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Conserved domains on  [gi|23312378|ref|NP_689412|]
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serine/threonine-protein phosphatase with EF-hands 1 isoform 3 [Homo sapiens]

Protein Classification

IQCD and EF-hand_7 domain-containing protein( domain architecture ID 12184142)

protein containing domains IQCD, MPP_superfamily, and EF-hand_7

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 115-390 3.07e-159

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.


The actual alignment was detected with superfamily member cd07420:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 297  Bit Score: 457.26  E-value: 3.07e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 115 PLTCTDIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQTSPSKEVTICGDLHGKLDDLFLIFYKNGLPSERN 194
Cdd:cd07420   1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 195 PYVFNGDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKLHGKRILQILEEFYAWLPIG 274
Cdd:cd07420  81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 275 TIVDNEILVIHGGISETTDLNLLHRVERNKMKSVlipPTETNRDHD---TDSKHNKvGVTFNAhgrIKTNGS---P--TE 346
Cdd:cd07420 161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVST---KTEWQQVVDilwSDPKATK-GCKPNT---FRGGGCyfgPdvTS 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23312378 347 HLTE----------HEWE----------QVVTIFSASNYYEEGSNRGAYIKLCSGTTPRFFQYQ 390
Cdd:cd07420 234 QFLQkhglsllirsHECKpegyefchnnKVITIFSASNYYEEGSNRGAYVKLGPQLTPHFVQYQ 297
EF-hand_7 pfam13499
EF-hand domain pair;
506-574 8.26e-13

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 63.43  E-value: 8.26e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23312378   506 RSDLEIIFNAIDTDHSGLISVEEFRAMwkLFSSHYNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAFY 574
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKL--LRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
425-573 6.67e-12

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 63.27  E-value: 6.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 425 DLTRAFQLQDHRKSGKLSVSQWAFCMENIlglnlpWRSLSSNLvniDQNGNveymssfQNIRIEKPVQEAHSTLVETLyr 504
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRL------WATLFSEA---DTDGD-------GRISREEFVAGMESLFEATV-- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23312378 505 yRSDLEIIFNAIDTDHSGLISVEEFRAMWKlfsshyNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAF 573
Cdd:COG5126  68 -EPFARAAFDLLDTDGDGKISADEFRRLLT------ALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 18-37 9.01e-05

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 39.62  E-value: 9.01e-05
                           10        20
                   ....*....|....*....|
gi 23312378     18 RAALIIQNWYRGYKARLKAR 37
Cdd:smart00015   4 RAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 115-390 3.07e-159

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: 457.26  E-value: 3.07e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 115 PLTCTDIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQTSPSKEVTICGDLHGKLDDLFLIFYKNGLPSERN 194
Cdd:cd07420   1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 195 PYVFNGDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKLHGKRILQILEEFYAWLPIG 274
Cdd:cd07420  81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 275 TIVDNEILVIHGGISETTDLNLLHRVERNKMKSVlipPTETNRDHD---TDSKHNKvGVTFNAhgrIKTNGS---P--TE 346
Cdd:cd07420 161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVST---KTEWQQVVDilwSDPKATK-GCKPNT---FRGGGCyfgPdvTS 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23312378 347 HLTE----------HEWE----------QVVTIFSASNYYEEGSNRGAYIKLCSGTTPRFFQYQ 390
Cdd:cd07420 234 QFLQkhglsllirsHECKpegyefchnnKVITIFSASNYYEEGSNRGAYVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 134-393 4.52e-77

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: 245.20  E-value: 4.52e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378    134 LHAHYVLEVLFETKKVLKQMPNFTHIqtspSKEVTICGDLHGKLDDLFLIFYKNGLPSErNPYVFNGDFVDRGKNSIEIL 213
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEV----SAPVTVCGDIHGQFDDLLRLFDKNGQPPE-TNYVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378    214 MILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYklhGKRILQILEEFYAWLPIGTIVDNEILVIHGGISEttD 293
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSP--D 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378    294 LNLLHRVERNKmKSVLIPPTETNRD---HDTDSKHNkvGVTFNAHGRIKTNGSP--TEHLTE----------------HE 352
Cdd:smart00156 151 LTTLDDIRKLK-RPQEPPDDGLLIDllwSDPDQPVN--GFGPSIRGASYIFGPDavDEFLKKnnlkliirahqvvddgYE 227

