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Conserved domains on  [gi|2217350802|ref|XP_047271699|]
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nuclear factor NF-kappa-B p105 subunit isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHD-n super family cl08275
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 1-112 9.87e-68

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).


The actual alignment was detected with superfamily member cd07935:

Pssm-ID: 447596  Cd Length: 202  Bit Score: 223.23  E-value: 9.87e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSV 80
Cdd:cd07935    91 MVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAVQQTKEMDLSV 170

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 112
Cdd:cd07935   171 VRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 119-220 7.62e-63

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: 206.02  E-value: 7.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 119 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASV 198
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80

                          90       100
                  ....*....|....*....|..
gi 2217350802 199 FVQLRRKSDLETSEPKPFLYYP 220
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
 684-759 6.09e-44

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: 152.75  E-value: 6.09e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217350802 684 VKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQA 759
Cdd:cd08797     1 VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
367-627 1.69e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 367 DNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINM 446
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 447 RNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHL 526
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 527 AMMSNSLPCLLLLVAAGADVNAQeQKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAAL 606
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                         250       260
                  ....*....|....*....|.
gi 2217350802 607 LKAAGADPLVENFEPLYDLDD 627
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLL 258
 
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 ...
 1-112 9.87e-68

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: 223.23  E-value: 9.87e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSV 80
Cdd:cd07935    91 MVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAVQQTKEMDLSV 170

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 112
Cdd:cd07935   171 VRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 119-220 7.62e-63

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: 206.02  E-value: 7.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 119 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASV 198
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80

                          90       100
                  ....*....|....*....|..
gi 2217350802 199 FVQLRRKSDLETSEPKPFLYYP 220
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 120-221 3.47e-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: 190.85  E-value: 3.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 120 KIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVF 199
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80

                          90       100
                  ....*....|....*....|..
gi 2217350802 200 VQLRRKSDLETSEPKPFLYYPE 221
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
 684-759 6.09e-44

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: 152.75  E-value: 6.09e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217350802 684 VKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQA 759
Cdd:cd08797     1 VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
367-627 1.69e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 367 DNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINM 446
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 447 RNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHL 526
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 527 AMMSNSLPCLLLLVAAGADVNAQeQKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAAL 606
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                         250       260
                  ....*....|....*....|.
gi 2217350802 607 LKAAGADPLVENFEPLYDLDD 627
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLL 258
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 1-111 8.72e-26

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: 104.69  E-value: 8.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLEARMteacirgynpgllvhpdlaylqaegggdrQLGDREKElIRQAALQQTKEMDLSV 80
Cdd:pfam00554  89 MVASFQNLGIQCVKKKDVEEALKERI-----------------------------ELNIDPFN-VGFEALRQIKDMDLNV 138

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDS 111
Cdd:pfam00554 139 VRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
455-549 4.27e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 4.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 455 LHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALlldhpNGDGLNAIHLAMMSNSLP 534
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*
gi 2217350802 535 CLLLLVAAGADVNAQ 549
Cdd:pfam12796  76 IVKLLLEKGADINVK 90
IPT smart00429
ig-like, plexins, transcription factors;
118-219 1.11e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.06  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802  118 NLKIVRMDRTAGCVTGGEEIyLLCDKVQKDDIQIRFYEeeengGVWEGFGDFSPTdvhRQFAIVFKTPKYKDINITKPAS 197
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV-----GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71

                           90       100
                   ....*....|....*....|..
gi 2217350802  198 VfVQLRRkSDLEtSEPKPFLYY 219
Cdd:smart00429  72 T-VGLRN-GGVP-SSPQPFTYV 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 444-595 4.04e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 444 INMRN-DLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLN 522
Cdd:PHA02878  160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNT 236

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217350802 523 AIHLAMMS-NSLPCLLLLVAAGADVNAQEQKSGRTALHLAVeHDNISLAgcLLLEGDAHVDSTTYDGTTPLHIA 595
Cdd:PHA02878  237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSI-KSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 682-760 6.10e-12

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: 62.04  E-value: 6.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802  682 EDVKLQLYKLLEIPdPDKNWATLAQKLGLG------ILNNAFRLSPAPSKTLMDNYEVSGG---TVRELVEALRQMGYTE 752
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80


                   ....*...
gi 2217350802  753 AIEVIQAA 760
Cdd:smart00005  81 AVELLRSE 88
Death pfam00531
Death domain;
685-761 3.04e-11

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 60.07  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 685 KLQLYKLLEIPDP-DKNWATLAQKLGLGIL-NNAFRLSPA----PSKTLMDNY---EVSGGTVRELVEALRQMGYTEAIE 755
Cdd:pfam00531   1 RKQLDRLLDPPPPlGKDWRELARKLGLSENeIDEIESENPrlrsQTYELLRLWeqrEGKNATVGTLLEALRKLGRRDAAE 80


                  ....*.
gi 2217350802 756 VIQAAS 761
Cdd:pfam00531  81 KIQSIL 86
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 412-601 1.37e-10

