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Conserved domains on  [gi|1370486992|ref|XP_024309836|]
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nuclear factor NF-kappa-B p105 subunit isoform X1 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12958902)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
43-244 2.20e-143

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: 425.08  E-value: 2.20e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 122
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 123 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAAL 202
Cdd:cd07935    81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370486992 203 QQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 244
Cdd:cd07935   161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
251-352 2.17e-62

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


:

Pssm-ID: 238582  Cd Length: 102  Bit Score: 206.02  E-value: 2.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 251 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASV 330
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                          90       100
                  ....*....|....*....|..
gi 1370486992 331 FVQLRRKSDLETSEPKPFLYYP 352
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
816-891 2.89e-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: 154.29  E-value: 2.89e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370486992 816 VKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQA 891
Cdd:cd08797     1 VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
499-759 1.49e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 499 DNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINM 578
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 579 RNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHL 658
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 659 AMMSNSLPCLLLLVAAGADVNAQeQKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAAL 738
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
                         250       260
                  ....*....|....*....|.
gi 1370486992 739 LKAAGADPLVENFEPLYDLDD 759
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 ...
43-244 2.20e-143

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: 425.08  E-value: 2.20e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 122
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 123 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAAL 202
Cdd:cd07935    81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370486992 203 QQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 244
Cdd:cd07935   161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
45-243 9.76e-84

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


Pssm-ID: 425749  Cd Length: 169  Bit Score: 266.86  E-value: 9.76e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  45 LQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGIC 124
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKDGVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 125 TVTAGPKDMVVGFANLGILHVTKKKVFETLEARMteacirgynpgllvhpdlaylqaegggdrQLGDREKElIRQAALQQ 204
Cdd:pfam00554  81 EVELGPEDMVASFQNLGIQCVKKKDVEEALKERI-----------------------------ELNIDPFN-VGFEALRQ 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370486992 205 TKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDS 243
Cdd:pfam00554 131 IKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
251-352 2.17e-62

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


Pssm-ID: 238582  Cd Length: 102  Bit Score: 206.02  E-value: 2.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 251 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASV 330
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                          90       100
                  ....*....|....*....|..
gi 1370486992 331 FVQLRRKSDLETSEPKPFLYYP 352
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
252-353 7.56e-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: 7.56e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 252 KIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVF 331
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 1370486992 332 VQLRRKSDLETSEPKPFLYYPE 353
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
816-891 2.89e-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: 154.29  E-value: 2.89e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370486992 816 VKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQA 891
Cdd:cd08797     1 VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
499-759 1.49e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 499 DNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINM 578
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 579 RNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHL 658
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 659 AMMSNSLPCLLLLVAAGADVNAQeQKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAAL 738
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
                         250       260
                  ....*....|....*....|.
gi 1370486992 739 LKAAGADPLVENFEPLYDLDD 759
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
587-681 3.27e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 587 LHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALlldhpNGDGLNAIHLAMMSNSLP 666
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLE 75
                          90
                  ....*....|....*
gi 1370486992 667 CLLLLVAAGADVNAQ 681
Cdd:pfam12796  76 IVKLLLEKGADINVK 90
IPT smart00429
ig-like, plexins, transcription factors;
250-351 1.29e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.06  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  250 NLKIVRMDRTAGCVTGGEEIyLLCDKVQKDDIQIRFYEeeengGVWEGFGDFSPTdvhRQFAIVFKTPKYKDINITKPAS 329
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV-----GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71
                           90       100
                   ....*....|....*....|..
gi 1370486992  330 VfVQLRRkSDLEtSEPKPFLYY 351
Cdd:smart00429  72 T-VGLRN-GGVP-SSPQPFTYV 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
576-727 4.07e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 576 INMRN-DLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLN 654
Cdd:PHA02878  160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNT 236
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370486992 655 AIHLAMMS-NSLPCLLLLVAAGADVNAQEQKSGRTALHLAVeHDNISLAgcLLLEGDAHVDSTTYDGTTPLHIA 727
Cdd:PHA02878  237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSI-KSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
814-892 2.55e-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: 63.58  E-value: 2.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  814 EDVKLQLYKLLEIPdPDKNWATLAQKLGLG------ILNNAFRLSPAPSKTLMDNYEVSGG---TVRELVEALRQMGYTE 884
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 1370486992  885 AIEVIQAA 892
Cdd:smart00005  81 AVELLRSE 88
Death pfam00531
Death domain;
817-893 2.15e-11

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 60.84  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 817 KLQLYKLLEIPDP-DKNWATLAQKLGLGIL-NNAFRLSPA----PSKTLMDNY---EVSGGTVRELVEALRQMGYTEAIE 887
Cdd:pfam00531   1 RKQLDRLLDPPPPlGKDWRELARKLGLSENeIDEIESENPrlrsQTYELLRLWeqrEGKNATVGTLLEALRKLGRRDAAE 80

