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Conserved domains on  [gi|1720412481|ref|XP_030110066|]
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serine/threonine-protein phosphatase with EF-hands 2 isoform X1 [Mus musculus]

Protein Classification

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

protein containing domains IQCD, MPP_RdgC, FRQ1, 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 ...
 162-581 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 1720412481 162 PLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPER 241
Cdd:cd07420     1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 242 AYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLA 321
Cdd:cd07420    81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 322 TLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVStmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhl 401
Cdd:cd07420   161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS----------------------------------------------- 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 402 gsgfkaykagrscsipcgspnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvlepTPEE 481
Cdd:cd07420   194 ----------------------------------------------------------------------------TKTE 197

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 482 WKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGS 561
Cdd:cd07420   198 WQQVVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGS 277

                         410       420
                  ....*....|....*....|
gi 1720412481 562 NRGAYVKLGPALTPHIVQYQ 581
Cdd:cd07420   278 NRGAYVKLGPQLTPHFVQYQ 297
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 701-766 3.23e-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: 64.88  E-value: 3.23e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412481 701 LETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDDGIcdlaRSIDFNKDGHIDINEFLEAFR 766
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI----REVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
621-766 1.40e-11

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.89  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 621 FRKRDPDESGVITLSDWATAVESVlhlglpWRMLRpqlvnssadnvleyrSWLDSLAKEQLSRE---NIQSSLLEKLYRN 697
Cdd:COG5126    11 FDLLDADGDGVLERDDFEALFRRL------WATLF---------------SEADTDGDGRISREefvAGMESLFEATVEP 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412481 698 RsnLETIFRIIDSDHSGFISLDEFRQTWKlfsshmSIDITDDGICDLARSIDFNKDGHIDINEFLEAFR 766
Cdd:COG5126    70 F--ARAAFDLLDTDGDGKISADEFRRLLT------ALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 61-82 2.20e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.37  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|..
gi 1720412481  61 KAAALIQRWYRRYMARLEMRRR 82
Cdd:cd23767    10 RAATLIQALWRGYKVRKELKKK 31
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 162-581 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 1720412481 162 PLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPER 241
Cdd:cd07420     1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 242 AYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLA 321
Cdd:cd07420    81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 322 TLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVStmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhl 401
Cdd:cd07420   161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS----------------------------------------------- 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 402 gsgfkaykagrscsipcgspnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvlepTPEE 481
Cdd:cd07420   194 ----------------------------------------------------------------------------TKTE 197

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 482 WKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGS 561
Cdd:cd07420   198 WQQVVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGS 277

                         410       420
                  ....*....|....*....|
gi 1720412481 562 NRGAYVKLGPALTPHIVQYQ 581
Cdd:cd07420   278 NRGAYVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 181-584 1.39e-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 [Multi-domain]  Cd Length: 271  Bit Score: 277.94  E-value: 1.39e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  181 LHARYVLNLLYETRKHLAQLPNINRVStcysEEVTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVL 260
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS----APVTVCGDIHGQFDDLLRLFDKNGQP-PETNYVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  261 MVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYkihGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDK-T 339
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDlT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  340 DLELLAKLDRHKIvstmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcg 419
Cdd:smart00156 153 TLDDIRKLKRPQE------------------------------------------------------------------- 165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  420 spnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvleptPEEWKQVVDILWSDPAA-QEG 498
Cdd:smart00156 166 -----------------------------------------------------------PPDDGLLIDLLWSDPDQpVNG 186

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  499 CKANAvRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIV 578
Cdd:smart00156 187 FGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFE 265


                   ....*.
gi 1720412481  579 QYQANK 584
Cdd:smart00156 266 QFKPGK 271
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 214-556 3.35e-33

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 130.03  E-value: 3.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 214 VTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFT 293
Cdd:PTZ00244   54 VRVCGDTHGQYYDLLRIFEKCGFP-PYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 294 KEVMHKYKIhgkKILRTLQDVFCWLPLATLVDEKVLVLHGGVS-DKTDLELLAKLDRhkivstmrcktrkesenreeqkr 372
Cdd:PTZ00244  133 DDVKRRYNI---KLFKAFTDVFNTMPVCCVISEKIICMHGGLSpDLTSLASVNEIER----------------------- 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 373 kdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsiPCGSPNSkelsrrgqvrrsvdleleqcrqqagflgi 452
Cdd:PTZ00244  187 --------------------------------------------PCDVPDR----------------------------- 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 453 rekgeslplapdadcvadggGVLeptpeewkqvVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSH 532
Cdd:PTZ00244  194 --------------------GIL----------CDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAH 243

