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Conserved domains on  [gi|77917564|ref|NP_001030107|]
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serine/threonine-protein phosphatase with EF-hands 1 isoform 1 [Rattus norvegicus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 13882280)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

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 ...
116-442 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: 597.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 116 PLTFTDINLLLQAFKQQQTLHAHYVLEVLFEARKILKQMPNFTRIQTFPAKEITICGDLHGKLDDLMLIFYKNGLPSEKN 195
Cdd:cd07420   1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 196 PYVFNGDFVDRGNNSMEILMILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYKLHGKKILQVLEELYTWLPIG 275
Cdd:cd07420  81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 276 TIIDNEILVIHGGISESTDLNILQQLQRNKMKSvlmppmstnqecnikknkagpseqsaseqlTKLEWEQIIDLLWSDPR 355
Cdd:cd07420 161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS------------------------------TKTEWQQVVDILWSDPK 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 356 GKKGCYPNTSRGGGCYFGPDVTSKVLNKNQLKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGAYIRLSYGTS 435
Cdd:cd07420 211 ATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLT 290

                ....*..
gi 77917564 436 PQFFQYQ 442
Cdd:cd07420 291 PHFVQYQ 297
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
474-636 1.09e-13

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 68.28  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 474 RKTDLINAFELRDHSRTGKISLAQWAFSMESIlglnlpWRSLSSHLVsTDSSGSVdymsSFDDIHiekpmKDMKSDLIET 553
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL------WATLFSEAD-TDGDGRI----SREEFV-----AGMESLFEAT 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 554 MyryRSDLKIIFNIIDTDQSGLISMDEFRTMWKLFNahykvhIDDSQIDELASTMDSNKDGNIDFNEFLRAfyvVHKYET 633
Cdd:COG5126  67 V---EPFARAAFDLLDTDGDGKISADEFRRLLTALG------VSEEEADELFARLDTDGDGKISFEEFVAA---VRDYYT 134

                ...
gi 77917564 634 PES 636
Cdd:COG5126 135 PDA 137
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
15-33 9.19e-04

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.92  E-value: 9.19e-04
                           10
                   ....*....|....*....
gi 77917564     15 KVVRAALIIQNWYRRYRAR 33
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLAR 19
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
116-442 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: 597.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 116 PLTFTDINLLLQAFKQQQTLHAHYVLEVLFEARKILKQMPNFTRIQTFPAKEITICGDLHGKLDDLMLIFYKNGLPSEKN 195
Cdd:cd07420   1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 196 PYVFNGDFVDRGNNSMEILMILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYKLHGKKILQVLEELYTWLPIG 275
Cdd:cd07420  81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 276 TIIDNEILVIHGGISESTDLNILQQLQRNKMKSvlmppmstnqecnikknkagpseqsaseqlTKLEWEQIIDLLWSDPR 355
Cdd:cd07420 161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS------------------------------TKTEWQQVVDILWSDPK 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 356 GKKGCYPNTSRGGGCYFGPDVTSKVLNKNQLKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGAYIRLSYGTS 435
Cdd:cd07420 211 ATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLT 290

                ....*..
gi 77917564 436 PQFFQYQ 442
Cdd:cd07420 291 PHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
135-445 1.29e-108

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: 328.40  E-value: 1.29e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564    135 LHAHYVLEVLFEARKILKQMPNFTRIqtfpAKEITICGDLHGKLDDLMLIFYKNGLPSEKNpYVFNGDFVDRGNNSMEIL 214
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEV----SAPVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564    215 MILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYklhGKKILQVLEELYTWLPIGTIIDNEILVIHGGISEstD 294
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSP--D 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564    295 LNILQQLqrNKMKSVLMPPmstnqecnikknkagpseqsaseqltklEWEQIIDLLWSDPRGKKGCYPNTSRGGGCYFGP 374
Cdd:smart00156 151 LTTLDDI--RKLKRPQEPP----------------------------DDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGP 200
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77917564    375 DVTSKVLNKNQLKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGAYIRLSYGTSPQFFQYQVTS 445
Cdd:smart00156 201 DAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
146-430 2.84e-37

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 141.34  E-value: 2.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  146 EARKILKQMPNFTRIQTfPAKeitICGDLHGKLDDLMLIFYKNGLPSEKNpYVFNGDFVDRGNNSMEILMILLVSFLVYP 225
Cdd:PTZ00480  43 KARDIFISQPILLELEA-PLK---ICGDVHGQYFDLLRLFEYGGYPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYP 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  226 TDLHLNRGNHEDFMMNLRYGFTKEILQKYKLhgkKILQVLEELYTWLPIGTIIDNEILVIHGGIseSTDLNILQQLQRnk 305
Cdd:PTZ00480 118 ENFFLLRGNHECASINRIYGFYDECKRRYTI---KLWKTFTDCFNCLPVAALIDEKILCMHGGL--SPELSNLEQIRR-- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  306 mksvLMPPMSTNQecnikknkagpseqsaseqlTKLeweqIIDLLWSDPRGKKGCYPNTSRGGGCYFGPDVTSKVLNKNQ 385
Cdd:PTZ00480 191 ----IMRPTDVPD--------------------TGL----LCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHE 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 77917564  386 LKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGAYIRL 430
Cdd:PTZ00480 243 LDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTI 287
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
474-636 1.09e-13

