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Conserved domains on  [gi|599131348|gb|AAF49044|]
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retinal degeneration C, isoform F [Drosophila melanogaster]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 10635669)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 184-494 0e+00

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


:

Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 554.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 184 PIRKNHIDLLIDVFRKKrgNRLHPKYVALILREAAKSLKQLPNISPVSTAVSQQVTVCGDLHGKLDDLLVVLHKNGLPSS 263
Cdd:cd07420    1 PLTKTHIDLLIEAFKLK--QRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 264 SNPYVFNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYPRNHKRILAFIDEVYRWLP 343
Cdd:cd07420   79 ENPYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 344 LGSVLNSRVLIVHGGFSDSTSLDLIKSIDRGKYVSilrppltdgeplDKTEWQQIFDIMWSDPQATMGCVPNTLRGAGVW 423
Cdd:cd07420  159 LATIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS------------TKTEWQQVVDILWSDPKATKGCKPNTFRGGGCY 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 599131348 424 FGPDVTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITIFSASNYYAIGSNKGAYIRLNNQLMPHFVQYI 494
Cdd:cd07420  227 FGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLTPHFVQYQ 297
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 616-681 7.42e-13

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


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 63.72  E-value: 7.42e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 599131348 616 LVAIFNIIDADNSGEITLDEFETAIDLLVAHMpgaySKAEMLEKCRMMDLNGDGKVDLNEFLEAFR 681
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGL----SEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
527-681 2.18e-09

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.34  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 527 HRDELEDEFRKYDPKDSGYISISHWCKVMENVtklglpWRLLRDKLAPGTDsqkvnynrtlDLLDTDvilEAEADGMSVM 606
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL------WATLFSEADTDGD----------GRISRE---EFVAGMESLF 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 599131348 607 DALYANKASlvAIFNIIDADNSGEITLDEFETAIDLLVAHMPGAyskAEMLEKcrmMDLNGDGKVDLNEFLEAFR 681
Cdd:COG5126   64 EATVEPFAR--AAFDLLDTDGDGKISADEFRRLLTALGVSEEEA---DELFAR---LDTDGDGKISFEEFVAAVR 130
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 89-111 5.75e-05

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.39  E-value: 5.75e-05
                           10        20
                   ....*....|....*....|...
gi 599131348    89 KTIRAAIFIQKWYRRHQARREMQ 111
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 184-494 0e+00

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


Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 554.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 184 PIRKNHIDLLIDVFRKKrgNRLHPKYVALILREAAKSLKQLPNISPVSTAVSQQVTVCGDLHGKLDDLLVVLHKNGLPSS 263
Cdd:cd07420    1 PLTKTHIDLLIEAFKLK--QRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 264 SNPYVFNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYPRNHKRILAFIDEVYRWLP 343
Cdd:cd07420   79 ENPYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 344 LGSVLNSRVLIVHGGFSDSTSLDLIKSIDRGKYVSilrppltdgeplDKTEWQQIFDIMWSDPQATMGCVPNTLRGAGVW 423
Cdd:cd07420  159 LATIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS------------TKTEWQQVVDILWSDPKATKGCKPNTFRGGGCY 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 599131348 424 FGPDVTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITIFSASNYYAIGSNKGAYIRLNNQLMPHFVQYI 494
Cdd:cd07420  227 FGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 205-496 1.08e-106

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: 326.48  E-value: 1.08e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348   205 LHPKYVALILREAAKSLKQLPNISPVStavsQQVTVCGDLHGKLDDLLVVLHKNGLPSSSNpYVFNGDFVDRGKRGLEVL 284
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS----APVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348   285 LLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYprnHKRILAFIDEVYRWLPLGSVLNSRVLIVHGGFS-DST 363
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSpDLT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348   364 SLDLIKSIDRgkyvsilrppltdgePLDKTEWQQIFDIMWSDP-QATMGCVPNTlRGAGVWFGPDVTDNFLQRHRLSYVI 442
Cdd:smart00156 153 TLDDIRKLKR---------------PQEPPDDGLLIDLLWSDPdQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLII 216