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: 64.65  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 412 GDSVLHLAIIHLHSQLVRDLLEVTSGLISDDiinMRNDLY--QTPLHLAVITKQEDVVEDLLRAGADLSL---------- 479
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEP---MTSDLYqgETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 480 ----LDRLGNSVLHLAAKEGHDKVLSILLKHkkaallldhpngdglnaihlammsnslpcllllvaaGADVNAQEQKsGR 555
Cdd:cd22192   128 gpknLIYYGEHPLSFAACVGNEEIVRLLIEH------------------------------------GADIRAQDSL-GN 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217350802 556 TALHLAVEHDNISLAgC----LLLEGDAHVDS------TTYDGTTPLHIAAGRGST 601
Cdd:cd22192   171 TVLHILVLQPNKTFA-CqmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNI 225
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 444-548 6.27e-06

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: 50.08  E-value: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 444 INMRNDLYQTPLHLAVItkqEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKV---LSILLKHKKAALLLDHPNGD- 519
Cdd:TIGR00870  45 INCPDRLGRSALFVAAI---ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVeaiLLHLLAAFRKSGPLELANDQy 121

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217350802 520 ------GLNAIHLAMMSNSLPCLLLLVAAGADVNA 548
Cdd:TIGR00870 122 tseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 453-477 4.38e-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: 35.26  E-value: 4.38e-03
                           10        20
                   ....*....|....*....|....*
gi 2217350802  453 TPLHLAVITKQEDVVEDLLRAGADL 477
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADI 28
 
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 ...
 1-112 9.87e-68

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: 223.23  E-value: 9.87e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSV 80
Cdd:cd07935    91 MVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAVQQTKEMDLSV 170

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 112
Cdd:cd07935   171 VRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 119-220 7.62e-63

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: 206.02  E-value: 7.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 119 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASV 198
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80

                          90       100
                  ....*....|....*....|..
gi 2217350802 199 FVQLRRKSDLETSEPKPFLYYP 220
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 120-221 3.47e-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: 190.85  E-value: 3.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 120 KIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVF 199
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80

                          90       100
                  ....*....|....*....|..
gi 2217350802 200 VQLRRKSDLETSEPKPFLYYPE 221
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
 1-112 2.33e-52

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: 181.14  E-value: 2.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDlaylqAEGGGDRQLGDREKELIRQAALQQTKEMDLSV 80
Cdd:cd07883    91 MTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPGDLVHVD-----AEGGGDRQLTDEEQAEIRQKAKQQAKSMDLSV 165

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 112
Cdd:cd07883   166 VRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 119-220 2.81e-45

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: 157.44  E-value: 2.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 119 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHrQFAIVFKTPKYKDINITKPASV 198
Cdd:cd00602     1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEKGPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79

                          90       100
                  ....*....|....*....|..
gi 2217350802 199 FVQLRRKSDLETSEPKPFLYYP 220
Cdd:cd00602    80 PIQLVRPDDRKRSEPLTFTYTP 101
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
 684-759 6.09e-44

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: 152.75  E-value: 6.09e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217350802 684 VKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQA 759
Cdd:cd08797     1 VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
367-627 1.69e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 367 DNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINM 446
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 447 RNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHL 526
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 527 AMMSNSLPCLLLLVAAGADVNAQeQKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAAL 606
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                         250       260
                  ....*....|....*....|.
gi 2217350802 607 LKAAGADPLVENFEPLYDLDD 627
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
367-613 1.28e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 367 DNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEvtsgliSDDIINM 446
Cdd:COG0666    42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE------AGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 447 RNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHL 526
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD---VNARDNDGETPLHL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 527 AMMSNSLPCLLLLVAAGADVNAQeQKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAAL 606
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVK-LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270


                  ....*..
gi 2217350802 607 LKAAGAD 613
Cdd:COG0666   271 LLLALLL 277
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 1-111 8.72e-26

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: 104.69  E-value: 8.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLEARMteacirgynpgllvhpdlaylqaegggdrQLGDREKElIRQAALQQTKEMDLSV 80
Cdd:pfam00554  89 MVASFQNLGIQCVKKKDVEEALKERI-----------------------------ELNIDPFN-VGFEALRQIKDMDLNV 138

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDS 111
Cdd:pfam00554 139 VRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
 684-758 3.39e-25

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: 99.24  E-value: 3.39e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217350802 684 VKLQLYKLLeipDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQ 758
Cdd:cd08310     1 TRLRLCKLL---DVGKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
 1-112 2.93e-23

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: 97.66  E-value: 2.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVhpdlaylqaegggdrqlgDREKELIRQAALQQTKEMDLSV 80
Cdd:cd07934    92 MTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTGPYKLT------------------EAEERELEQEAKELKKVMDLSI 153