                  ....*.
gi 1370486992 888 VIQAAS 893
Cdd:pfam00531  81 KIQSIL 86
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
544-733 1.68e-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: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 544 GDSVLHLAIIHLHSQLVRDLLEVTSGLISDDiinMRNDLY--QTPLHLAVITKQEDVVEDLLRAGADLSL---------- 611
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEP---MTSDLYqgETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 612 ----LDRLGNSVLHLAAKEGHDKVLSILLKHkkaallldhpngdglnaihlammsnslpcllllvaaGADVNAQEQKsGR 687
Cdd:cd22192   128 gpknLIYYGEHPLSFAACVGNEEIVRLLIEH------------------------------------GADIRAQDSL-GN 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370486992 688 TALHLAVEHDNISLAgC----LLLEGDAHVDS------TTYDGTTPLHIAAGRGST 733
Cdd:cd22192   171 TVLHILVLQPNKTFA-CqmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNI 225
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
576-680 7.55e-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: 7.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 576 INMRNDLYQTPLHLAVItkqEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKV---LSILLKHKKAALLLDHPNGD- 651
Cdd:TIGR00870  45 INCPDRLGRSALFVAAI---ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVeaiLLHLLAAFRKSGPLELANDQy 121
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1370486992 652 ------GLNAIHLAMMSNSLPCLLLLVAAGADVNA 680
Cdd:TIGR00870 122 tseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
585-609 4.64e-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: 35.64  E-value: 4.64e-03
                           10        20
                   ....*....|....*....|....*
gi 1370486992  585 TPLHLAVITKQEDVVEDLLRAGADL 609
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 ...
43-244 2.20e-143

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: 425.08  E-value: 2.20e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 122
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 123 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAAL 202
Cdd:cd07935    81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370486992 203 QQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 244
Cdd:cd07935   161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
43-244 2.34e-129

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


Pssm-ID: 143643  Cd Length: 197  Bit Score: 388.37  E-value: 2.34e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 122
Cdd:cd07883     1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 123 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDlaylqAEGGGDRQLGDREKELIRQAAL 202
Cdd:cd07883    81 ICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPGDLVHVD-----AEGGGDRQLTDEEQAEIRQKAK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370486992 203 QQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 244
Cdd:cd07883   156 QQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
45-243 9.76e-84

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


Pssm-ID: 425749  Cd Length: 169  Bit Score: 266.86  E-value: 9.76e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  45 LQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGIC 124
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKDGVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 125 TVTAGPKDMVVGFANLGILHVTKKKVFETLEARMteacirgynpgllvhpdlaylqaegggdrQLGDREKElIRQAALQQ 204
Cdd:pfam00554  81 EVELGPEDMVASFQNLGIQCVKKKDVEEALKERI-----------------------------ELNIDPFN-VGFEALRQ 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370486992 205 TKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDS 243
Cdd:pfam00554 131 IKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
43-244 4.29e-80

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: 257.90  E-value: 4.29e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHC-ED 121
Cdd:cd07934     1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCnES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 122 GICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVhpdlaylqaegggdrqlgDREKELIRQAA 201
Cdd:cd07934    81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTGPYKLT------------------EAEERELEQEA 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370486992 202 LQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 244
Cdd:cd07934   143 KELKKVMDLSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
251-352 2.17e-62

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


Pssm-ID: 238582  Cd Length: 102  Bit Score: 206.02  E-value: 2.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 251 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASV 330
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                          90       100
                  ....*....|....*....|..
gi 1370486992 331 FVQLRRKSDLETSEPKPFLYYP 352
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
43-244 1.72e-59

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


Pssm-ID: 143640  Cd Length: 174  Bit Score: 201.06  E-value: 1.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKH-CED 121
Cdd:cd07827     1 PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPHQLVGKTdCRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 122 GICTVTAGPK-DMVVGFANLGILHVTKKKVFETLEARMTeaciRGYNPGLLVhpdlaylqaegggdrqlgdrekelirQA 200
Cdd:cd07827    81 GVCEVRLGPKnNMTASFNNLGIQCVRKKDVEEALGQRIQ----LGIDPFMVH--------------------------KG 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1370486992 201 ALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 244
Cdd:cd07827   131 PEGNASDIDLNRVRLCFQAFIEDSDGGFTLPLPPVLSNPIYDKK 174
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
252-353 7.56e-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: 7.56e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 252 KIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVF 331
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 1370486992 332 VQLRRKSDLETSEPKPFLYYPE 353
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
RHD-n_c-Rel cd07933
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ...
43-244 1.52e-48

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


Pssm-ID: 143649  Cd Length: 172  Bit Score: 170.06  E-value: 1.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 122
Cdd:cd07933     1 PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPHDLVGKDCRDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 123 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTeaciRGYNPgllvhpdlaylqaegggdrqLGDREKELIrqaal 202
Cdd:cd07933    81 YYEAEFGPERRVLAFQNLGIQCVRRREVKEAIMLRIS----RGINP--------------------FNVPEEQLL----- 131
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370486992 203 qQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 244
Cdd:cd07933   132 -QIEEYDLNVVRLCFQIFLPDEHGNYTTALPPIVSNPIYDNR 172
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
43-244 2.72e-45