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 599131348   443 RSHECKPNGHEFMHDNKIITIFSASNYYAIGSNKGAYIRLNNQLMPHFVQYISA 496
Cdd:smart00156 217 RAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPG 270
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 193-491 3.05e-39

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 146.97  E-value: 3.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 193 LIDVFRKKRGNRLHPKyvALI----LREAAKSLKQLPNISPVSTAVSQQVTVCGDLHGKLDDLLVVLHKNGLPSSSNpYV 268
Cdd:PTZ00244   7 LIEKMLTVKGNRTQRQ--ILIreedIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSN-YL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 269 FNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYprNHKRILAFIDeVYRWLPLGSVL 348
Cdd:PTZ00244  84 FLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRY--NIKLFKAFTD-VFNTMPVCCVI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 349 NSRVLIVHGGFS-DSTSLDLIKSIDRgkyvsilrppltdgePLDKTEWQQIFDIMWSDPQATMGCVPNTLRGAGVWFGPD 427
Cdd:PTZ00244 161 SEKIICMHGGLSpDLTSLASVNEIER---------------PCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFGED 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 599131348 428 VTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITIFSASNYYAIGSNKGAYIRLNNQLMPHFV 491
Cdd:PTZ00244 226 IVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFL 289
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 616-681 7.42e-13

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 63.72  E-value: 7.42e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 599131348 616 LVAIFNIIDADNSGEITLDEFETAIDLLVAHMpgaySKAEMLEKCRMMDLNGDGKVDLNEFLEAFR 681
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGL----SEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 238-348 3.75e-10

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 57.99  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348  238 VTVCGDLH--GKLDDLLVVLHKngLPSSSNPYVF--NGDFVDRGKRGLEVLLLLLSLYLAFPnaVFLNRGNHEDsvmnaR 313
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELLKK--LLEEGKPDLVlhAGDLVDRGPPSEEVLELLERLIKYVP--VYLVRGNHDF-----D 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 599131348  314 YGFIREVESKYPRNHKRILAFIDeVYRWLPLGSVL 348
Cdd:pfam00149  74 YGECLRLYPYLGLLARPWKRFLE-VFNFLPLAGIL 107
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
527-681 2.18e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.34  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 527 HRDELEDEFRKYDPKDSGYISISHWCKVMENVtklglpWRLLRDKLAPGTDsqkvnynrtlDLLDTDvilEAEADGMSVM 606
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL------WATLFSEADTDGD----------GRISRE---EFVAGMESLF 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 599131348 607 DALYANKASlvAIFNIIDADNSGEITLDEFETAIDLLVAHMPGAyskAEMLEKcrmMDLNGDGKVDLNEFLEAFR 681
Cdd:COG5126   64 EATVEPFAR--AAFDLLDTDGDGKISADEFRRLLTALGVSEEEA---DELFAR---LDTDGDGKISFEEFVAAVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
619-681 1.44e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.79  E-value: 1.44e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 599131348  619 IFNIIDADNSGEITLDEFETAidLLVAHMPGAYSKAEMLEKCRMMDLNGDGKVDLNEFLEAFR 681
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKL--LRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
577-689 2.81e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 577 DSQKVNYNRTLDLLDTD---VIleAEADGMSVMDALYAnkaslvAIFNIIDADNSGEITLDEFETAidllVAHMPGAYSK 653
Cdd:COG5126    1 DLQRRKLDRRFDLLDADgdgVL--ERDDFEALFRRLWA------TLFSEADTDGDGRISREEFVAG----MESLFEATVE 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 599131348 654 AEMLEKCRMMDLNGDGKVDLNEFLEAFRLSDLHRKE 689
Cdd:COG5126   69 PFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEE 104
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 89-111 5.75e-05

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.39  E-value: 5.75e-05
                           10        20
                   ....*....|....*....|...
gi 599131348    89 KTIRAAIFIQKWYRRHQARREMQ 111
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRYK 23
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 655-681 6.05e-04