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 112
Cdd:cd07934   154 VRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
384-590 3.69e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.41  E-value: 3.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 384 ALFDYAVTGDVKMLLAVQRHLTAV--QDENGDSVLHLAIIHLHSQLVRDLLEvtSGliSDdiINMRNDLYQTPLHLAVIT 461
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVnaRDKDGETPLHLAAYNGNLEIVKLLLE--AG--AD--VNAQDNDGNTPLHLAAAN 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 462 KQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHLAMMSNSLPCLLLLVA 541
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217350802 542 AGADVNAQeQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTT 590
Cdd:COG0666   241 AGADLNAK-DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
455-549 4.27e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 4.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 455 LHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALlldhpNGDGLNAIHLAMMSNSLP 534
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*
gi 2217350802 535 CLLLLVAAGADVNAQ 549
Cdd:pfam12796  76 IVKLLLEKGADINVK 90
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 1-112 1.45e-15

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: 75.48  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLEARMTeaciRGYNPGLLVhpdlaylqaegggdrqlgdrekelirQAALQQTKEMDLSV 80
Cdd:cd07827    93 MTASFNNLGIQCVRKKDVEEALGQRIQ----LGIDPFMVH--------------------------KGPEGNASDIDLNR 142

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 112
Cdd:cd07827   143 VRLCFQAFIEDSDGGFTLPLPPVLSNPIYDKK 174
IPT smart00429
ig-like, plexins, transcription factors;
118-219 1.11e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.06  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802  118 NLKIVRMDRTAGCVTGGEEIyLLCDKVQKDDIQIRFYEeeengGVWEGFGDFSPTdvhRQFAIVFKTPKYKDINITKPAS 197
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV-----GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71

                           90       100
                   ....*....|....*....|..
gi 2217350802  198 VfVQLRRkSDLEtSEPKPFLYY 219
Cdd:smart00429  72 T-VGLRN-GGVP-SSPQPFTYV 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 444-595 4.04e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 444 INMRN-DLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLN 522
Cdd:PHA02878  160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNT 236

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217350802 523 AIHLAMMS-NSLPCLLLLVAAGADVNAQEQKSGRTALHLAVeHDNISLAgcLLLEGDAHVDSTTYDGTTPLHIA 595
Cdd:PHA02878  237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSI-KSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
RHD-n_c-Rel cd07933
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ...
 2-112 5.13e-13

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: 67.98  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   2 VVGFANLGILHVTKKKVFETLEARMTeaciRGYNPgllvhpdlaylqaegggdrqLGDREKELIrqaalqQTKEMDLSVV 81
Cdd:cd07933    92 VLAFQNLGIQCVRRREVKEAIMLRIS----RGINP--------------------FNVPEEQLL------QIEEYDLNVV 141

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217350802  82 RLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 112
Cdd:cd07933   142 RLCFQIFLPDEHGNYTTALPPIVSNPIYDNR 172
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 682-760 6.10e-12

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: 62.04  E-value: 6.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802  682 EDVKLQLYKLLEIPdPDKNWATLAQKLGLG------ILNNAFRLSPAPSKTLMDNYEVSGG---TVRELVEALRQMGYTE 752
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80


                   ....*...
gi 2217350802  753 AIEVIQAA 760
Cdd:smart00005  81 AVELLRSE 88
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 119-220 1.59e-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: 60.94  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 119 LKIVRMDRTAGCVTGGEEIYLLCDKVQKD-DIQIRFYEEEEnggvwegfgdFSPTDVHrQFAIVFKTPKYKDINitkPAS 197
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFGGGVP----------CSVLSVS-STAIVCTTPPYANPG---PGP 66

                          90       100
                  ....*....|....*....|...
gi 2217350802 198 VFVQLRRKSDLETSEPKPFLYYP 220
Cdd:cd00102    67 VEVTVDRGNGGITSSPLTFTYVP 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 444-596 2.00e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 444 INMRNDLYQTPLHL-----AVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAA--KEGHDKVLSILLKHKKAALLLdhp 516
Cdd:PHA03100   61 INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIK--- 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 517 NGDGLNAIHLAMMSNS--LPCLLLLVAAGADVNAQEQ---------------KSGRTALHLAVEHDNISLAGcLLLEGDA 579
Cdd:PHA03100  138 NSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVK-YLLDLGA 216

                         170
                  ....*....|....*..
gi 2217350802 580 HVDSTTYDGTTPLHIAA 596
Cdd:PHA03100  217 NPNLVNKYGDTPLHIAI 233
Death pfam00531
Death domain;
685-761 3.04e-11

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 60.07  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 685 KLQLYKLLEIPDP-DKNWATLAQKLGLGIL-NNAFRLSPA----PSKTLMDNY---EVSGGTVRELVEALRQMGYTEAIE 755
Cdd:pfam00531   1 RKQLDRLLDPPPPlGKDWRELARKLGLSENeIDEIESENPrlrsQTYELLRLWeqrEGKNATVGTLLEALRKLGRRDAAE 80


