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Conserved domains on  [gi|85567685|gb|AAI12262|]
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Polycystin 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 464-687 4.65e-88

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


:

Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 280.70  E-value: 4.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   464 RYVTTFDFFLAACEIIFCFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLEDQ- 542
Cdd:pfam08016   1 RYVTNRSLFILLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   543 NTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQ 622
Cdd:pfam08016  81 VTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85567685   623 VDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEV 687
Cdd:pfam08016 161 APNFSNFVKSILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
 269-463 1.56e-85

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


:

Pssm-ID: 466668  Cd Length: 199  Bit Score: 273.15  E-value: 1.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   269 NFKTLSSMEDFWKFTEGSLLDGLYwkmqpSNQTE-ADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDV 347
Cdd:pfam20519   1 GLLTVTDLDDIWDWLSSVLLPALH-----SNKTPsGLPGSFIAYESLLLGVPRLRQLRVRNSSCLVHDKFVREINECHAG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   348 YSVSSEDR--------APFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGT 419
Cdd:pfam20519  76 YSPPSEDRklysalpyKPVHYGSKYWFIYTPPGLLMGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 85567685   420 RATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLI 463
Cdd:pfam20519 156 RAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
Fer4_24 super family cl39498
Ferredoxin I 4Fe-4S cluster domain; This is domain is found in Ferredoxin I (FdI), an ...
 834-868 3.41e-05

Ferredoxin I 4Fe-4S cluster domain; This is domain is found in Ferredoxin I (FdI), an Iron-sulfur ([Fe-S]) cluster-containing protein, present in species such as Azotobacter vinelandii. [Fe-S] proteins participate in electron transfer, catalytic, regulatory, and structural function. The FdI cluster exhibits a pH-dependent reduction potential and reversible protonation in the reduced state.


The actual alignment was detected with superfamily member pfam18109:

Pssm-ID: 436280 [Multi-domain]  Cd Length: 35  Bit Score: 41.58  E-value: 3.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 85567685   834 VSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLE 868
Cdd:pfam18109   1 VSGEEFQTLTAQVLQLERSLAGVMSNIDAIGGKLE 35
EFh_HEF super family cl23634
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 724-792 7.99e-04

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


The actual alignment was detected with superfamily member cd15902:

Pssm-ID: 355006 [Multi-domain]  Cd Length: 254  Bit Score: 42.34  E-value: 7.99e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685 724 DISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQ-MRDDLEKEREDLDLD 792
Cdd:cd15902 152 ELDEMAKLLPVQENFLLKFQILGAMDLTKEDFEKVFEHYDKDNNGVIEGNELDAlLKDLLEKNKADIDKP 221
 
Name Accession Description Interval E-value
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 464-687 4.65e-88

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 280.70  E-value: 4.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   464 RYVTTFDFFLAACEIIFCFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLEDQ- 542
Cdd:pfam08016   1 RYVTNRSLFILLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   543 NTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQ 622
Cdd:pfam08016  81 VTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85567685   623 VDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEV 687
Cdd:pfam08016 161 APNFSNFVKSILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
 269-463 1.56e-85

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 273.15  E-value: 1.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   269 NFKTLSSMEDFWKFTEGSLLDGLYwkmqpSNQTE-ADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDV 347
Cdd:pfam20519   1 GLLTVTDLDDIWDWLSSVLLPALH-----SNKTPsGLPGSFIAYESLLLGVPRLRQLRVRNSSCLVHDKFVREINECHAG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   348 YSVSSEDR--------APFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGT 419
Cdd:pfam20519  76 YSPPSEDRklysalpyKPVHYGSKYWFIYTPPGLLMGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 85567685   420 RATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLI 463
Cdd:pfam20519 156 RAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 388-769 1.52e-22

