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Conserved domains on  [gi|299115261|ref|NP_001177376|]
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serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPP2R3A cd21506
serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha; Heterotrimeric ...
 51-334 0e+00

serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This group contains protein phosphatase subunit PR130 (also known as protein phosphatase 2A regulatory subunit B'' subunit alpha, PR72, or PPP2R3) that is encoded by the PPP2R3A gene. PR130 and PR72 subunits are derived from the same gene through differential splicing; they harbor specific N-terminal domains of different lengths that are encoded by alternatively spliced exons and have identical C-termini. The common C-terminus contains a two-domain elongated structure with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity. The PR130 subunit has been shown to interact with the LIM domain of lipoma-preferred partner (LPP) through a conserved Zn2+-finger-like motif in the N-terminus of PR130.


:

Pssm-ID: 410339  Cd Length: 284  Bit Score: 623.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261  51 WRKLLNNHHDDASKFICLLAKPNCSSLEQEDFIPLLQDVVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKIT 130
Cdd:cd21506    1 WRKLLNNCHDDASKFVYLLAKPNCSYLEQEDFIPLLQDIVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 131 STEIRKSNFLQTLALLEEEEDINQITDYFSYEHFYVIYCKFWELDTDHDLYISQADLSRYNDQASSSRIIERIFSGAVTR 210
Cdd:cd21506   81 LTELRKSNFLQTLALLEEEDDINQITDYFSYEHFYVIYCKFWELDTDHDLYIDQKDLARYNDQASSSRIIERIFSGAVTR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 211 GKTIQKEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDVDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQML 290
Cdd:cd21506  161 GNSVQKEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDLDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQML 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 299115261 291 DLVKPAVDGKITLRDLKRCRMAHIFYDTFFNLEKYLDHEQRDPF 334
Cdd:cd21506  241 DLVKPEVDGKITLRDLKRCRMAHIFYDTFFNLEKYLDHEQRDPF 284
 
Name Accession Description Interval E-value
PPP2R3A cd21506
serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha; Heterotrimeric ...
 51-334 0e+00

serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This group contains protein phosphatase subunit PR130 (also known as protein phosphatase 2A regulatory subunit B'' subunit alpha, PR72, or PPP2R3) that is encoded by the PPP2R3A gene. PR130 and PR72 subunits are derived from the same gene through differential splicing; they harbor specific N-terminal domains of different lengths that are encoded by alternatively spliced exons and have identical C-termini. The common C-terminus contains a two-domain elongated structure with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity. The PR130 subunit has been shown to interact with the LIM domain of lipoma-preferred partner (LPP) through a conserved Zn2+-finger-like motif in the N-terminus of PR130.


Pssm-ID: 410339  Cd Length: 284  Bit Score: 623.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261  51 WRKLLNNHHDDASKFICLLAKPNCSSLEQEDFIPLLQDVVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKIT 130
Cdd:cd21506    1 WRKLLNNCHDDASKFVYLLAKPNCSYLEQEDFIPLLQDIVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 131 STEIRKSNFLQTLALLEEEEDINQITDYFSYEHFYVIYCKFWELDTDHDLYISQADLSRYNDQASSSRIIERIFSGAVTR 210
Cdd:cd21506   81 LTELRKSNFLQTLALLEEEDDINQITDYFSYEHFYVIYCKFWELDTDHDLYIDQKDLARYNDQASSSRIIERIFSGAVTR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 211 GKTIQKEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDVDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQML 290
Cdd:cd21506  161 GNSVQKEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDLDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQML 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 299115261 291 DLVKPAVDGKITLRDLKRCRMAHIFYDTFFNLEKYLDHEQRDPF 334
Cdd:cd21506  241 DLVKPEVDGKITLRDLKRCRMAHIFYDTFFNLEKYLDHEQRDPF 284
EF-hand_13 pfam17958
EF-hand domain; This entry represents an EF-hand domain found in one of the regulatory B ...
 60-149 4.33e-45

EF-hand domain; This entry represents an EF-hand domain found in one of the regulatory B subunits of PP2A.


