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Conserved domains on  [gi|42561672|ref|NP_171892|]
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Calcium-binding EF hand family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PPP2R3A_B-like cd21504
serine/threonine protein phosphatase 2A regulatory subunit B" alpha and beta subunits, and ...
197-470 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: 513.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 197 WIDGNMLTMDTASQIYNILRQQGCSYLRQADFKPVLDELLATHPGLEFLRTISEFQERYAETVIYRIFYYINRSGTGCLT 276
Cdd:cd21504   1 WKKILAGCHDDASRFFRILKKPDRNYLVPEDFKPFLQDLLDTHPGLEFLQDTPEFQERYAETVIYRIFYSVNRSWSGRIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 277 LRELRRGNLIAAMQQLDEEDDINKIIRYFSYEHFYVIYCKFWELDGDHDCFIDKDNLIKYGNNALTYRIVDRIFSQIPRK 356
Cdd:cd21504  81 LRELRRSNLLQALLLLDEEEDINKVLRYFSYEHFYVIYCKFWELDTDHDLLIDKDDLLRYGDHALSPRIVDRIFSGAVRR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 357 FTSKVEGKMSYEDFVYFILAEEDKSSEPSLEYWFKCVDLDGNGVITSNEMQFFFEEQLHRMECITQEAVLFSDILCQIID 436
Cdd:cd21504 161 FKSGKEGKMSYEDFVWFILSEEDKTSPTSIEYWFRCMDLDGDGVLSMYEMEYFYEEQLQRMECLGIEPVPFEDILCQMLD 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 42561672 437 MIGPEKENCITLQDLKGSKLSANVFNILFNLNKF 470
Cdd:cd21504 241 MIKPENEGKITLRDLKRCKLAGNFFNTLFNLNKF 274
 
Name Accession Description Interval E-value
PPP2R3A_B-like cd21504
serine/threonine protein phosphatase 2A regulatory subunit B" alpha and beta subunits, and ...
197-470 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: 513.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 197 WIDGNMLTMDTASQIYNILRQQGCSYLRQADFKPVLDELLATHPGLEFLRTISEFQERYAETVIYRIFYYINRSGTGCLT 276
Cdd:cd21504   1 WKKILAGCHDDASRFFRILKKPDRNYLVPEDFKPFLQDLLDTHPGLEFLQDTPEFQERYAETVIYRIFYSVNRSWSGRIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 277 LRELRRGNLIAAMQQLDEEDDINKIIRYFSYEHFYVIYCKFWELDGDHDCFIDKDNLIKYGNNALTYRIVDRIFSQIPRK 356
Cdd:cd21504  81 LRELRRSNLLQALLLLDEEEDINKVLRYFSYEHFYVIYCKFWELDTDHDLLIDKDDLLRYGDHALSPRIVDRIFSGAVRR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 357 FTSKVEGKMSYEDFVYFILAEEDKSSEPSLEYWFKCVDLDGNGVITSNEMQFFFEEQLHRMECITQEAVLFSDILCQIID 436
Cdd:cd21504 161 FKSGKEGKMSYEDFVWFILSEEDKTSPTSIEYWFRCMDLDGDGVLSMYEMEYFYEEQLQRMECLGIEPVPFEDILCQMLD 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 42561672 437 MIGPEKENCITLQDLKGSKLSANVFNILFNLNKF 470
Cdd:cd21504 241 MIKPENEGKITLRDLKRCKLAGNFFNTLFNLNKF 274
EF-hand_13 pfam17958
EF-hand domain; This entry represents an EF-hand domain found in one of the regulatory B ...
206-295 4.14e-38

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: 134.80  E-value: 4.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672   206 DTASQIYNILRQQGCSYLRQADFKPVLDELLATHPGLEFLRTISEFQERYAETVIYRIFYYINRSGTGCLTLRELRRGNL 285
Cdd:pfam17958   1 DEAARFFRLLKGPGKNYLSREDFYPFVQDVVDTHPGLEFLREAEEFQDKYIQTVIARIFYVVNRSWSGKITLLELRKSDL 80
                          90
                  ....*....|
gi 42561672   286 IAAMQQLDEE 295
Cdd:pfam17958  81 LKAVRQLDEE 90
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
317-412 2.26e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.32  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 317 FWELDGDHDCFIDKDNLikygnNALTYRIVDRIFSqiprKFTSKVEGKMSYEDFVYFILAEEDKSSEPSLEYWFKCVDLD 396
Cdd:COG5126  11 FDLLDADGDGVLERDDF-----EALFRRLWATLFS----EADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTD 81
                        90
                ....*....|....*.
gi 42561672 397 GNGVITSNEMQFFFEE 412
Cdd:COG5126  82 GDGKISADEFRRLLTA 97
 