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 68.28  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 474 RKTDLINAFELRDHSRTGKISLAQWAFSMESIlglnlpWRSLSSHLVsTDSSGSVdymsSFDDIHiekpmKDMKSDLIET 553
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL------WATLFSEAD-TDGDGRI----SREEFV-----AGMESLFEAT 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 554 MyryRSDLKIIFNIIDTDQSGLISMDEFRTMWKLFNahykvhIDDSQIDELASTMDSNKDGNIDFNEFLRAfyvVHKYET 633
Cdd:COG5126  67 V---EPFARAAFDLLDTDGDGKISADEFRRLLTALG------VSEEEADELFARLDTDGDGKISFEEFVAA---VRDYYT 134

                ...
gi 77917564 634 PES 636
Cdd:COG5126 135 PDA 137
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
168-278 1.56e-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: 64.54  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564   168 ITICGDLH--GKLDDLMLIFykNGLPSEKNPYVF--NGDFVDRGNNSMEILmiLLVSFLVYPTDLHLNRGNHEDFMMNLr 243
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELL--KKLLEEGKPDLVlhAGDLVDRGPPSEEVL--ELLERLIKYVPVYLVRGNHDFDYGEC- 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 77917564   244 ygftkEILQKYKLHGKKILQVLEELYTWLPIGTII 278
Cdd:pfam00149  78 -----LRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
EF-hand_7 pfam13499
EF-hand domain pair;
558-626 6.16e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 58.42  E-value: 6.16e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 77917564   558 RSDLKIIFNIIDTDQSGLISMDEFRTMwkLFNAHYKVHIDDSQIDELASTMDSNKDGNIDFNEFLRAFY 626
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKL--LRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
560-625 7.77e-11

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: 57.94  E-value: 7.77e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77917564 560 DLKIIFNIIDTDQSGLISMDEFRTMWKLFNAHYkvhiDDSQIDELASTMDSNKDGNIDFNEFLRAF 625
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGL----SEEEIDEMIREVDKDGDGKIDFEEFLELM 62
PTZ00183 PTZ00183
centrin; Provisional
481-623 1.43e-07

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 51.23  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  481 AFELRDHSRTGKISLAQWAFSMESiLGLNLPWRSLSSHL--VSTDSSGSVDYMSSFDDIHIEKPMKDMKSDLIEtmyryr 558
Cdd:PTZ00183  22 AFDLFDTDGSGTIDPKELKVAMRS-LGFEPKKEEIKQMIadVDKDGSGKIDFEEFLDIMTKKLGERDPREEILK------ 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77917564  559 sdlkiIFNIIDTDQSGLISMDEFRTMWKLFNAHykvhIDDSQIDELASTMDSNKDGNIDFNEFLR 623
Cdd:PTZ00183  95 -----AFRLFDDDKTGKISLKNLKRVAKELGET----ITDEELQEMIDEADRNGDGEISEEEFYR 150
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
15-33 9.19e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.92  E-value: 9.19e-04
                           10
                   ....*....|....*....
gi 77917564     15 KVVRAALIIQNWYRRYRAR 33
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLAR 19
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
564-628 1.51e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 38.41  E-value: 1.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77917564    564 IFNIIDTDQSGLISMDEFRTMWklfnahYKVHIDDSQIDELASTMDSNKDGNIDFNEFLRAFYVV 628
Cdd:smart00027  15 IFRSLDKNQDGTVTGAQAKPIL------LKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLI 73
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
116-442 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: 597.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 116 PLTFTDINLLLQAFKQQQTLHAHYVLEVLFEARKILKQMPNFTRIQTFPAKEITICGDLHGKLDDLMLIFYKNGLPSEKN 195
Cdd:cd07420   1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 196 PYVFNGDFVDRGNNSMEILMILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYKLHGKKILQVLEELYTWLPIG 275
Cdd:cd07420  81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 276 TIIDNEILVIHGGISESTDLNILQQLQRNKMKSvlmppmstnqecnikknkagpseqsaseqlTKLEWEQIIDLLWSDPR 355
Cdd:cd07420 161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS------------------------------TKTEWQQVVDILWSDPK 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 356 GKKGCYPNTSRGGGCYFGPDVTSKVLNKNQLKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGAYIRLSYGTS 435
Cdd:cd07420 211 ATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLT 290

                ....*..
gi 77917564 436 PQFFQYQ 442
Cdd:cd07420 291 PHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
135-445 1.29e-108