Pssm-ID: 465586 [Multi-domain]  Cd Length: 90  Bit Score: 150.98  E-value: 4.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261   60 DDASKFICLLAKPNCSSLEQEDFIPLLQDVVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKITSTEIRKSNF 139
Cdd:pfam17958   1 DEAARFFRLLKGPGKNYLSREDFYPFVQDVVDTHPGLEFLREAEEFQDKYIQTVIARIFYVVNRSWSGKITLLELRKSDL 80

                          90
                  ....*....|
gi 299115261  140 LQTLALLEEE 149
Cdd:pfam17958  81 LKAVRQLDEE 90
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
171-267 7.64e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 7.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 171 FWELDTDHDLYISQADLsryndQASSSRIIERIFSGAVTRGktiqkEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDV 250
Cdd:COG5126   11 FDLLDADGDGVLERDDF-----EALFRRLWATLFSEADTDG-----DGRISREEFVAGMESLFEATVEPFARAAFDLLDT 80

                         90
                 ....*....|....*..
gi 299115261 251 DGDGVLSMYELEYFYEE 267
Cdd:COG5126   81 DGDGKISADEFRRLLTA 97
 
Name Accession Description Interval E-value
PPP2R3A cd21506
serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha; Heterotrimeric ...
 51-334 0e+00

serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This group contains protein phosphatase subunit PR130 (also known as protein phosphatase 2A regulatory subunit B'' subunit alpha, PR72, or PPP2R3) that is encoded by the PPP2R3A gene. PR130 and PR72 subunits are derived from the same gene through differential splicing; they harbor specific N-terminal domains of different lengths that are encoded by alternatively spliced exons and have identical C-termini. The common C-terminus contains a two-domain elongated structure with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity. The PR130 subunit has been shown to interact with the LIM domain of lipoma-preferred partner (LPP) through a conserved Zn2+-finger-like motif in the N-terminus of PR130.


Pssm-ID: 410339  Cd Length: 284  Bit Score: 623.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261  51 WRKLLNNHHDDASKFICLLAKPNCSSLEQEDFIPLLQDVVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKIT 130
Cdd:cd21506    1 WRKLLNNCHDDASKFVYLLAKPNCSYLEQEDFIPLLQDIVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 131 STEIRKSNFLQTLALLEEEEDINQITDYFSYEHFYVIYCKFWELDTDHDLYISQADLSRYNDQASSSRIIERIFSGAVTR 210
Cdd:cd21506   81 LTELRKSNFLQTLALLEEEDDINQITDYFSYEHFYVIYCKFWELDTDHDLYIDQKDLARYNDQASSSRIIERIFSGAVTR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 211 GKTIQKEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDVDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQML 290
Cdd:cd21506  161 GNSVQKEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDLDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQML 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 299115261 291 DLVKPAVDGKITLRDLKRCRMAHIFYDTFFNLEKYLDHEQRDPF 334
Cdd:cd21506  241 DLVKPEVDGKITLRDLKRCRMAHIFYDTFFNLEKYLDHEQRDPF 284
PPP2R3B cd21507
serine/threonine protein phosphatase 2A regulatory subunit B" subunit beta; Heterotrimeric ...
 4-331 0e+00

serine/threonine protein phosphatase 2A regulatory subunit B" subunit beta; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This group contains protein phosphatase subunit PR70 (also known as protein phosphatase 2 regulatory subunit B'' subunit beta, PR48, NYREN8, PPP2R3L, or PPP2R3LY) that is encoded by the PPP2R3B gene. This substrate-recognizing subunit of PP2A has a two-domain elongated structure with two calcium EF-hands, each displaying different affinities to Ca2+. PPP2R3B/PR70 is a gonosomal melanoma tumor suppressor gene; PR70 decreased melanoma growth by negatively interfering with DNA replication and cell cycle progression through its role in stabilizing the cell division cycle 6 (CDC6)-chromatin licensing and DNA replication factor 1 (CDT1) interaction, which delays the firing of origins of DNA replication.


Pssm-ID: 410340  Cd Length: 355  Bit Score: 600.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261   4 EEQKADIYEMGKIAKVCGCPLYWKAPMFRAAGGEKTGFVTAQSFIAMWRKLLNNHHDDASKFICLLAKPNCSSLEQEDFI 83
Cdd:cd21507   28 PNERATLDDMGKVAKACDCPLYWKGPLFYAAGGERTGSVSVHKFVAMWRKILQNCHDDAAKFVHLLMKPGCNYLVQEDFI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261  84 PLLQDVVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKITSTEIRKSNFLQTLALLEEEEDINQITDYFSYEH 163
Cdd:cd21507  108 PFLQDVVNTHPGLSFLKEASEFHSRYITTVIQRIFYTVNRSWSGRITCTELRRSSFLQNVALLEEEADINQLTEFFSYEH 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 164 FYVIYCKFWELDTDHDLYISQADLSRYNDQASSSRIIERIFSGAVTRGKTIQKEGRMSYADFVWFLISEEDKRNPTSIEY 243
Cdd:cd21507  188 FYVIYCKFWELDTDHDLYIDQKDLARHNDHAISNRMIERIFSGAVTRGRKAQKEGKISYADFVWFLISEEDKKTPTSIEY 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 244 WFRCMDVDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQMLDLVKPAVDGKITLRDLKRCRMAHIFYDTFFNLE 323
Cdd:cd21507  268 WFRCMDLDGDGALSMYELEYFYEEQCQKLDNMAIEPLPFEDCLCQMLDLVKPRTEGKITLHDLKRCKLANVFFDTFFNIE 347