Name Accession Description Interval E-value
PPP2R3A_B-like cd21504
serine/threonine protein phosphatase 2A regulatory subunit B" alpha and beta subunits, and ...
197-470 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: 513.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 197 WIDGNMLTMDTASQIYNILRQQGCSYLRQADFKPVLDELLATHPGLEFLRTISEFQERYAETVIYRIFYYINRSGTGCLT 276
Cdd:cd21504   1 WKKILAGCHDDASRFFRILKKPDRNYLVPEDFKPFLQDLLDTHPGLEFLQDTPEFQERYAETVIYRIFYSVNRSWSGRIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 277 LRELRRGNLIAAMQQLDEEDDINKIIRYFSYEHFYVIYCKFWELDGDHDCFIDKDNLIKYGNNALTYRIVDRIFSQIPRK 356
Cdd:cd21504  81 LRELRRSNLLQALLLLDEEEDINKVLRYFSYEHFYVIYCKFWELDTDHDLLIDKDDLLRYGDHALSPRIVDRIFSGAVRR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 357 FTSKVEGKMSYEDFVYFILAEEDKSSEPSLEYWFKCVDLDGNGVITSNEMQFFFEEQLHRMECITQEAVLFSDILCQIID 436
Cdd:cd21504 161 FKSGKEGKMSYEDFVWFILSEEDKTSPTSIEYWFRCMDLDGDGVLSMYEMEYFYEEQLQRMECLGIEPVPFEDILCQMLD 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 42561672 437 MIGPEKENCITLQDLKGSKLSANVFNILFNLNKF 470
Cdd:cd21504 241 MIKPENEGKITLRDLKRCKLAGNFFNTLFNLNKF 274
PPP2R3A cd21506
serine/threonine protein phosphatase 2A regulatory subunit B" subunit alpha; Heterotrimeric ...
206-479 3.49e-107

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: 321.50  E-value: 3.49e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 206 DTASQIYNILRQQGCSYLRQADFKPVLDELLATHPGLEFLRTISEFQERYAETVIYRIFYYINRSGTGCLTLRELRRGNL 285
Cdd:cd21506  10 DDASKFVYLLAKPNCSYLEQEDFIPLLQDIVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWSGKITLTELRKSNF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 286 IAAMQQLDEEDDINKIIRYFSYEHFYVIYCKFWELDGDHDCFIDKDNLIKYGNNALTYRIVDRIFS-QIPRKFTSKVEGK 364
Cdd:cd21506  90 LQTLALLEEEDDINQITDYFSYEHFYVIYCKFWELDTDHDLYIDQKDLARYNDQASSSRIIERIFSgAVTRGNSVQKEGR 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 365 MSYEDFVYFILAEEDKSSEPSLEYWFKCVDLDGNGVITSNEMQFFFEEQLHRMECITQEAVLFSDILCQIIDMIGPEKEN 444
Cdd:cd21506 170 MSYADFVWFLISEEDKRNPTSIEYWFRCMDLDGDGVLSMYELEYFYEEQCERMEAMGIEPLPFHDLLCQMLDLVKPEVDG 249
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42561672 445 CITLQDLKGSKLSANVFNILFNLNKFMAFETRDPF 479
Cdd:cd21506 250 KITLRDLKRCRMAHIFYDTFFNLEKYLDHEQRDPF 284
PPP2R3B cd21507
serine/threonine protein phosphatase 2A regulatory subunit B" subunit beta; Heterotrimeric ...
123-476 1.68e-106

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: 322.68  E-value: 1.68e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 123 YYQHGRPPAKELKEQCLSMVDQVFSNYIDGLHVDEFKSITKQVCKLPSFLSPALFRKIDPNCTDIVTRDAFIKYWIDGNM 202
Cdd:cd21507   1 YFPRGCPKDSVNVDAVIAKIENTFSQFPNERATLDDMGKVAKACDCPLYWKGPLFYAAGGERTGSVSVHKFVAMWRKILQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 203 LTMDTASQIYNILRQQGCSYLRQADFKPVLDELLATHPGLEFLRTISEFQERYAETVIYRIFYYINRSGTGCLTLRELRR 282
Cdd:cd21507  81 NCHDDAAKFVHLLMKPGCNYLVQEDFIPFLQDVVNTHPGLSFLKEASEFHSRYITTVIQRIFYTVNRSWSGRITCTELRR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 283 GNLIAAMQQLDEEDDINKIIRYFSYEHFYVIYCKFWELDGDHDCFIDKDNLIKYGNNALTYRIVDRIFS-QIPRKFTSKV 361
Cdd:cd21507 161 SSFLQNVALLEEEADINQLTEFFSYEHFYVIYCKFWELDTDHDLYIDQKDLARHNDHAISNRMIERIFSgAVTRGRKAQK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 362 EGKMSYEDFVYFILAEEDKSSEPSLEYWFKCVDLDGNGVITSNEMQFFFEEQLHRMECITQEAVLFSDILCQIIDMIGPE 441
Cdd:cd21507 241 EGKISYADFVWFLISEEDKKTPTSIEYWFRCMDLDGDGALSMYELEYFYEEQCQKLDNMAIEPLPFEDCLCQMLDLVKPR 320
                       330       340       350
                ....*....|....*....|....*....|....*
gi 42561672 442 KENCITLQDLKGSKLSANVFNILFNLNKFMAFETR 476
Cdd:cd21507 321 TEGKITLHDLKRCKLANVFFDTFFNIEKYLDHEQK 355
PPP2R3 cd21339
serine/threonine protein phosphatase 2A regulatory subunit B"; Heterotrimeric serine/threonine ...
208-461 3.06e-88