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 104.64  E-value: 1.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   388 GAGYYLDLSRTREETAAQVASLKKNVWLDRG-TRATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLIRYV 466
Cdd:PLN03223 1089 GFPYFFDINLSAAEAQTWLDYMIYGLMIDDVkTRKVTAQVVVYNAELGYFGNVMVFFEFTDGGKIEVTHRLNTIRVELYE 1168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   467 TTFDFFLAACEIIFCFFIFYYVVEEILEI------RIHKLHYFRSFWNCLDVVIVVLSVVAIGI---------------- 524
Cdd:PLN03223 1169 TYEDWVRFAMEILLAIGAVYSVYEEAMDFgsskktRGSYLAYFLSGWNYVDFASIGLHLATIMMwfvfswsyarafepdi 1248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   525 --NIYRTSNVEVLLQFLEDQNTFPN----FEHLA----YWQIQFNnIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCA 594
Cdd:PLN03223 1249 hyDIYKNLSASANFTALRIPNELPEmndmFLEMKnlvdYFQWYMT-LSGINIILLLGRILKLMDFQPRLGVITRTLWLAG 1327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   595 KDLFGFAIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEAN-----RVLGPIYFTTFVFFMF 669
Cdd:PLN03223 1328 ADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENLLGDITYFNEDLKNltglqFVVGMIYFYSYNIFVF 1407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   670 FILLNMFLAIINDTYSEVKSDLAQQ-KAEMELSDLIRKGYHKALVKLKLKkntvDDISESlrqgggKLNfDELRQdLKGK 748
Cdd:PLN03223 1408 MILFNFLLAIICDAFGEVKANAAETvSVHTELFPMLRDKWRSMFKGWFYK----NHIPEA------RVR-RQLRI-WKGE 1475

                         410       420
                  ....*....|....*....|....*...
gi 85567685   749 GHTDAEIEA-------IFTKYDQDGDQE 769
Cdd:PLN03223 1476 NPDEEEEEAfreekekVFTYLNKELDEA 1503
Fer4_24 pfam18109
Ferredoxin I 4Fe-4S cluster domain; This is domain is found in Ferredoxin I (FdI), an ...
 834-868 3.41e-05

Ferredoxin I 4Fe-4S cluster domain; This is domain is found in Ferredoxin I (FdI), an Iron-sulfur ([Fe-S]) cluster-containing protein, present in species such as Azotobacter vinelandii. [Fe-S] proteins participate in electron transfer, catalytic, regulatory, and structural function. The FdI cluster exhibits a pH-dependent reduction potential and reversible protonation in the reduced state.


Pssm-ID: 436280 [Multi-domain]  Cd Length: 35  Bit Score: 41.58  E-value: 3.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 85567685   834 VSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLE 868
Cdd:pfam18109   1 VSGEEFQTLTAQVLQLERSLAGVMSNIDAIGGKLE 35
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 597-690 5.88e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   597 LFGFAIMFFIIFLAYAQLAYL--------VFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEAN-RVLGPIYFTTFVFF 667
Cdd:TIGR00870 519 LFGFACGLNQLYQYYDELKLNecsnpharSCEKQGNAYSTLFETSQELFWAIIGLGDLLANEHKFtEFVGLLLFGAYNVI 598

                          90       100
                  ....*....|....*....|...
gi 85567685   668 MFFILLNMFLAIINDTYSEVKSD 690
Cdd:TIGR00870 599 MYILLLNMLIAMMGNTYQLIADD 621
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 724-792 7.99e-04

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


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 42.34  E-value: 7.99e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685 724 DISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQ-MRDDLEKEREDLDLD 792
Cdd:cd15902 152 ELDEMAKLLPVQENFLLKFQILGAMDLTKEDFEKVFEHYDKDNNGVIEGNELDAlLKDLLEKNKADIDKP 221
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
734-774 5.32e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 5.32e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 85567685 734 GKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHE 774
Cdd:COG5126  84 GKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEE 124
 
Name Accession Description Interval E-value
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 464-687 4.65e-88

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 280.70  E-value: 4.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   464 RYVTTFDFFLAACEIIFCFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLEDQ- 542
Cdd:pfam08016   1 RYVTNRSLFILLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   543 NTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQ 622
Cdd:pfam08016  81 VTFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 85567685   623 VDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEV 687
Cdd:pfam08016 161 APNFSNFVKSILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSYVEV 225
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
 269-463 1.56e-85

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 273.15  E-value: 1.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   269 NFKTLSSMEDFWKFTEGSLLDGLYwkmqpSNQTE-ADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDV 347
Cdd:pfam20519   1 GLLTVTDLDDIWDWLSSVLLPALH-----SNKTPsGLPGSFIAYESLLLGVPRLRQLRVRNSSCLVHDKFVREINECHAG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   348 YSVSSEDR--------APFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGT 419
Cdd:pfam20519  76 YSPPSEDRklysalpyKPVHYGSKYWFIYTPPGLLMGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 85567685   420 RATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLI 463
Cdd:pfam20519 156 RAVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 388-769 1.52e-22