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.74  E-value: 6.05e-04
                           10        20
                   ....*....|....*....|....*..
gi 599131348   655 EMLEKCRMMDLNGDGKVDLNEFLEAFR 681
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLK 27
PTZ00183 PTZ00183
centrin; Provisional
 620-696 1.26e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.06  E-value: 1.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 599131348 620 FNIIDADNSGEITLDEFETAIDLLvahmpGAYSKAEMLEKCRM-MDLNGDGKVDLNEFLEAFRlSDLHRKEQQDENIR 696
Cdd:PTZ00183  23 FDLFDTDGSGTIDPKELKVAMRSL-----GFEPKKEEIKQMIAdVDKDGSGKIDFEEFLDIMT-KKLGERDPREEILK 94
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 88-113 1.89e-03

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


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.37  E-value: 1.89e-03
                         10        20
                 ....*....|....*....|....*.
gi 599131348  88 EKTIRAAIFIQKWYRRHQARREMQRR 113
Cdd:cd23767    6 QRMNRAATLIQALWRGYKVRKELKKK 31
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 92-111 7.52e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.22  E-value: 7.52e-03
                          10        20
                  ....*....|....*....|
gi 599131348   92 RAAIFIQKWYRRHQARREMQ 111
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRYK 21
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 184-494 0e+00

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


Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 554.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 184 PIRKNHIDLLIDVFRKKrgNRLHPKYVALILREAAKSLKQLPNISPVSTAVSQQVTVCGDLHGKLDDLLVVLHKNGLPSS 263
Cdd:cd07420    1 PLTKTHIDLLIEAFKLK--QRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 264 SNPYVFNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYPRNHKRILAFIDEVYRWLP 343
Cdd:cd07420   79 ENPYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 344 LGSVLNSRVLIVHGGFSDSTSLDLIKSIDRGKYVSilrppltdgeplDKTEWQQIFDIMWSDPQATMGCVPNTLRGAGVW 423
Cdd:cd07420  159 LATIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS------------TKTEWQQVVDILWSDPKATKGCKPNTFRGGGCY 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 599131348 424 FGPDVTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITIFSASNYYAIGSNKGAYIRLNNQLMPHFVQYI 494
Cdd:cd07420  227 FGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 205-496 1.08e-106

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: 326.48  E-value: 1.08e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348   205 LHPKYVALILREAAKSLKQLPNISPVStavsQQVTVCGDLHGKLDDLLVVLHKNGLPSSSNpYVFNGDFVDRGKRGLEVL 284
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS----APVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348   285 LLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYprnHKRILAFIDEVYRWLPLGSVLNSRVLIVHGGFS-DST 363
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSpDLT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348   364 SLDLIKSIDRgkyvsilrppltdgePLDKTEWQQIFDIMWSDP-QATMGCVPNTlRGAGVWFGPDVTDNFLQRHRLSYVI 442
Cdd:smart00156 153 TLDDIRKLKR---------------PQEPPDDGLLIDLLWSDPdQPVNGFGPSI-RGASYIFGPDAVDEFLKKNNLKLII 216

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 599131348   443 RSHECKPNGHEFMHDNKIITIFSASNYYAIGSNKGAYIRLNNQLMPHFVQYISA 496
Cdd:smart00156 217 RAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPG 270
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 190-493 3.41e-90

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: 285.30  E-value: 3.41e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 190 IDLLIDVFrkKRGNRLHPKYVALILREAAKSLKQLPNISPVSTAVSQQVTVCGDLHGKLDDLLVVLHKNGLPSSSNPYVF 269
Cdd:cd07417   16 VKEMMEWF--KDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFELNGLPSETNPYLF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 270 NGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYprnHKRILAFIDEVYRWLPLGSVLN 349
Cdd:cd07417   94 NGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKY---NEQMFNLFSEVFNWLPLAHLIN 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 350 SRVLIVHGG-FS-DSTSLDLIKSIDRGKyvsilRPPltDGEPldktewqqIFDIMWSDPQATMGCVPNTlRGAGVWFGPD 427
Cdd:cd07417  171 GKVLVVHGGlFSdDGVTLDDIRKIDRFR-----QPP--DSGL--------MCELLWSDPQPQPGRGPSK-RGVGCQFGPD 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 599131348 428 VTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITIFSASNYYAIGSNKGAYIRLN-NQLMPHFVQY 493
Cdd:cd07417  235 VTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKgSDLKPKFTQF 301
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 239-482 3.51e-63