                         330       340
                  ....*....|....*....|....
gi 1720412481 533 ECKPEGYEFCHNRKVLTIFSASNY 556
Cdd:PTZ00244  244 QVMERGYGFFASRQLVTVFSAPNY 267
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 701-766 3.23e-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: 64.88  E-value: 3.23e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412481 701 LETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDDGIcdlaRSIDFNKDGHIDINEFLEAFR 766
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI----REVDKDGDGKIDFEEFLELMA 63
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 214-324 2.12e-12

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 64.16  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 214 VTVCGDLH--GQLDDLIFIFykNGLPSPERAYVF--NGDFVDRGKDSVEVLmvLFAFMLVYPKEFHLNRGNHEDHLVNLr 289
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELL--KKLLEEGKPDLVlhAGDLVDRGPPSEEVL--ELLERLIKYVPVYLVRGNHDFDYGEC- 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720412481 290 ygftkEVMHKYKIHGKKILRTLQDVFCWLPLATLV 324
Cdd:pfam00149  78 -----LRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
EF-hand_7 pfam13499
EF-hand domain pair;
698-766 2.27e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 62.66  E-value: 2.27e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412481 698 RSNLETIFRIIDSDHSGFISLDEFRQTwkLFSSHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAFR 766
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKL--LRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
621-766 1.40e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.89  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 621 FRKRDPDESGVITLSDWATAVESVlhlglpWRMLRpqlvnssadnvleyrSWLDSLAKEQLSRE---NIQSSLLEKLYRN 697
Cdd:COG5126    11 FDLLDADGDGVLERDDFEALFRRL------WATLF---------------SEADTDGDGRISREefvAGMESLFEATVEP 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412481 698 RsnLETIFRIIDSDHSGFISLDEFRQTWKlfsshmSIDITDDGICDLARSIDFNKDGHIDINEFLEAFR 766
Cdd:COG5126    70 F--ARAAFDLLDTDGDGKISADEFRRLLT------ALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
PTZ00184 PTZ00184
calmodulin; Provisional
 701-761 1.04e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 43.21  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412481 701 LETIFRIIDSDHSGFISLDEFRQTWklfsSHMSIDITDDGICDLARSIDFNKDGHIDINEF 761
Cdd:PTZ00184   86 IKEAFKVFDRDGNGFISAAELRHVM----TNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
PTZ00183 PTZ00183
centrin; Provisional
 625-762 7.34e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.83  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 625 DPDESGVITLSDWATAVESvlhLGLPWRmlRPQL------VNSSADNVLEYRSWLDSLAKEQLSRENiqsslleklyrnR 698
Cdd:PTZ00183   27 DTDGSGTIDPKELKVAMRS---LGFEPK--KEEIkqmiadVDKDGSGKIDFEEFLDIMTKKLGERDP------------R 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412481 699 SNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMsidiTDDGICDLARSIDFNKDGHIDINEFL 762
Cdd:PTZ00183   90 EEILKAFRLFDDDKTGKISLKNLKRVAKELGETI----TDEELQEMIDEADRNGDGEISEEEFY 149
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 61-82 2.20e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.37  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|..
gi 1720412481  61 KAAALIQRWYRRYMARLEMRRR 82
Cdd:cd23767    10 RAATLIQALWRGYKVRKELKKK 31
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 61-80 3.63e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.38  E-value: 3.63e-03
                           10        20
                   ....*....|....*....|
gi 1720412481   61 KAAALIQRWYRRYMARLEMR 80
Cdd:smart00015   4 RAAIIIQAAWRGYLARKRYK 23
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 704-723 4.89e-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: 4.89e-03
                           10        20
                   ....*....|....*....|
gi 1720412481  704 IFRIIDSDHSGFISLDEFRQ 723
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKD 24
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 162-581 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 1720412481 162 PLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPER 241
Cdd:cd07420     1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 242 AYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLA 321
Cdd:cd07420    81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 322 TLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVStmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhl 401
Cdd:cd07420   161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS----------------------------------------------- 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 402 gsgfkaykagrscsipcgspnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvlepTPEE 481
Cdd:cd07420   194 ----------------------------------------------------------------------------TKTE 197

