NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564338938|ref|XP_006233422|]
View 

nuclear factor NF-kappa-B p105 subunit isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
41-242 6.76e-146

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa B1); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B1 is involved in the canonical NF-kappa B signaling pathway which is activated by many agonists and is essential in immune and inflammatory responses, as well as cell survival. p105 is involved in its own specific NF-kappa B signaling pathway which is also implicated in immune and inflammatory responses. p105 may also act as an I-kappa B due to its C-terminal ankyrin repeats. It is also involved in mitogen-activated protein kinase (MAPK) signaling as its degradation leads to the activation of TPL-2, a MAPK kinase kinase which activates ERK pathways.


:

Pssm-ID: 143651  Cd Length: 202  Bit Score: 429.31  E-value: 6.76e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 120
Cdd:cd07935    1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 121 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAAL 200
Cdd:cd07935   81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564338938 201 QQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 242
Cdd:cd07935  161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
249-350 4.80e-62

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


:

Pssm-ID: 238582  Cd Length: 102  Bit Score: 204.47  E-value: 4.80e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 249 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASV 328
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 564338938 329 FVQLRRKSDLETSEPKPFLYYP 350
Cdd:cd01177   81 KIQLKRPSDGERSESVPFTYVP 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
494-767 1.75e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 494 FQDNLFLEKALQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGSISDDII 573
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 574 NMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNsKAAllINHPNGEGLNAI 653
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GAD--VNAQDNDGNTPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 654 HIAVMSNSLSCLQLLVAAGAEVNAQeQKSGRTALHLAVEYDNISLAGcLLLEGDALVDSTTYDGTTPLHIAAGRGSTRLA 733
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564338938 734 ALLKAAGADPLVENFEPLYDLDDSWEKAGEDEGV 767
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
814-863 1.02e-26

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08797:

Pssm-ID: 472698  Cd Length: 76  Bit Score: 103.83  E-value: 1.02e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564338938 814 RLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEMS 863
Cdd:cd08797    2 KQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVS 51
 
Name Accession Description Interval E-value
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
41-242 6.76e-146

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa B1); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B1 is involved in the canonical NF-kappa B signaling pathway which is activated by many agonists and is essential in immune and inflammatory responses, as well as cell survival. p105 is involved in its own specific NF-kappa B signaling pathway which is also implicated in immune and inflammatory responses. p105 may also act as an I-kappa B due to its C-terminal ankyrin repeats. It is also involved in mitogen-activated protein kinase (MAPK) signaling as its degradation leads to the activation of TPL-2, a MAPK kinase kinase which activates ERK pathways.


Pssm-ID: 143651  Cd Length: 202  Bit Score: 429.31  E-value: 6.76e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 120
Cdd:cd07935    1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 121 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAAL 200
Cdd:cd07935   81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564338938 201 QQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 242
Cdd:cd07935  161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
43-241 1.93e-84

Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain.


Pssm-ID: 425749  Cd Length: 169  Bit Score: 267.63  E-value: 1.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938   43 LQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGIC 122
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKDGVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  123 TVTAGPKDMVVGFANLGILHVTKKKVFETLEARMteacirgynpgllvhsdlaylqaegggdrQLTDREKEiIRQAALQQ 202
Cdd:pfam00554  81 EVELGPEDMVASFQNLGIQCVKKKDVEEALKERI-----------------------------ELNIDPFN-VGFEALRQ 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564338938  203 TKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDS 241
Cdd:pfam00554 131 IKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
249-350 4.80e-62

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


Pssm-ID: 238582  Cd Length: 102  Bit Score: 204.47  E-value: 4.80e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 249 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASV 328
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 564338938 329 FVQLRRKSDLETSEPKPFLYYP 350
Cdd:cd01177   81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
250-351 6.73e-57

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 190.47  E-value: 6.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  250 KIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASVF 329
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 564338938  330 VQLRRKSDLETSEPKPFLYYPE 351
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
494-767 1.75e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 494 FQDNLFLEKALQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGSISDDII 573
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 574 NMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNsKAAllINHPNGEGLNAI 653
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GAD--VNAQDNDGNTPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 654 HIAVMSNSLSCLQLLVAAGAEVNAQeQKSGRTALHLAVEYDNISLAGcLLLEGDALVDSTTYDGTTPLHIAAGRGSTRLA 733
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564338938 734 ALLKAAGADPLVENFEPLYDLDDSWEKAGEDEGV 767
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
814-863 1.02e-26

Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the Nuclear Factor-KappaB1 (NF-kB1) precursor protein p105. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). NF-kB1 (or p50) is produced from the processing of the precursor protein p105, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the classical (or canonical) NF-kB pathway. In the cytosol, p50 forms an inactive complex with RelA (or p65) and the Inhibitor of NF-kB (IkB). Activation is triggered by the phosphorylation and degradation of IkB, resulting in the active DNA-binding p50-RelA dimer to migrate to the nucleus. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260063  Cd Length: 76  Bit Score: 103.83  E-value: 1.02e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564338938 814 RLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEMS 863
Cdd:cd08797    2 KQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVS 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
584-678 2.16e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  584 LHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKIlgvllknskAALLINHPNGE----GLNAIHIAVMS 659
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI---------VKLLLEHADVNlkdnGRTALHYAARS 71
                          90
                  ....*....|....*....
gi 564338938  660 NSLSCLQLLVAAGAEVNAQ 678
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
573-724 2.20e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.84  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 573 INMRN-DLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNSKAallINHPNGEGLN 651
Cdd:PHA02878 160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNT 236
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564338938 652 AIHIAVMS-NSLSCLQLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLagcLLLEGDALVDSTTYDGTTPLHIA 724
Cdd:PHA02878 237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK---LLLEYGADINSLNSYKLTPLSSA 307
IPT smart00429
ig-like, plexins, transcription factors;
248-349 4.76e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 65.52  E-value: 4.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938   248 NLKIVRMDRTAGCVTGGEEIyLLCDKVQKDDIQIRFYEeeengGVWEGFGDFSPTdvhRQFAIVFKTPKYKDVNITKPAS 327
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV-----GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71
                           90       100
                   ....*....|....*....|..
gi 564338938   328 VfVQLRRkSDLEtSEPKPFLYY 349
Cdd:smart00429  72 T-VGLRN-GGVP-SSPQPFTYV 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
541-730 2.67e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 541 GDSVLHLAIIHLHAQLVRDLLEVTSGsisddIIN--MRNDLY--QTPLHLAVITKQEDVVEDLLRVGADLSL-------- 608
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPE-----LVNepMTSDLYqgETALHIAVVNQNLNLVRELIARGADVVSpratgtff 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 609 ------LDRWGNSVLHLAAKEGHDKIlgvllknskaallinhpngeglnaihiavmsnslscLQLLVAAGAEVNAQEQKs 682
Cdd:cd22192  126 rpgpknLIYYGEHPLSFAACVGNEEI------------------------------------VRLLIEHGADIRAQDSL- 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564338938 683 GRTALHLAVEYDNISLAgC----LLLEGDALVDS------TTYDGTTPLHIAAGRGST 730
Cdd:cd22192  169 GNTVLHILVLQPNKTFA-CqmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNI 225
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
810-863 2.47e-05

