481 EKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALT 534
Cdd:cd07419 250 EENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLV 303
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
174-516 2.59e-33

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 130.03  E-value: 2.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  174 VTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFT 253
Cdd:PTZ00244  54 VRVCGDTHGQYYDLLRIFEKCGFP-PYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  254 KEVMHKYKIhgkKILRTLQDVFCWLPLATLVDEKVLVLHGGVS-DKTDLELLAKLDRhkivstmrcktrkesenreeqkr 332
Cdd:PTZ00244 133 DDVKRRYNI---KLFKAFTDVFNTMPVCCVISEKIICMHGGLSpDLTSLASVNEIER----------------------- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  333 kdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsiPCGSPNSkelsrrgqvrrsvdleleqcrqqagflgi 412
Cdd:PTZ00244 187 --------------------------------------------PCDVPDR----------------------------- 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  413 rekgeslplapdadcvadggGVLeptpeewkqvVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSH 492
Cdd:PTZ00244 194 --------------------GIL----------CDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAH 243
                        330       340
                 ....*....|....*....|....
gi 12230412  493 ECKPEGYEFCHNRKVLTIFSASNY 516
Cdd:PTZ00244 244 QVMERGYGFFASRQLVTVFSAPNY 267
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
174-533 1.41e-31

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 125.54  E-value: 1.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  174 VTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFT 253
Cdd:PTZ00480  61 LKICGDVHGQYFDLLRLFEYGGYP-PESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  254 KEVMHKYKIhgkKILRTLQDVFCWLPLATLVDEKVLVLHGGVsdktdlellakldrhkivstmrcktrkesenreeqkrk 333
Cdd:PTZ00480 140 DECKRRYTI---KLWKTFTDCFNCLPVAALIDEKILCMHGGL-------------------------------------- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  334 dnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcgspnSKELSRRGQVRRsvdleleqcrqqagflgir 413
Cdd:PTZ00480 179 -------------------------------------------------SPELSNLEQIRR------------------- 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  414 ekgeslplapdadcvadgggVLEPTP-EEWKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSH 492
Cdd:PTZ00480 191 --------------------IMRPTDvPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAH 250
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 12230412  493 ECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPAL 533
Cdd:PTZ00480 251 QVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESL 291
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
174-296 2.24e-26

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 109.91  E-value: 2.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  174 VTVCGDLHGQLDDLIFIFYKNGlPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFT 253
Cdd:PTZ00239  45 VNVCGDIHGQFYDLQALFKEGG-DIPNANYIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFY 123
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 12230412  254 KEVMHKYKihGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVS 296
Cdd:PTZ00239 124 EEILRKYG--NSNPWRLFMDVFDCLPLAALIEGQILCVHGGLS 164
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
661-726 5.04e-13

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 64.11  E-value: 5.04e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12230412 661 LETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDDGIcdlaRSIDFNKDGHIDINEFLEAFR 726
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI----REVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
658-726 8.14e-12

EF-hand domain pair;


Pssm-ID: 338778 [Multi-domain]  Cd Length: 68  Bit Score: 60.75  E-value: 8.14e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12230412   658 RSNLETIFRIIDSDHSGFISLDEFRQTWKLFSsHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAFR 726
Cdd:pfam13499   1 EEKLKEAFKLLDKDGDGYLDVEELKKLLRKLF-EEGEKLSDEEVEELFKEFDLDKDGRISFEEFLELYR 68
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
174-242 1.70e-09

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: 333878 [Multi-domain]  Cd Length: 79  Bit Score: 54.70  E-value: 1.70e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12230412   174 VTVCGDLH--GQLDDLIFIFykNGLPSPERAYVF--NGDFVDRGKDSVEVLmvLFAFMLVYPKEFHLNRGNHE 242
Cdd:pfam00149   3 ILVIGDLHgpGQLDDLLELL--KKLLEEEKPDLVlhAGDLVDRGPWETEVL--ELLERLIAYVPVYLVRGNHD 71
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
85-162 3.43e-07

PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine phosphatases and contains TPR repeats.