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 104.64  E-value: 1.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   388 GAGYYLDLSRTREETAAQVASLKKNVWLDRG-TRATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLIRYV 466
Cdd:PLN03223 1089 GFPYFFDINLSAAEAQTWLDYMIYGLMIDDVkTRKVTAQVVVYNAELGYFGNVMVFFEFTDGGKIEVTHRLNTIRVELYE 1168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   467 TTFDFFLAACEIIFCFFIFYYVVEEILEI------RIHKLHYFRSFWNCLDVVIVVLSVVAIGI---------------- 524
Cdd:PLN03223 1169 TYEDWVRFAMEILLAIGAVYSVYEEAMDFgsskktRGSYLAYFLSGWNYVDFASIGLHLATIMMwfvfswsyarafepdi 1248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   525 --NIYRTSNVEVLLQFLEDQNTFPN----FEHLA----YWQIQFNnIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCA 594
Cdd:PLN03223 1249 hyDIYKNLSASANFTALRIPNELPEmndmFLEMKnlvdYFQWYMT-LSGINIILLLGRILKLMDFQPRLGVITRTLWLAG 1327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   595 KDLFGFAIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEAN-----RVLGPIYFTTFVFFMF 669
Cdd:PLN03223 1328 ADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENLLGDITYFNEDLKNltglqFVVGMIYFYSYNIFVF 1407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   670 FILLNMFLAIINDTYSEVKSDLAQQ-KAEMELSDLIRKGYHKALVKLKLKkntvDDISESlrqgggKLNfDELRQdLKGK 748
Cdd:PLN03223 1408 MILFNFLLAIICDAFGEVKANAAETvSVHTELFPMLRDKWRSMFKGWFYK----NHIPEA------RVR-RQLRI-WKGE 1475

                         410       420
                  ....*....|....*....|....*...
gi 85567685   749 GHTDAEIEA-------IFTKYDQDGDQE 769
Cdd:PLN03223 1476 NPDEEEEEAfreekekVFTYLNKELDEA 1503
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 477-690 9.17e-18

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 83.47  E-value: 9.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   477 EIIFCFFIFYYVVEEILEIRI--HKLHYFRSFWNCLDVvivvlsvvaiginiyrtsnVEVLLQFLEdqntfpnfeHLAYW 554
Cdd:pfam00520  36 EILDYVFTGIFTLEMLLKIIAagFKKRYFRSPWNILDF-------------------VVVLPSLIS---------LVLSS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   555 QIQFNNIAAVTVFFVwIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQVD---------- 624
Cdd:pfam00520  88 VGSLSGLRVLRLLRL-LRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKtwenpdngrt 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   625 DFSTFQECIFTQFRII----LGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEVKSD 690
Cdd:pfam00520 167 NFDNFPNAFLWLFQTMttegWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTER 236
Fer4_24 pfam18109
Ferredoxin I 4Fe-4S cluster domain; This is domain is found in Ferredoxin I (FdI), an ...
 834-868 3.41e-05

Ferredoxin I 4Fe-4S cluster domain; This is domain is found in Ferredoxin I (FdI), an Iron-sulfur ([Fe-S]) cluster-containing protein, present in species such as Azotobacter vinelandii. [Fe-S] proteins participate in electron transfer, catalytic, regulatory, and structural function. The FdI cluster exhibits a pH-dependent reduction potential and reversible protonation in the reduced state.


Pssm-ID: 436280 [Multi-domain]  Cd Length: 35  Bit Score: 41.58  E-value: 3.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 85567685   834 VSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLE 868
Cdd:pfam18109   1 VSGEEFQTLTAQVLQLERSLAGVMSNIDAIGGKLE 35
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 597-690 5.88e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685   597 LFGFAIMFFIIFLAYAQLAYL--------VFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEAN-RVLGPIYFTTFVFF 667
Cdd:TIGR00870 519 LFGFACGLNQLYQYYDELKLNecsnpharSCEKQGNAYSTLFETSQELFWAIIGLGDLLANEHKFtEFVGLLLFGAYNVI 598

                          90       100
                  ....*....|....*....|...
gi 85567685   668 MFFILLNMFLAIINDTYSEVKSD 690
Cdd:TIGR00870 599 MYILLLNMLIAMMGNTYQLIADD 621
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 724-792 7.99e-04

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


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 42.34  E-value: 7.99e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567685 724 DISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQ-MRDDLEKEREDLDLD 792
Cdd:cd15902 152 ELDEMAKLLPVQENFLLKFQILGAMDLTKEDFEKVFEHYDKDNNGVIEGNELDAlLKDLLEKNKADIDKP 221
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
734-774 5.32e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 5.32e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 85567685 734 GKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHE 774
Cdd:COG5126  84 GKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEE 124
 
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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