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 482 WKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGS 561
Cdd:cd07420   198 WQQVVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGS 277

                         410       420
                  ....*....|....*....|
gi 1720412481 562 NRGAYVKLGPALTPHIVQYQ 581
Cdd:cd07420   278 NRGAYVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 181-584 1.39e-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 [Multi-domain]  Cd Length: 271  Bit Score: 277.94  E-value: 1.39e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  181 LHARYVLNLLYETRKHLAQLPNINRVStcysEEVTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVL 260
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS----APVTVCGDIHGQFDDLLRLFDKNGQP-PETNYVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  261 MVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYkihGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDK-T 339
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDlT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  340 DLELLAKLDRHKIvstmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcg 419
Cdd:smart00156 153 TLDDIRKLKRPQE------------------------------------------------------------------- 165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  420 spnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvleptPEEWKQVVDILWSDPAA-QEG 498
Cdd:smart00156 166 -----------------------------------------------------------PPDDGLLIDLLWSDPDQpVNG 186

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481  499 CKANAvRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIV 578
Cdd:smart00156 187 FGPSI-RGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFE 265


                   ....*.
gi 1720412481  579 QYQANK 584
Cdd:smart00156 266 QFKPGK 271
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 154-582 6.64e-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 [Multi-domain]  Cd Length: 316  Bit Score: 275.29  E-value: 6.64e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 154 YTGPRLSFPLLP-DHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFY 232
Cdd:cd07417     1 YSGPKLEDGKVTlEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 233 KNGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYkihGKKILRTLQ 312
Cdd:cd07417    81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKY---NEQMFNLFS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 313 DVFCWLPLATLVDEKVLVLHGGV--SDKTDLELLAKLDRHkivstmrcktrkesenreeqkrkdnqtssgqkptpwflpq 390
Cdd:cd07417   158 EVFNWLPLAHLINGKVLVVHGGLfsDDGVTLDDIRKIDRF---------------------------------------- 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 391 srslpsspfhlgsgfkaykagrscsipcgspnskelsrrgqvrrsvdleleqcrqqagflgiREKGESLPLapdadCvad 470
Cdd:cd07417   198 --------------------------------------------------------------RQPPDSGLM-----C--- 207

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 471 gggvleptpeewkqvvDILWSDPAAQEGcKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTI 550
Cdd:cd07417   208 ----------------ELLWSDPQPQPG-RGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITV 270

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1720412481 551 FSASNYYEVGSNRGAYVKL-GPALTPHIVQYQA 582
Cdd:cd07417   271 FSAPNYCDQMGNKGAFIRFkGSDLKPKFTQFEA 303
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 215-569 2.93e-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: 216.85  E-value: 2.93e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 215 TVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTK 294
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFP-PEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 295 EVMHKYKI-HGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDktdlellakldrhkivstmrcktrkesenreeqkrk 373
Cdd:cd00144    80 ERTLRCLRkGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSP------------------------------------ 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 374 dnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcgspnskelsrrgqvrrsvDLELEQCRQQagflgir 453
Cdd:cd00144   124 ---------------------------------------------------------------DLTLLDQIRN------- 133

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 454 ekgeslplapdadcvadgggvLEPTPEEWKQVV-DILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSH 532
Cdd:cd00144   134 ---------------------IRPIENPDDQLVeDLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGH 192