Pssm-ID: 311981  Cd Length: 92  Bit Score: 48.62  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412    85 NRMFTEERFAQDVETEEGG------DFESIEVPDSYTGPRLSF-PLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHL 157
Cdd:pfam08321   5 EKLVRRIAFEKAIAVEDEKsaaetiDLESIDVEDSYDGPRLEDeKVTLEFVKDMIERFKDGKKLHKKYAYQILLKVKEIL 84

                  ....*
gi 12230412   158 AQLPN 162
Cdd:pfam08321  85 KKEPS 89
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
581-725 1.09e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 48.84  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 581 FRKRDPDESGVITLSDWATavesvlhlglpwrMLRPQLVNSSADNVLEYRSWLDSlAKEQLSRENIQSSLLEKLYRN--R 658
Cdd:COG5126  26 FQLFDRDSDGLIDRNELGK-------------ILRSLGFNPSEAEINKLFEEIDA-GNETVDFPEFLTVMSVKLKRGdkE 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12230412 659 SNLETIFRIIDSDHSGFISLDEFRQTWKlfssHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAF 725
Cdd:COG5126  92 EELREAFKLFDKDHDGYISIGELRRVLK----SLGERLSDEEVEKLLKEYDEDGDGEIDYEEFKKLI 154
PHA02239 PHA02239
putative protein phosphatase
174-248 2.16e-06

putative protein phosphatase


Pssm-ID: 107154  Cd Length: 235  Bit Score: 49.22  E-value: 2.16e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12230412  174 VTVCGDLHGQLDDLIFIFYK-NGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLnRGNHEDHLVNL 248
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTL-LGNHDDEFYNI 77
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
662-732 1.27e-05

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 43.36  E-value: 1.27e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12230412 662 ETIFRIIDSDHSGFISLDEFRQTWKlfSSHMSIDITDDgICDLArsiDFNKDGHIDINEFLEAFRLVEQSC 732
Cdd:cd00052   2 DQIFRSLDPDGDGLISGDEARPFLG--KSGLPRSVLAQ-IWDLA---DTDKDGKLDKEEFAIAMHLIALAL 66
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
660-721 3.03e-05

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997  Cd Length: 101  Bit Score: 43.27  E-value: 3.03e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12230412 660 NLETIFRIIDSDHSGFISLDEFRQTWKLFSSHmSIDITDDGICDLARSIDFNKDGHIDINEF 721
Cdd:cd16254  35 DVKKVFHILDKDKSGFIEEDELKFVLKGFSPD-GRDLSDKETKALLAAGDKDGDGKIGIDEF 95
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
178-298 4.82e-05

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: 45.20  E-value: 4.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 178 GDLHGQLDDLI-------FIFYKNGLPS-PE-RAYVFNGDFVDRGKDSVEVLmvLFAFMLVYPKEFHLNRGNHEDHL--- 245
Cdd:cd07423   4 GDVHGCYDELVelleklgYQKKEEGLYVhPEgRKLVFLGDLVDRGPDSIDVL--RLVMNMVKAGKALYVPGNHCNKLyry 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12230412 246 -----VNLRYGFTKEVM-------HKYKIHGKKILRTLQDvfcwLPLATLVDEKVLVL-HGGVSDK 298
Cdd:cd07423  82 lkgrnVQLAHGLETTVEelealskEERPEFRERFAEFLES----LPSHLVLDGGRLVVaHAGIKEE 143
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
176-295 6.07e-05

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 45.08  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  176 VCGDLHGQLDDLIFIFYK------NGLP-SPE-RAYVFNGDFVDRGKDSVEvlMVLFAFMLVYPKEFHLNRGNHEDHLVN 247
Cdd:PRK13625   5 IIGDIHGCYQEFQALTEKlgynwsSGLPvHPDqRKLAFVGDLTDRGPHSLR--MIEIVWELVEKKAAYYVPGNHCNKLYR 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  248 LRYGFTKEVMH-------KYKIHGKKILRTLQDVFCWL----PLATLVDEKVLVL-HGGV 295
Cdd:PRK13625  83 FFLGRNVTIAHglettvaEYEALPSHKQNMIKEKFITLyeqaPLYHILDEGRLVVaHAGI 142
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
176-242 6.13e-05