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: 328.40  E-value: 1.29e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564    135 LHAHYVLEVLFEARKILKQMPNFTRIqtfpAKEITICGDLHGKLDDLMLIFYKNGLPSEKNpYVFNGDFVDRGNNSMEIL 214
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEV----SAPVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564    215 MILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYklhGKKILQVLEELYTWLPIGTIIDNEILVIHGGISEstD 294
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSP--D 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564    295 LNILQQLqrNKMKSVLMPPmstnqecnikknkagpseqsaseqltklEWEQIIDLLWSDPRGKKGCYPNTSRGGGCYFGP 374
Cdd:smart00156 151 LTTLDDI--RKLKRPQEPP----------------------------DDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGP 200
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77917564    375 DVTSKVLNKNQLKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGAYIRLSYGTSPQFFQYQVTS 445
Cdd:smart00156 201 DAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
108-442 2.37e-99

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: 306.11  E-value: 2.37e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 108 YDGPRLQF-PLTFTDINLLLQAFKQQQTLHAHYVLEVLFEARKILKQMPNFTRIQTFPAKEITICGDLHGKLDDLMLIFY 186
Cdd:cd07417   1 YSGPKLEDgKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 187 KNGLPSEKNPYVFNGDFVDRGNNSMEILMILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYklhGKKILQVLE 266
Cdd:cd07417  81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKY---NEQMFNLFS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 267 ELYTWLPIGTIIDNEILVIHGGI--SESTDLNILQQLQRNKmksvlMPPMStnqecnikknkaGPseqsaseqltklewe 344
Cdd:cd07417 158 EVFNWLPLAHLINGKVLVVHGGLfsDDGVTLDDIRKIDRFR-----QPPDS------------GL--------------- 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 345 qIIDLLWSDPRGKKGCYPnTSRGGGCYFGPDVTSKVLNKNQLKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNR 424
Cdd:cd07417 206 -MCELLWSDPQPQPGRGP-SKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNK 283
                       330
                ....*....|....*....
gi 77917564 425 GAYIRLSYGTS-PQFFQYQ 442
Cdd:cd07417 284 GAFIRFKGSDLkPKFTQFE 302
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
169-430 3.68e-70

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: 226.87  E-value: 3.68e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 169 TICGDLHGKLDDLMLIFYKNGLPSEKNpYVFNGDFVDRGNNSMEILMILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTK 248
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPPEDK-YLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 249 E-ILQKYKLHGKKILQVLEELYTWLPIGTIIDNEILVIHGGISEstDLNILQQLQRnkmksvlMPPMSTNQECNIKknka 327
Cdd:cd00144  80 ErTLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSP--DLTLLDQIRN-------IRPIENPDDQLVE---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 328 gpseqsaseqltkleweqiiDLLWSDPRGKKGCYPNTSRGGGCYFGPDVTSKVLNKNQLKMVIRSHECKPDGYEICHDGK 407
Cdd:cd00144 147 --------------------DLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGK 206
                       250       260
                ....*....|....*....|...
gi 77917564 408 VITVFSASNYYEEGSNRGAYIRL 430
Cdd:cd00144 207 LITIFSAPNYCGKGGNKLAALVV 229
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
142-442 3.12e-57

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: 197.71  E-value: 3.12e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 142 EVLFEARKILKQMPNFTRIQTFPAKEITICGDLHGKLDDLMLIFYKNGLPSEKNPYVFNGDFVDRGNNSMEILMILLVSF 221
Cdd:cd07418  42 SLVLTAHKILHREPNCVRIDVEDVCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWK 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 222 LVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYKLHGKKILQVLEELYTWLPIGTIIDNEILVIHGGISESTDLNILQQL 301
Cdd:cd07418 122 VLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPKRKKQ 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 302 QRNKMKSVLMPPMSTNQECNIKKNKagpseQSASEQLTKLEWE--QII--DLLWSDPRGKKGCYPNTSRGGGCYFGPDVT 377
Cdd:cd07418 202 KGKNRRVLLLEPESESLKLGTLDDL-----MKARRSVLDPPGEgsNLIpgDVLWSDPSLTPGLSPNKQRGIGLLWGPDCT 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 378 SKVLNKNQLKMVIRSHEcKPD-------------GYEICHD---GKVITVFSASNY------YEEGSNRGAYIRLSYGTS 435
Cdd:cd07418 277 EEFLEKNNLKLIIRSHE-GPDarekrpglagmnkGYTVDHDvesGKLITLFSAPDYpqfqatEERYNNKGAYIILQPPDF 355

                ....*....
gi 77917564 436 --PQFFQYQ 442
Cdd:cd07418 356 sdPQFHTFE 364
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
147-418 2.53e-55