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 23312378    353 WE---QVVTIFSASNYYEEGSNRGAYIKLCSGTTPRFFQYQVTK 393
Cdd:smart00156 228 FFadgKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 120-289 1.55e-24

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 104.13  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378  120 DIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQtSPskeVTICGDLHGKLDDLFLIFYKNGLPSERNpYVFN 199
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVR-AP---VNVCGDIHGQFYDLQALFKEGGDIPNAN-YIFI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378  200 GDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKlhGKRILQILEEFYAWLPIGTIVDN 279
Cdd:PTZ00239  77 GDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYG--NSNPWRLFMDVFDCLPLAALIEG 154

                        170
                 ....*....|
gi 23312378  280 EILVIHGGIS 289
Cdd:PTZ00239 155 QILCVHGGLS 164
EF-hand_7 pfam13499
EF-hand domain pair;
506-574 8.26e-13

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 63.43  E-value: 8.26e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23312378   506 RSDLEIIFNAIDTDHSGLISVEEFRAMwkLFSSHYNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAFY 574
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKL--LRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
425-573 6.67e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 63.27  E-value: 6.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 425 DLTRAFQLQDHRKSGKLSVSQWAFCMENIlglnlpWRSLSSNLvniDQNGNveymssfQNIRIEKPVQEAHSTLVETLyr 504
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRL------WATLFSEA---DTDGD-------GRISREEFVAGMESLFEATV-- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23312378 505 yRSDLEIIFNAIDTDHSGLISVEEFRAMWKlfsshyNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAF 573
Cdd:COG5126  68 -EPFARAAFDLLDTDGDGKISADEFRRLLT------ALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 508-573 6.88e-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: 6.88e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23312378 508 DLEIIFNAIDTDHSGLISVEEFRAMWKLFSSHYnvhiDDSQVNKLANIMDLNKDGSIDFNEFLKAF 573
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGL----SEEEIDEMIREVDKDGDGKIDFEEFLELM 62
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 167-277 3.81e-09

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 54.53  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378   167 VTICGDLH--GKLDDLFLIFykNGLPSERNPYVF--NGDFVDRGKNSIEILMILCvsFLVYPNDLHLNRGNHEDFMMNLr 242
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELL--KKLLEEGKPDLVlhAGDLVDRGPPSEEVLELLE--RLIKYVPVYLVRGNHDFDYGEC- 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 23312378   243 ygftkEILHKYKLHGKRILQILEEFYAWLPIGTIV 277
Cdd:pfam00149  78 -----LRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 512-578 2.69e-05

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: 43.03  E-value: 2.69e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23312378    512 IFNAIDTDHSGLISVEEFRAMWklfsshYNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAFYVVHR 578
Cdd:smart00027  15 IFRSLDKNQDGTVTGAQAKPIL------LKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYR 75
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
506-587 4.89e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.63  E-value: 4.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 506 RSDLEIIFNAIDTDHSGLISVEEFRAMWklfsshynvhidDSQVNKLANIMDLNKDGSIDFNEFLKafYVVHRYEDLMKP 585
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEALF------------RRLWATLFSEADTDGDGRISREEFVA--GMESLFEATVEP 69


                ..
gi 23312378 586 DV 587
Cdd:COG5126  70 FA 71
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 18-37 9.01e-05

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 39.62  E-value: 9.01e-05
                           10        20
                   ....*....|....*....|
gi 23312378     18 RAALIIQNWYRGYKARLKAR 37
Cdd:smart00015   4 RAAIIIQAAWRGYLARKRYK 23
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 18-37 5.88e-04

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


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 37.52  E-value: 5.88e-04
                        10        20
                ....*....|....*....|
gi 23312378  18 RAALIIQNWYRGYKARLKAR 37
Cdd:cd23767  10 RAATLIQALWRGYKVRKELK 29
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 18-37 5.48e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.60  E-value: 5.48e-03
                          10        20
                  ....*....|....*....|
gi 23312378    18 RAALIIQNWYRGYKARLKAR 37
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRYK 21
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 115-390 3.07e-159