                 ....*...
gi 299115261 324 KYLDHEQR 331
Cdd:cd21507  348 KYLDHEQK 355
PPP2R3A_B-like cd21504
serine/threonine protein phosphatase 2A regulatory subunit B" alpha and beta subunits, and ...
 51-325 0e+00

serine/threonine protein phosphatase 2A regulatory subunit B" alpha and beta subunits, and similar proteins; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. These B-family regulatory subunits play various roles including regulation of cytoskeletal assembly, neuronal differentiation, mitogen-activated protein kinase signaling, and apoptosis. This subfamily includes protein phosphatase 2A regulatory subunit B'' subunits alpha and beta, encoded by PPP2R3A and PPP2R3B. It also includes subunit delta encoded by PPP2R3D in mouse. They contain two-domain elongated structures with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity.


Pssm-ID: 410337  Cd Length: 274  Bit Score: 532.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261  51 WRKLLNNHHDDASKFICLLAKPNCSSLEQEDFIPLLQDVVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKIT 130
Cdd:cd21504    1 WKKILAGCHDDASRFFRILKKPDRNYLVPEDFKPFLQDLLDTHPGLEFLQDTPEFQERYAETVIYRIFYSVNRSWSGRIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 131 STEIRKSNFLQTLALLEEEEDINQITDYFSYEHFYVIYCKFWELDTDHDLYISQADLSRYNDQASSSRIIERIFSGAVTR 210
Cdd:cd21504   81 LRELRRSNLLQALLLLDEEEDINKVLRYFSYEHFYVIYCKFWELDTDHDLLIDKDDLLRYGDHALSPRIVDRIFSGAVRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 211 GKTiQKEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDVDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQML 290
Cdd:cd21504  161 FKS-GKEGKMSYEDFVWFILSEEDKTSPTSIEYWFRCMDLDGDGVLSMYEMEYFYEEQLQRMECLGIEPVPFEDILCQML 239

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 299115261 291 DLVKPAVDGKITLRDLKRCRMAHIFYDTFFNLEKY 325
Cdd:cd21504  240 DMIKPENEGKITLRDLKRCKLAGNFFNTLFNLNKF 274
PPP2R3 cd21339
serine/threonine protein phosphatase 2A regulatory subunit B"; Heterotrimeric serine/threonine ...
 61-319 1.36e-166

serine/threonine protein phosphatase 2A regulatory subunit B"; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This family includes PP2A regulatory B'' subunits alpha, beta and gamma, encoded by PPP2R3A, PPP2R3B and PPP2R3C, respectively. It also includes subunit delta encoded by PPP2R3D in mouse. These B-family regulatory subunits play various roles including regulation of cytoskeletal assembly, neuronal differentiation, mitogen-activated protein kinase signaling, and apoptosis. Subunits alpha and beta contain two-domain elongated structure with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity.


Pssm-ID: 410336  Cd Length: 259  Bit Score: 467.44  E-value: 1.36e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261  61 DASKFICLLAKPNCSSLEQEDFIPLLQDVVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKITSTEIRKSNFL 140
Cdd:cd21339    1 DATKFGLLLYDPGCGYLRQEDFEPYLQDVVPTHPGLDFLKKAPEFHSRYITTVIQRIFYFVNRSWSGKITIQEIRASSFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 141 QTLALLEEEEDINQITDYFSYEHFYVIYCKFWELDTDHDLYISQADLSRYNDQASSSRIIERIFSGAVTRGKTIQKEGRM 220
Cdd:cd21339   81 QDLALLEEEEDINQETNWFSYEHFYVIYCKFWELDTDHDLMISKEDLSRYNDAAMSNVFIDRIFSGAVTRGKTIQKEGEM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 221 SYADFVWFLISEEDKRNPTSIEYWFRCMDVDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQMLDLVKPAVDGK 300
Cdd:cd21339  161 SYADFVWFLISEEDKKEPTSIEYWFRCLDIDGDGYLSVFELEYFYEEQCERMKIHGIEPLPFQDVLCQILDLVKPKDPGK 240

                        250
                 ....*....|....*....
gi 299115261 301 ITLRDLKRCRMAHIFYDTF 319
Cdd:cd21339  241 ITLQDLKRCNIALNFFDTF 259
EF-hand_13 pfam17958
EF-hand domain; This entry represents an EF-hand domain found in one of the regulatory B ...
 60-149 4.33e-45

EF-hand domain; This entry represents an EF-hand domain found in one of the regulatory B subunits of PP2A.