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 43.02  E-value: 6.13e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12230412 176 VCGDLHGQLDDLIFIFYKNgLPSPERA--YVFNGDFVDRGKDSVEVLMVLFAFMLvYPKEFHLNRGNHE 242
Cdd:cd00838   2 VISDIHGNLEALEAVLEAA-LAKAEKPdlVICLGDLVDYGPDPEEVELKALRLLL-AGIPVYVVPGNHD 68
PTZ00184 PTZ00184
calmodulin; Provisional
661-721 1.17e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.83  E-value: 1.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12230412  661 LETIFRIIDSDHSGFISLDEFRQTWklfsSHMSIDITDDGICDLARSIDFNKDGHIDINEF 721
Cdd:PTZ00184  86 IKEAFKVFDRDGNGFISAAELRHVM----TNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
661-686 1.35e-04

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 333786 [Multi-domain]  Cd Length: 27  Bit Score: 39.29  E-value: 1.35e-04
                          10        20
                  ....*....|....*....|....*.
gi 12230412   661 LETIFRIIDSDHSGFISLDEFRQTWK 686
Cdd:pfam00036   1 LKEIFRLFDKDGDGKIDFEEFKELLK 26
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
659-721 1.51e-04

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994  Cd Length: 101  Bit Score: 41.36  E-value: 1.51e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12230412 659 SNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHmSIDITDDGICDLARSIDFNKDGHIDINEF 721
Cdd:cd16251  34 DQIKKVFQILDKDKSGFIEEEELKYILKGFSIA-GRDLTDEETKALLAAGDTDGDGKIGVEEF 95
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
447-517 1.87e-04

Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal transduction mechanisms];


Pssm-ID: 223712  Cd Length: 155  Bit Score: 42.34  E-value: 1.87e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12230412 447 DILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYY 517
Cdd:COG0639  84 DLLWSDPDGGDRRIWNPGPRGVPRDGGDVTAVFGIVHTPKLIERAHVLYDIDTGAVFGGGLLTAFSAPNYC 154
EF-hand_8 pfam13833
EF-hand domain pair;
672-725 2.21e-04

EF-hand domain pair;


Pssm-ID: 316358 [Multi-domain]  Cd Length: 53  Bit Score: 39.48  E-value: 2.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 12230412   672 HSGFISLDEFRQTWKLFSSHmsiDITDDGICDLARSIDFNKDGHIDINEFLEAF 725
Cdd:pfam13833   1 EKGVITREDLRRALALLGLK---GLSEEEVDILFREFDTDGDGYISFEEFCVLL 51
bacter_Pnkp TIGR04075
polynucleotide kinase-phosphatase; Members of this protein family are the bacterial ...
163-246 3.24e-04

polynucleotide kinase-phosphatase; Members of this protein family are the bacterial polynucleotide kinase-phosphatase (Pnkp) whose genes occur paired with genes for the 3' terminal RNA ribose 2'-O-methyltransferase Hen1. All members of the seed alignment belong to a cassette with the Hen1. The pair acts in bacterial RNA repair. This enzyme performs end-healing reactions on broken RNA, preparing from the RNA ligase to close the break. The working hypothesis is that the combination of Pnkp (RNA repair) and Hen1 (RNA modification) serves to first repair RNA damage from ribotoxins and then perform a modification that prevents the damage from recurring. [Transcription, RNA processing]


Pssm-ID: 274963 [Multi-domain]  Cd Length: 851  Bit Score: 43.83  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412   163 INRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPERAYVFNGDFVDRGKDSVEVL-----MVLFAFMLVYPkefhln 237
Cdd:TIGR04075 185 IGDVHGCRDELETLLEELGYQIERDEGGRGVDVTHPEGRKAVFVGDLVDRGPDSPGVLrlvmgMVAAGTALCVP------ 258

                  ....*....
gi 12230412   238 rGNHEDHLV 246
Cdd:TIGR04075 259 -GNHDVKLL 266
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
178-296 4.55e-04

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277368  Cd Length: 209  Bit Score: 41.90  E-value: 4.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 178 GDLHGQLDDLIFIFYKNGLPSPERAYVFN-------GDFVDRGkdsVEVLMVLFAFMLVYPK------EFHLNRGNHEdh 244
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRG---DDEIEILKLLEKLKRQarkaggKVILLLGNHE-- 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12230412 245 LVNL----RY-------GFTKEVMHKYKIHGK-----KILRTLQdvfcwlplATLVDEKVLVLHGGVS 296
Cdd:cd07425  79 LMNLcgdfRYvhprglnEFGGVAKRRYALLSDggyigRYLRTHP--------VVLVVNDILFVHGGLG 138
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
624-730 4.58e-04