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 43.55  E-value: 2.47e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938   810 TEDTRLQLCKLLEIPdPDKNWATLAQKLGLG------ILNNAFRLSPAPSKTLMDNYEMS 863
Cdd:smart00005   1 PELTRQKLAKLLDHP-LGLDWRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQR 59
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
573-677 3.32e-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: 47.77  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  573 INMRNDLYQTPLHLAVItkqEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHD---KILGVLLKNSKAALLINHPNGE- 648
Cdd:TIGR00870  45 INCPDRLGRSALFVAAI---ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDaveAILLHLLAAFRKSGPLELANDQy 121
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564338938  649 ------GLNAIHIAVMSNSLSCLQLLVAAGAEVNA 677
Cdd:TIGR00870 122 tseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
Death pfam00531
Death domain;
814-863 1.89e-03

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 38.11  E-value: 1.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564338938  814 RLQLCKLLEIPDP-DKNWATLAQKLGLGIL-NNAFRLSPA----PSKTLMDNYEMS 863
Cdd:pfam00531   1 RKQLDRLLDPPPPlGKDWRELARKLGLSENeIDEIESENPrlrsQTYELLRLWEQR 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
648-677 6.18e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 6.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 564338938   648 EGLNAIHIAVMSNSLSCLQLLVAAGAEVNA 677
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
41-242 6.76e-146

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa B1); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B1 is involved in the canonical NF-kappa B signaling pathway which is activated by many agonists and is essential in immune and inflammatory responses, as well as cell survival. p105 is involved in its own specific NF-kappa B signaling pathway which is also implicated in immune and inflammatory responses. p105 may also act as an I-kappa B due to its C-terminal ankyrin repeats. It is also involved in mitogen-activated protein kinase (MAPK) signaling as its degradation leads to the activation of TPL-2, a MAPK kinase kinase which activates ERK pathways.


Pssm-ID: 143651  Cd Length: 202  Bit Score: 429.31  E-value: 6.76e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 120
Cdd:cd07935    1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 121 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHSDLAYLQAEGGGDRQLTDREKEIIRQAAL 200
Cdd:cd07935   81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564338938 201 QQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 242
Cdd:cd07935  161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
41-242 2.18e-129

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light polypeptide gene enhancer in B-cells (NF-kappa B); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 and B2 families of transcription factors, also referred to as class I members of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. Family members include NF-kappa B1 and NF-kappa B2. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form), while NF-kappa B2 is called p100 or p52 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). p105 and p100 may also act as I-kappa Bs due to their C-terminal ankyrin repeats.


Pssm-ID: 143643  Cd Length: 197  Bit Score: 386.45  E-value: 2.18e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 120
Cdd:cd07883    1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCEDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 121 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHSDlaylqAEGGGDRQLTDREKEIIRQAAL 200
Cdd:cd07883   81 ICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPGDLVHVD-----AEGGGDRQLTDEEQAEIRQKAK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564338938 201 QQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 242
Cdd:cd07883  156 QQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
43-241 1.93e-84

Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain.


Pssm-ID: 425749  Cd Length: 169  Bit Score: 267.63  E-value: 1.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938   43 LQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGIC 122
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKDGVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  123 TVTAGPKDMVVGFANLGILHVTKKKVFETLEARMteacirgynpgllvhsdlaylqaegggdrQLTDREKEiIRQAALQQ 202
Cdd:pfam00554  81 EVELGPEDMVASFQNLGIQCVKKKDVEEALKERI-----------------------------ELNIDPFN-VGFEALRQ 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564338938  203 TKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDS 241
Cdd:pfam00554 131 IKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
41-242 3.99e-82

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B2 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B2 is commonly referred to as p100 or p52 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B2 is involved in the alternative NF-kappa B signaling pathway which is activated by few agonists and plays an important role in secondary lymphoid organogenesis, maturation of B-cells, and adaptive humoral immunity. p100 may also act as an I-kappa B due to its C-terminal ankyrin repeats.


Pssm-ID: 143650  Cd Length: 185  Bit Score: 262.14  E-value: 3.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHC-ED 119
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCnES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 120 GICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLlvhsdlaylqaegggdrqLTDREKEIIRQAA 199
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTGPYK------------------LTEAEERELEQEA 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564338938 200 LQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 242
Cdd:cd07934  143 KELKKVMDLSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
249-350 4.80e-62

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


Pssm-ID: 238582  Cd Length: 102  Bit Score: 204.47  E-value: 4.80e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 249 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASV 328
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 564338938 329 FVQLRRKSDLETSEPKPFLYYP 350
Cdd:cd01177   81 KIQLKRPSDGERSESVPFTYVP 102
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
41-242 1.08e-59

N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal sub-domain, which may be distantly related to the DNA-binding domain found in P53. The C-terminal sub-domain has an immunoglobulin-like fold and serves as a dimerization module that also binds DNA (see cd00102). The RHD is found in NF-kappa B, nuclear factor of activated T-cells (NFAT), the tonicity-responsive enhancer binding protein (TonEBP), and the arthropod proteins Dorsal and Relish (Rel).