                  ....*.
gi 2217350802 756 VIQAAS 761
Cdd:pfam00531  81 KIQSIL 86
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
 688-757 3.07e-11

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: 59.83  E-value: 3.07e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 688 LYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVI 757
Cdd:cd08798     5 LEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLL 74
PHA03095 PHA03095
ankyrin-like protein; Provisional
 444-594 3.71e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 444 INMRNDLYQtplhlaVITKQEDV----VEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGD 519
Cdd:PHA03095    9 IIMEAALYD------YLLNASNVtveeVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERC 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217350802 520 GLNAIHLAMMSNS-LPCLLLLVAAGADVNAqEQKSGRTALH--LAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHI 594
Cdd:PHA03095   83 GFTPLHLYLYNATtLDVIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIR-LLLRKGADVNALDLYGMTPLAV 158
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 412-601 1.37e-10

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: 64.65  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 412 GDSVLHLAIIHLHSQLVRDLLEVTSGLISDDiinMRNDLY--QTPLHLAVITKQEDVVEDLLRAGADLSL---------- 479
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEP---MTSDLYqgETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 480 ----LDRLGNSVLHLAAKEGHDKVLSILLKHkkaallldhpngdglnaihlammsnslpcllllvaaGADVNAQEQKsGR 555
Cdd:cd22192   128 gpknLIYYGEHPLSFAACVGNEEIVRLLIEH------------------------------------GADIRAQDSL-GN 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217350802 556 TALHLAVEHDNISLAgC----LLLEGDAHVDS------TTYDGTTPLHIAAGRGST 601
Cdd:cd22192   171 TVLHILVLQPNKTFA-CqmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNI 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
524-600 4.39e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 4.39e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217350802 524 IHLAMMSNSLPCLLLLVAAGADVNAQEQKsGRTALHLAVEHDNISLAGCLLLEGDAHVDSttyDGTTPLHIAAGRGS 600
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGH 73
PHA03095 PHA03095
ankyrin-like protein; Provisional
 407-592 4.56e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 407 VQDENGDSVLHlaiIHLHSQLVR-DLLEVtsgLISDDI-INMRNDLYQTPLHLAVITKQEDV--VEDLLRAGADLSLLDR 482
Cdd:PHA03095  112 AKDKVGRTPLH---VYLSGFNINpKVIRL---LLRKGAdVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDD 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 483 LGNSVLHLAAKEGHD--KVLSILLKHKKAALLLdhpNGDGLNAIHLAMMSNSLPCLLL--LVAAGADVNAQEqKSGRTAL 558
Cdd:PHA03095  186 RFRSLLHHHLQSFKPraRIVRELIRAGCDPAAT---DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARN-RYGQTPL 261

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217350802 559 HLAVEHDNISLAGCLLLEGdAHVDSTTYDGTTPL 592
Cdd:PHA03095  262 HYAAVFNNPRACRRLIALG-ADINAVSSDGNTPL 294
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 413-577 1.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 413 DSVLHLAIIHLHSQLVRDLLEvtSGLISDDIINMRNDlyqTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAA 492
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLD--LGKFADDVFYKDGM---TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 493 KEGHDKVLSILLKHKKAallLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGC 572
Cdd:PHA02875  144 MMGDIKGIELLIDHKAC---LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRL 220


                  ....*
gi 2217350802 573 LLLEG 577
Cdd:PHA02875  221 FIKRG 225
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 452-592 1.62e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 452 QTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILlkHKKAALLLDHPNGDGLNaihLAMMSN 531
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL--YHFASISDPHAAGDLLC---TAAKRN 633

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217350802 532 SLPCLLLLVAAGADVNAqEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPL 592
Cdd:PLN03192  634 DLTAMKELLKQGLNVDS-EDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPT 693
PHA03095 PHA03095
ankyrin-like protein; Provisional
 381-602 3.49e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 381 HANALFDYAVTGDVKMLLAVQRHLTAVQDEN-----GDSVLHLaiiHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPL 455
Cdd:PHA03095   11 MEAALYDYLLNASNVTVEEVRRLLAAGADVNfrgeyGKTPLHL---YLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 456 HLAVITKQ-EDVVEDLLRAGADLSLLDRLGNSVLH--LAAKEGHDKVLSILLKHKkaaLLLDHPNGDGLNAIHLAMMSN- 531
Cdd:PHA03095   88 HLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG---ADVNALDLYGMTPLAVLLKSRn 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 532 -SLPCLLLLVAAGADVNAQEQkSGRTALHL---------AVEHDNISlAGCL---------------------------- 573
Cdd:PHA03095  165 aNVELLRLLIDAGADVYAVDD-RFRSLLHHhlqsfkpraRIVRELIR-AGCDpaatdmlgntplhsmatgssckrslvlp 242