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: 189.72  E-value: 2.53e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 147 ARKILKQMPNFTRIQTfPakeITICGDLHGKLDDLMLIFYKNGLPSEKNpYVFNGDFVDRGNNSMEILMILLVSFLVYPT 226
Cdd:cd07415  27 AKEILVKESNVQRVRS-P---VTVCGDIHGQFYDLLELFRIGGDVPDTN-YLFLGDYVDRGYYSVETFLLLLALKVRYPD 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 227 DLHLNRGNHEDFMMNLRYGFTKEILQKYKlhGKKILQVLEELYTWLPIGTIIDNEILVIHGGISESTD-LNILQQLQRNK 305
Cdd:cd07415 102 RITLLRGNHESRQITQVYGFYDECLRKYG--NANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQtLDQIRALDRFQ 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 306 mksvlMPPMStnqecnikknkaGPseqsaseqltkleweqIIDLLWSDPRGKKGCYPNtSRGGGCYFGPDVTSKVLNKNQ 385
Cdd:cd07415 180 -----EVPHE------------GP----------------MCDLLWSDPDDREGWGIS-PRGAGYLFGQDVVEEFNHNNG 225
                       250       260       270
                ....*....|....*....|....*....|...
gi 77917564 386 LKMVIRSHECKPDGYEICHDGKVITVFSASNYY 418
Cdd:cd07415 226 LTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYC 258
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
135-430 8.99e-52

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: 181.10  E-value: 8.99e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 135 LHAHYVLEVLFEARKILKQMPNFTRIQTfPAKeitICGDLHGKLDDLMLIFYKNGLPS-------EKNPYVFNGDFVDRG 207
Cdd:cd07419  21 FDCQEIAELCDEAERIFRQEPSVLRLRA-PIK---IFGDIHGQFGDLMRLFDEYGSPVteeagdiEYIDYLFLGDYVDRG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 208 NNSMEILMILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYKLH---GKKILQVLEELYTWLPIGTIIDNEILV 284
Cdd:cd07419  97 SHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDirdGDSVWQRINRLFNWLPLAALIEDKIIC 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 285 IHGGISES-TDLNILQQLQRnkmksvlmppmstnqecnikknkagPSEQSASEQLtkleweqIIDLLWSDPRGK---KGC 360
Cdd:cd07419 177 VHGGIGRSiNHIHQIENLKR-------------------------PITMEAGSPV-------VMDLLWSDPTENdsvLGL 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77917564 361 YPNT--SRGGGCY--FGPDVTSKVLNKNQLKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGAYIRL 430
Cdd:cd07419 225 RPNAidPRGTGLIvkFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVL 298
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
146-426 2.90e-47

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: 168.29  E-value: 2.90e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 146 EARKILKQMPNFTRIQTfPAKeitICGDLHGKLDDLMLIFYKNGLPSEKNpYVFNGDFVDRGNNSMEILMILLVSFLVYP 225
Cdd:cd07414  34 KSREIFLSQPILLELEA-PLK---ICGDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYP 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 226 TDLHLNRGNHEDFMMNLRYGFTKEILQKYKLhgkKILQVLEELYTWLPIGTIIDNEILVIHGGIseSTDLNILQQLQRnk 305
Cdd:cd07414 109 ENFFLLRGNHECASINRIYGFYDECKRRYNI---KLWKTFTDCFNCLPVAAIVDEKIFCCHGGL--SPDLQSMEQIRR-- 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 306 mksvlmppmstnqecnIKKnkagPSEQSASEQLTkleweqiiDLLWSDPRGKKGCYPNTSRGGGCYFGPDVTSKVLNKNQ 385
Cdd:cd07414 182 ----------------IMR----PTDVPDQGLLC--------DLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHD 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 77917564 386 LKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGA 426
Cdd:cd07414 234 LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGA 274
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
121-430 6.36e-46

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: 164.79  E-value: 6.36e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 121 DINLLLQAFKQQQTLHAHYVLEVLFEARKILKQMPNFTRIQTfpakEITICGDLHGKLDDLMLIFYKNGLPSEkNPYVFN 200
Cdd:cd07416   2 RVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEA----PVTVCGDIHGQFYDLLKLFEVGGSPAN-TRYLFL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 201 GDFVDRGNNSMEILMILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYklhGKKILQVLEELYTWLPIGTIIDN 280
Cdd:cd07416  77 GDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY---SERVYDACMEAFDCLPLAALMNQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 281 EILVIHGGIseSTDLNILQQLqrNKMKSVLMPPMStnqecnikknkaGPseqsaseqltkleweqIIDLLWSDPRGKKG- 359
Cdd:cd07416 154 QFLCVHGGL--SPELKTLDDI--RKLDRFREPPSY------------GP----------------MCDLLWSDPLEDFGn 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 360 ------CYPNTSRGGGCYFGPDVTSKVLNKNQLKMVIRSHECKPDGYEICHDGK------VITVFSASNYYEEGSNRGAY 427
Cdd:cd07416 202 ektqehFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAV 281

                ...
gi 77917564 428 IRL 430
Cdd:cd07416 282 LKY 284
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
146-430 2.84e-37