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1720412481 533 ECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKL 569
Cdd:cd00144   193 TPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 189-571 4.61e-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: 186.16  E-value: 4.61e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 189 LLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFML 268
Cdd:cd07418    43 LVLTAHKILHREPNCVRIDVEDVCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 269 VYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTDLELlakld 348
Cdd:cd07418   123 LLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPK----- 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 349 rhkivstmrcktrkesenREEQKRKDNQTSSGQkptpwflPQSRSLPsspfhLGSgfkaykagrscsipcgspnSKELSr 428
Cdd:cd07418   198 ------------------RKKQKGKNRRVLLLE-------PESESLK-----LGT-------------------LDDLM- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 429 rgQVRRSVdleleqcrqqagflgIREKGESLPLAPDadcvadgggvleptpeewkqvvDILWSDPAAQEGCKANAVRGGG 508
Cdd:cd07418   228 --KARRSV---------------LDPPGEGSNLIPG----------------------DVLWSDPSLTPGLSPNKQRGIG 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 509 CYFGPDVTERLMEKYKLQLLIRSHEC------KPE------GYEFCHN---RKVLTIFSASNY------YEVGSNRGAYV 567
Cdd:cd07418   269 LLWGPDCTEEFLEKNNLKLIIRSHEGpdarekRPGlagmnkGYTVDHDvesGKLITLFSAPDYpqfqatEERYNNKGAYI 348


                  ....
gi 1720412481 568 KLGP 571
Cdd:cd07418   349 ILQP 352
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 197-582 4.25e-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: 166.22  E-value: 4.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 197 LAQLPNINRVSTcyseEVTVCGDLHGQLDDLIFIFyKNGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHL 276
Cdd:cd07415    31 LVKESNVQRVRS----PVTVCGDIHGQFYDLLELF-RIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 277 NRGNHEDHLVNLRYGFTKEVMHKYKihGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTD-LELLAKLDRHkivst 355
Cdd:cd07415   106 LRGNHESRQITQVYGFYDECLRKYG--NANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQtLDQIRALDRF----- 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 356 mrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcgspnsKELSRRGqvrrs 435
Cdd:cd07415   179 --------------------------------------------------------------------QEVPHEG----- 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 436 vdleleqcrqqagflgirekgeslPLApdadcvadgggvleptpeewkqvvDILWSDPAAQEGCKANAvRGGGCYFGPDV 515
Cdd:cd07415   186 ------------------------PMC------------------------DLLWSDPDDREGWGISP-RGAGYLFGQDV 216

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412481 516 TERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQA 582
Cdd:cd07415   217 VEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEA 283
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 180-565 9.93e-40

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: 148.64  E-value: 9.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 180 QLHARYVLNLLYETRKHLAQLPNINRVSTcyseEVTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEV 259
Cdd:cd07414    22 QLTEAEIRGLCLKSREIFLSQPILLELEA----PLKICGDIHGQYYDLLRLFEYGGFP-PESNYLFLGDYVDRGKQSLET 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 260 LMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIhgkKILRTLQDVFCWLPLATLVDEKVLVLHGGVsdkt 339
Cdd:cd07414    97 ICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNI---KLWKTFTDCFNCLPVAAIVDEKIFCCHGGL---- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 340 dlellakldrhkivstmrcktrkesenreeqkrkdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcg 419
Cdd:cd07414       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 420 spnSKELSRRGQVRRsvdleleqcrqqagflgirekgeslplapdadcvadgggVLEPT--PEEwKQVVDILWSDPAAQE 497
Cdd:cd07414   170 ---SPDLQSMEQIRR---------------------------------------IMRPTdvPDQ-GLLCDLLWSDPDKDV 206

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412481 498 GCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGA 565
Cdd:cd07414   207 QGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGA 274
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 165-569 1.27e-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: 137.05  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 165 PDHaTALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVStcysEEVTVCGDLHGQLDDLIFIFYKNGLPSPERaYV 244
Cdd:cd07416     1 PRV-DILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIE----APVTVCGDIHGQFYDLLKLFEVGGSPANTR-YL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 245 FNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIhgkKILRTLQDVFCWLPLATLV 324
Cdd:cd07416    75 FLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSE---RVYDACMEAFDCLPLAALM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 325 DEKVLVLHGGVS-DKTDLELLAKLDRHkivstmrcktrkesenreeqkrkdnqtssgqkptpwflpqsRSLPSSpfhlgs 403
Cdd:cd07416   152 NQQFLCVHGGLSpELKTLDDIRKLDRF-----------------------------------------REPPSY------ 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 404 gfkaykaGRSCsipcgspnskelsrrgqvrrsvdleleqcrqqagflgirekgeslplapdadcvadgggvleptpeewk 483
Cdd:cd07416   185 -------GPMC--------------------------------------------------------------------- 188