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: 210.69  E-value: 3.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 239 TVCGDLHGKLDDLLVVLHKNGLPSSSNpYVFNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIR 318
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDK-YLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 319 EV-ESKYPRNHKRILAFIDEVYRWLPLGSVLNSRVLIVHGGFS-DSTSLDLIKSIdrgkyvsilRPPLTDGEPLdktewq 396
Cdd:cd00144   80 ERtLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSpDLTLLDQIRNI---------RPIENPDDQL------ 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 397 qIFDIMWSDPQATMGCVPNTLRGAGVWFGPDVTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITIFSASNYYAIGSNK 476
Cdd:cd00144  145 -VEDLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNK 223


                 ....*.
gi 599131348 477 GAYIRL 482
Cdd:cd00144  224 LAALVV 229
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 200-493 1.49e-50

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: 178.16  E-value: 1.49e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 200 KRGNRLHPKYVALILREAAKSLKQLPNISPVSTAVsqqvTVCGDLHGKLDDLLVVLHKNGLPSSSNpYVFNGDFVDRGKR 279
Cdd:cd07415   10 KKCELLPESEVKSLCEKAKEILVKESNVQRVRSPV----TVCGDIHGQFYDLLELFRIGGDVPDTN-YLFLGDYVDRGYY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 280 GLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYprNHKRILAFIDEVYRWLPLGSVLNSRVLIVHGGF 359
Cdd:cd07415   85 SVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKY--GNANVWKYFTDLFDYLPLAALIDGQIFCVHGGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 360 SDS-TSLDLIKSIDRGKYVsilrPPltDGePLdktewqqiFDIMWSDPQATMGCVPNTlRGAGVWFGPDVTDNFLQRHRL 438
Cdd:cd07415  163 SPSiQTLDQIRALDRFQEV----PH--EG-PM--------CDLLWSDPDDREGWGISP-RGAGYLFGQDVVEEFNHNNGL 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 599131348 439 SYVIRSHECKPNGHEFMHDNKIITIFSASNYYAIGSNKGAYIRLNNQLMPHFVQY 493
Cdd:cd07415  227 TLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQF 281
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 217-482 9.01e-50

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: 179.23  E-value: 9.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 217 AAKSLKQLPNISPVSTAVSQQVTVCGDLHGKLDDLLVVLHKNGLPSSSNPYVFNGDFVDRGKRGLEVLLLLLSLYLAFPN 296
Cdd:cd07418   47 AHKILHREPNCVRIDVEDVCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 297 AVFLNRGNHEDSVMNARYGFIREVESKYPRNHKRILAFIDEVYRWLPLGSVLNSRVLIVHGGFSDSTSLDLIKSIDRGKY 376
Cdd:cd07418  127 RVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPKRKKQKGKNR 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 377 VSILR------PPLTDGEPLDK---------TEWQQIF--DIMWSDPQATMGCVPNTLRGAGVWFGPDVTDNFLQRHRLS 439
Cdd:cd07418  207 RVLLLepesesLKLGTLDDLMKarrsvldppGEGSNLIpgDVLWSDPSLTPGLSPNKQRGIGLLWGPDCTEEFLEKNNLK 286

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 599131348 440 YVIRSHEC------KP------NGHEFMHD---NKIITIFSASNYYAIGS------NKGAYIRL 482
Cdd:cd07418  287 LIIRSHEGpdarekRPglagmnKGYTVDHDvesGKLITLFSAPDYPQFQAteerynNKGAYIIL 350
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 190-487 1.20e-47