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 141.34  E-value: 2.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  146 EARKILKQMPNFTRIQTfPAKeitICGDLHGKLDDLMLIFYKNGLPSEKNpYVFNGDFVDRGNNSMEILMILLVSFLVYP 225
Cdd:PTZ00480  43 KARDIFISQPILLELEA-PLK---ICGDVHGQYFDLLRLFEYGGYPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYP 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  226 TDLHLNRGNHEDFMMNLRYGFTKEILQKYKLhgkKILQVLEELYTWLPIGTIIDNEILVIHGGIseSTDLNILQQLQRnk 305
Cdd:PTZ00480 118 ENFFLLRGNHECASINRIYGFYDECKRRYTI---KLWKTFTDCFNCLPVAALIDEKILCMHGGL--SPELSNLEQIRR-- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  306 mksvLMPPMSTNQecnikknkagpseqsaseqlTKLeweqIIDLLWSDPRGKKGCYPNTSRGGGCYFGPDVTSKVLNKNQ 385
Cdd:PTZ00480 191 ----IMRPTDVPD--------------------TGL----LCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHE 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 77917564  386 LKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGAYIRL 430
Cdd:PTZ00480 243 LDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTI 287
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
128-426 1.74e-36

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 138.50  E-value: 1.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  128 AFKQQQTLHAHYVLEVLFEARKILKQMPNFTRIQtfpaKEITICGDLHGKLDDLMLIFYKNGLPSEKNpYVFNGDFVDRG 207
Cdd:PTZ00244  18 RTQRQILIREEDIRAVLTEVREIFMSQPMLLEIR----PPVRVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  208 NNSMEILMILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYKLhgkKILQVLEELYTWLPIGTIIDNEILVIHG 287
Cdd:PTZ00244  93 KHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNI---KLFKAFTDVFNTMPVCCVISEKIICMHG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  288 GIS-ESTDLNILQQLQRnkmksvlmppmstnqECNIKKNKAgpseqsaseqltkleweqIIDLLWSDPRGKKGCYPNTSR 366
Cdd:PTZ00244 170 GLSpDLTSLASVNEIER---------------PCDVPDRGI------------------LCDLLWADPEDEVRGFLESDR 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  367 GGGCYFGPDVTSKVLNKNQLKMVIRSHECKPDGYEICHDGKVITVFSASNYYEEGSNRGA 426
Cdd:PTZ00244 217 GVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAA 276
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
121-451 2.36e-34

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 132.63  E-value: 2.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  121 DINLLLQAFKQQQTLHAHYVLEVLFEARKILKQMPNFTRIQTfpakEITICGDLHGKLDDLMLIFYKNGLPSEKNpYVFN 200
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRA----PVNVCGDIHGQFYDLQALFKEGGDIPNAN-YIFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  201 GDFVDRGNNSMEILMILLVSFLVYPTDLHLNRGNHEDFMMNLRYGFTKEILQKYKlhGKKILQVLEELYTWLPIGTIIDN 280
Cdd:PTZ00239  77 GDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYG--NSNPWRLFMDVFDCLPLAALIEG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  281 EILVIHGGIseSTDLNILQQLqRNKMKSVLMPpmstnqecnikknKAGPseqsaseqltkleweqIIDLLWSDPRGKKGC 360
Cdd:PTZ00239 155 QILCVHGGL--SPDMRTIDQI-RTIDRKIEIP-------------HEGP----------------FCDLMWSDPEEVEYW 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  361 YPNtSRGGGCYFGPDVTSKVLNKNQLKMVIRSHECKPDGYEICH-DGKVITVFSASNYYEEGSNRGAYIRLSYGTSPQF- 438
Cdd:PTZ00239 203 AVN-SRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYWFpDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWk 281
                        330
                 ....*....|....
gi 77917564  439 -FQYQVTSTSCLNP 451
Cdd:PTZ00239 282 tFKEVPESAKSINP 295
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
474-636 1.09e-13

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 68.28  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 474 RKTDLINAFELRDHSRTGKISLAQWAFSMESIlglnlpWRSLSSHLVsTDSSGSVdymsSFDDIHiekpmKDMKSDLIET 553
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL------WATLFSEAD-TDGDGRI----SREEFV-----AGMESLFEAT 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 554 MyryRSDLKIIFNIIDTDQSGLISMDEFRTMWKLFNahykvhIDDSQIDELASTMDSNKDGNIDFNEFLRAfyvVHKYET 633
Cdd:COG5126  67 V---EPFARAAFDLLDTDGDGKISADEFRRLLTALG------VSEEEADELFARLDTDGDGKISFEEFVAA---VRDYYT 134

                ...
gi 77917564 634 PES 636
Cdd:COG5126 135 PDA 137
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
168-278 1.56e-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: 64.54  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564   168 ITICGDLH--GKLDDLMLIFykNGLPSEKNPYVF--NGDFVDRGNNSMEILmiLLVSFLVYPTDLHLNRGNHEDFMMNLr 243
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELL--KKLLEEGKPDLVlhAGDLVDRGPPSEEVL--ELLERLIKYVPVYLVRGNHDFDYGEC- 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 77917564   244 ygftkEILQKYKLHGKKILQVLEELYTWLPIGTII 278
Cdd:pfam00149  78 -----LRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
EF-hand_7 pfam13499
EF-hand domain pair;
558-626 6.16e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 58.42  E-value: 6.16e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 77917564   558 RSDLKIIFNIIDTDQSGLISMDEFRTMwkLFNAHYKVHIDDSQIDELASTMDSNKDGNIDFNEFLRAFY 626
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKL--LRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
560-625 7.77e-11