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: 457.26  E-value: 3.07e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 115 PLTCTDIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQTSPSKEVTICGDLHGKLDDLFLIFYKNGLPSERN 194
Cdd:cd07420   1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 195 PYVFNGDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKLHGKRILQILEEFYAWLPIG 274
Cdd:cd07420  81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 275 TIVDNEILVIHGGISETTDLNLLHRVERNKMKSVlipPTETNRDHD---TDSKHNKvGVTFNAhgrIKTNGS---P--TE 346
Cdd:cd07420 161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVST---KTEWQQVVDilwSDPKATK-GCKPNT---FRGGGCyfgPdvTS 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23312378 347 HLTE----------HEWE----------QVVTIFSASNYYEEGSNRGAYIKLCSGTTPRFFQYQ 390
Cdd:cd07420 234 QFLQkhglsllirsHECKpegyefchnnKVITIFSASNYYEEGSNRGAYVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 134-393 4.52e-77

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: 245.20  E-value: 4.52e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378    134 LHAHYVLEVLFETKKVLKQMPNFTHIqtspSKEVTICGDLHGKLDDLFLIFYKNGLPSErNPYVFNGDFVDRGKNSIEIL 213
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEV----SAPVTVCGDIHGQFDDLLRLFDKNGQPPE-TNYVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378    214 MILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYklhGKRILQILEEFYAWLPIGTIVDNEILVIHGGISEttD 293
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSP--D 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378    294 LNLLHRVERNKmKSVLIPPTETNRD---HDTDSKHNkvGVTFNAHGRIKTNGSP--TEHLTE----------------HE 352
Cdd:smart00156 151 LTTLDDIRKLK-RPQEPPDDGLLIDllwSDPDQPVN--GFGPSIRGASYIFGPDavDEFLKKnnlkliirahqvvddgYE 227

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 23312378    353 WE---QVVTIFSASNYYEEGSNRGAYIKLCSGTTPRFFQYQVTK 393
Cdd:smart00156 228 FFadgKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 107-390 2.05e-61

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: 205.95  E-value: 2.05e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 107 YNGPRLQF-PLTCTDIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQTSPSKEVTICGDLHGKLDDLFLIFY 185
Cdd:cd07417   1 YSGPKLEDgKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 186 KNGLPSERNPYVFNGDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYklhGKRILQILE 265
Cdd:cd07417  81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKY---NEQMFNLFS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 266 EFYAWLPIGTIVDNEILVIHGGI--SETTDLNLLHRVERNK-------MKSVLI--PPTETNRdhdTDSK---------- 324
Cdd:cd07417 158 EVFNWLPLAHLINGKVLVVHGGLfsDDGVTLDDIRKIDRFRqppdsglMCELLWsdPQPQPGR---GPSKrgvgcqfgpd 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23312378 325 -------HNKVGVTFNAHgRIKTNGSPTEHLTeheweQVVTIFSASNYYEEGSNRGAYIKLCSGT-TPRFFQYQ 390
Cdd:cd07417 235 vtkrfleENNLDYIIRSH-EVKDEGYEVEHDG-----KCITVFSAPNYCDQMGNKGAFIRFKGSDlKPKFTQFE 302
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 168-378 7.83e-40

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: 145.21  E-value: 7.83e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 168 TICGDLHGKLDDLFLIFYKNGLPSERNpYVFNGDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTK 247
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPPEDK-YLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 248 E-ILHKYKLHGKRILQILEEFYAWLPIGTIVDNEILVIHGGIS---ETTDLNLLHRVERNKMKSVLIP-----PTETNRd 318
Cdd:cd00144  80 ErTLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSpdlTLLDQIRNIRPIENPDDQLVEDllwsdPDESVG- 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23312378 319 hDTDSKHNKVGVTFNAHGRIKTNGSPTEHL--TEHEWEQ----------VVTIFSASNYYEEGSNRGAYIKL 378
Cdd:cd00144 159 -DFESSSRGGGYLFGEDAVDEFLKKNGLKLivRGHTPVEggyeflhggkLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 120-289 2.03e-30