                         250       260
                  ....*....|....*....|....*....
gi 2217350802 574 LLEGDAHVDSTTYDGTTPLHIAAGRGSTR 602
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPR 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
416-506 4.69e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 416 LHLAIIHLHSQLVRDLLEVTSGlisddiINMRNDLYQTPLHLAVITKQEDVVEdLLRAGADLSLLDRlGNSVLHLAAKEG 495
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD------ANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSG 72

                          90
                  ....*....|.
gi 2217350802 496 HDKVLSILLKH 506
Cdd:pfam12796  73 HLEIVKLLLEK 83
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 411-595 6.19e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 6.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 411 NGDSVLHLAIIHLHSQLVRDLLEvtSGLIsddiINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHL 490
Cdd:PHA02874   90 NGVDTSILPIPCIEKDMIKTILD--CGID----VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 491 AAKEGHDKVLSILLKhKKAALLLDHPNGDglNAIHLAMMSNSLPCLLLLVAAGADVnAQEQKSGRTALHLAVEHDNISLA 570
Cdd:PHA02874  164 AIKHNFFDIIKLLLE-KGAYANVKDNNGE--SPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLHNAIIHNRSAIE 239

                         170       180
                  ....*....|....*....|....*
gi 2217350802 571 gclLLEGDAHVDSTTYDGTTPLHIA 595
Cdd:PHA02874  240 ---LLINNASINDQDIDGSTPLHHA 261
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
 1-112 8.24e-09

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: 55.57  E-value: 8.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLEARmTEACIRGYNPGLlVHPDlaylqaegggdrqlgdrekelirqaalqQTKEMDLSV 80
Cdd:cd07887    92 MRIVFQKLGIQCVKKKDVEESLKLR-EEINVDPFRTGF-DHKD----------------------------QINSIDLNV 141

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 112
Cdd:cd07887   142 VRLCFQVFLEDENGRFTVPLPPVVSDPIYDKK 173
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-521 1.38e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 407 VQDENGDSVLHLAIIHLHSQLVRDLLEvtsgliSDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNS 486
Cdd:COG0666   181 ARDNDGETPLHLAAENGHLEIVKLLLE------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217350802 487 VLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGL 521
Cdd:COG0666   255 ALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 481-602 2.15e-08

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 54.11  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 481 DRLGNSVLHLAAKEGHdkvLSILLKHKKAAL-----LLDHPNGDGLNAIHLAM---MSNSLPCLLLLVAAGADVNAQEQK 552
Cdd:PHA02736   14 DIEGENILHYLCRNGG---VTDLLAFKNAISdenryLVLEYNRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERV 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217350802 553 SGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTR 602
Cdd:PHA02736   91 FGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAK 140
Ank_4 pfam13637
Ankyrin repeats (many copies);
520-574 2.71e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.71e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217350802 520 GLNAIHLAMMSNSLPCLLLLVAAGADVNAQEqKSGRTALHLAVEHDNISLAGCLL 574
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 380-595 3.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 380 RHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLhlAIIHLHSQLVRDLLEVTSGLISDDI------------INMR 447
Cdd:PHA02876  192 KMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK--AIIDNRSNINKNDLSLLKAIRNEDLetslllydagfsVNSI 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 448 NDLYQTPLHLAVITKQ-EDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHD----KVL---------------------S 501
Cdd:PHA02876  270 DDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDteniRTLimlgadvnaadrlyitplhqaS 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 502 ILLKHKKAALLLDHPnGDGLNA--------IHLAMMSNSLPCLLLLVAAGADVNAQEQKSGrTALHLAVEHDNISLAGCL 573
Cdd:PHA02876  350 TLDRNKDIVITLLEL-GANVNArdycdktpIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTNPYMSVKT 427

                         250       260
                  ....*....|....*....|..
gi 2217350802 574 LLEGDAHVDSTTYDGTTPLHIA 595
Cdd:PHA02876  428 LIDRGANVNSKNKDLSTPLHYA 449
Ank_2 pfam12796
Ankyrin repeats (3 copies);
407-481 3.79e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 3.79e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217350802 407 VQDENGDSVLHLAIIHLHSQLVRDLLEVtsglisdDIINMRNDlYQTPLHLAVITKQEDVVEDLLRAGADLSLLD 481
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLEH-------ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
464-601 1.16e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 464 EDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHpngDGLNAIHLAMMSNSLPCLLLLVAAG 543
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADA---LGALLLLAAALAGDLLVALLLLAAG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217350802 544 ADVNAQEqKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGST 601
Cdd:COG0666    78 ADINAKD-DGGNTLLHAAARNGDLEIVK-LLLEAGADVNARDKDGETPLHLAAYNGNL 133
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 432-599 2.78e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 432 LEVTSGLISD--DIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKA 509
Cdd:PHA02874   14 IEAIEKIIKNkgNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 510 ALLLDHP--NGDGLNAI------------------HLAMMSNSLPCLLLLVAAGADVNAqEQKSGRTALHLAVEHDNISL 569
Cdd:PHA02874   94 TSILPIPciEKDMIKTIldcgidvnikdaelktflHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDI 172