Pssm-ID: 143640  Cd Length: 174  Bit Score: 201.06  E-value: 1.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKH-CED 119
Cdd:cd07827    1 PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPHQLVGKTdCRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 120 GICTVTAGPK-DMVVGFANLGILHVTKKKVFETLEARMTeaciRGYNPGLLVhsdlaylqaegggdrqltdrekeiirQA 198
Cdd:cd07827   81 GVCEVRLGPKnNMTASFNNLGIQCVRKKDVEEALGQRIQ----LGIDPFMVH--------------------------KG 130
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564338938 199 ALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 242
Cdd:cd07827  131 PEGNASDIDLNRVRLCFQAFIEDSDGGFTLPLPPVLSNPIYDKK 174
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
250-351 6.73e-57

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 190.47  E-value: 6.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  250 KIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDVNITKPASVF 329
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 564338938  330 VQLRRKSDLETSEPKPFLYYPE 351
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
RHD-n_c-Rel cd07933
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ...
41-242 5.11e-48

N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the c-Rel family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). c-Rel plays an important role in B cell proliferation and survival.


Pssm-ID: 143649  Cd Length: 172  Bit Score: 168.13  E-value: 5.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 120
Cdd:cd07933    1 PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPHDLVGKDCRDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 121 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTeaciRGYNPGllvhsdlaylqaegggdrqltdrekeIIRQAAL 200
Cdd:cd07933   81 YYEAEFGPERRVLAFQNLGIQCVRRREVKEAIMLRIS----RGINPF--------------------------NVPEEQL 130
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564338938 201 QQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 242
Cdd:cd07933  131 LQIEEYDLNVVRLCFQIFLPDEHGNYTTALPPIVSNPIYDNR 172
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
41-242 1.58e-45

N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Dorsal and Dif (Dorsal-related immunity factor), and similar proteins. Dorsal and Dif are Rel-like transcription factors, which play roles in mediating innate immunity in Drosophila. They are activated via the Toll pathway. Cytoplasmic Dorsal/Dif are inactivated via forming a complex with Cactus, the Drosophila homologue of mammalian I-kappa B proteins. In response to signals, Cactus is degraded and Dorsal/Dif can be transported into the nucleus, where they act as transcription factors. Dorsal is also an essential gene in establishing the proper dorsal/ventral polarity in the developing embryo.


Pssm-ID: 143647  Cd Length: 173  Bit Score: 161.12  E-value: 1.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGK-HCED 119
Cdd:cd07887    1 PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPHNLVGKeGCKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 120 GICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARmTEACIRGYNPGlLVHSDlaylqaegggdrqltdrekeiirqaa 199
Cdd:cd07887   81 GVCTKKINPTEMRIVFQKLGIQCVKKKDVEESLKLR-EEINVDPFRTG-FDHKD-------------------------- 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564338938 200 lqQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 242
Cdd:cd07887  133 --QINSIDLNVVRLCFQVFLEDENGRFTVPLPPVVSDPIYDKK 173
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
249-350 1.37e-44

IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated Tcells (NFAT), and recombination signal J-kappa binding protein (RBP-Jkappa). The IPT domains in these proteins are involved in DNA binding. Most NF-kappaB/Rel proteins form homo- and heterodimers, while NFAT proteins are largely monomeric (with TonEBP being an exception). While the majority of sequence-specific DNA binding elements are found in the N-terminal domain, several are found in the IPT domain in loops adjacent to, and including, the linker region.


Pssm-ID: 238336  Cd Length: 101  Bit Score: 155.90  E-value: 1.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 249 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHrQFAIVFKTPKYKDVNITKPASV 328
Cdd:cd00602    1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEKGPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79
                         90       100
                 ....*....|....*....|..
gi 564338938 329 FVQLRRKSDLETSEPKPFLYYP 350
Cdd:cd00602   80 PIQLVRPDDRKRSEPLTFTYTP 101
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
41-242 1.92e-36

N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Relish protein, in which the RHD domain co-occurs with C-terminal ankyrin repeats. Family members are sometimes referred to as p110 or p68 (proteolytically processed form). Relish is an NF-kappa B-like transcription factor, which plays a role in mediating innate immunity in Drosophila. It is activated via the Imd (immune deficiency) pathway, which triggers phosphorylation of Relish. IKK-dependent proteolytic cleavage of Relish (which involves Dredd) results in a smaller active form (without the C-terminal ankyrin repeats), which is transported into the nucleus and functions as a transactivator.


Pssm-ID: 143644  Cd Length: 159  Bit Score: 134.87  E-value: 1.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRgFRFRYVCE-GPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVT-NGKNIHLHAHSLVGKHCE 118
Cdd:cd07884    1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQaDDNRRKPHVHKLVGKQGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 119 DGICTVTAGPK----DMVVGFANLGILHVTKKKVFETlearmteacirgynpgllvhsdlaylqaegggdrqltdrekei 194
Cdd:cd07884   80 DDVCDPHDIEVspegDYVAMFQNMGIIHTAKKNIPEE------------------------------------------- 116
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564338938 195 irqaaLQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 242
Cdd:cd07884  117 -----LYKKKNMNLNQVVLRFQAFAVSANGHLRPICPPVYSNPINNLK 159
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
41-242 2.30e-35

N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD domain of the RelA family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). RelA (also called p65) forms heterodimers with NF-kappa B1 (p50) and B2 (p52). RelA also forms homodimers.


Pssm-ID: 143645  Cd Length: 169  Bit Score: 132.30  E-value: 2.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 120
Cdd:cd07885    1 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPHELVGKDCKDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 121 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARmteacIRGYNPGLLVHSDlaylqaegggdrqltdrekeiirqaal 200
Cdd:cd07885   81 YYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQR-----IQTNNNPFNVPIE--------------------------- 128
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564338938 201 QQTKEMDLSVVRLMFTAFLPDSTGSFTrRLEPVVSDAIYDSK 242
Cdd:cd07885  129 EQRADYDLNAVRLCFQVTVRDPSGRLL-PLPPVLSQPIYDNR 169
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
41-242 1.15e-33

N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral oncogene homolog B (RelB) protein; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the RelB family of transcription factors, categorized as class II NF-kappa B family members. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). RelB, is unable to homodimerize but is a potent transactivator in a heterodimer with NF-kappa B1 (p50) or B2 (p52). It is involved in the regulation of genes that play roles in inflammatory processes and the immune response.