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 42.34  E-value: 4.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 624 DNVLEYRSwldsLAKEQLSRENiqsSLLEKLYRNRSNLE----TIFRIIDSDHSGFISLDEFRQTWK-LFS---SHMSID 695
Cdd:cd15902  58 DGKIEIRE----LANILPTEEN---FLLLFRREQPLISSvefmKIWRKYDTDGSGFIEAKELKGFLKdLLLknkKHVSPP 130
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 12230412 696 ITDDGICDLARSIDFNKDGHIDINEFL------EAFRLVEQ 730
Cdd:cd15902 131 KLDEYTKLILKEFDANKDGKLELDEMAkllpvqENFLLKFQ 171
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
635-731 5.78e-04

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 42.29  E-value: 5.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 635 SLAKEQLSR---ENIQSSLLEKLYRNrsnlETIFRIIDSDHSGFISLDEFR------------QTWKLFSSHMSIDITDD 699
Cdd:cd16225  50 FLSAEELEDwimEKTQEHFQEAVEEN----EQIFKAVDTDKDGNVSWEEYRvhfllskgyseeEAEEKIKNNEELKLDED 125
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 12230412 700 GICDLAR------SIDFNKDGHIDINEFLeAFRLVEQS 731
Cdd:cd16225 126 DKEVLDRykdrwsQADEPEDGLLDVEEFL-SFRHPEHS 162
PTZ00183 PTZ00183
centrin; Provisional
585-722 7.21e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.83  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412  585 DPDESGVITLSDWATAVESvlhLGLPWRmlRPQL------VNSSADNVLEYRSWLDSLAKEQLSRENiqsslleklyrnR 658
Cdd:PTZ00183  27 DTDGSGTIDPKELKVAMRS---LGFEPK--KEEIkqmiadVDKDGSGKIDFEEFLDIMTKKLGERDP------------R 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12230412  659 SNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMsidiTDDGICDLARSIDFNKDGHIDINEFL 722
Cdd:PTZ00183  90 EEILKAFRLFDDDKTGKISLKNLKRVAKELGETI----TDEELQEMIDEADRNGDGEISEEEFY 149
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
176-247 7.24e-04

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: 41.15  E-value: 7.24e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12230412 176 VCGDLHGQLDDLififyKNGLPS----PERAYVFN-GDFVDRGKDSVEVLMVLfafmlvypKE--FHLNRGNHEDHLVN 247
Cdd:cd07424   5 VVGDIHGHFQRL-----QRALDAvgfdPARDRLISvGDLVDRGPESLEVLELL--------KQpwFHAVQGNHEQMAID 70
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
660-750 8.86e-04

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 40.32  E-value: 8.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 660 NLETIFRIIDSDHSGFISLDEFRQ-----TWKLFsshmsiditDDGICDLARSI-DFNKDGHIDINEFLEAFRLVEQscl 733
Cdd:cd16183   1 FLWNVFQRVDKDRSGQISATELQQalsngTWTPF---------NPETVRLMIGMfDRDNSGTINFQEFAALWKYITD--- 68
                        90
                ....*....|....*..
gi 12230412 734 eghASACLQSTDTAESG 750
Cdd:cd16183  69 ---WQNCFRSFDRDNSG 82
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
664-721 8.92e-04

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998  Cd Length: 101  Bit Score: 38.94  E-value: 8.92e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 12230412 664 IFRIIDSDHSGFISLDEFRQTWKLFSSHMSiDITDDGICDLARSIDFNKDGHIDINEF 721
Cdd:cd16255  39 VFEIIDQDKSGFIEEEELKLFLQNFSSGAR-ELTDAETKAFLKAGDSDGDGKIGVEEF 95
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
665-730 1.16e-03

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 40.33  E-value: 1.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12230412 665 FRIIDSDHSGFISLDEFRQT-----WKLFSshmsiditdDGICDLARSI-DFNKDGHIDINEFLEAFRLVEQ 730
Cdd:cd16184   6 FQAVDRDRSGKISAKELQQAlvngnWSHFN---------DETCRLMIGMfDKDKSGTIDIYEFQALWNYIQQ 68
EF-hand_6 pfam13405
EF-hand domain;
661-683 1.31e-03

EF-hand domain;