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 484 qvvDILWSDPAAQEGCKA-------NAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRK------VLTI 550
Cdd:cd07416   189 ---DLLWSDPLEDFGNEKtqehfvhNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITI 265

                         410
                  ....*....|....*....
gi 1720412481 551 FSASNYYEVGSNRGAYVKL 569
Cdd:cd07416   266 FSAPNYLDVYNNKAAVLKY 284
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 218-574 4.28e-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: 135.65  E-value: 4.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 218 GDLHGQLDDLIFIFYKNGLPSPERA-------YVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRY 290
Cdd:cd07419    54 GDIHGQFGDLMRLFDEYGSPVTEEAgdieyidYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALF 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 291 GFTKEVMHKYKIH---GKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTdlellakldrHKIvstmrcktrkesenr 367
Cdd:cd07419   134 GFREECIERLGEDirdGDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRSI----------NHI--------------- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 368 eeqkrkdNQTSSGQKPTPwflpqsrslpsspfhlgsgfkaykagrscsIPCGSPnskelsrrgqvrrsvdleleqcrqqa 447
Cdd:cd07419   189 -------HQIENLKRPIT------------------------------MEAGSP-------------------------- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 448 gflgirekgeslplapdadcvadgggvleptpeewkQVVDILWSDPA---AQEGCKANAV--RGGGCY--FGPDVTERLM 520
Cdd:cd07419   206 ------------------------------------VVMDLLWSDPTendSVLGLRPNAIdpRGTGLIvkFGPDRVMEFL 249

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720412481 521 EKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALT 574
Cdd:cd07419   250 EENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLV 303
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 214-556 3.35e-33

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 130.03  E-value: 3.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 214 VTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFT 293
Cdd:PTZ00244   54 VRVCGDTHGQYYDLLRIFEKCGFP-PYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 294 KEVMHKYKIhgkKILRTLQDVFCWLPLATLVDEKVLVLHGGVS-DKTDLELLAKLDRhkivstmrcktrkesenreeqkr 372
Cdd:PTZ00244  133 DDVKRRYNI---KLFKAFTDVFNTMPVCCVISEKIICMHGGLSpDLTSLASVNEIER----------------------- 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 373 kdnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsiPCGSPNSkelsrrgqvrrsvdleleqcrqqagflgi 452
Cdd:PTZ00244  187 --------------------------------------------PCDVPDR----------------------------- 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 453 rekgeslplapdadcvadggGVLeptpeewkqvVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSH 532
Cdd:PTZ00244  194 --------------------GIL----------CDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAH 243

                         330       340
                  ....*....|....*....|....
gi 1720412481 533 ECKPEGYEFCHNRKVLTIFSASNY 556
Cdd:PTZ00244  244 QVMERGYGFFASRQLVTVFSAPNY 267
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 214-573 1.61e-31

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 125.54  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 214 VTVCGDLHGQLDDLIFIFYKNGLPsPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFT 293
Cdd:PTZ00480   61 LKICGDVHGQYFDLLRLFEYGGYP-PESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 294 KEVMHKYKIhgkKILRTLQDVFCWLPLATLVDEKVLVLHGGVsdktdlellakldrhkivstmrcktrkesenreeqkrk 373
Cdd:PTZ00480  140 DECKRRYTI---KLWKTFTDCFNCLPVAALIDEKILCMHGGL-------------------------------------- 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 374 dnqtssgqkptpwflpqsrslpsspfhlgsgfkaykagrscsipcgspnSKELSRRGQVRRsvdleleqcrqqagflgir 453
Cdd:PTZ00480  179 -------------------------------------------------SPELSNLEQIRR------------------- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 454 ekgeslplapdadcvadgggVLEPTP-EEWKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSH 532
Cdd:PTZ00480  191 --------------------IMRPTDvPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAH 250

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1720412481 533 ECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPAL 573
Cdd:PTZ00480  251 QVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESL 291
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 214-336 2.48e-26