Pssm-ID: 465586 [Multi-domain]  Cd Length: 90  Bit Score: 150.98  E-value: 4.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261   60 DDASKFICLLAKPNCSSLEQEDFIPLLQDVVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKITSTEIRKSNF 139
Cdd:pfam17958   1 DEAARFFRLLKGPGKNYLSREDFYPFVQDVVDTHPGLEFLREAEEFQDKYIQTVIARIFYVVNRSWSGKITLLELRKSDL 80

                          90
                  ....*....|
gi 299115261  140 LQTLALLEEE 149
Cdd:pfam17958  81 LKAVRQLDEE 90
PPP2R3C cd21505
serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric ...
 80-332 1.53e-36

serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This subfamily includes protein phosphatase subunit G5PR (also known as serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma, G4-1, G5pr, GDRM, SPGF36, or C14orf10) that is encoded by the PPP2R3C gene. It is involved in the control of the dynamic organization of the cortical cytoskeleton and plays an important role in the organization of interphase microtubule arrays in part through the regulation of nucleation geometry. G5PR is involved in the ontogeny of multiple organs, especially critical for testis development and spermatogenesis. PPP2R3C gene variants cause syndromic 46,XY gonadal dysgenesis and impaired spermatogenesis in humans, and thus is emerging as a potential therapeutic target for male infertility.


Pssm-ID: 410338 [Multi-domain]  Cd Length: 382  Bit Score: 137.32  E-value: 1.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261  80 EDFIpllQDVVDTHPGLTFLkdAPEFHSRYITTVIQRIFYTVNRSWSGKITSTEIRKSNFLQTLALL--EEEEDINQITD 157
Cdd:cd21505  139 ENYI---LELIPTLPQLSGL--EESFYSFYVCTAVRKFFFFLDPLRRGKIRIKDILASPFLDELLELrdEELSEELQESN 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 158 YFSYEHFYVIYCKFWELDTDHDLYISQADLSRYNDQASSSRIIERIFSGAVTRgktiqkEGRMSYADFVWFLISEEDKRN 237
Cdd:cd21505  214 WFSAPSALRVYGQYLNLDKDHNGMLSKQELSRYGKGTLTSVFIDRVFQECLTY------NGEMDYKTFLDFVLAMENRKE 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 238 PTSIEYWFRCMDVDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQMLDLVKPAVDGKITLRDLKRCRMAHIFYD 317
Cdd:cd21505  288 PQALQYFFRILDLKGQGYLTPFTLNYFFRAIQEKMKEHGQEPVSFEDVKDEIFDMVKPKDPLKITLQDLINSGQGDTVVS 367

                        250
                 ....*....|....*
gi 299115261 318 TFFNLEKYLDHEQRD 332
Cdd:cd21505  368 ILIDLNGFWAYENRE 382
EF-hand_7 pfam13499
EF-hand domain pair;
164-265 2.24e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.94  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261  164 FYVIYCKFWELDTDHDLYISQADLSRYndqasssriierifsgavtrgktIQKegrmsyadfvwflISEEDKRNPTSIEY 243
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKL-----------------------LRK-------------LEEGEPLSDEEVEE 44

                          90       100
                  ....*....|....*....|..
gi 299115261  244 WFRCMDVDGDGVLSMYELEYFY 265
Cdd:pfam13499  45 LFKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
171-267 7.64e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 7.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299115261 171 FWELDTDHDLYISQADLsryndQASSSRIIERIFSGAVTRGktiqkEGRMSYADFVWFLISEEDKRNPTSIEYWFRCMDV 250
Cdd:COG5126   11 FDLLDADGDGVLERDDF-----EALFRRLWATLFSEADTDG-----DGRISREEFVAGMESLFEATVEPFARAAFDLLDT 80

                         90
                 ....*....|....*..
gi 299115261 251 DGDGVLSMYELEYFYEE 267
Cdd:COG5126   81 DGDGKISADEFRRLLTA 97
 
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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