                         170       180       190
                  ....*....|....*....|....*....|
gi 2217350802 570 AGcLLLEGDAHVDSTTYDGTTPLHIAAGRG 599
Cdd:PHA02874  173 IK-LLLEKGAYANVKDNNGESPLHNAAEYG 201
Ank_4 pfam13637
Ankyrin repeats (many copies);
484-540 3.68e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 3.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217350802 484 GNSVLHLAAKEGHDKVLSILLKHKkaaLLLDHPNGDGLNAIHLAMMSNSLPCLLLLV 540
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG---ADINAVDGNGETALHFAASNGNVEVLKLLL 54
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 1-112 3.82e-06

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: 47.81  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   1 MVVGFANLGILHVTKKKVFETLearmteacirgynpgllvhpdlaylqaegggdrqlgdrekelirqaalQQTKEMDLSV 80
Cdd:cd07884    96 YVAMFQNMGIIHTAKKNIPEEL------------------------------------------------YKKKNMNLNQ 127

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217350802  81 VRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 112
Cdd:cd07884   128 VVLRFQAFAVSANGHLRPICPPVYSNPINNLK 159
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 438-539 4.72e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 438 LISDDI-INMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILL------KHKKAA 510
Cdd:PHA03100  178 LLSYGVpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLnngpsiKTIIET 257

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217350802 511 LLLDhpNGDGLNAI-HLAMMSNSLPCLLLL 539
Cdd:PHA03100  258 LLYF--KDKDLNTItKIKMLKKSIMYMFLL 285
Ank_4 pfam13637
Ankyrin repeats (many copies);
453-504 5.30e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 5.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217350802 453 TPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILL 504
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
 684-758 5.50e-06

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: 44.96  E-value: 5.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217350802 684 VKLQLYKLLEIPDPDKN-WATLAQKLGLGILNNAFRLSPAPSKTLMDNYEV---SGGTVRELVEALRQMGYTEAIEVIQ 758
Cdd:cd08781     5 IRQKLCSLLDPPNARGNdWRLLAQKLSVDRYINYFATKPSPTEVILDLWEArnrDDGALNSLAAILREMGRHDAATILE 83
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 444-548 6.27e-06

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: 50.08  E-value: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 444 INMRNDLYQTPLHLAVItkqEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKV---LSILLKHKKAALLLDHPNGD- 519
Cdd:TIGR00870  45 INCPDRLGRSALFVAAI---ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVeaiLLHLLAAFRKSGPLELANDQy 121

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217350802 520 ------GLNAIHLAMMSNSLPCLLLLVAAGADVNA 548
Cdd:TIGR00870 122 tseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 452-506 1.57e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217350802 452 QTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKH 506
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
 70-112 2.37e-05

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: 45.62  E-value: 2.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217350802  70 LQQTKEMDLSVVRLMFTAFLPDSTGsFTRRLEPVVSDAIYDSK 112
Cdd:cd07886   131 LKNHEEVDMNVVRLCFQASYRDDDG-RKDCLSPVLSEPIYDKK 172
PHA02741 PHA02741
hypothetical protein; Provisional
 484-595 2.62e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.42  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 484 GNSVLHLAAKEGHDKVL---SILLKHKKAALLLDHPNGDGLNAIHLAMMSN----SLPCLLLLVAAGADVNAQEQKSGRT 556
Cdd:PHA02741   21 GENFFHEAARCGCFDIIarfTPFIRGDCHAAALNATDDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEMLEGDT 100

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217350802 557 ALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIA 595
Cdd:PHA02741  101 ALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 514-595 3.16e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 45.19  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 514 DHpngDGLNAIHLAM---MSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTT 590
Cdd:PHA02743   54 DH---HGRQCTHMVAwydRANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHET 130


                  ....*
gi 2217350802 591 PLHIA 595
Cdd:PHA02743  131 AYHIA 135
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 394-482 3.89e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 394 VKMLLAVQRHLTAVqDENGDSVLHLAIIHLHSQLVRDLLEVTSGlisddiINMRNDLYQTPLHLAVITKQEDVVEDLLRA 473
Cdd:PHA03100  175 VNYLLSYGVPINIK-DVYGFTPLHYAVYNNNPEFVKYLLDLGAN------PNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247


                  ....*....
gi 2217350802 474 GADLSLLDR 482
Cdd:PHA03100  248 GPSIKTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
558-601 4.03e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 4.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217350802 558 LHLAVEHDNISLAgCLLLEGDAHVDSTTYDGTTPLHIAAGRGST 601
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHL 43
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 454-595 4.18e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.80  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 454 PLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKE----GHDKVLSILLKHK--------------------KA 509
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSvfytlvaikdafnnrnveifKI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 510 ALLLDHPNGDGLNAIHLAMMSNS----LPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGdAHVDSTT 585
Cdd:PHA02878  120 ILTNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYG-ANVNIPD 198