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: 170.95  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 190 IDLLIDVFrkKRGNRLHPKYVALILREAAKSLKQLPNIspvsTAVSQQVTVCGDLHGKLDDLLVVLHKNGLPSSSNpYVF 269
Cdd:cd07416    3 VDILKAHF--MREGRLSEEDALRIITEGAEILRQEPNL----LRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTR-YLF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 270 NGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYprnHKRILAFIDEVYRWLPLGSVLN 349
Cdd:cd07416   76 LGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY---SERVYDACMEAFDCLPLAALMN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 350 SRVLIVHGGFS-DSTSLDLIKSIDRgkyvsiLRPPLTDGePLdktewqqiFDIMWSDPQATMG-------CVPNTLRGAG 421
Cdd:cd07416  153 QQFLCVHGGLSpELKTLDDIRKLDR------FREPPSYG-PM--------CDLLWSDPLEDFGnektqehFVHNTVRGCS 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 599131348 422 VWFGPDVTDNFLQRHRLSYVIRSHECKPNGHEFMHDNK------IITIFSASNYYAIGSNKGAYIRLNNQLM 487
Cdd:cd07416  218 YFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVM 289
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 238-492 1.30e-42

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: 156.35  E-value: 1.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 238 VTVCGDLHGKLDDLLVVLHKNGLPSSSNpYVFNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFI 317
Cdd:cd07414   52 LKICGDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 318 REVESKYprNHKRILAFIDeVYRWLPLGSVLNSRVLIVHGGFS-DSTSLDLIKSIDRgkyvsilrppltdgePLDKTEWQ 396
Cdd:cd07414  131 DECKRRY--NIKLWKTFTD-CFNCLPVAAIVDEKIFCCHGGLSpDLQSMEQIRRIMR---------------PTDVPDQG 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 397 QIFDIMWSDPQATMGCVPNTLRGAGVWFGPDVTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITIFSASNYYAIGSNK 476
Cdd:cd07414  193 LLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNA 272

                        250
                 ....*....|....*.
gi 599131348 477 GAYIRLNNQLMPHFVQ 492
Cdd:cd07414  273 GAMMSVDETLMCSFQI 288
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 193-491 3.05e-39

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 146.97  E-value: 3.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 193 LIDVFRKKRGNRLHPKyvALI----LREAAKSLKQLPNISPVSTAVSQQVTVCGDLHGKLDDLLVVLHKNGLPSSSNpYV 268
Cdd:PTZ00244   7 LIEKMLTVKGNRTQRQ--ILIreedIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSN-YL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 269 FNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYprNHKRILAFIDeVYRWLPLGSVL 348
Cdd:PTZ00244  84 FLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRY--NIKLFKAFTD-VFNTMPVCCVI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 349 NSRVLIVHGGFS-DSTSLDLIKSIDRgkyvsilrppltdgePLDKTEWQQIFDIMWSDPQATMGCVPNTLRGAGVWFGPD 427
Cdd:PTZ00244 161 SEKIICMHGGLSpDLTSLASVNEIER---------------PCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFGED 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 599131348 428 VTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITIFSASNYYAIGSNKGAYIRLNNQLMPHFV 491
Cdd:PTZ00244 226 IVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFL 289
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 242-486 3.65e-38

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: 144.51  E-value: 3.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 242 GDLHGKLDDLLVVLHKNGLPS-------SSNPYVFNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARY 314
Cdd:cd07419   54 GDIHGQFGDLMRLFDEYGSPVteeagdiEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALF 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 315 GFIREVESK---YPRNHKRILAFIDEVYRWLPLGSVLNSRVLIVHGGFsdSTSLDLIKSIdrgkyVSILRP-PLTDGEPL 390
Cdd:cd07419  134 GFREECIERlgeDIRDGDSVWQRINRLFNWLPLAALIEDKIICVHGGI--GRSINHIHQI-----ENLKRPiTMEAGSPV 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 391 dktewqqIFDIMWSDP---QATMGCVPNTL--RGAG--VWFGPDVTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITI 463
Cdd:cd07419  207 -------VMDLLWSDPtenDSVLGLRPNAIdpRGTGliVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITL 279

                        250       260
                 ....*....|....*....|...
gi 599131348 464 FSASNYYAIGSNKGAYIRLNNQL 486
Cdd:cd07419  280 FSATNYCGTAGNAGAILVLGRDL 302
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 200-507 6.66e-37