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 109.91  E-value: 2.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 214 VTVCGDLHGQLDDLIFIFYKNGlPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFT 293
Cdd:PTZ00239   45 VNVCGDIHGQFYDLQALFKEGG-DIPNANYIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFY 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720412481 294 KEVMHKYKihGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVS 336
Cdd:PTZ00239  124 EEILRKYG--NSNPWRLFMDVFDCLPLAALIEGQILCVHGGLS 164
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 701-766 3.23e-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: 64.88  E-value: 3.23e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412481 701 LETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDDGIcdlaRSIDFNKDGHIDINEFLEAFR 766
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI----REVDKDGDGKIDFEEFLELMA 63
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 214-324 2.12e-12

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 64.16  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 214 VTVCGDLH--GQLDDLIFIFykNGLPSPERAYVF--NGDFVDRGKDSVEVLmvLFAFMLVYPKEFHLNRGNHEDHLVNLr 289
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELL--KKLLEEGKPDLVlhAGDLVDRGPPSEEVL--ELLERLIKYVPVYLVRGNHDFDYGEC- 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720412481 290 ygftkEVMHKYKIHGKKILRTLQDVFCWLPLATLV 324
Cdd:pfam00149  78 -----LRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
EF-hand_7 pfam13499
EF-hand domain pair;
698-766 2.27e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 62.66  E-value: 2.27e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412481 698 RSNLETIFRIIDSDHSGFISLDEFRQTwkLFSSHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAFR 766
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKL--LRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
621-766 1.40e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.89  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 621 FRKRDPDESGVITLSDWATAVESVlhlglpWRMLRpqlvnssadnvleyrSWLDSLAKEQLSRE---NIQSSLLEKLYRN 697
Cdd:COG5126    11 FDLLDADGDGVLERDDFEALFRRL------WATLF---------------SEADTDGDGRISREefvAGMESLFEATVEP 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412481 698 RsnLETIFRIIDSDHSGFISLDEFRQTWKlfsshmSIDITDDGICDLARSIDFNKDGHIDINEFLEAFR 766
Cdd:COG5126    70 F--ARAAFDLLDTDGDGKISADEFRRLLT------ALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 130-202 1.67e-06

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


Pssm-ID: 462427  Cd Length: 92  Bit Score: 46.70  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 130 EERFAQDVETE------EGGDFESIEVPDSYTGPRLSF-PLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPN 202
Cdd:pfam08321  10 RIAFEKAIAVEekpsaaETIDLESIVVEDSYDGPRLEDeKITLEFVKDMIERFKKGKKLHKKYAYQILLKVKEILKKEPS 89
PHA02239 PHA02239
putative protein phosphatase
 214-288 2.70e-06