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: 120.77  E-value: 2.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 120 DIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQtSPskeVTICGDLHGKLDDLFLIFYKNGLPSERNpYVFN 199
Cdd:cd07415   1 DLDQWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVR-SP---VTVCGDIHGQFYDLLELFRIGGDVPDTN-YLFL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 200 GDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKlhGKRILQILEEFYAWLPIGTIVDN 279
Cdd:cd07415  76 GDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYG--NANVWKYFTDLFDYLPLAALIDG 153

                       170
                ....*....|
gi 23312378 280 EILVIHGGIS 289
Cdd:cd07415 154 QIFCVHGGLS 163
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 145-374 3.46e-30

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: 120.14  E-value: 3.46e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 145 ETKKVLKQMPNFTHIQTSpskeVTICGDLHGKLDDLFLIFYKNGLPSERNpYVFNGDFVDRGKNSIEILMILCVSFLVYP 224
Cdd:cd07414  34 KSREIFLSQPILLELEAP----LKICGDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYP 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 225 NDLHLNRGNHEDFMMNLRYGFTKEILHKYKLhgkRILQILEEFYAWLPIGTIVDNEILVIHGGIS-ETTDLNLLHRVERn 303
Cdd:cd07414 109 ENFFLLRGNHECASINRIYGFYDECKRRYNI---KLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSpDLQSMEQIRRIMR- 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 304 kmksvlipPTETN----------RDHDTDSK---HNKVGVTFNAHGRIKtngspTEHLTEHEWE---------------- 354
Cdd:cd07414 185 --------PTDVPdqgllcdllwSDPDKDVQgwgENDRGVSFTFGADVV-----AKFLHKHDLDlicrahqvvedgyeff 251

                       250       260
                ....*....|....*....|...
gi 23312378 355 ---QVVTIFSASNYYEEGSNRGA 374
Cdd:cd07414 252 akrQLVTLFSAPNYCGEFDNAGA 274
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 120-378 1.57e-29

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: 118.56  E-value: 1.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 120 DIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQTSpskeVTICGDLHGKLDDLFLIFYKNGLPSErNPYVFN 199
Cdd:cd07416   2 RVDILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIEAP----VTVCGDIHGQFYDLLKLFEVGGSPAN-TRYLFL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 200 GDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYklhGKRILQILEEFYAWLPIGTIVDN 279
Cdd:cd07416  77 GDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY---SERVYDACMEAFDCLPLAALMNQ 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 280 EILVIHGGIS-ETTDLNLLHRVERNKMksvliPPT---------------ETNRDHDTDSKHNKV-GVTFN--------- 333
Cdd:cd07416 154 QFLCVHGGLSpELKTLDDIRKLDRFRE-----PPSygpmcdllwsdpledFGNEKTQEHFVHNTVrGCSYFysyravcef 228

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23312378 334 -----------AHG----------RIKTNGSPTehlteheweqVVTIFSASNYYEEGSNRGAYIKL 378
Cdd:cd07416 229 lqknnllsiirAHEaqdagyrmyrKSQTTGFPS----------LITIFSAPNYLDVYNNKAAVLKY 284
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 148-316 1.15e-28

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: 117.59  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 148 KVLKQMPNFTHIQTSPSKEVTICGDLHGKLDDLFLIFYKNGLPSERNPYVFNGDFVDRGKNSIEILMILCVSFLVYPNDL 227
Cdd:cd07418  49 KILHREPNCVRIDVEDVCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRV 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 228 HLNRGNHEDFMMNLRYGFTKEILHKYKLHGKRILQILEEFYAWLPIGTIVDNEILVIHGGISETTDLNLLHRVERNKMKS 307
Cdd:cd07418 129 YLLRGNHESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPKRKKQKGKNRRV 208


                ....*....
gi 23312378 308 VLIPPTETN 316
Cdd:cd07418 209 LLLEPESES 217
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 133-378 8.13e-25