Pssm-ID: 338723 [Multi-domain]  Cd Length: 30  Bit Score: 36.40  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|...
gi 12230412   661 LETIFRIIDSDHSGFISLDEFRQ 683
Cdd:pfam13405   2 LREAFKLFDKDGDGYISLEELRK 24
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
660-721 1.78e-03

EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319996  Cd Length: 101  Bit Score: 38.31  E-value: 1.78e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12230412 660 NLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSiDITDDGICDLARSIDFNKDGHIDINEF 721
Cdd:cd16253  35 DIKKVFNILDQDKSGFIEEEELKLFLKNFSDGAR-VLSDKETKNFLAAGDSDGDGKIGVDEF 95
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
660-726 3.15e-03

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 38.77  E-value: 3.15e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 660 NLETIFRII---DSDHSGFISLDEFRQTWKLfsshmsidITDDGICdlARSIDFNKDGHIDINEFLEAFR 726
Cdd:cd16183  35 NPETVRLMIgmfDRDNSGTINFQEFAALWKY--------ITDWQNC--FRSFDRDNSGNIDKNELKQALT 94
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
21-40 3.58e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470  Cd Length: 23  Bit Score: 34.99  E-value: 3.58e-03
                           10        20
                   ....*....|....*....|
gi 12230412     21 KAAALIQRWYRRYMARLEMR 40
Cdd:smart00015   4 RAAIIIQAAWRGYLARKRYK 23
EF-hand_5 pfam13202
EF hand;
661-683 3.68e-03

EF hand;


Pssm-ID: 338631  Cd Length: 25  Bit Score: 34.97  E-value: 3.68e-03
                          10        20
                  ....*....|....*....|...
gi 12230412   661 LETIFRIIDSDHSGFISLDEFRQ 683
Cdd:pfam13202   1 LKDAFRQFDLNGDGKISKEELKR 23
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
664-683 4.25e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.05  E-value: 4.25e-03
                           10        20
                   ....*....|....*....|
gi 12230412    664 IFRIIDSDHSGFISLDEFRQ 683
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKD 24
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
661-734 4.98e-03

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 37.65  E-value: 4.98e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12230412 661 LETIFRIIDSDHSGFISLDEFRqtwKLFSsHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAFR-LVEQSCLE 734
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIK---KLLK-RLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKsLTERPELE 72
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
660-726 6.13e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 37.89  E-value: 6.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412 660 NLETIFRIIDSDHSGFISLDEFRQ-----TW------------KLFSSHMSIDITDDGICDLARSI----------DFNK 712
Cdd:cd16180   1 ELRRIFQAVDRDRSGRISAKELQRalsngDWtpfsietvrlmiNMFDRDRSGTINFDEFVGLWKYIqdwrrlfrrfDRDR 80
                        90
                ....*....|....
gi 12230412 713 DGHIDINEFLEAFR 726
Cdd:cd16180  81 SGSIDFNELQNALS 94
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
178-302 7.10e-03

bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273208 [Multi-domain]  Cd Length: 279  Bit Score: 39.10  E-value: 7.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12230412   178 GDLHGQLDDLIFIFYKNGLPSPERAYVFNGDFVDRGKDSVEVLMvlfaFMLVYPKEFHLNRGNHEDHLVNLRYGFTKevm 257
Cdd:TIGR00668   7 GDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLR----YVKSLGDAVRLVLGNHDLHLLAVFAGISR--- 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 12230412   258 HKYKIHGKKILRT--LQDVFCWL---PLATLVDEKVLVL-HGGVSDKTDLE 302
Cdd:TIGR00668  80 NKPKDRLDPLLEApdADELLNWLrrqPLLQHDEEKKLVMaHAGITPQWDLQ 130
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
174-242 7.23e-03

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: 39.02  E-value: 7.23e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12230412 174 VTVC-GDLHGQLDDL--IFIFYKNGLPSPERA---YVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNR-GNHE 242
Cdd:cd07421   3 VVICvGDIHGYISKLnnLWLNLQSALGPSDFAsalVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHVFLcGNHD 78
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
665-723 8.78e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 37.58  E-value: 8.78e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 12230412 665 FRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDdgicDLARSIDFNKDGHIDINEFLE 723
Cdd:cd16185   6 FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAE----KLIRMFDRDGNGTIDFEEFAA 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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