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 49.22  E-value: 2.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412481 214 VTVCGDLHGQLDDLIFIFYK-NGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLnRGNHEDHLVNL 288
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIMDKiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTL-LGNHDDEFYNI 77
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 702-772 1.25e-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: 1.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412481 702 ETIFRIIDSDHSGFISLDEFRQTWKlfSSHMSIDITDDgICDLArsiDFNKDGHIDINEFLEAFRLVEQSC 772
Cdd:cd00052     2 DQIFRSLDPDGDGLISGDEARPFLG--KSGLPRSVLAQ-IWDLA---DTDKDGKLDKEEFAIAMHLIALAL 66
EF-hand_8 pfam13833
EF-hand domain pair;
712-765 3.67e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 41.92  E-value: 3.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720412481 712 HSGFISLDEFRQTWKLFSSHmsiDITDDGICDLARSIDFNKDGHIDINEFLEAF 765
Cdd:pfam13833   1 EKGVITREELKRALALLGLK---DLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 700-761 3.75e-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 [Multi-domain]  Cd Length: 101  Bit Score: 43.27  E-value: 3.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412481 700 NLETIFRIIDSDHSGFISLDEFRQTWKLFSSHmSIDITDDGICDLARSIDFNKDGHIDINEF 761
Cdd:cd16254    35 DVKKVFHILDKDKSGFIEEDELKFVLKGFSPD-GRDLSDKETKALLAAGDKDGDGKIGIDEF 95
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 216-282 6.58e-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: 43.41  E-value: 6.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412481 216 VCGDLHGQLDDLIFIFYKNgLPSPERA--YVFNGDFVDRGKDSVEVLMVLFAFMLvYPKEFHLNRGNHE 282
Cdd:cd00838     2 VISDIHGNLEALEAVLEAA-LAKAEKPdlVICLGDLVDYGPDPEEVELKALRLLL-AGIPVYVVPGNHD 68
PTZ00184 PTZ00184
calmodulin; Provisional
 701-761 1.04e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 43.21  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412481 701 LETIFRIIDSDHSGFISLDEFRQTWklfsSHMSIDITDDGICDLARSIDFNKDGHIDINEF 761
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 ...
 701-728 1.39e-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: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 39.31  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|....*...
gi 1720412481 701 LETIFRIIDSDHSGFISLDEFRQTWKLF 728
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 699-761 1.86e-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 [Multi-domain]  Cd Length: 101  Bit Score: 41.36  E-value: 1.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720412481 699 SNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHmSIDITDDGICDLARSIDFNKDGHIDINEF 761
Cdd:cd16251    34 DQIKKVFQILDKDKSGFIEEEELKYILKGFSIA-GRDLTDEETKALLAAGDTDGDGKIGVEEF 95
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 664-770 3.07e-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: 43.11  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 664 DNVLEYRSwldsLAKEQLSRENiqsSLLEKLYRNRSNLE----TIFRIIDSDHSGFISLDEFRQTWK-LFS---SHMSID 735
Cdd:cd15902    58 DGKIEIRE----LANILPTEEN---FLLLFRREQPLISSvefmKIWRKYDTDGSGFIEAKELKGFLKdLLLknkKHVSPP 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720412481 736 ITDDGICDLARSIDFNKDGHIDINEFL------EAFRLVEQ 770
Cdd:cd15902   131 KLDEYTKLILKEFDANKDGKLELDEMAkllpvqENFLLKFQ 171
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 675-771 4.05e-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: 43.06  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 675 SLAKEQLSR---ENIQSSLLEKLYRNrsnlETIFRIIDSDHSGFISLDEFR------------QTWKLFSSHMSIDITDD 739
Cdd:cd16225    50 FLSAEELEDwimEKTQEHFQEAVEEN----EQIFKAVDTDKDGNVSWEEYRvhfllskgyseeEAEEKIKNNEELKLDED 125

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720412481 740 GICDLAR------SIDFNKDGHIDINEFLeAFRLVEQS 771
Cdd:cd16225   126 DKEVLDRykdrwsQADEPEDGLLDVEEFL-SFRHPEHS 162
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 218-336 5.51e-04

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


Pssm-ID: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 41.90  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 218 GDLHGQLDDLIFIFYKNGLPSPERAYVFN-------GDFVDRGkdsVEVLMVLFAFMLVYPK------EFHLNRGNHEdh 284
Cdd:cd07425     4 GDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRG---DDEIEILKLLEKLKRQarkaggKVILLLGNHE-- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412481 285 LVNL----RY-------GFTKEVMHKYKIHGK-----KILRTLQdvfcwlplATLVDEKVLVLHGGVS 336
Cdd:cd07425    79 LMNLcgdfRYvhprglnEFGGVAKRRYALLSDggyigRYLRTHP--------VVLVVNDILFVHGGLG 138
PTZ00183 PTZ00183
centrin; Provisional
 625-762 7.34e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.83  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 625 DPDESGVITLSDWATAVESvlhLGLPWRmlRPQL------VNSSADNVLEYRSWLDSLAKEQLSRENiqsslleklyrnR 698
Cdd:PTZ00183   27 DTDGSGTIDPKELKVAMRS---LGFEPK--KEEIkqmiadVDKDGSGKIDFEEFLDIMTKKLGERDP------------R 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412481 699 SNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMsidiTDDGICDLARSIDFNKDGHIDINEFL 762
Cdd:PTZ00183   90 EEILKAFRLFDDDKTGKISLKNLKRVAKELGETI----TDEELQEMIDEADRNGDGEISEEEFY 149
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 216-287 7.56e-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: 41.53  E-value: 7.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412481 216 VCGDLHGQLDDLififyKNGLPS----PERAYVFN-GDFVDRGKDSVEVLMVLfafmlvypKE--FHLNRGNHEDHLVN 287
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 ...
 700-790 7.91e-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: 41.09  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 700 NLETIFRIIDSDHSGFISLDEFRQ-----TWKLFsshmsiditDDGICDLARSI-DFNKDGHIDINEFLEAFRLVEQscl 773
Cdd:cd16183     1 FLWNVFQRVDKDRSGQISATELQQalsngTWTPF---------NPETVRLMIGMfDRDNSGTINFQEFAALWKYITD--- 68