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


Pssm-ID: 143647  Cd Length: 173  Bit Score: 160.73  E-value: 2.72e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGK-HCED 121
Cdd:cd07887     1 PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPHNLVGKeGCKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 122 GICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARmTEACIRGYNPGlLVHPDlaylqaegggdrqlgdrekelirqaa 201
Cdd:cd07887    81 GVCTKKINPTEMRIVFQKLGIQCVKKKDVEESLKLR-EEINVDPFRTG-FDHKD-------------------------- 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370486992 202 lqQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 244
Cdd:cd07887   133 --QINSIDLNVVRLCFQVFLEDENGRFTVPLPPVVSDPIYDKK 173
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
251-352 3.81e-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: 3.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 251 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHrQFAIVFKTPKYKDINITKPASV 330
Cdd:cd00602     1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEKGPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79
                          90       100
                  ....*....|....*....|..
gi 1370486992 331 FVQLRRKSDLETSEPKPFLYYP 352
Cdd:cd00602    80 PIQLVRPDDRKRSEPLTFTYTP 101
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
816-891 2.89e-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: 154.29  E-value: 2.89e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370486992 816 VKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQA 891
Cdd:cd08797     1 VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
43-244 2.31e-36

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


Pssm-ID: 143644  Cd Length: 159  Bit Score: 134.87  E-value: 2.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRgFRFRYVCE-GPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVT-NGKNIHLHAHSLVGKHCE 120
Cdd:cd07884     1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQaDDNRRKPHVHKLVGKQGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 121 DGICTVTAGPK----DMVVGFANLGILHVTKKKVFETlearmteacirgynpgllvhpdlaylqaegggdrqlgdrekel 196
Cdd:cd07884    80 DDVCDPHDIEVspegDYVAMFQNMGIIHTAKKNIPEE------------------------------------------- 116
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370486992 197 irqaaLQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSK 244
Cdd:cd07884   117 -----LYKKKNMNLNQVVLRFQAFAVSANGHLRPICPPVYSNPINNLK 159
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
43-244 6.49e-36

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: 133.84  E-value: 6.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 122
Cdd:cd07885     1 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPHELVGKDCKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 123 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARmteacIRGYNPGLLVHPDlaylqaegggdrqlgdrekelirqaal 202
Cdd:cd07885    81 YYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQR-----IQTNNNPFNVPIE--------------------------- 128
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370486992 203 QQTKEMDLSVVRLMFTAFLPDSTGSFTrRLEPVVSDAIYDSK 244
Cdd:cd07885   129 EQRADYDLNAVRLCFQVTVRDPSGRLL-PLPPVLSQPIYDNR 169
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
499-759 1.49e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 499 DNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINM 578
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 579 RNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHL 658
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 659 AMMSNSLPCLLLLVAAGADVNAQeQKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAAL 738
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
                         250       260
                  ....*....|....*....|.
gi 1370486992 739 LKAAGADPLVENFEPLYDLDD 759
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLL 258
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
43-244 1.69e-33

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


Pssm-ID: 143646  Cd Length: 172  Bit Score: 126.90  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  43 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKV--IVQLVTNGKNIHLHAHSLVGKHCE 120
Cdd:cd07886     1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVtvTVCLVWKDPPHRVHPHGLVGKDCP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 121 DGICTVT----AGPKDmvvGFANLGILHVTKKKVFETLEARMTEAcIRGYNPGllvhpdlaylqaegggdrqlgdrekel 196
Cdd:cd07886    81 NGICQVTlnphSSPRH---SFSNLGIQCVRKREIEAAIETRLQLN-IDPFKAG--------------------------- 129
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370486992 197 irqaALQQTKEMDLSVVRLMFTAFLPDSTGsFTRRLEPVVSDAIYDSK 244
Cdd:cd07886   130 ----SLKNHEEVDMNVVRLCFQASYRDDDG-RKDCLSPVLSEPIYDKK 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
499-745 1.02e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 499 DNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEvtsgliSDDIINM 578
Cdd:COG0666    42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE------AGADVNA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 579 RNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHL 658
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD---VNARDNDGETPLHL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 659 AMMSNSLPCLLLLVAAGADVNAQeQKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAAL 738
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVK-LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                  ....*..
gi 1370486992 739 LKAAGAD 745
Cdd:COG0666   271 LLLALLL 277
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
816-890 1.12e-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: 100.78  E-value: 1.12e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370486992 816 VKLQLYKLLeipDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQ 890
Cdd:cd08310     1 TRLRLCKLL---DVGKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-722 3.65e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 3.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 516 ALFDYAVTGD---VKMLLAVQRHLTAvQDENGDSVLHLAIIHLHSQLVRDLLEvtSGliSDdiINMRNDLYQTPLHLAVI 592
Cdd:COG0666    90 LLHAAARNGDleiVKLLLEAGADVNA-RDKDGETPLHLAAYNGNLEIVKLLLE--AG--AD--VNAQDNDGNTPLHLAAA 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 593 TKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLNAIHLAMMSNSLPCLLLLV 672
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370486992 673 AAGADVNAQeQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTT 722
Cdd:COG0666   240 EAGADLNAK-DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
587-681 3.27e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 587 LHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALlldhpNGDGLNAIHLAMMSNSLP 666
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLE 75
                          90
                  ....*....|....*
gi 1370486992 667 CLLLLVAAGADVNAQ 681
Cdd:pfam12796  76 IVKLLLEKGADINVK 90
IPT smart00429
ig-like, plexins, transcription factors;
250-351 1.29e-13