Pssm-ID: 143646  Cd Length: 172  Bit Score: 127.28  E-value: 1.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  41 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKV--IVQLVTNGKNIHLHAHSLVGKHCE 118
Cdd:cd07886    1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVtvTVCLVWKDPPHRVHPHGLVGKDCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 119 DGICTVT----AGPKDmvvGFANLGILHVTKKKVFETLEARMTEAcIRGYNPGllvhsdlaylqaegggdrqltdrekei 194
Cdd:cd07886   81 NGICQVTlnphSSPRH---SFSNLGIQCVRKREIEAAIETRLQLN-IDPFKAG--------------------------- 129
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564338938 195 irqaALQQTKEMDLSVVRLMFTAFLPDSTGsFTRRLEPVVSDAIYDSK 242
Cdd:cd07886  130 ----SLKNHEEVDMNVVRLCFQASYRDDDG-RKDCLSPVLSEPIYDKK 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
494-767 1.75e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 494 FQDNLFLEKALQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGSISDDII 573
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 574 NMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNsKAAllINHPNGEGLNAI 653
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GAD--VNAQDNDGNTPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 654 HIAVMSNSLSCLQLLVAAGAEVNAQeQKSGRTALHLAVEYDNISLAGcLLLEGDALVDSTTYDGTTPLHIAAGRGSTRLA 733
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564338938 734 ALLKAAGADPLVENFEPLYDLDDSWEKAGEDEGV 767
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
496-742 1.36e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 496 DNLFLEKALQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEvtsgsiSDDIINM 575
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE------AGADVNA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 576 RNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNsKAAllINHPNGEGLNAIHI 655
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GAD--VNARDNDGETPLHL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 656 AVMSNSLSCLQLLVAAGAEVNAQeQKSGRTALHLAVEYDNISLAGcLLLEGDALVDSTTYDGTTPLHIAAGRGSTRLAAL 735
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVK-LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                 ....*..
gi 564338938 736 LKAAGAD 742
Cdd:COG0666  271 LLLALLL 277
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
814-863 1.02e-26

Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the Nuclear Factor-KappaB1 (NF-kB1) precursor protein p105. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). NF-kB1 (or p50) is produced from the processing of the precursor protein p105, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the classical (or canonical) NF-kB pathway. In the cytosol, p50 forms an inactive complex with RelA (or p65) and the Inhibitor of NF-kB (IkB). Activation is triggered by the phosphorylation and degradation of IkB, resulting in the active DNA-binding p50-RelA dimer to migrate to the nucleus. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260063  Cd Length: 76  Bit Score: 103.83  E-value: 1.02e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564338938 814 RLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEMS 863
Cdd:cd08797    2 KQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVS 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
584-678 2.16e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  584 LHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKIlgvllknskAALLINHPNGE----GLNAIHIAVMS 659
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI---------VKLLLEHADVNlkdnGRTALHYAARS 71
                          90
                  ....*....|....*....
gi 564338938  660 NSLSCLQLLVAAGAEVNAQ 678
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVK 90
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
813-862 2.06e-15

Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear Factor-KappaB (NF-kB) precursor proteins. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). Two of these, NF-kB1 and NF-kB2 are produced from the processing of the precursor proteins p105 and p100, respectively. In addition to RHD, p105 and p100 contain ANK repeats and a C-terminal DD. NF-kBs are regulated by the Inhibitor of NF-kB (IkB) Kinase (IKK) complex through classical and non-canonical pathways, which differ in the IKK subunits involved and downstream targets. IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. The precursor proteins p105 and p100 function as IkBs and as NF-kB proteins after being processed by the proteasome. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260024  Cd Length: 72  Bit Score: 71.50  E-value: 2.06e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564338938 813 TRLQLCKLLeipDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEM 862
Cdd:cd08310    1 TRLRLCKLL---DVGKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEA 47
PHA02878 PHA02878
ankyrin repeat protein; Provisional
573-724 2.20e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.84  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 573 INMRN-DLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNSKAallINHPNGEGLN 651
Cdd:PHA02878 160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNT 236
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564338938 652 AIHIAVMS-NSLSCLQLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLagcLLLEGDALVDSTTYDGTTPLHIA 724
Cdd:PHA02878 237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK---LLLEYGADINSLNSYKLTPLSSA 307
IPT smart00429
ig-like, plexins, transcription factors;
248-349 4.76e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 65.52  E-value: 4.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938   248 NLKIVRMDRTAGCVTGGEEIyLLCDKVQKDDIQIRFYEeeengGVWEGFGDFSPTdvhRQFAIVFKTPKYKDVNITKPAS 327
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV-----GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71
                           90       100
                   ....*....|....*....|..
gi 564338938   328 VfVQLRRkSDLEtSEPKPFLYY 349
Cdd:smart00429  72 T-VGLRN-GGVP-SSPQPFTYV 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
573-725 7.51e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 7.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 573 INMRNDLYQTPLHL-----AVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAA--KEGHDKILGVLLKNSKAallINHP 645
Cdd:PHA03100  61 INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGAN---VNIK 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 646 NGEGLNAIHIAVMSNS--LSCLQLLVAAGAEVNAQEQ---------------KSGRTALHLAVEYDNISLAGcLLLEGDA 708
Cdd:PHA03100 138 NSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVK-YLLDLGA 216
                        170
                 ....*....|....*..
gi 564338938 709 LVDSTTYDGTTPLHIAA 725
Cdd:PHA03100 217 NPNLVNKYGDTPLHIAI 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
653-729 8.90e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 8.90e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564338938  653 IHIAVMSNSLSCLQLLVAAGAEVNAQEQKsGRTALHLAVEYDNISLAGCLLLEGDALVDSttyDGTTPLHIAAGRGS 729
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGH 73
PHA02874 PHA02874
ankyrin repeat protein; Provisional
573-724 2.76e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 573 INMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNSkAALLINHPNGEglNA 652
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGE--SP 193
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564338938 653 IHIAVMSNSLSCLQLLVAAGAEVnAQEQKSGRTALHLAVEYDNISLAgclLLEGDALVDSTTYDGTTPLHIA 724
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLHNAIIHNRSAIE---LLINNASINDQDIDGSTPLHHA 261
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
249-350 2.95e-11

Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers.