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: 57.94  E-value: 7.77e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77917564 560 DLKIIFNIIDTDQSGLISMDEFRTMWKLFNAHYkvhiDDSQIDELASTMDSNKDGNIDFNEFLRAF 625
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGL----SEEEIDEMIREVDKDGDGKIDFEEFLELM 62
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
102-158 3.07e-09

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: 54.40  E-value: 3.07e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77917564   102 IDVPDSYDGPRLqfplTFTDINL-----LLQAFKQQQTLHAHYVLEVLFEARKILKQMPNFT 158
Cdd:pfam08321  34 IVVEDSYDGPRL----EDEKITLefvkdMIERFKKGKKLHKKYAYQILLKVKEILKKEPSLV 91
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
524-621 2.89e-08

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: 51.75  E-value: 2.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 524 SSGSVDYMSSFDDIHIEKpmkdmKSDlietmyryrSDLKIIFNIIDTDQSGLISMDEFRTMWKLFNAHYKvHIDDSQIDE 603
Cdd:cd16254  13 AADSFDYKKFFEMVGLKK-----KSA---------DDVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGR-DLSDKETKA 77
                        90
                ....*....|....*...
gi 77917564 604 LASTMDSNKDGNIDFNEF 621
Cdd:cd16254  78 LLAAGDKDGDGKIGIDEF 95
PTZ00183 PTZ00183
centrin; Provisional
481-623 1.43e-07

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 51.23  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  481 AFELRDHSRTGKISLAQWAFSMESiLGLNLPWRSLSSHL--VSTDSSGSVDYMSSFDDIHIEKPMKDMKSDLIEtmyryr 558
Cdd:PTZ00183  22 AFDLFDTDGSGTIDPKELKVAMRS-LGFEPKKEEIKQMIadVDKDGSGKIDFEEFLDIMTKKLGERDPREEILK------ 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77917564  559 sdlkiIFNIIDTDQSGLISMDEFRTMWKLFNAHykvhIDDSQIDELASTMDSNKDGNIDFNEFLR 623
Cdd:PTZ00183  95 -----AFRLFDDDKTGKISLKNLKRVAKELGET----ITDEELQEMIDEADRNGDGEISEEEFYR 150
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
526-621 2.77e-06

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: 46.37  E-value: 2.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 526 GSVDYMSSFDDIHIEKpmkdmKSDlietmyryrSDLKIIFNIIDTDQSGLISMDEFRTMWKLFNAHYKVhIDDSQIDELA 605
Cdd:cd16251  15 GSFNYKKFFEHVGLKQ-----KSE---------DQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGRD-LTDEETKALL 79
                        90
                ....*....|....*.
gi 77917564 606 STMDSNKDGNIDFNEF 621
Cdd:cd16251  80 AAGDTDGDGKIGVEEF 95
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
519-621 2.94e-06

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: 46.01  E-value: 2.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 519 LVSTDSSGSVDYMSSFDDIHIEKpmkdmKSDlietmyryrSDLKIIFNIIDTDQSGLISMDEFRTMWKLFNAHYKVhIDD 598
Cdd:cd16253   8 LAACQAADSFDHKAFFKAVGLSK-----KSP---------ADIKKVFNILDQDKSGFIEEEELKLFLKNFSDGARV-LSD 72
                        90       100
                ....*....|....*....|...
gi 77917564 599 SQIDELASTMDSNKDGNIDFNEF 621
Cdd:cd16253  73 KETKNFLAAGDSDGDGKIGVDEF 95
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
560-621 5.26e-06

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: 45.49  E-value: 5.26e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77917564 560 DLKIIFNIIDTDQSGLISMDEFRTMWKLFNAHYKVhIDDSQIDELASTMDSNKDGNIDFNEF 621
Cdd:cd16255  35 DVKKVFEIIDQDKSGFIEEEELKLFLQNFSSGARE-LTDAETKAFLKAGDSDGDGKIGVEEF 95
PTZ00184 PTZ00184
calmodulin; Provisional
481-623 9.09e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 45.91  E-value: 9.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  481 AFELRDHSRTGKISLAQWAFSMESiLGLNLPWRSLSSHL--VSTDSSGSVDYMSSFddIHIEKPMKDMKSDlietmyryr 558
Cdd:PTZ00184  16 AFSLFDKDGDGTITTKELGTVMRS-LGQNPTEAELQDMIneVDADGNGTIDFPEFL--TLMARKMKDTDSE--------- 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77917564  559 SDLKIIFNIIDTDQSGLISMDEFRTMwkLFNAHYKvhIDDSQIDELASTMDSNKDGNIDFNEFLR 623
Cdd:PTZ00184  84 EEIKEAFKVFDRDGNGFISAAELRHV--MTNLGEK--LTDEEVDEMIREADVDGDGQINYEEFVK 144
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
569-623 3.20e-05

EF-hand, calcium binding motif, found in secretagogin (SCGN); 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 calcium sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. It also serves as a calcium buffer in neurons. Thus, SCGN may be linked to the pathogenesis of neurological diseases such as Alzheimer's, and also acts as a serum marker of neuronal damage, or as a tumor biomarker. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. All six EF hand motifs of SCGN in some eukaryotes, including D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, could potentially bind six calcium ions. In contrast, SCGNs from higher eukaryotes have at least one non-functional EF-hand motif due to the mutation(s) or deletions. For instance, the EF1 loop does not coordinate calcium ion due to the key residue asparagine replaced by lysine in SCGNs of many mammalian species. Moreover, the EF2 loop seems to be competent for calcium-binding in most mammalian SCGNs except for human and chimpanzee orthologs.