                         170
                  ....*....|
gi 2217350802 586 YDGTTPLHIA 595
Cdd:PHA02878  199 KTNNSPLHHA 208
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 412-527 4.39e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 412 GDSVLHLAIIHLHSQLVRDLLEvtSG------------LISDdiinMRNDLY--QTPLHLAVITKQEDVVEDLLRAGADL 477
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLE--RGasvparacgdffVKSQ----GVDSFYhgESPLNAAACLGSPSIVALLSEDPADI 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217350802 478 SLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDH-------------PNGDGLNAIHLA 527
Cdd:TIGR00870 202 LTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLldklrdskeleviLNHQGLTPLKLA 264
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 385-547 7.21e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 385 LFDYAVTGDVK---MLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSgliSDDIINMRNdlyQTPLHLAVIT 461
Cdd:PHA02875   72 LHDAVEEGDVKaveELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDK---FSPLHLAVMM 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 462 KQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKhKKAALLLDHPNGDgLNAIHLAMMSNSLPCLLLLVA 541
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD-SGANIDYFGKNGC-VAALCYAIENNKIDIVRLFIK 223


                  ....*.
gi 2217350802 542 AGADVN 547
Cdd:PHA02875  224 RGADCN 229
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 412-489 9.89e-05

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: 46.03  E-value: 9.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 412 GDSVLHLAIIHLHSQLVRDLLE----VTSGLISDDI-INMRNDLY--QTPLHLAVITKQEDVVEDLLRAGAD---LSLLD 481
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVEngadVSARATGRFFrKSPGNLFYfgELPLSLAACTNQEEIVRLLLENGAQpaaLEAQD 152


                  ....*...
gi 2217350802 482 RLGNSVLH 489
Cdd:cd21882   153 SLGNTVLH 160
PHA03095 PHA03095
ankyrin-like protein; Provisional
 381-505 1.06e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 381 HANALFDYAvtGDVKMLLAVQRHLTAVqDENGDSVLHLAIIHLHSQ--LVRDLLEvtSGLIsddiINMRNDLYQTPLHLA 458
Cdd:PHA03095  194 HLQSFKPRA--RIVRELIRAGCDPAAT-DMLGNTPLHSMATGSSCKrsLVLPLLI--AGIS----INARNRYGQTPLHYA 264

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217350802 459 VITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLK 505
Cdd:PHA03095  265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
Ank_4 pfam13637
Ankyrin repeats (many copies);
554-602 1.17e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217350802 554 GRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTR 602
Cdd:pfam13637   1 ELTALHAAAASGHLELLR-LLLEKGADINAVDGNGETALHFAASNGNVE 48
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 453-601 1.73e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 453 TPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALllDHPNGDGLNAIHLAMMSNS 532
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217350802 533 LPCLLLLVAAGADVNAQEQKSgRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGST 601
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDK-FSPLHLAVMMGDIKGIE-LLIDHKACLDIEDCCGCTPLIIAMAKGDI 181
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 423-599 1.76e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 423 LHSQLVRDLLEVTSGLISDDI-INMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLS 501
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGAdVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 502 ILLKHKKaallldHPNGDGLNAIHlAMMSNSLPCLLLLVAAGADVNAQEQKSgRTALHLAVEHDNISLAGCLLLEGDAHV 581
Cdd:PHA02876  229 AIIDNRS------NINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCK-NTPLHHASQAPSLSRLVPKLLERGADV 300

                         170
                  ....*....|....*...
gi 2217350802 582 DSTTYDGTTPLHIAAGRG 599
Cdd:PHA02876  301 NAKNIKGETPLYLMAKNG 318
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 684-757 3.66e-04

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: 40.02  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 684 VKLQLYKLLEIPDP-DKNWATLAQKLGLG----ILNNAFRLSPAPSKTLMD---NYEVSggTVRELVEALRQMGYTEAIE 755
Cdd:cd08782     2 TRRKLARLLDPPDPmGRDWCLLAVNLGLTdlvaKLDSTSSPLPSPTDRLLQewtARPPS--TIGALLRKLRELGRRDAAD 79


                  ..
gi 2217350802 756 VI 757
Cdd:cd08782    80 FL 81
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 412-527 4.50e-04