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.06  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  250 NLKIVRMDRTAGCVTGGEEIyLLCDKVQKDDIQIRFYEeeengGVWEGFGDFSPTdvhRQFAIVFKTPKYKDINITKPAS 329
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV-----GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71
                           90       100
                   ....*....|....*....|..
gi 1370486992  330 VfVQLRRkSDLEtSEPKPFLYY 351
Cdd:smart00429  72 T-VGLRN-GGVP-SSPQPFTYV 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
576-727 4.07e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 576 INMRN-DLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAallLDHPNGDGLN 654
Cdd:PHA02878  160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNT 236
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370486992 655 AIHLAMMS-NSLPCLLLLVAAGADVNAQEQKSGRTALHLAVeHDNISLAgcLLLEGDAHVDSTTYDGTTPLHIA 727
Cdd:PHA02878  237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSI-KSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
814-892 2.55e-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: 63.58  E-value: 2.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992  814 EDVKLQLYKLLEIPdPDKNWATLAQKLGLG------ILNNAFRLSPAPSKTLMDNYEVSGG---TVRELVEALRQMGYTE 884
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 1370486992  885 AIEVIQAA 892
Cdd:smart00005  81 AVELLRSE 88
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
251-352 1.85e-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: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 251 LKIVRMDRTAGCVTGGEEIYLLCDKVQKD-DIQIRFYEEEEnggvwegfgdFSPTDVHrQFAIVFKTPKYKDINitkPAS 329
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFGGGVP----------CSVLSVS-STAIVCTTPPYANPG---PGP 66
                          90       100
                  ....*....|....*....|...
gi 1370486992 330 VFVQLRRKSDLETSEPKPFLYYP 352
Cdd:cd00102    67 VEVTVDRGNGGITSSPLTFTYVP 89
Death pfam00531
Death domain;
817-893 2.15e-11

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 60.84  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 817 KLQLYKLLEIPDP-DKNWATLAQKLGLGIL-NNAFRLSPA----PSKTLMDNY---EVSGGTVRELVEALRQMGYTEAIE 887
Cdd:pfam00531   1 RKQLDRLLDPPPPlGKDWRELARKLGLSENeIDEIESENPrlrsQTYELLRLWeqrEGKNATVGTLLEALRKLGRRDAAE 80

                  ....*.
gi 1370486992 888 VIQAAS 893
Cdd:pfam00531  81 KIQSIL 86
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
820-889 2.36e-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: 60.22  E-value: 2.36e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 820 LYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVI 889
Cdd:cd08798     5 LEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLL 74
PHA03100 PHA03100
ankyrin repeat protein; Provisional
576-728 2.45e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 576 INMRNDLYQTPLHL-----AVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAA--KEGHDKVLSILLKHKKAALLLdhp 648
Cdd:PHA03100   61 INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIK--- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 649 NGDGLNAIHLAMMSNS--LPCLLLLVAAGADVNAQEQ---------------KSGRTALHLAVEHDNISLAGcLLLEGDA 711
Cdd:PHA03100  138 NSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVK-YLLDLGA 216
                         170
                  ....*....|....*..
gi 1370486992 712 HVDSTTYDGTTPLHIAA 728
Cdd:PHA03100  217 NPNLVNKYGDTPLHIAI 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
576-726 4.54e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 4.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 576 INMRNDLYQtplhlaVITKQEDV----VEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGD 651
Cdd:PHA03095    9 IIMEAALYD------YLLNASNVtveeVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERC 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370486992 652 GLNAIHLAMMSNS-LPCLLLLVAAGADVNAqEQKSGRTALH--LAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHI 726
Cdd:PHA03095   83 GFTPLHLYLYNATtLDVIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIR-LLLRKGADVNALDLYGMTPLAV 158
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
544-733 1.68e-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: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 544 GDSVLHLAIIHLHSQLVRDLLEVTSGLISDDiinMRNDLY--QTPLHLAVITKQEDVVEDLLRAGADLSL---------- 611
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEP---MTSDLYqgETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 612 ----LDRLGNSVLHLAAKEGHDKVLSILLKHkkaallldhpngdglnaihlammsnslpcllllvaaGADVNAQEQKsGR 687
Cdd:cd22192   128 gpknLIYYGEHPLSFAACVGNEEIVRLLIEH------------------------------------GADIRAQDSL-GN 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370486992 688 TALHLAVEHDNISLAgC----LLLEGDAHVDS------TTYDGTTPLHIAAGRGST 733
Cdd:cd22192   171 TVLHILVLQPNKTFA-CqmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNI 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
656-732 3.67e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 3.67e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370486992 656 IHLAMMSNSLPCLLLLVAAGADVNAQEQKsGRTALHLAVEHDNISLAGCLLLEGDAHVDSttyDGTTPLHIAAGRGS 732
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGH 73
PHA03095 PHA03095
ankyrin-like protein; Provisional
539-724 5.57e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 539 VQDENGDSVLHlaiIHLHSQLVR-DLLEVtsgLISDDI-INMRNDLYQTPLHLAVITKQEDV--VEDLLRAGADLSLLDR 614
Cdd:PHA03095  112 AKDKVGRTPLH---VYLSGFNINpKVIRL---LLRKGAdVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDD 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 615 LGNSVLHLAAKEGHD--KVLSILLKHKKAALLLdhpNGDGLNAIHLAMMSNSLPCLLL--LVAAGADVNAQEqKSGRTAL 690
Cdd:PHA03095  186 RFRSLLHHHLQSFKPraRIVRELIRAGCDPAAT---DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARN-RYGQTPL 261
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370486992 691 HLAVEHDNISLAGCLLLEGdAHVDSTTYDGTTPL 724
Cdd:PHA03095  262 HYAAVFNNPRACRRLIALG-ADINAVSSDGNTPL 294
PHA02875 PHA02875
ankyrin repeat protein; Provisional
545-709 1.22e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 545 DSVLHLAIIHLHSQLVRDLLEvtSGLISDDIINMRNDlyqTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAA 624
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLD--LGKFADDVFYKDGM---TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 625 KEGHDKVLSILLKHKKAallLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGC 704
Cdd:PHA02875  144 MMGDIKGIELLIDHKAC---LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRL 220