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 140.72  E-value: 6.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 200 KRGNRLHPKYVALILREAAKSLKQLPNISPVSTAVsqqvTVCGDLHGKLDDLLVVLHKNGLPSSSNpYVFNGDFVDRGKR 279
Cdd:PTZ00239  11 LNGGCLPERDLKLICERAKEIFLEESNVQPVRAPV----NVCGDIHGQFYDLQALFKEGGDIPNAN-YIFIGDFVDRGYN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 280 GLEVLLLLLSLYLAFPNAVFLNRGNHEDSVMNARYGFIREVESKYPrNHKRILAFIDeVYRWLPLGSVLNSRVLIVHGGF 359
Cdd:PTZ00239  86 SVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYG-NSNPWRLFMD-VFDCLPLAALIEGQILCVHGGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 360 S-DSTSLDLIKSIDRgkyvsilrppltdgepldKTEWQQ---IFDIMWSDPQATMGCVPNTlRGAGVWFGPDVTDNFLQR 435
Cdd:PTZ00239 164 SpDMRTIDQIRTIDR------------------KIEIPHegpFCDLMWSDPEEVEYWAVNS-RGAGYLFGAKVTKEFCRL 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 599131348 436 HRLSYVIRSHECKPNGHEF-MHDNKIITIFSASNY-YAIGsNKGAYIRLNNQLMPHFVQYISAASQTKRLSFKQ 507
Cdd:PTZ00239 225 NDLTLICRAHQLVMEGYKYwFPDQNLVTVWSAPNYcYRCG-NIASILCLDENLQQTWKTFKEVPESAKSINPKN 297
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 229-508 6.18e-36

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 138.25  E-value: 6.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 229 PVSTAVSQQVTVCGDLHGKLDDLLVVLHKNGLPSSSNpYVFNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLNRGNHEDS 308
Cdd:PTZ00480  52 PILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 309 VMNARYGFIREVESKYPrnhKRILAFIDEVYRWLPLGSVLNSRVLIVHGGFSDSTS-LDLIKSIDRgkyvsilrppltdg 387
Cdd:PTZ00480 131 SINRIYGFYDECKRRYT---IKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSnLEQIRRIMR-------------- 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 388 ePLDKTEWQQIFDIMWSDPQATMGCVPNTLRGAGVWFGPDVTDNFLQRHRLSYVIRSHECKPNGHEFMHDNKIITIFSAS 467
Cdd:PTZ00480 194 -PTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAP 272

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 599131348 468 NYYAIGSNKGAYIRLNNQLMPHFvQYISAASQTKRLSFKQR 508
Cdd:PTZ00480 273 NYCGEFDNAGSMMTIDESLMCSF-QILKPAEQGQGASQQNK 312
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 616-681 7.42e-13

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 63.72  E-value: 7.42e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 599131348 616 LVAIFNIIDADNSGEITLDEFETAIDLLVAHMpgaySKAEMLEKCRMMDLNGDGKVDLNEFLEAFR 681
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGL----SEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 238-348 3.75e-10

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 57.99  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348  238 VTVCGDLH--GKLDDLLVVLHKngLPSSSNPYVF--NGDFVDRGKRGLEVLLLLLSLYLAFPnaVFLNRGNHEDsvmnaR 313
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELLKK--LLEEGKPDLVlhAGDLVDRGPPSEEVLELLERLIKYVP--VYLVRGNHDF-----D 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 599131348  314 YGFIREVESKYPRNHKRILAFIDeVYRWLPLGSVL 348
Cdd:pfam00149  74 YGECLRLYPYLGLLARPWKRFLE-VFNFLPLAGIL 107
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
527-681 2.18e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.34  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 527 HRDELEDEFRKYDPKDSGYISISHWCKVMENVtklglpWRLLRDKLAPGTDsqkvnynrtlDLLDTDvilEAEADGMSVM 606
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRL------WATLFSEADTDGD----------GRISRE---EFVAGMESLF 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 599131348 607 DALYANKASlvAIFNIIDADNSGEITLDEFETAIDLLVAHMPGAyskAEMLEKcrmMDLNGDGKVDLNEFLEAFR 681
Cdd:COG5126   64 EATVEPFAR--AAFDLLDTDGDGKISADEFRRLLTALGVSEEEA---DELFAR---LDTDGDGKISFEEFVAAVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
619-681 1.44e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.79  E-value: 1.44e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 599131348  619 IFNIIDADNSGEITLDEFETAidLLVAHMPGAYSKAEMLEKCRMMDLNGDGKVDLNEFLEAFR 681
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKL--LRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
577-689 2.81e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 577 DSQKVNYNRTLDLLDTD---VIleAEADGMSVMDALYAnkaslvAIFNIIDADNSGEITLDEFETAidllVAHMPGAYSK 653
Cdd:COG5126    1 DLQRRKLDRRFDLLDADgdgVL--ERDDFEALFRRLWA------TLFSEADTDGDGRISREEFVAG----MESLFEATVE 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 599131348 654 AEMLEKCRMMDLNGDGKVDLNEFLEAFRLSDLHRKE 689
Cdd:COG5126   69 PFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEE 104
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 616-687 2.58e-05