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: 272.15  E-value: 3.06e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 208 ASQIYNILRQQGCSYLRQADFKPVLDELLATHPGLEFLRTISEFQERYAETVIYRIFYYINRSGTGCLTLRELRRGNLIA 287
Cdd:cd21339   2 ATKFGLLLYDPGCGYLRQEDFEPYLQDVVPTHPGLDFLKKAPEFHSRYITTVIQRIFYFVNRSWSGKITIQEIRASSFLQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 288 AMQQLDEEDDINKIIRYFSYEHFYVIYCKFWELDGDHDCFIDKDNLIKYGNNALTYRIVDRIFSQ-IPRKFTSKVEGKMS 366
Cdd:cd21339  82 DLALLEEEEDINQETNWFSYEHFYVIYCKFWELDTDHDLMISKEDLSRYNDAAMSNVFIDRIFSGaVTRGKTIQKEGEMS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 367 YEDFVYFILAEEDKSSEPSLEYWFKCVDLDGNGVITSNEMQFFFEEQLHRMECITQEAVLFSDILCQIIDMIGPEKENCI 446
Cdd:cd21339 162 YADFVWFLISEEDKKEPTSIEYWFRCLDIDGDGYLSVFELEYFYEEQCERMKIHGIEPLPFQDVLCQILDLVKPKDPGKI 241
                       250
                ....*....|....*
gi 42561672 447 TLQDLKGSKLSANVF 461
Cdd:cd21339 242 TLQDLKRCNIALNFF 256
EF-hand_13 pfam17958
EF-hand domain; This entry represents an EF-hand domain found in one of the regulatory B ...
206-295 4.14e-38

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: 134.80  E-value: 4.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672   206 DTASQIYNILRQQGCSYLRQADFKPVLDELLATHPGLEFLRTISEFQERYAETVIYRIFYYINRSGTGCLTLRELRRGNL 285
Cdd:pfam17958   1 DEAARFFRLLKGPGKNYLSREDFYPFVQDVVDTHPGLEFLREAEEFQDKYIQTVIARIFYVVNRSWSGKITLLELRKSDL 80
                          90
                  ....*....|
gi 42561672   286 IAAMQQLDEE 295
Cdd:pfam17958  81 LKAVRQLDEE 90
PPP2R3C cd21505
serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric ...
219-477 1.27e-33

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: 131.15  E-value: 1.27e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 219 GCSYLRQADFKPVLDELLATHPGLEFLRtiSEFQERYAETVIYRIFYYI--NRSGT---------GCLT-LRELRRgnli 286
Cdd:cd21505 129 GDGFLTESDLENYILELIPTLPQLSGLE--ESFYSFYVCTAVRKFFFFLdpLRRGKirikdilasPFLDeLLELRD---- 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 287 aamQQLDEEDDINKiirYFSYEHFYVIYCKFWELDGDHDCFIDKDNLIKYGNNALTYRIVDRIFSQIPRKftskvEGKMS 366
Cdd:cd21505 203 ---EELSEELQESN---WFSAPSALRVYGQYLNLDKDHNGMLSKQELSRYGKGTLTSVFIDRVFQECLTY-----NGEMD 271
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 367 YEDFVYFILAEEDKSSEPSLEYWFKCVDLDGNGVITSNEMQFFFEEQLHRMECITQEAVLFSDILCQIIDMIGPEKENCI 446
Cdd:cd21505 272 YKTFLDFVLAMENRKEPQALQYFFRILDLKGQGYLTPFTLNYFFRAIQEKMKEHGQEPVSFEDVKDEIFDMVKPKDPLKI 351
                       250       260       270
                ....*....|....*....|....*....|.
gi 42561672 447 TLQDLKGSKLSANVFNILFNLNKFMAFETRD 477
Cdd:cd21505 352 TLQDLINSGQGDTVVSILIDLNGFWAYENRE 382
EF-hand_7 pfam13499
EF-hand domain pair;
310-410 1.57e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672   310 FYVIYCKFWELDGDHDcfidkdnlikygnnaltyrivdrifsqiprkftskveGKMSYEDFVYFI--LAEEDKSSEPSLE 387
Cdd:pfam13499   1 EEKLKEAFKLLDSDGD-------------------------------------GYLDVEELKKLLrkLEEGEPLSDEEVE 43
                          90       100
                  ....*....|....*....|...
gi 42561672   388 YWFKCVDLDGNGVITSNEMQFFF 410
Cdd:pfam13499  44 ELFKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
317-412 2.26e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.32  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42561672 317 FWELDGDHDCFIDKDNLikygnNALTYRIVDRIFSqiprKFTSKVEGKMSYEDFVYFILAEEDKSSEPSLEYWFKCVDLD 396
Cdd:COG5126  11 FDLLDADGDGVLERDDF-----EALFRRLWATLFS----EADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTD 81
                        90
                ....*....|....*.
gi 42561672 397 GNGVITSNEMQFFFEE 412
Cdd:COG5126  82 GDGKISADEFRRLLTA 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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