                  ....*
gi 1370486992 705 LLLEG 709
Cdd:PHA02875  221 FIKRG 225
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
584-724 1.59e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 584 QTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILlkHKKAALLLDHPNGDGLNaihLAMMSN 663
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL--YHFASISDPHAAGDLLC---TAAKRN 633
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370486992 664 SLPCLLLLVAAGADVNAqEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPL 724
Cdd:PLN03192  634 DLTAMKELLKQGLNVDS-EDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPT 693
Ank_2 pfam12796
Ankyrin repeats (3 copies);
548-638 3.67e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.74  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 548 LHLAIIHLHSQLVRDLLEVTSGlisddiINMRNDLYQTPLHLAVITKQEDVVEdLLRAGADLSLLDRlGNSVLHLAAKEG 627
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD------ANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSG 72
                          90
                  ....*....|.
gi 1370486992 628 HDKVLSILLKH 638
Cdd:pfam12796  73 HLEIVKLLLEK 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
513-734 4.25e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 513 HANALFDYAVTGDVKMLLAVQRHLTAVQDEN-----GDSVLHLaiiHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPL 587
Cdd:PHA03095   11 MEAALYDYLLNASNVTVEEVRRLLAAGADVNfrgeyGKTPLHL---YLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 588 HLAVITKQ-EDVVEDLLRAGADLSLLDRLGNSVLH--LAAKEGHDKVLSILLKHKkaaLLLDHPNGDGLNAIHLAMMSN- 663
Cdd:PHA03095   88 HLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG---ADVNALDLYGMTPLAVLLKSRn 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 664 -SLPCLLLLVAAGADVNAQEQkSGRTALHL---------AVEHDNISlAGCL---------------------------- 705
Cdd:PHA03095  165 aNVELLRLLIDAGADVYAVDD-RFRSLLHHhlqsfkpraRIVRELIR-AGCDpaatdmlgntplhsmatgssckrslvlp 242
                         250       260
                  ....*....|....*....|....*....
gi 1370486992 706 LLEGDAHVDSTTYDGTTPLHIAAGRGSTR 734
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPR 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
539-653 5.62e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 5.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 539 VQDENGDSVLHLAIIHLHSQLVRDLLEvtsgliSDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNS 618
Cdd:COG0666   181 ARDNDGETPLHLAAENGHLEIVKLLLE------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1370486992 619 VLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGL 653
Cdd:COG0666   255 ALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
543-727 6.82e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 6.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 543 NGDSVLHLAIIHLHSQLVRDLLEvtSGLIsddiINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHL 622
Cdd:PHA02874   90 NGVDTSILPIPCIEKDMIKTILD--CGID----VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 623 AAKEGHDKVLSILLKhKKAALLLDHPNGDglNAIHLAMMSNSLPCLLLLVAAGADVnAQEQKSGRTALHLAVEHDNISLA 702
Cdd:PHA02874  164 AIKHNFFDIIKLLLE-KGAYANVKDNNGE--SPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLHNAIIHNRSAIE 239
                         170       180
                  ....*....|....*....|....*
gi 1370486992 703 gclLLEGDAHVDSTTYDGTTPLHIA 727
Cdd:PHA02874  240 ---LLINNASINDQDIDGSTPLHHA 261
PHA02736 PHA02736
Viral ankyrin protein; Provisional
613-734 2.53e-08