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: 45.28  E-value: 2.58e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 599131348 616 LVAIFNIIDADNSGEITLDEFETAidLLVAHMPGAYSKAEMLekCRMMDLNGDGKVDLNEFLEafrlsdLHR 687
Cdd:cd16185    2 LRQWFRAVDRDRSGSIDVNELQKA--LAGGGLLFSLATAEKL--IRMFDRDGNGTIDFEEFAA------LHQ 63
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 89-111 5.75e-05

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.39  E-value: 5.75e-05
                           10        20
                   ....*....|....*....|...
gi 599131348    89 KTIRAAIFIQKWYRRHQARREMQ 111
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRYK 23
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
510-640 2.43e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.70  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 510 GIVESSALKELAVRMRDHRdeledeFRKYDPKDSGYISISHWCKVMENVTKlglpwRLLRDKLApgtdsqkvnynRTLDL 589
Cdd:COG5126   20 GVLERDDFEALFRRLWATL------FSEADTDGDGRISREEFVAGMESLFE-----ATVEPFAR-----------AAFDL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 599131348 590 LDTDvileaeADG-------MSVMDALYANKASLVAIFNIIDADNSGEITLDEFETAI 640
Cdd:COG5126   78 LDTD------GDGkisadefRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
EF-hand_8 pfam13833
EF-hand domain pair;
628-680 5.50e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.45  E-value: 5.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 599131348  628 SGEITLDEFETAIDLLVAHMPGAYSKAEMLekcRMMDLNGDGKVDLNEFLEAF 680
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILF---REFDTDGDGYISFDEFCVLL 51
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 655-681 6.05e-04

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.74  E-value: 6.05e-04
                           10        20
                   ....*....|....*....|....*..
gi 599131348   655 EMLEKCRMMDLNGDGKVDLNEFLEAFR 681
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLK 27
PTZ00183 PTZ00183
centrin; Provisional
 620-696 1.26e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.06  E-value: 1.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 599131348 620 FNIIDADNSGEITLDEFETAIDLLvahmpGAYSKAEMLEKCRM-MDLNGDGKVDLNEFLEAFRlSDLHRKEQQDENIR 696
Cdd:PTZ00183  23 FDLFDTDGSGTIDPKELKVAMRSL-----GFEPKKEEIKQMIAdVDKDGSGKIDFEEFLDIMT-KKLGERDPREEILK 94
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 240-306 1.46e-03

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 39.56  E-value: 1.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 599131348 240 VCGDLHGKLDDLLVVLHKNgLPSSSNP--YVFNGDFVDRGKrGLEVLLLLLSLYLAFPNAVFLNRGNHE 306
Cdd:cd00838    2 VISDIHGNLEALEAVLEAA-LAKAEKPdlVICLGDLVDYGP-DPEEVELKALRLLLAGIPVYVVPGNHD 68
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 88-113 1.89e-03

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


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 36.37  E-value: 1.89e-03
                         10        20
                 ....*....|....*....|....*.
gi 599131348  88 EKTIRAAIFIQKWYRRHQARREMQRR 113
Cdd:cd23767    6 QRMNRAATLIQALWRGYKVRKELKKK 31
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 620-694 2.17e-03