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: 105.22  E-value: 8.13e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 133 ILHAHYVLEVLFETKKVLKQMPNFTHIQtSPSKevtICGDLHGKLDDLFLIFYKNGLPS-------ERNPYVFNGDFVDR 205
Cdd:cd07419  20 FFDCQEIAELCDEAERIFRQEPSVLRLR-APIK---IFGDIHGQFGDLMRLFDEYGSPVteeagdiEYIDYLFLGDYVDR 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 206 GKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKLH---GKRILQILEEFYAWLPIGTIVDNEIL 282
Cdd:cd07419  96 GSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGEDirdGDSVWQRINRLFNWLPLAALIEDKII 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 283 VIHGGISETtdLNLLHRVERNKMKSVLIP------------PTETN-----RDHDTDSKHNKVGVTFN---AHGRIKTNG 342
Cdd:cd07419 176 CVHGGIGRS--INHIHQIENLKRPITMEAgspvvmdllwsdPTENDsvlglRPNAIDPRGTGLIVKFGpdrVMEFLEEND 253

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23312378 343 SPTEhLTEHE-----WEQ-----VVTIFSASNYYEEGSNRGAYIKL 378
Cdd:cd07419 254 LQMI-IRAHEcvmdgFERfaqghLITLFSATNYCGTAGNAGAILVL 298
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 120-289 1.55e-24

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 104.13  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378  120 DIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQtSPskeVTICGDLHGKLDDLFLIFYKNGLPSERNpYVFN 199
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVR-AP---VNVCGDIHGQFYDLQALFKEGGDIPNAN-YIFI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378  200 GDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKlhGKRILQILEEFYAWLPIGTIVDN 279
Cdd:PTZ00239  77 GDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYG--NSNPWRLFMDVFDCLPLAALIEG 154

                        170
                 ....*....|
gi 23312378  280 EILVIHGGIS 289
Cdd:PTZ00239 155 QILCVHGGLS 164
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 114-302 1.82e-24

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 103.83  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378  114 FPLTCTDIDLLL----EAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQTSpskeVTICGDLHGKLDDLFLIFYKNGL 189
Cdd:PTZ00244   1 MSLVQTLIEKMLtvkgNRTQRQILIREEDIRAVLTEVREIFMSQPMLLEIRPP----VRVCGDTHGQYYDLLRIFEKCGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378  190 PSERNpYVFNGDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKLhgkRILQILEEFYA 269
Cdd:PTZ00244  77 PPYSN-YLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNI---KLFKAFTDVFN 152

                        170       180       190
                 ....*....|....*....|....*....|....
gi 23312378  270 WLPIGTIVDNEILVIHGGIS-ETTDLNLLHRVER 302
Cdd:PTZ00244 153 TMPVCCVISEKIICMHGGLSpDLTSLASVNEIER 186
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 167-378 3.28e-24

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 103.59  E-value: 3.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378  167 VTICGDLHGKLDDLFLIFYKNGLPSERNpYVFNGDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFT 246
Cdd:PTZ00480  61 LKICGDVHGQYFDLLRLFEYGGYPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378  247 KEILHKYKLhgkRILQILEEFYAWLPIGTIVDNEILVIHGGIS-ETTDLNLLHRVernkMKSVLIPPTE-------TNRD 318
Cdd:PTZ00480 140 DECKRRYTI---KLWKTFTDCFNCLPVAALIDEKILCMHGGLSpELSNLEQIRRI----MRPTDVPDTGllcdllwSDPD 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378  319 HDTDS-KHNKVGVTFnahgrIKTNGSPTEHLTEHEWE-------------------QVVTIFSASNYYEEGSNRGAYIKL 378
Cdd:PTZ00480 213 KDVQGwADNERGVSY-----VFSQEIVQVFLKKHELDlicrahqvvedgyeffskrQLVTLFSAPNYCGEFDNAGSMMTI 287
EF-hand_7 pfam13499
EF-hand domain pair;
506-574 8.26e-13