Pssm-ID: 320078 [Multi-domain]  Cd Length: 257  Bit Score: 45.86  E-value: 3.20e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 569 DTDQSGLISMDEFRTMWK-LFNAHYKVhIDDSQIDELASTM----DSNKDGNIDFNEFLR 623
Cdd:cd16178 102 DADSSGYISAAELKNFLRdLFLQHKKV-ITEDKLDEYTDTMmkifDKNKDGRLDLNDMAR 160
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
561-625 5.59e-05

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: 43.43  E-value: 5.59e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77917564 561 LKIIFNIIDTDQSGLISMDEFRTMWKLFNahykVHIDDSQIDELASTMDSNKDGNIDFNEFLRAF 625
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIKKLLKRLN----IRVSEKELKKLFKEVDTNGDGTLTFDEFEELY 62
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
172-290 6.42e-05

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: 44.60  E-value: 6.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 172 GDLHGKLDDLMLIFYKNGLPSEKNPYVFN-------GDFVDRGNNSMEIlMILLVSflVYP------TDLHLNRGNHEdf 238
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIEI-LKLLEK--LKRqarkagGKVILLLGNHE-- 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77917564 239 MMNL----RY-------GFTKEILQKYKLHGKKilqvlEELYTWL-PIGTIID-NEILVIHGGIS 290
Cdd:cd07425  79 LMNLcgdfRYvhprglnEFGGVAKRRYALLSDG-----GYIGRYLrTHPVVLVvNDILFVHGGLG 138
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
565-631 1.37e-04

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: 42.97  E-value: 1.37e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77917564 565 FNIIDTDQSGLISMDEFRTMwklfNAHYKVHIDDSQIDELASTMDSNKDGNIDFNEFLRafyvVHKY 631
Cdd:cd16185   6 FRAVDRDRSGSIDVNELQKA----LAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAA----LHQF 64
EF-hand_8 pfam13833
EF-hand domain pair;
572-626 2.21e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 39.22  E-value: 2.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 77917564   572 QSGLISMDEFRTMWKLFNahyKVHIDDSQIDELASTMDSNKDGNIDFNEFLRAFY 626
Cdd:pfam13833   1 EKGVITREELKRALALLG---LKDLSEDEVDILFREFDTDGDGYISFDEFCVLLE 52
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
170-236 3.37e-04

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: 41.10  E-value: 3.37e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 170 ICGDLHGKLDDLMLIFYKNgLPSEKNP--YVFNGDFVDRGN-NSMEILMILLVSFLVYPTdlHLNRGNHE 236
Cdd:cd00838   2 VISDIHGNLEALEAVLEAA-LAKAEKPdlVICLGDLVDYGPdPEEVELKALRLLLAGIPV--YVVPGNHD 68
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
564-628 4.60e-04

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: 38.74  E-value: 4.60e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77917564 564 IFNIIDTDQSGLISMDEFRTMWKLFNAHYKVHiddSQIDELAstmDSNKDGNIDFNEFLRAFYVV 628
Cdd:cd00052   4 IFRSLDPDGDGLISGDEARPFLGKSGLPRSVL---AQIWDLA---DTDKDGKLDKEEFAIAMHLI 62
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
561-626 5.99e-04

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 42.19  E-value: 5.99e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77917564 561 LKIIFNIIDTDQSGLISMDEFRTmWKLFNAhyKVHIDDSqIDELASTMDSNKDGNIDFNEFLRAFY 626
Cdd:cd16226  37 LGIIVDKIDKNGDGFVTEEELKD-WIKYVQ--KKYIRED-VDRQWKEYDPNKDGKLSWEEYKKATY 98
PLN02964 PLN02964
phosphatidylserine decarboxylase
549-634 7.07e-04

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 7.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  549 DLIETMYRYrsdLKIIFNIIDTDQSGLISMDEFRTMWKLFNAhykvHIDDSQIDELASTMDSNKDGNIDFNEfLRAFYVV 628
Cdd:PLN02964 172 DPVETERSF---ARRILAIVDYDEDGQLSFSEFSDLIKAFGN----LVAANKKEELFKAADLNGDGVVTIDE-LAALLAL 243