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: 40.64  E-value: 2.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 599131348 620 FNIIDADNSGEITLDEFetaIDLL----VAHMPGAYSkAEMLEKcrmMDLNGDGKVDLNEFleafrLSDLHRKEQQDEN 694
Cdd:cd16226  125 WKAADQDGDGKLTKEEF---TAFLhpeeFPHMRDIVV-QETLED---IDKNKDGFISLEEY-----IGDMYRDDDEEED 191
PTZ00183 PTZ00183
centrin; Provisional
 566-673 2.31e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.29  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 566 RLLRDKLAPG-TDSQKVNYNRTLDLLDTDVILEAEADGMSV-MDALYAN--KASLVAIFNIIDADNSGEITLDEFetaID 641
Cdd:PTZ00183   1 MRKRRSERPGlTEDQKKEIREAFDLFDTDGSGTIDPKELKVaMRSLGFEpkKEEIKQMIADVDKDGSGKIDFEEF---LD 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 599131348 642 LLVAHMPGAYSKAEMLEKCRMMDLNGDGKVDL 673
Cdd:PTZ00183  78 IMTKKLGERDPREEILKAFRLFDDDKTGKISL 109
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 616-676 3.28e-03

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


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 39.16  E-value: 3.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 599131348 616 LVAIFNIIDADNSGEITLDEFETAIdllvahMPGAYSKAEMlEKCRMM----DLNGDGKVDLNEF 676
Cdd:cd16183    2 LWNVFQRVDKDRSGQISATELQQAL------SNGTWTPFNP-ETVRLMigmfDRDNSGTINFQEF 59
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 242-360 6.57e-03

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: 38.82  E-value: 6.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 242 GDLHGKLDDLLVVLHKNGLPSSSNPYVFN-------GDFVDRGKRGLEVL---LLLLSLYLAFPNAVFLNRGNHEdsVMN 311
Cdd:cd07425    4 GDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIEILkllEKLKRQARKAGGKVILLLGNHE--LMN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 599131348 312 A----RYGFIREVESKYPRNHKRILAFIDE--VYRWL---PLGSVLNSrVLIVHGGFS 360
Cdd:cd07425   82 LcgdfRYVHPRGLNEFGGVAKRRYALLSDGgyIGRYLrthPVVLVVND-ILFVHGGLG 138
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 92-111 7.52e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.22  E-value: 7.52e-03
                          10        20
                  ....*....|....*....|
gi 599131348   92 RAAIFIQKWYRRHQARREMQ 111
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRYK 21
PHA02239 PHA02239
putative protein phosphatase
 238-311 7.83e-03

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 38.82  E-value: 7.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 599131348 238 VTVCGDLHGKLDDLLVVLHK-NGLPSSSNPYVFNGDFVDRGKRGLEVLLLLLSLYLAFPNAVFLnRGNHEDSVMN 311
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTL-LGNHDDEFYN 76
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 661-681 9.34e-03

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.30  E-value: 9.34e-03
                          10        20
                  ....*....|....*....|.
gi 599131348  661 RMMDLNGDGKVDLNEFLEAFR 681
Cdd:pfam00036   7 RLFDKDGDGKIDFEEFKELLK 27
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 625-688 9.35e-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: 37.59  E-value: 9.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599131348 625 ADNSGEITLDEFETaidLLVAHMPGAYSKAEM--LEKCR----MMDLNGDGKVDLNEFLE----------AFRLSDLHRK 688
Cdd:cd16182   10 AGEDEEIDAVELQK---LLNASLLKDMPKFDGfsLETCRsliaLMDTNGSGRLDLEEFKTlwsdlkkwqaIFKKFDTDRS 86
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 620-676 9.74e-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: 37.63  E-value: 9.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 599131348 620 FNIIDADNSGEITLDEFETAIdllvahMPGAYSKAEmLEKCRMM----DLNGDGKVDLNEF 676
Cdd:cd16184    6 FQAVDRDRSGKISAKELQQAL------VNGNWSHFN-DETCRLMigmfDKDKSGTIDIYEF 59
 
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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