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 60.55  E-value: 2.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 249 LKIVRMDRTAGCVTGGEEIYLLCDKVQKD-DIQIRFYEEEEnggvwegfgdFSPTDVHrQFAIVFKTPKYKDVNitkPAS 327
Cdd:cd00102    1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFGGGVP----------CSVLSVS-STAIVCTTPPYANPG---PGP 66
                         90       100
                 ....*....|....*....|...
gi 564338938 328 VFVQLRRKSDLETSEPKPFLYYP 350
Cdd:cd00102   67 VEVTVDRGNGGITSSPLTFTYVP 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
536-650 7.14e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 7.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 536 VQDENGDSVLHLAIIHLHAQLVRDLLEvtsgsiSDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNS 615
Cdd:COG0666  181 ARDNDGETPLHLAAENGHLEIVKLLLE------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564338938 616 VLHLAAKEGHDKILGVLLKNSKAALLINHPNGEGL 650
Cdd:COG0666  255 ALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
510-731 9.28e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 9.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 510 HANALFDYAVTGDVKMLLAVQRHLTAVQDEN-----GDSVLHL---AIIHLHAQLVRDLLE----VTSGSISDDiinmrn 577
Cdd:PHA03095  11 MEAALYDYLLNASNVTVEEVRRLLAAGADVNfrgeyGKTPLHLylhYSSEKVKDIVRLLLEagadVNAPERCGF------ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 578 dlyqTPLHLAVITKQ-EDVVEDLLRVGADLSLLDRWGNSVLH--LAAKEGHDKILGVLLKNsKAAllINHPNGEGLNAIH 654
Cdd:PHA03095  85 ----TPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRK-GAD--VNALDLYGMTPLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 655 IAVMSN--SLSCLQLLVAAGAEVNAQEQkSGRTALHLAVEY--------DNISLAGCL---------------------- 702
Cdd:PHA03095 158 VLLKSRnaNVELLRLLIDAGADVYAVDD-RFRSLLHHHLQSfkprarivRELIRAGCDpaatdmlgntplhsmatgssck 236
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564338938 703 ------LLEGDALVDSTTYDGTTPLHIAAGRGSTR 731
Cdd:PHA03095 237 rslvlpLLIAGISINARNRYGQTPLHYAAVFNNPR 271
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
538-721 1.54e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 538 DENGDSVLHLAIIHLHAQLVRDLLEvtsGSISDDIINMRNdlyQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVL 617
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLK---AKLDPDIGDSKG---RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 618 HLAAKEGHDKILGVLLKNSKAAllinHPNGEGlNAIHIAVMSNSLSCLQLLVAAGAEVNAqEQKSGRTALHLAVEYDNIS 697
Cdd:PLN03192 596 WNAISAKHHKIFRILYHFASIS----DPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS-EDHQGATALQVAMAEDHVD 669
                        170       180
                 ....*....|....*....|....
gi 564338938 698 LAGCLLLEGDALVDSTTYDGTTPL 721
Cdd:PLN03192 670 MVRLLIMNGADVDKANTDDDFSPT 693
PHA02875 PHA02875
ankyrin repeat protein; Provisional
542-706 1.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 542 DSVLHLAIIHLHAQLVRDLLEvtSGSISDDIINMRNDlyqTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAA 621
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLD--LGKFADDVFYKDGM---TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 622 KEGHDKILGVLLKNsKAALliNHPNGEGLNAIHIAVMSNSLSCLQLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLAGC 701
Cdd:PHA02875 144 MMGDIKGIELLIDH-KACL--DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRL 220

                 ....*
gi 564338938 702 LLLEG 706
Cdd:PHA02875 221 FIKRG 225
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
541-730 2.67e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 541 GDSVLHLAIIHLHAQLVRDLLEVTSGsisddIIN--MRNDLY--QTPLHLAVITKQEDVVEDLLRVGADLSL-------- 608
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPE-----LVNepMTSDLYqgETALHIAVVNQNLNLVRELIARGADVVSpratgtff 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 609 ------LDRWGNSVLHLAAKEGHDKIlgvllknskaallinhpngeglnaihiavmsnslscLQLLVAAGAEVNAQEQKs 682
Cdd:cd22192  126 rpgpknLIYYGEHPLSFAACVGNEEI------------------------------------VRLLIEHGADIRAQDSL- 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564338938 683 GRTALHLAVEYDNISLAgC----LLLEGDALVDS------TTYDGTTPLHIAAGRGST 730
Cdd:cd22192  169 GNTVLHILVLQPNKTFA-CqmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNI 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
613-669 3.43e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 3.43e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564338938  613 GNSVLHLAAKEGHDKILGVLLKNSkaaLLINHPNGEGLNAIHIAVMSNSLSCLQLLV 669
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG---ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
536-610 5.72e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 5.72e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564338938  536 VQDENGDSVLHLAIIHLHAQLVRDLLEVtsgsisdDIINMRNDlYQTPLHLAVITKQEDVVEDLLRVGADLSLLD 610
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLEH-------ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
545-635 6.76e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 6.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  545 LHLAIIHLHAQLVRDLLEVTSGsisddiINMRNDLYQTPLHLAVITKQEDVVEDLLRVgADLSLLDRwGNSVLHLAAKEG 624
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD------ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
                          90
                  ....*....|.
gi 564338938  625 HDKILGVLLKN 635
Cdd:pfam12796  73 HLEIVKLLLEK 83
PHA02736 PHA02736
Viral ankyrin protein; Provisional
610-731 7.12e-08

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 52.57  E-value: 7.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 610 DRWGNSVLHLAAKEGhdkilGVL-LKNSKAAL------LINHPNGEGLNAIHIAV---MSNSLSCLQLLVAAGAEVNAQE 679
Cdd:PHA02736  14 DIEGENILHYLCRNG-----GVTdLLAFKNAIsdenryLVLEYNRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKE 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564338938 680 QKSGRTALHLAVEYDNISLAGCLLLEGDALVDSTTYDGTTPLHIAAGRGSTR 731
Cdd:PHA02736  89 RVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAK 140
PHA03095 PHA03095
ankyrin-like protein; Provisional
573-723 1.23e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 573 INMRNDLYQtplhlaVITKQEDV----VEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNSKAALLINHPNGE 648
Cdd:PHA03095   9 IIMEAALYD------YLLNASNVtveeVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 649 GLNAIHIAVMSNS-LSCLQLLVAAGAEVNAqEQKSGRTALH-----LAVEYDNISlagcLLLEGDALVDSTTYDGTTPLH 722
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLIKAGADVNA-KDKVGRTPLHvylsgFNINPKVIR----LLLRKGADVNALDLYGMTPLA 157