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 54.11  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 613 DRLGNSVLHLAAKEGHdkvLSILLKHKKAAL-----LLDHPNGDGLNAIHLAM---MSNSLPCLLLLVAAGADVNAQEQK 684
Cdd:PHA02736   14 DIEGENILHYLCRNGG---VTDLLAFKNAISdenryLVLEYNRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERV 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370486992 685 SGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTR 734
Cdd:PHA02736   91 FGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAK 140
Ank_4 pfam13637
Ankyrin repeats (many copies);
652-706 2.53e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370486992 652 GLNAIHLAMMSNSLPCLLLLVAAGADVNAQEqKSGRTALHLAVEHDNISLAGCLL 706
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
512-727 2.65e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 512 RHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLhlAIIHLHSQLVRDLLEVTSGLISDDI------------INMR 579
Cdd:PHA02876  192 KMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK--AIIDNRSNINKNDLSLLKAIRNEDLetslllydagfsVNSI 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 580 NDLYQTPLHLAVITKQ-EDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHD----KVL---------------------S 633
Cdd:PHA02876  270 DDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDteniRTLimlgadvnaadrlyitplhqaS 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 634 ILLKHKKAALLLDHPnGDGLNA--------IHLAMMSNSLPCLLLLVAAGADVNAQEQKSGrTALHLAVEHDNISLAGCL 705
Cdd:PHA02876  350 TLDRNKDIVITLLEL-GANVNArdycdktpIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTNPYMSVKT 427
                         250       260
                  ....*....|....*....|..
gi 1370486992 706 LLEGDAHVDSTTYDGTTPLHIA 727
Cdd:PHA02876  428 LIDRGANVNSKNKDLSTPLHYA 449
Ank_2 pfam12796
Ankyrin repeats (3 copies);
539-613 3.05e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 3.05e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370486992 539 VQDENGDSVLHLAIIHLHSQLVRDLLEVtsglisdDIINMRNDlYQTPLHLAVITKQEDVVEDLLRAGADLSLLD 613
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLEH-------ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
596-733 4.39e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.73  E-value: 4.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 596 EDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHpngDGLNAIHLAMMSNSLPCLLLLVAAG 675
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADA---LGALLLLAAALAGDLLVALLLLAAG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370486992 676 ADVNAQEqKSGRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGST 733
Cdd:COG0666    78 ADINAKD-DGGNTLLHAAARNGDLEIVK-LLLEAGADVNARDKDGETPLHLAAYNGNL 133
PHA02874 PHA02874
ankyrin repeat protein; Provisional
564-731 3.05e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 564 LEVTSGLISD--DIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKA 641
Cdd:PHA02874   14 IEAIEKIIKNkgNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 642 ALLLDHP--NGDGLNAI------------------HLAMMSNSLPCLLLLVAAGADVNAqEQKSGRTALHLAVEHDNISL 701
Cdd:PHA02874   94 TSILPIPciEKDMIKTIldcgidvnikdaelktflHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDI 172
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370486992 702 AGcLLLEGDAHVDSTTYDGTTPLHIAAGRG 731
Cdd:PHA02874  173 IK-LLLEKGAYANVKDNNGESPLHNAAEYG 201
Ank_4 pfam13637
Ankyrin repeats (many copies);
616-672 3.69e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370486992 616 GNSVLHLAAKEGHDKVLSILLKHKkaaLLLDHPNGDGLNAIHLAMMSNSLPCLLLLV 672
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG---ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
585-636 5.10e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370486992 585 TPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILL 636
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
570-671 5.67e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 570 LISDDI-INMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILL------KHKKAA 642
Cdd:PHA03100  178 LLSYGVpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLnngpsiKTIIET 257
                          90       100       110
                  ....*....|....*....|....*....|
gi 1370486992 643 LLLDhpNGDGLNAI-HLAMMSNSLPCLLLL 671
Cdd:PHA03100  258 LLYF--KDKDLNTItKIKMLKKSIMYMFLL 285
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
816-890 5.86e-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: 45.34  E-value: 5.86e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370486992 816 VKLQLYKLLEIPDPDKN-WATLAQKLGLGILNNAFRLSPAPSKTLMDNYEV---SGGTVRELVEALRQMGYTEAIEVIQ 890
Cdd:cd08781     5 IRQKLCSLLDPPNARGNdWRLLAQKLSVDRYINYFATKPSPTEVILDLWEArnrDDGALNSLAAILREMGRHDAATILE 83
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
576-680 7.55e-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: 7.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 576 INMRNDLYQTPLHLAVItkqEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKV---LSILLKHKKAALLLDHPNGD- 651
Cdd:TIGR00870  45 INCPDRLGRSALFVAAI---ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVeaiLLHLLAAFRKSGPLELANDQy 121
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1370486992 652 ------GLNAIHLAMMSNSLPCLLLLVAAGADVNA 680
Cdd:TIGR00870 122 tseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
584-638 1.75e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370486992 584 QTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKH 638
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02741 PHA02741
hypothetical protein; Provisional
616-727 3.09e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.42  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 616 GNSVLHLAAKEGHDKVL---SILLKHKKAALLLDHPNGDGLNAIHLAMMSN----SLPCLLLLVAAGADVNAQEQKSGRT 688
Cdd:PHA02741   21 GENFFHEAARCGCFDIIarfTPFIRGDCHAAALNATDDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEMLEGDT 100
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370486992 689 ALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIA 727
Cdd:PHA02741  101 ALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139
PHA02743 PHA02743
Viral ankyrin protein; Provisional
646-727 3.29e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 45.19  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 646 DHpngDGLNAIHLAM---MSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTT 722
Cdd:PHA02743   54 DH---HGRQCTHMVAwydRANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHET 130