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: 43.98  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 412 GDSVLHLAIIHLHSQLVRDLLEVTSGL---ISDDIIN--MRNDLY---QTPLHLAVITKQEDVVEDLL-RAGADLSLLDR 482
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVnahAKGVFFNpkYKHEGFyfgETPLALAACTNQPEIVQLLMeKESTDITSQDS 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217350802 483 LGNSVLHLA------AKEGHDKVL----SILLKHKKAAlLLDHPNGDGLNAIHLA 527
Cdd:cd22194   221 RGNTVLHALvtvaedSKTQNDFVKrmydMILLKSENKN-LETIRNNEGLTPLQLA 274
Ank_4 pfam13637
Ankyrin repeats (many copies);
412-471 6.48e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 6.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 412 GDSVLHLAIIHLHSQLVRDLLEvtSGLIsddiINMRNDLYQTPLHLAVITKQEDVVEDLL 471
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE--KGAD----INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 484-594 7.93e-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: 42.94  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 484 GNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNG-----------DGLNAIHLAMMSNSLPCLLLLVAAGADVNAQE-- 550
Cdd:cd21882    26 GKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217350802 551 ---QKSGRTALHLAvEHDnISLAGC--------LLLEGDAHVDSTTYD---GTTPLHI 594
Cdd:cd21882   106 rffRKSPGNLFYFG-ELP-LSLAACtnqeeivrLLLENGAQPAALEAQdslGNTVLHA 161
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 387-493 8.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 387 DYAVtgdVKMLLAVQRHLTaVQDENGDSVLHLAIIHLHSqlvrdlleVTSGLISDDIINMRNDLYQTPLHLAVITK-QED 465
Cdd:PHA02874  202 DYAC---IKLLIDHGNHIM-NKCKNGFTPLHNAIIHNRS--------AIELLINNASINDQDIDGSTPLHHAINPPcDID 269

                          90       100
                  ....*....|....*....|....*...
gi 2217350802 466 VVEDLLRAGADLSLLDRLGNSVLHLAAK 493
Cdd:PHA02874  270 IIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_5 pfam13857
Ankyrin repeats (many copies);
539-595 9.07e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 9.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217350802 539 LVAAG-ADVNAQEQKsGRTALHLAVEHDNISLAgCLLLEGDAHVDSTTYDGTTPLHIA 595
Cdd:pfam13857   1 LLEHGpIDLNRLDGE-GYTPLHVAAKYGALEIV-RVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 452-482 2.47e-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: 36.11  E-value: 2.47e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2217350802 452 QTPLHLAVI-TKQEDVVEDLLRAGADLSLLDR 482
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
444-491 2.68e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 2.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217350802 444 INMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLA 491
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 412-489 3.65e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 412 GDSVLHLAIIHLHSQLVRDLLEvtSGliSDDIINMRNDLYQT-----------PLHLAVITKQEDVVEDLLRAGADLSLL 480
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVE--NG--ADVHARACGRFFQKkqgtcfyfgelPLSLAACTKQWDVVNYLLENPHQPASL 169

                          90
                  ....*....|..
gi 2217350802 481 ---DRLGNSVLH 489
Cdd:cd22197   170 qaqDSLGNTVLH 181
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 453-594 4.03e-03

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: 40.77  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 453 TPLHLAVitKQEDV--VEDLLR-AGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKhkKAALLLDHP-NGD---GLNAIH 525
Cdd:cd22192    19 SPLLLAA--KENDVqaIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmTSDlyqGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 526 LAMMSNSLPCLLLLVAAGADVNAQEQ-----KSGRTALHLAVEHDnISLAGC--------LLLEGDAHVDSTTYDGTTPL 592
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSPRAtgtffRPGPKNLIYYGEHP-LSFAACvgneeivrLLIEHGADIRAQDSLGNTVL 173


                  ..
gi 2217350802 593 HI 594
Cdd:cd22192   174 HI 175
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 409-548 4.20e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802 409 DENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVL 488
Cdd:PHA02876  333 DVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217350802 489 HLAAKeGHDKVLSILLKHKKAAlLLDHPNGDGLNAIHLAMMSNSLPCLL-LLVAAGADVNA 548
Cdd:PHA02876  413 HFALC-GTNPYMSVKTLIDRGA-NVNSKNKDLSTPLHYACKKNCKLDVIeMLLDNGADVNA 471
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 453-477 4.38e-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: 35.26  E-value: 4.38e-03
                           10        20
                   ....*....|....*....|....*
gi 2217350802  453 TPLHLAVITKQEDVVEDLLRAGADL 477
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADI 28
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
 5-112 4.65e-03

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: 38.70  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217350802   5 FANLGILHVTKKKVFETLEARmteacIRGYNPGLLVHPDlaylqaegggdrqlgdrekelirqaalQQTKEMDLSVVRLM 84
Cdd:cd07885    95 FQNLGIQCVKKRDLEQAVSQR-----IQTNNNPFNVPIE---------------------------EQRADYDLNAVRLC 142

                          90       100
                  ....*....|....*....|....*...
gi 2217350802  85 FTAFLPDSTGSFTrRLEPVVSDAIYDSK 112
Cdd:cd07885   143 FQVTVRDPSGRLL-PLPPVLSQPIYDNR 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 526-596 4.78e-03

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: 40.38  E-value: 4.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217350802 526 LAMMSNSLPCL-LLLVAAGADVnAQEQKSGRTALHLAVEHDNISLAgCLLLEGDAH-----VDSTTYDGTTPLHIAA 596
Cdd:cd22192    23 LAAKENDVQAIkKLLKCPSCDL-FQRGALGETALHVAALYDNLEAA-VVLMEAAPElvnepMTSDLYQGETALHIAV 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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