                 .
gi 564338938 723 I 723
Cdd:PHA03095 158 V 158
PHA02876 PHA02876
ankyrin repeat protein; Provisional
573-724 1.71e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 573 INMRNDLYQTPLHLAVITKQE-DVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNSKAAllINHPNGEGLN 651
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN--VNARDYCDKT 377
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564338938 652 AIHIAVMSNSLSCLQLLVAAGAEVNAQEQKSGrTALHLAVEYDNISLAGCLLLEGDALVDSTTYDGTTPLHIA 724
Cdd:PHA02876 378 PIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
Ank_4 pfam13637
Ankyrin repeats (many copies);
649-703 1.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.80e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564338938  649 GLNAIHIAVMSNSLSCLQLLVAAGAEVNAQEqKSGRTALHLAVEYDNISLAGCLL 703
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PHA02741 PHA02741
hypothetical protein; Provisional
613-724 6.10e-07

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 50.43  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 613 GNSVLHLAAKEGHDKILGVL---LKNSKAALLINHPNGEGLNAIHIAVMSN----SLSCLQLLVAAGAEVNAQEQKSGRT 685
Cdd:PHA02741  21 GENFFHEAARCGCFDIIARFtpfIRGDCHAAALNATDDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEMLEGDT 100
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564338938 686 ALHLAVEYDNISLAGCLLLEGDALVDSTTYDGTTPLHIA 724
Cdd:PHA02741 101 ALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139
PHA02874 PHA02874
ankyrin repeat protein; Provisional
571-728 1.45e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 571 DIINMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNS-------------- 636
Cdd:PHA02874  26 NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtsilpipciekd 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 637 ------KAALLINHPNGEGLNAIHIAVMSNSLSCLQLLVAAGAEVNAqEQKSGRTALHLAVEYDNISLAGcLLLEGDALV 710
Cdd:PHA02874 106 miktilDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDIIK-LLLEKGAYA 183
                        170
                 ....*....|....*...
gi 564338938 711 DSTTYDGTTPLHIAAGRG 728
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYG 201
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
541-669 5.29e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 541 GDSVLHLAIIHLHAQLVRDLLEvtSGSisdDIINMR-----------NDLY--QTPLHLAVITKQEDVVEDLLRVGADLS 607
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIA--RGA---DVVSPRatgtffrpgpkNLIYygEHPLSFAACVGNEEIVRLLIEHGADIR 163
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 608 LLDRWGNSVLHL--------AAKEGHDKILGvLLKNSKAALLINHPNGEGLNAIHIAVMSNSLSCLQLLV 669
Cdd:cd22192  164 AQDSLGNTVLHIlvlqpnktFACQMYDLILS-YDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
514-676 7.15e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 514 LFDYAVTGDVK---MLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGSisdDIINMRNdlyQTPLHLAVIT 590
Cdd:PHA02875  72 LHDAVEEGDVKaveELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADP---DIPNTDK---FSPLHLAVMM 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 591 KQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLkNSKAALLINHPNGEgLNAIHIAVMSNSLSCLQLLVA 670
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL-DSGANIDYFGKNGC-VAALCYAIENNKIDIVRLFIK 223

                 ....*.
gi 564338938 671 AGAEVN 676
Cdd:PHA02875 224 RGADCN 229
PHA02743 PHA02743
Viral ankyrin protein; Provisional
648-724 1.74e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 45.96  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 648 EGLNAIHIAV---MSNSLSCLQLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLAGCLLLEGDALVDSTTYDGTTPLHIA 724
Cdd:PHA02743  56 HGRQCTHMVAwydRANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIA 135
PHA03095 PHA03095
ankyrin-like protein; Provisional
510-673 1.86e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 510 HANALFDYAvtGDVKMLLAVQRHLTAVqDENGDSVLHLAIIH--LHAQLVRDLLEvtSGSIsddiINMRNDLYQTPLHLA 587
Cdd:PHA03095 194 HLQSFKPRA--RIVRELIRAGCDPAAT-DMLGNTPLHSMATGssCKRSLVLPLLI--AGIS----INARNRYGQTPLHYA 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 588 VITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILgvllknskAALLINHPNGEGL--------NAIHIAVMS 659
Cdd:PHA03095 265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV--------RAALAKNPSAETVaatlntasVAGGDIPSD 336
                        170
                 ....*....|....
gi 564338938 660 NSLSCLQLLVAAGA 673
Cdd:PHA03095 337 ATRLCVAKVVLRGA 350
PHA03100 PHA03100
ankyrin repeat protein; Provisional
573-635 1.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 1.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564338938 573 INMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKN 635
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
810-863 2.47e-05

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 43.55  E-value: 2.47e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938   810 TEDTRLQLCKLLEIPdPDKNWATLAQKLGLG------ILNNAFRLSPAPSKTLMDNYEMS 863
Cdd:smart00005   1 PELTRQKLAKLLDHP-LGLDWRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQR 59
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
573-677 3.32e-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: 47.77  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  573 INMRNDLYQTPLHLAVItkqEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHD---KILGVLLKNSKAALLINHPNGE- 648
Cdd:TIGR00870  45 INCPDRLGRSALFVAAI---ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDaveAILLHLLAAFRKSGPLELANDQy 121
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564338938  649 ------GLNAIHIAVMSNSLSCLQLLVAAGAEVNA 677
Cdd:TIGR00870 122 tseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
582-633 3.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 3.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564338938  582 TPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLL 633
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
640-690 3.78e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564338938  640 LLINHPNGEGLNAIHIAVMSNSLSCLQLLVAAGAEVNAQEqKSGRTALHLA 690
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
583-724 4.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 583 PLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGH-------------DKILGVLLKNSKA----------A 639
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmkemirsinkCSVFYTLVAIKDAfnnrnveifkI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 640 LLINHPNGE-GLNAIHIAVMSNSLSC----LQLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLAGCLLLEGdALVDSTT 714
Cdd:PHA02878 120 ILTNRYKNIqTIDLVYIDKKSKDDIIeaeiTKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYG-ANVNIPD 198
                        170
                 ....*....|
gi 564338938 715 YDGTTPLHIA 724
Cdd:PHA02878 199 KTNNSPLHHA 208
PHA02876 PHA02876
ankyrin repeat protein; Provisional
573-728 5.86e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 5.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 573 INMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNSKAallINHPNGEGLNA 652
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN---INKNDLSLLKA 247
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564338938 653 IHIAVMSNSLsclqLLVAAGAEVNAQEQKSgRTALHLAVEYDNISLAGCLLLEGDALVDSTTYDGTTPLHIAAGRG 728
Cdd:PHA02876 248 IRNEDLETSL----LLYDAGFSVNSIDDCK-NTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318
PHA03100 PHA03100
ankyrin repeat protein; Provisional
523-611 8.25e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 8.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 523 VKMLLAVQRHLTAVqDENGDSVLHLAIIHLHAQLVRDLLEVTSGsisddiINMRNDLYQTPLHLAVITKQEDVVEDLLRV 602
Cdd:PHA03100 175 VNYLLSYGVPINIK-DVYGFTPLHYAVYNNNPEFVKYLLDLGAN------PNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247