                  ....*
gi 1370486992 723 PLHIA 727
Cdd:PHA02743  131 AYHIA 135
Ank_2 pfam12796
Ankyrin repeats (3 copies);
690-733 3.58e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 3.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1370486992 690 LHLAVEHDNISLAgCLLLEGDAHVDSTTYDGTTPLHIAAGRGST 733
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHL 43
PHA02878 PHA02878
ankyrin repeat protein; Provisional
586-727 4.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 586 PLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKE----GHDKVLSILLKHK--------------------KA 641
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSvfytlvaikdafnnrnveifKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 642 ALLLDHPNGDGLNAIHLAMMSNS----LPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGdAHVDSTT 717
Cdd:PHA02878  120 ILTNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYG-ANVNIPD 198
                         170
                  ....*....|
gi 1370486992 718 YDGTTPLHIA 727
Cdd:PHA02878  199 KTNNSPLHHA 208
PHA03100 PHA03100
ankyrin repeat protein; Provisional
526-614 4.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 526 VKMLLAVQRHLTAVqDENGDSVLHLAIIHLHSQLVRDLLEVTSGlisddiINMRNDLYQTPLHLAVITKQEDVVEDLLRA 605
Cdd:PHA03100  175 VNYLLSYGVPINIK-DVYGFTPLHYAVYNNNPEFVKYLLDLGAN------PNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247

                  ....*....
gi 1370486992 606 GADLSLLDR 614
Cdd:PHA03100  248 GPSIKTIIE 256
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
544-659 5.27e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 544 GDSVLHLAIIHLHSQLVRDLLEvtSG------------LISDdiinMRNDLY--QTPLHLAVITKQEDVVEDLLRAGADL 609
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLE--RGasvparacgdffVKSQ----GVDSFYhgESPLNAAACLGSPSIVALLSEDPADI 201
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370486992 610 SLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDH-------------PNGDGLNAIHLA 659
Cdd:TIGR00870 202 LTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLldklrdskeleviLNHQGLTPLKLA 264
PHA02875 PHA02875
ankyrin repeat protein; Provisional
517-679 7.19e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 517 LFDYAVTGDVK---MLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSgliSDDIINMRNdlyQTPLHLAVIT 593
Cdd:PHA02875   72 LHDAVEEGDVKaveELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDK---FSPLHLAVMM 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 594 KQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKhKKAALLLDHPNGDgLNAIHLAMMSNSLPCLLLLVA 673
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD-SGANIDYFGKNGC-VAALCYAIENNKIDIVRLFIK 223

                  ....*.
gi 1370486992 674 AGADVN 679
Cdd:PHA02875  224 RGADCN 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
686-734 1.14e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370486992 686 GRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTR 734
Cdd:pfam13637   1 ELTALHAAAASGHLELLR-LLLEKGADINAVDGNGETALHFAASNGNVE 48
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
544-621 1.19e-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: 46.03  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 544 GDSVLHLAIIHLHSQLVRDLLE----VTSGLISDDI-INMRNDLY--QTPLHLAVITKQEDVVEDLLRAGAD---LSLLD 613
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVEngadVSARATGRFFrKSPGNLFYfgELPLSLAACTNQEEIVRLLLENGAQpaaLEAQD 152

                  ....*...
gi 1370486992 614 RLGNSVLH 621
Cdd:cd21882   153 SLGNTVLH 160
PHA03095 PHA03095
ankyrin-like protein; Provisional
513-637 1.26e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 513 HANALFDYAvtGDVKMLLAVQRHLTAVqDENGDSVLHLAIIHLHSQ--LVRDLLEvtSGLIsddiINMRNDLYQTPLHLA 590
Cdd:PHA03095  194 HLQSFKPRA--RIVRELIRAGCDPAAT-DMLGNTPLHSMATGSSCKrsLVLPLLI--AGIS----INARNRYGQTPLHYA 264
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370486992 591 VITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLK 637
Cdd:PHA03095  265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
555-731 1.55e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 555 LHSQLVRDLLEVTSGLISDDI-INMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLS 633
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGAdVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 634 ILLKHKKaallldHPNGDGLNAIHlAMMSNSLPCLLLLVAAGADVNAQEQKSgRTALHLAVEHDNISLAGCLLLEGDAHV 713
Cdd:PHA02876  229 AIIDNRS------NINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCK-NTPLHHASQAPSLSRLVPKLLERGADV 300
                         170
                  ....*....|....*...
gi 1370486992 714 DSTTYDGTTPLHIAAGRG 731
Cdd:PHA02876  301 NAKNIKGETPLYLMAKNG 318
PHA02875 PHA02875
ankyrin repeat protein; Provisional
585-733 1.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 585 TPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALllDHPNGDGLNAIHLAMMSNS 664
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKDGMTPLHLATILKK 114
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370486992 665 LPCLLLLVAAGADVNAQEQKSgRTALHLAVEHDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGST 733
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDK-FSPLHLAVMMGDIKGIE-LLIDHKACLDIEDCCGCTPLIIAMAKGDI 181
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
43-117 2.30e-04

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


Pssm-ID: 143648  Cd Length: 161  Bit Score: 42.65  E-value: 2.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370486992  43 PYLQILEQPKQRgFRFRYVCEGpSHGGLPGASSEknkkSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGK 117
Cdd:cd07927     1 YELRIEVQPEPH-HRARYETEG-SRGAVKAPSTG----GFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHR 69
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
816-889 2.79e-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: 40.40  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 816 VKLQLYKLLEIPDP-DKNWATLAQKLGLG----ILNNAFRLSPAPSKTLMD---NYEVSggTVRELVEALRQMGYTEAIE 887
Cdd:cd08782     2 TRRKLARLLDPPDPmGRDWCLLAVNLGLTdlvaKLDSTSSPLPSPTDRLLQewtARPPS--TIGALLRKLRELGRRDAAD 79