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 63.43  E-value: 8.26e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23312378   506 RSDLEIIFNAIDTDHSGLISVEEFRAMwkLFSSHYNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAFY 574
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKL--LRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
425-573 6.67e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 63.27  E-value: 6.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 425 DLTRAFQLQDHRKSGKLSVSQWAFCMENIlglnlpWRSLSSNLvniDQNGNveymssfQNIRIEKPVQEAHSTLVETLyr 504
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRL------WATLFSEA---DTDGD-------GRISREEFVAGMESLFEATV-- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23312378 505 yRSDLEIIFNAIDTDHSGLISVEEFRAMWKlfsshyNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAF 573
Cdd:COG5126  68 -EPFARAAFDLLDTDGDGKISADEFRRLLT------ALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 508-573 6.88e-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: 6.88e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23312378 508 DLEIIFNAIDTDHSGLISVEEFRAMWKLFSSHYnvhiDDSQVNKLANIMDLNKDGSIDFNEFLKAF 573
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGL----SEEEIDEMIREVDKDGDGKIDFEEFLELM 62
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 167-277 3.81e-09

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 54.53  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378   167 VTICGDLH--GKLDDLFLIFykNGLPSERNPYVF--NGDFVDRGKNSIEILMILCvsFLVYPNDLHLNRGNHEDFMMNLr 242
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELL--KKLLEEGKPDLVlhAGDLVDRGPPSEEVLELLE--RLIKYVPVYLVRGNHDFDYGEC- 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 23312378   243 ygftkEILHKYKLHGKRILQILEEFYAWLPIGTIV 277
Cdd:pfam00149  78 -----LRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 98-157 2.25e-08

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: 51.71  E-value: 2.25e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23312378    98 VDSIDVPDSYNGPRLQF-PLTCTDIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFT 157
Cdd:pfam08321  31 LESIVVEDSYDGPRLEDeKITLEFVKDMIERFKKGKKLHKKYAYQILLKVKEILKKEPSLV 91
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 513-579 6.65e-08

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: 52.22  E-value: 6.65e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23312378 513 FNAIDTDHSGLISVEEFRAMwklfSSHYNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKafyvVHRY 579
Cdd:cd16185   6 FRAVDRDRSGSIDVNELQKA----LAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAA----LHQF 64
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 171-289 2.81e-06

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: 48.45  E-value: 2.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 171 GDLHGKLDDLFLIFYKNGLPSERNPYVFN-------GDFVDRGKNSIEILmilcvsFLVYPND---------LHLNRGNH 234
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIEIL------KLLEKLKrqarkaggkVILLLGNH 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23312378 235 EdfMMNL----RY-------GFTKEILHKYKLHGKR--ILQILEEFYAwlpigTIVDNEILVIHGGIS 289
Cdd:cd07425  78 E--LMNLcgdfRYvhprglnEFGGVAKRRYALLSDGgyIGRYLRTHPV-----VLVVNDILFVHGGLG 138
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
425-534 5.75e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.32  E-value: 5.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 425 DLTRAFQLQDHRKSGKLSVSQWAFCMENILGLNLPwRSLSSNLVNIDQNGN-----VEYMSSFQNIRIEkpvqeahstlv 499
Cdd:COG5126  34 LWATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDgkisaDEFRRLLTALGVS----------- 101

                        90       100       110
                ....*....|....*....|....*....|....*
gi 23312378 500 etlyryRSDLEIIFNAIDTDHSGLISVEEFRAMWK 534
Cdd:COG5126 102 ------EEEADELFARLDTDGDGKISFEEFVAAVR 130
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 512-569 7.27e-06

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: 46.37  E-value: 7.27e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23312378 512 IFNAIDTDHSGLISVEEFRAmwkLFSSHYNVHIDDSQVNKLANIMDLNKDGSIDFNEF 569
Cdd:cd16180   5 IFQAVDRDRSGRISAKELQR---ALSNGDWTPFSIETVRLMINMFDRDRSGTINFDEF 59
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 512-578 2.69e-05