                 ....*.
gi 77917564  629 HKYETP 634
Cdd:PLN02964 244 QQEQEP 249
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
564-623 9.14e-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: 41.57  E-value: 9.14e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77917564 564 IFNIIDTDQSGLISMDEFRTMWKLFNAHYKVHIDDSQIDELASTM----DSNKDGNIDFNEFLR 623
Cdd:cd15902  95 IWRKYDTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLIlkefDANKDGKLELDEMAK 158
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
15-33 9.19e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.92  E-value: 9.19e-04
                           10
                   ....*....|....*....
gi 77917564     15 KVVRAALIIQNWYRRYRAR 33
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLAR 19
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
560-588 1.28e-03

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: 36.61  E-value: 1.28e-03
                          10        20
                  ....*....|....*....|....*....
gi 77917564   560 DLKIIFNIIDTDQSGLISMDEFRTMWKLF 588
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
ASKHA_NBD_ROK_FnNanK-like cd24068
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ...
248-328 1.35e-03

nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and similar proteins; The family includes Fusobacterium nucleatum N-acetylmannosamine kinase (NanK; EC 2.7.1.60) and beta-glucoside kinase (BglK; EC 2.7.1.85) from Klebsiella pneumoniae and Listeria innocua. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. BglK catalyzes the ATP-dependent phosphorylation of cellobiose to produce cellobiose-6'-P. It may have a dual role of kinase and transcriptional regulator of the cellobiose-PTS operon. The subfamily belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.


Pssm-ID: 466918 [Multi-domain]  Cd Length: 294  Bit Score: 41.00  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 248 KEILQKYKLHGKKILQVLEELYTWLPIG-----TIIDNEILVIHGGISESTDLnILQQLqRNKMKSVLMPPMstNQECNI 322
Cdd:cd24068 202 REIFDLADAGDPLAKEVVEEFAEDLATGlanlvHIFDPEVIVIGGGISAQGEL-FLEEL-REELRKLLMPPL--LDATKI 277
                        90
                ....*....|
gi 77917564 323 K----KNKAG 328
Cdd:cd24068 278 EpaklGNDAG 287
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
564-628 1.51e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 38.41  E-value: 1.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77917564    564 IFNIIDTDQSGLISMDEFRTMWklfnahYKVHIDDSQIDELASTMDSNKDGNIDFNEFLRAFYVV 628
Cdd:smart00027  15 IFRSLDKNQDGTVTGAQAKPIL------LKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLI 73
PHA02239 PHA02239
putative protein phosphatase
168-242 1.98e-03

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 40.36  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564  168 ITICGDLHGKLDDLMLIFykNGLPSEKNP---YVFNGDFVDRGNNSMEILMILLvsflvyptDLHLNR-------GNHED 237
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIM--DKINNERKPeetIVFLGDYVDRGKRSKDVVNYIF--------DLMSNDdnvvtllGNHDD 72

                 ....*
gi 77917564  238 FMMNL 242
Cdd:PHA02239  73 EFYNI 77
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
172-241 2.46e-03

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: 39.61  E-value: 2.46e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 172 GDLHGKLDDLMLIFYKNGLPSEKNPYVFNGDFVDRGNNSMEILMILLVSFlvyptdLHLNRGNHEDFMMN 241
Cdd:cd07424   7 GDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPW------FHAVQGNHEQMAID 70
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
562-626 3.10e-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: 38.66  E-value: 3.10e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 77917564 562 KIIFNIIDTDQSGLISMDEFRTMWKlfnahykvHIDDSQidELASTMDSNKDGNIDFNEFLRAFY 626
Cdd:cd16180  40 RLMINMFDRDRSGTINFDEFVGLWK--------YIQDWR--RLFRRFDRDRSGSIDFNELQNALS 94
EF-hand_5 pfam13202
EF hand;
561-585 3.31e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 35.37  E-value: 3.31e-03
                          10        20
                  ....*....|....*....|....*
gi 77917564   561 LKIIFNIIDTDQSGLISMDEFRTMW 585
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
563-623 3.95e-03

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 38.36  E-value: 3.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77917564 563 IIFNIIDTDQSGLISMDEFRTMWKLF---NAHYKVHIDDSQIDELASTMDSN-------KDGN--IDFNEFLR 623
Cdd:cd15900   4 IAFKMFDLDGDGELDKEEFNKVQSIIrsqTSVGQRHRDHTNGESTKLGMNSTlaryffgKDGKqkLSIEKFLE 76
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
543-622 5.70e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 39.22  E-value: 5.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917564 543 MKDMKSDLIETMYRYRSDLKIIFNIIDTDQSGLISMDEFRtmwKLFNAHYKVHIDDSQIDELASTMDSNKDGNIDFNEFL 622
Cdd:cd16227 106 NEEMIKDSTEDDLKLLEDDKEMFEAADLNKDGKLDKTEFS---AFQHPEEYPHMHPVLIEQTLRDKDKDNDGFISFQEFL 182
EF-hand_6 pfam13405
EF-hand domain;
560-589 6.36e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.46  E-value: 6.36e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 77917564   560 DLKIIFNIIDTDQSGLISMDEFRTMWKLFN 589
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
 
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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