                  ..
gi 1370486992 888 VI 889
Cdd:cd08782    80 FL 81
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
544-659 4.03e-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: 44.36  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 544 GDSVLHLAIIHLHSQLVRDLLEVTSGL---ISDDIIN--MRNDLY---QTPLHLAVITKQEDVVEDLL-RAGADLSLLDR 614
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVnahAKGVFFNpkYKHEGFyfgETPLALAACTNQPEIVQLLMeKESTDITSQDS 220
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370486992 615 LGNSVLHLA------AKEGHDKVL----SILLKHKKAAlLLDHPNGDGLNAIHLA 659
Cdd:cd22194   221 RGNTVLHALvtvaedSKTQNDFVKrmydMILLKSENKN-LETIRNNEGLTPLQLA 274
Ank_4 pfam13637
Ankyrin repeats (many copies);
544-603 6.00e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 6.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 544 GDSVLHLAIIHLHSQLVRDLLEvtSGLIsddiINMRNDLYQTPLHLAVITKQEDVVEDLL 603
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE--KGAD----INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
671-727 7.60e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 7.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370486992 671 LVAAG-ADVNAQEQKsGRTALHLAVEHDNISLAgCLLLEGDAHVDSTTYDGTTPLHIA 727
Cdd:pfam13857   1 LLEHGpIDLNRLDGE-GYTPLHVAAKYGALEIV-RVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
616-726 9.47e-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: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 616 GNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNG-----------DGLNAIHLAMMSNSLPCLLLLVAAGADVNAQE-- 682
Cdd:cd21882    26 GKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370486992 683 ---QKSGRTALHLAvEHDnISLAGC--------LLLEGDAHVDSTTYD---GTTPLHI 726
Cdd:cd21882   106 rffRKSPGNLFYFG-ELP-LSLAACtnqeeivrLLLENGAQPAALEAQdslGNTVLHA 161
PHA02874 PHA02874
ankyrin repeat protein; Provisional
519-625 9.78e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 9.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 519 DYAVtgdVKMLLAVQRHLTaVQDENGDSVLHLAIIHLHSqlvrdlleVTSGLISDDIINMRNDLYQTPLHLAVITK-QED 597
Cdd:PHA02874  202 DYAC---IKLLIDHGNHIM-NKCKNGFTPLHNAIIHNRS--------AIELLINNASINDQDIDGSTPLHHAINPPcDID 269
                          90       100
                  ....*....|....*....|....*...
gi 1370486992 598 VVEDLLRAGADLSLLDRLGNSVLHLAAK 625
Cdd:PHA02874  270 IIDILLYHKADISIKDNKGENPIDTAFK 297
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
584-614 2.51e-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: 36.50  E-value: 2.51e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370486992 584 QTPLHLAVI-TKQEDVVEDLLRAGADLSLLDR 614
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
576-623 2.53e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370486992 576 INMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLA 623
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
544-621 3.52e-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: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 544 GDSVLHLAIIHLHSQLVRDLLEvtSGliSDDIINMRNDLYQT-----------PLHLAVITKQEDVVEDLLRAGADLSLL 612
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVE--NG--ADVHARACGRFFQKkqgtcfyfgelPLSLAACTKQWDVVNYLLENPHQPASL 169
                          90
                  ....*....|..
gi 1370486992 613 ---DRLGNSVLH 621
Cdd:cd22197   170 qaqDSLGNTVLH 181
PHA02876 PHA02876
ankyrin repeat protein; Provisional
541-680 3.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 541 DENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVL 620
Cdd:PHA02876  333 DVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370486992 621 HLAAKeGHDKVLSILLKHKKAAlLLDHPNGDGLNAIHLAMMSNSLPCLL-LLVAAGADVNA 680
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 ...
585-609 4.64e-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: 35.64  E-value: 4.64e-03
                           10        20
                   ....*....|....*....|....*
gi 1370486992  585 TPLHLAVITKQEDVVEDLLRAGADL 609
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
585-726 4.80e-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: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 585 TPLHLAVitKQEDV--VEDLLR-AGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKhkKAALLLDHP-NGD---GLNAIH 657
Cdd:cd22192    19 SPLLLAA--KENDVqaIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmTSDlyqGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370486992 658 LAMMSNSLPCLLLLVAAGADVNAQEQ-----KSGRTALHLAVEHDnISLAGC--------LLLEGDAHVDSTTYDGTTPL 724
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVSPRAtgtffRPGPKNLIYYGEHP-LSFAACvgneeivrLLIEHGADIRAQDSLGNTVL 173

                  ..
gi 1370486992 725 HI 726
Cdd:cd22192   174 HI 175
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
658-728 5.70e-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: 5.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370486992 658 LAMMSNSLPCL-LLLVAAGADVnAQEQKSGRTALHLAVEHDNISLAgCLLLEGDAH-----VDSTTYDGTTPLHIAA 728
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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