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: 43.03  E-value: 2.69e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23312378    512 IFNAIDTDHSGLISVEEFRAMWklfsshYNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAFYVVHR 578
Cdd:smart00027  15 IFRSLDKNQDGTVTGAQAKPIL------LKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYR 75
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
506-587 4.89e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.63  E-value: 4.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 506 RSDLEIIFNAIDTDHSGLISVEEFRAMWklfsshynvhidDSQVNKLANIMDLNKDGSIDFNEFLKafYVVHRYEDLMKP 585
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEALF------------RRLWATLFSEADTDGDGRISREEFVA--GMESLFEATVEP 69


                ..
gi 23312378 586 DV 587
Cdd:COG5126  70 FA 71
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 509-584 7.72e-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: 43.04  E-value: 7.72e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23312378 509 LEIIFNAIDTDHSGLISVEEFRAMWKLFsshyNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAFYVVHRYEDLMK 584
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIKKLLKRL----NIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPELEP 73
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 18-37 9.01e-05

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 39.62  E-value: 9.01e-05
                           10        20
                   ....*....|....*....|
gi 23312378     18 RAALIIQNWYRGYKARLKAR 37
Cdd:smart00015   4 RAAIIIQAAWRGYLARKRYK 23
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 512-576 1.23e-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: 40.28  E-value: 1.23e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23312378 512 IFNAIDTDHSGLISVEEFRAMWKlfSSHynvhIDDSQVNKLANIMDLNKDGSIDFNEFLKAFYVV 576
Cdd:cd00052   4 IFRSLDPDGDGLISGDEARPFLG--KSG----LPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLI 62
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 512-571 1.44e-04

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


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 43.88  E-value: 1.44e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23312378 512 IFNAIDTDHSGLISVEEFRAMWK-LFSSHyNVHIDDSQVNKLANIM----DLNKDGSIDFNEFLK 571
Cdd:cd15902  95 IWRKYDTDGSGFIEAKELKGFLKdLLLKN-KKHVSPPKLDEYTKLIlkefDANKDGKLELDEMAK 158
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 509-574 2.94e-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: 42.96  E-value: 2.94e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23312378 509 LEIIFNAIDTDHSGLISVEEFRAmWKLFSShyNVHIDDSqVNKLANIMDLNKDGSIDFNEFLKAFY 574
Cdd:cd16226  37 LGIIVDKIDKNGDGFVTEEELKD-WIKYVQ--KKYIRED-VDRQWKEYDPNKDGKLSWEEYKKATY 98
EF-hand_8 pfam13833
EF-hand domain pair;
520-574 2.96e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.84  E-value: 2.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 23312378   520 HSGLISVEEFRAMWKLFSshyNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAFY 574
Cdd:pfam13833   1 EKGVITREELKRALALLG---LKDLSEDEVDILFREFDTDGDGYISFDEFCVLLE 52
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 508-536 5.27e-04

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 37.38  E-value: 5.27e-04
                          10        20
                  ....*....|....*....|....*....
gi 23312378   508 DLEIIFNAIDTDHSGLISVEEFRAMWKLF 536
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 18-37 5.88e-04

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


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 37.52  E-value: 5.88e-04
                        10        20
                ....*....|....*....|
gi 23312378  18 RAALIIQNWYRGYKARLKAR 37
Cdd:cd23767  10 RAATLIQALWRGYKVRKELK 29
EF-hand_5 pfam13202
EF hand;
509-533 1.18e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 36.53  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|....*
gi 23312378   509 LEIIFNAIDTDHSGLISVEEFRAMW 533
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
 508-569 1.60e-03

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


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 38.31  E-value: 1.60e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23312378 508 DLEIIFNAIDTDHSGLISVEEFRAMWKLFSSHYNVhIDDSQVNKLANIMDLNKDGSIDFNEF 569
Cdd:cd16253  35 DIKKVFNILDQDKSGFIEEEELKLFLKNFSDGARV-LSDKETKNFLAAGDSDGDGKIGVDEF 95
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 513-569 2.51e-03