                 ....*....
gi 564338938 603 GADLSLLDR 611
Cdd:PHA03100 248 GPSIKTIIE 256
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
817-864 1.05e-04

Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the Nuclear Factor-KappaB2 (NF-kB2) precursor protein p100. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). NF-kB2 (or p52) is produced from the processing of the precursor protein p100, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the non-canonical NF-kB pathway. The p100 precursor is cytosolic and interacts with RelB. Upon phosphorylation by IKKalpha, p100 is processed to its 52kDa active, DNA-binding form and the p52/RelB complex is translocated into the nucleus. The non-canonical pathway plays a role in adaptive immunity and lymphorganogenesis. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176776  Cd Length: 76  Bit Score: 41.34  E-value: 1.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 564338938 817 LCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEMSS 864
Cdd:cd08798    5 LEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAG 52
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
809-861 1.38e-04

Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in Uncoordinated-5 (UNC-5) homolog family, which includes Unc5A, B, C and D in vertebrates. UNC5 proteins are receptors for secreted netrins (netrin-1, -3 and -4) that are involved in diverse processes like axonal guidance, neuronal migration, blood vessel patterning, and apoptosis. They are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260051  Cd Length: 83  Bit Score: 41.11  E-value: 1.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564338938 809 LTEDTRLQLCKLLEIPDPDKN-WATLAQKLGLGILNNAFRLSPAPSKTLMDNYE 861
Cdd:cd08781    1 LPYSIRQKLCSLLDPPNARGNdWRLLAQKLSVDRYINYFATKPSPTEVILDLWE 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
581-636 1.45e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564338938 581 QTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNS 636
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
Ank_2 pfam12796
Ankyrin repeats (3 copies);
687-730 1.59e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.25  E-value: 1.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 564338938  687 LHLAVEYDNISLAgCLLLEGDALVDSTTYDGTTPLHIAAGRGST 730
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHL 43
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
606-706 1.61e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 606 LSLLDRWGNSVLHLAAKEGHDKILGVLLKNSKAALLINHPNGEglNAIHIAVMSNSLSCLQLLVAAGAEVNAQEQKS--- 682
Cdd:cd22192   10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGE--TALHVAALYDNLEAAVVLMEAAPELVNEPMTSdly 87
                         90       100
                 ....*....|....*....|....*
gi 564338938 683 -GRTALHLAVEYDNISLAGCLLLEG 706
Cdd:cd22192   88 qGETALHIAVVNQNLNLVRELIARG 112
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
41-115 1.64e-04

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells (NFAT) proteins and similar proteins; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes that are mainly involved in cell-cell interaction. Upon de-phosphorylation of the nuclear localization signal, NFAT enters the nucleus and acts as a transcription factor; its export from the nucleus is triggered by phosphorylation via export kinases. NFATs play important roles in mediating the immune response, and are found in T cells, B Cells, NK cells, mast cells, and monocytes. NFATs are also found in various non-hematopoietic cell types, where they play roles in development. This group also contains the N-terminal RHD sub-domain of the non-calcium regulated tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt.


Pssm-ID: 143648  Cd Length: 161  Bit Score: 43.03  E-value: 1.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564338938  41 PYLQILEQPKQRgFRFRYVCEGpSHGGLPGASSEknkkSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGK 115
Cdd:cd07927    1 YELRIEVQPEPH-HRARYETEG-SRGAVKAPSTG----GFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHR 69
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
552-730 2.57e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 552 LHAQLVRDLLEVTSGSisDDIINMRNDLYQtplhlAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGV 631
Cdd:PLN03192 504 LHDLNVGDLLGDNGGE--HDDPNMASNLLT-----VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLV 576
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 632 LLKNskaALLINHPNGEGLNAIHIAVMSNSLSCLQLLVAAGAEVNAQeqkSGRTALHLAVEYDNISLAGCLLLEGdALVD 711
Cdd:PLN03192 577 LLKH---ACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH---AAGDLLCTAAKRNDLTAMKELLKQG-LNVD 649
                        170
                 ....*....|....*....
gi 564338938 712 STTYDGTTPLHIAAGRGST 730
Cdd:PLN03192 650 SEDHQGATALQVAMAEDHV 668
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
541-618 4.09e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.10  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 541 GDSVLHLAIIHLHAQLVRDLLE----VTSGSISDDI-INMRNDLY--QTPLHLAVITKQEDVVEDLLRVGAD---LSLLD 610
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVEngadVSARATGRFFrKSPGNLFYfgELPLSLAACTNQEEIVRLLLENGAQpaaLEAQD 152