                          90
                  ....*....|....*..
gi 1720412481 774 eghASACLQSTDTAESG 790
Cdd:cd16183    69 ---WQNCFRSFDRDNSG 82
EF-hand_5 pfam13202
EF hand;
701-723 1.09e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 36.91  E-value: 1.09e-03
                          10        20
                  ....*....|....*....|...
gi 1720412481 701 LETIFRIIDSDHSGFISLDEFRQ 723
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRR 23
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 705-770 1.09e-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: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412481 705 FRIIDSDHSGFISLDEFRQT-----WKLFSshmsiDITddgiCDLARSI-DFNKDGHIDINEFLEAFRLVEQ 770
Cdd:cd16184     6 FQAVDRDRSGKISAKELQQAlvngnWSHFN-----DET----CRLMIGMfDKDKSGTIDIYEFQALWNYIQQ 68
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 704-761 1.10e-03

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 [Multi-domain]  Cd Length: 101  Bit Score: 38.94  E-value: 1.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412481 704 IFRIIDSDHSGFISLDEFRQTWKLFSSHMSiDITDDGICDLARSIDFNKDGHIDINEF 761
Cdd:cd16255    39 VFEIIDQDKSGFIEEEELKLFLQNFSSGAR-ELTDAETKAFLKAGDSDGDGKIGVEEF 95
EF-hand_6 pfam13405
EF-hand domain;
700-723 1.70e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.39  E-value: 1.70e-03
                          10        20
                  ....*....|....*....|....
gi 1720412481 700 NLETIFRIIDSDHSGFISLDEFRQ 723
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRK 24
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 61-82 2.20e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.37  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|..
gi 1720412481  61 KAAALIQRWYRRYMARLEMRRR 82
Cdd:cd23767    10 RAATLIQALWRGYKVRKELKKK 31
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
 700-761 2.21e-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 [Multi-domain]  Cd Length: 101  Bit Score: 38.31  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412481 700 NLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSiDITDDGICDLARSIDFNKDGHIDINEF 761
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 ...
 700-766 2.90e-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: 39.16  E-value: 2.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 700 NLETIFRII---DSDHSGFISLDEFRQTWKLfsshmsidITDDGICdlARSIDFNKDGHIDINEFLEAFR 766
Cdd:cd16183    35 NPETVRLMIgmfDRDNSGTINFQEFAALWKY--------ITDWQNC--FRSFDRDNSGNIDKNELKQALT 94
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 61-80 3.63e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.38  E-value: 3.63e-03
                           10        20
                   ....*....|....*....|
gi 1720412481   61 KAAALIQRWYRRYMARLEMR 80
Cdd:smart00015   4 RAAIIIQAAWRGYLARKRYK 23
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 701-774 4.06e-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: 38.42  E-value: 4.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412481 701 LETIFRIIDSDHSGFISLDEFRqtwKLFSsHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAFR-LVEQSCLE 774
Cdd:cd15898     2 LRRQWIKADKDGDGKLSLKEIK---KLLK-RLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKsLTERPELE 72
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 704-723 4.89e-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: 4.89e-03
                           10        20
                   ....*....|....*....|
gi 1720412481  704 IFRIIDSDHSGFISLDEFRQ 723
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKD 24
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 700-766 5.43e-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: 38.28  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412481 700 NLETIFRIIDSDHSGFISLDEFRQ-----TW------------KLFSSHMSIDITDDGICDLARSI----------DFNK 752
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQRalsngDWtpfsietvrlmiNMFDRDRSGTINFDEFVGLWKYIqdwrrlfrrfDRDR 80

                          90
                  ....*....|....
gi 1720412481 753 DGHIDINEFLEAFR 766
Cdd:cd16180    81 SGSIDFNELQNALS 94
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 705-763 8.87e-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: 37.96  E-value: 8.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412481 705 FRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDdgicDLARSIDFNKDGHIDINEFLE 763
Cdd:cd16185     6 FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAE----KLIRMFDRDGNGTIDFEEFAA 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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