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


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 39.17  E-value: 2.51e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23312378 513 FNAIDTDHSGLISVEEFR-----AMWklfsSHYNvhidDSQVNKLANIMDLNKDGSIDFNEF 569
Cdd:cd16184   6 FQAVDRDRSGKISAKELQqalvnGNW----SHFN----DETCRLMIGMFDKDKSGTIDIYEF 59
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 512-569 3.05e-03

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


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 38.77  E-value: 3.05e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23312378 512 IFNAIDTDHSGLISVEEFRAM-----WklfsSHYNvhidDSQVNKLANIMDLNKDGSIDFNEF 569
Cdd:cd16183   5 VFQRVDKDRSGQISATELQQAlsngtW----TPFN----PETVRLMIGMFDRDNSGTINFQEF 59
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 507-569 3.29e-03

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: 37.51  E-value: 3.29e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23312378 507 SDLEIIFNAIDTDHSGLISVEEFRAMWKLFSSHYNVhIDDSQVNKLANIMDLNKDGSIDFNEF 569
Cdd:cd16251  34 DQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGRD-LTDEETKALLAAGDTDGDGKIGVEEF 95
EF-hand_8 pfam13833
EF-hand domain pair;
507-535 3.50e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.75  E-value: 3.50e-03
                          10        20
                  ....*....|....*....|....*....
gi 23312378   507 SDLEIIFNAIDTDHSGLISVEEFRAMWKL 535
Cdd:pfam13833  25 DEVDILFREFDTDGDGYISFDEFCVLLER 53
PHA02239 PHA02239
putative protein phosphatase
 172-241 3.60e-03

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 39.21  E-value: 3.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23312378  172 DLHGKLDDLFLIFykNGLPSERNP---YVFNGDFVDRGKNSIEILMILcvsFLVYPNDLHLNR--GNHEDFMMNL 241
Cdd:PHA02239   8 DIHGEYQKLLTIM--DKINNERKPeetIVFLGDYVDRGKRSKDVVNYI---FDLMSNDDNVVTllGNHDDEFYNI 77
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 510-574 4.00e-03

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 38.28  E-value: 4.00e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23312378 510 EIIFNAIDTDHSGLISVEEFRAMWKlfsshynvHIDDSQvnKLANIMDLNKDGSIDFNEFLKAFY 574
Cdd:cd16180  40 RLMINMFDRDRSGTINFDEFVGLWK--------YIQDWR--RLFRRFDRDRSGSIDFNELQNALS 94
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 502-589 4.23e-03

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 38.28  E-value: 4.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 502 LYRYRSDLEIIFNAIDTDHSGLISVEEFRAMwkLFSSHYNvhIDDSQVNKLANIMDLNKDGSIDFNEFLKAFYVVHRYED 581
Cdd:cd16180  62 LWKYIQDWRRLFRRFDRDRSGSIDFNELQNA--LSSFGYR--LSPQFVQLLVRKFDRRRRGSISFDDFVEACVTLKRLTD 137


                ....*...
gi 23312378 582 LMKPDVTN 589
Cdd:cd16180 138 AFRKYDTN 145
EF-hand_6 pfam13405
EF-hand domain;
508-536 4.78e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 4.78e-03
                          10        20
                  ....*....|....*....|....*....
gi 23312378   508 DLEIIFNAIDTDHSGLISVEEFRAMWKLF 536
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 18-37 5.48e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.60  E-value: 5.48e-03
                          10        20
                  ....*....|....*....|
gi 23312378    18 RAALIIQNWYRGYKARLKAR 37
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRYK 21
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 497-591 9.74e-03

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 37.20  E-value: 9.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23312378 497 TLVETLYRYRSdleiIFNAIDTDHSGLISVEEFRamwKLFSS---HYNVHIDDSQVNKLAnimdlNKDGSIDFNEF---- 569
Cdd:cd16182  66 TLWSDLKKWQA----IFKKFDTDRSGTLSSYELR---KALESagfHLSNKVLQALVLRYA-----DSTGRITFEDFvscl 133

                        90       100
                ....*....|....*....|....
gi 23312378 570 --LKAFYVVHRYEDLMKPDVTNLG 591
Cdd:cd16182 134 vrLKTAFETFSALDKKNEGVIPLT 157
 
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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