                 ....*...
gi 564338938 611 RWGNSVLH 618
Cdd:cd21882  153 SLGNTVLH 160
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
613-723 7.58e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 7.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 613 GNSVLHLAAKEGHDKILG---VLLKNSKAAL----LINHPNG----EGLNAIHIAVMSNSLSCLQLLVAAGAEVNAQE-- 679
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEaimLLLEAAPDSGnpkeLVNAPCTdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564338938 680 ---QKSGRTALHLAvEYDnISLAGC--------LLLEGDALVDSTTYD---GTTPLHI 723
Cdd:cd21882  106 rffRKSPGNLFYFG-ELP-LSLAACtnqeeivrLLLENGAQPAALEAQdslGNTVLHA 161
PHA02874 PHA02874
ankyrin repeat protein; Provisional
516-661 8.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 8.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 516 DYAVtgdVKMLLAVQRHLTaVQDENGDSVLHLAIIHLHAqlVRDLLeVTSGSISDDIINMrndlyQTPLHLAVITK-QED 594
Cdd:PHA02874 202 DYAC---IKLLIDHGNHIM-NKCKNGFTPLHNAIIHNRS--AIELL-INNASINDQDIDG-----STPLHHAINPPcDID 269
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564338938 595 VVEDLLRVGADLSLLDRWGNSVLHLAAKE-GHDKILGVLLKNskaALLINH----PNGEGLNaiHIAVMSNS 661
Cdd:PHA02874 270 IIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIAN---AVLIKEadklKDSDFLE--HIEIKDNK 336
PHA02876 PHA02876
ankyrin repeat protein; Provisional
573-729 1.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 573 INMRNDLYQTPLHLAVITKQ-EDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKilgvllknskaallinhpngegln 651
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDT------------------------ 321
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564338938 652 aihiavmsnslSCLQLLVAAGAEVNAQEQKSgRTALHLAVEYDNISLAGCLLLEGDALVDSTTYDGTTPLHIAAGRGS 729
Cdd:PHA02876 322 -----------ENIRTLIMLGADVNAADRLY-ITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
PHA02875 PHA02875
ankyrin repeat protein; Provisional
582-730 1.18e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 582 TPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDKILGVLLKNSKAALLINHPngEGLNAIHIAVMSNS 661
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYK--DGMTPLHLATILKK 114
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564338938 662 LSCLQLLVAAGAEVNAQEQKSgRTALHLAVEYDNISLAGcLLLEGDALVDSTTYDGTTPLHIAAGRGST 730
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDK-FSPLHLAVMMGDIKGIE-LLIDHKACLDIEDCCGCTPLIIAMAKGDI 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
683-731 1.47e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564338938  683 GRTALHLAVEYDNISLAGcLLLEGDALVDSTTYDGTTPLHIAAGRGSTR 731
Cdd:pfam13637   1 ELTALHAAAASGHLELLR-LLLEKGADINAVDGNGETALHFAASNGNVE 48
Ank_5 pfam13857
Ankyrin repeats (many copies);
573-620 1.61e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 564338938  573 INMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLA 620
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death pfam00531
Death domain;
814-863 1.89e-03

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 38.11  E-value: 1.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564338938  814 RLQLCKLLEIPDP-DKNWATLAQKLGLGIL-NNAFRLSPA----PSKTLMDNYEMS 863
Cdd:pfam00531   1 RKQLDRLLDPPPPlGKDWRELARKLGLSENeIDEIESENPrlrsQTYELLRLWEQR 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
541-623 3.48e-03

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: 41.22  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  541 GDSVLHLAIIHLHAQLVRDLLEvtSG-SIS-----DD--IINMRNDLY--QTPLHLAVITKQEDVVEDLLRVGADLSLLD 610
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLE--RGaSVParacgDFfvKSQGVDSFYhgESPLNAAACLGSPSIVALLSEDPADILTAD 205
                          90
                  ....*....|...
gi 564338938  611 RWGNSVLHLAAKE 623
Cdd:TIGR00870 206 SLGNTLLHLLVME 218
PHA02876 PHA02876
ankyrin repeat protein; Provisional
573-712 3.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 3.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 573 INMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKeGHDKILGVLLKNSKAAlLINHPNGEGLNA 652
Cdd:PHA02876 368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALC-GTNPYMSVKTLIDRGA-NVNSKNKDLSTP 445
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564338938 653 IHIAVMSN-SLSCLQLLVAAGAEVNAQEQKSgRTALHLAVEYDNIslAGCLLLEGDALVDS 712
Cdd:PHA02876 446 LHYACKKNcKLDVIEMLLDNGADVNAINIQN-QYPLLIALEYHGI--VNILLHYGAELRDS 503
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
541-666 3.73e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.90  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938 541 GDSVLHLAIIHLHAQLVRDLLEVTSG---SISDDIIN--MRNDLY---QTPLHLAVITKQEDVVEDLL-RVGADLSLLDR 611
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADvnaHAKGVFFNpkYKHEGFyfgETPLALAACTNQPEIVQLLMeKESTDITSQDS 220
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564338938 612 WGNSVLH---LAA----------KEGHDKIlgvlLKNSKAALLINHPNGEGLNAIHIAVMSNSLSCLQ 666
Cdd:cd22194  221 RGNTVLHalvTVAedsktqndfvKRMYDMI----LLKSENKNLETIRNNEGLTPLQLAAKMGKAEILK 284
Ank_4 pfam13637
Ankyrin repeats (many copies);
541-600 3.74e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 3.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338938  541 GDSVLHLAIIHLHAQLVRDLLEvtsgsiSDDIINMRNDLYQTPLHLAVITKQEDVVEDLL 600
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE------KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
813-857 4.29e-03

Death domain found in death-associated protein kinase 1; Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260052  Cd Length: 82  Bit Score: 36.94  E-value: 4.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564338938 813 TRLQLCKLLEIPDP-DKNWATLAQKLGLG----ILNNAFRLSPAPSKTLM 857
Cdd:cd08782    2 TRRKLARLLDPPDPmGRDWCLLAVNLGLTdlvaKLDSTSSPLPSPTDRLL 51
Ank_5 pfam13857
Ankyrin repeats (many copies);
668-724 4.43e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564338938  668 LVAAG-AEVNAQEQKsGRTALHLAVEYDNISLAgCLLLEGDALVDSTTYDGTTPLHIA 724
Cdd:pfam13857   1 LLEHGpIDLNRLDGE-GYTPLHVAAKYGALEIV-RVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
648-677 6.18e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 6.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 564338938   648 EGLNAIHIAVMSNSLSCLQLLVAAGAEVNA 677
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
581-611 8.86e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 8.86e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 564338938  581 QTPLHLAVI-TKQEDVVEDLLRVGADLSLLDR 611
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH