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Conserved domains on  [gi|1215484311|gb|OXB77562|]
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hypothetical protein H355_015854 [Colinus virginianus]

Protein Classification

RHD-n_NFkB1 and IPT_NFkappaB domain-containing protein( domain architecture ID 12958902)

protein containing domains RHD-n_NFkB1, IPT_NFkappaB, ANKYR, and Death_NFkB1_p105

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 ...
47-248 3.48e-147

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: 435.09  E-value: 3.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFCEDG 126
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 127 VCTVNAGPKDMVVGFANLGILHVTKKKVFETLETRMIDACKKGYNPGLLVHPELGYLQAEGCGDRQLTEREREIIRQAAV 206
Cdd:cd07935    81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1215484311 207 QQTKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSK 248
Cdd:cd07935   161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
255-356 4.79e-61

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: 202.55  E-value: 4.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 255 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEDENGGMWEGFGDFSPTDVHRQFAIVFKTPKYRDVNITKPASV 334
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                          90       100
                  ....*....|....*....|..
gi 1215484311 335 FVQLRRKSDLETSEPKPFLYYP 356
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
808-883 7.09e-43

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: 150.06  E-value: 7.09e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 808 SKQQLYKLLEAPDPRKNWSTLAEKLGLGILNNAFRLSPSPSKTLLDNYKISGGTVQELLAALRQMDHTEAIEVIEK 883
Cdd:cd08797     1 VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
517-742 2.03e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 2.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 517 DVRMLLAAQRHLTAVQDDNGDNVLHLSIIHLHRELVKNLLEvmpdvNYTNIINMRNDLYQTPLHLAVITKQAEVVDDLLK 596
Cdd:COG0666    34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL-----AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 597 AGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHqKASsmIDLCNGEGLGAIHMVVMANSLSCLKLLIAAGVNVNAQeQK 676
Cdd:COG0666   109 AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GAD--VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR-DN 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 677 SGRTALHLAVEQENLPLAGcLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGADPHVEN 742
Cdd:COG0666   185 DGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
 
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 ...
47-248 3.48e-147

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: 435.09  E-value: 3.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFCEDG 126
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 127 VCTVNAGPKDMVVGFANLGILHVTKKKVFETLETRMIDACKKGYNPGLLVHPELGYLQAEGCGDRQLTEREREIIRQAAV 206
Cdd:cd07935    81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1215484311 207 QQTKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSK 248
Cdd:cd07935   161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
49-247 9.95e-81

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: 259.16  E-value: 9.95e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  49 LQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFCEDGVC 128
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKDGVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 129 TVNAGPKDMVVGFANLGILHVTKKKVFETLETRMidackkgynpgllvhpelgylqaegcgdrQLTEREREiIRQAAVQQ 208
Cdd:pfam00554  81 EVELGPEDMVASFQNLGIQCVKKKDVEEALKERI-----------------------------ELNIDPFN-VGFEALRQ 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1215484311 209 TKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDS 247
Cdd:pfam00554 131 IKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
255-356 4.79e-61

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: 202.55  E-value: 4.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 255 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEDENGGMWEGFGDFSPTDVHRQFAIVFKTPKYRDVNITKPASV 334
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                          90       100
                  ....*....|....*....|..
gi 1215484311 335 FVQLRRKSDLETSEPKPFLYYP 356
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
256-357 5.05e-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: 191.24  E-value: 5.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 256 KIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEDENGGMWEGFGDFSPTDVHRQFAIVFKTPKYRDVNITKPASVF 335
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 1215484311 336 VQLRRKSDLETSEPKPFLYYPE 357
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
808-883 7.09e-43

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: 150.06  E-value: 7.09e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 808 SKQQLYKLLEAPDPRKNWSTLAEKLGLGILNNAFRLSPSPSKTLLDNYKISGGTVQELLAALRQMDHTEAIEVIEK 883
Cdd:cd08797     1 VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
517-742 2.03e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 2.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 517 DVRMLLAAQRHLTAVQDDNGDNVLHLSIIHLHRELVKNLLEvmpdvNYTNIINMRNDLYQTPLHLAVITKQAEVVDDLLK 596
Cdd:COG0666    34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL-----AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 597 AGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHqKASsmIDLCNGEGLGAIHMVVMANSLSCLKLLIAAGVNVNAQeQK 676
Cdd:COG0666   109 AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GAD--VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR-DN 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 677 SGRTALHLAVEQENLPLAGcLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGADPHVEN 742
Cdd:COG0666   185 DGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
PHA03100 PHA03100
ankyrin repeat protein; Provisional
509-720 5.30e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 5.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 509 LFDYAVSGDVRMLLAAQRHLTAVQDDNGD-------NVLHLSIIHLHRELVKNLLEVMPDVNYTNIINMrndlyqTPLHL 581
Cdd:PHA03100    1 LYSYIVLTKSRIIKVKNIKYIIMEDDLNDysykkpvLPLYLAKEARNIDVVKILLDNGADINSSTKNNS------TPLHY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 582 -----AVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAE--GDDKILSVFLKHQKAssmIDLCNGEGLGAIHMVVMA 654
Cdd:PHA03100   75 lsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGAN---VNIKNSDGENLLHLYLES 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 655 NS--LSCLKLLIAAGVNVNAQEQ---------------KSGRTALHLAVEQENLPLAGcLLLEGDADVDSTTYDGTTPLH 717
Cdd:PHA03100  152 NKidLKILKLLIDKGVDINAKNRvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVK-YLLDLGANPNLVNKYGDTPLH 230

                  ...
gi 1215484311 718 IAA 720
Cdd:PHA03100  231 IAI 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
648-742 1.87e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 648 IHMVVMANSLSCLKLLIAAGVNVNAQEQKsGRTALHLAVEQENLPLAGCLLLEGDADVDSttyDGTTPLHIAAGRGFTKL 727
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 1215484311 728 AAVLKAAGADPHVEN 742
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Death pfam00531
Death domain;
809-885 3.01e-14

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 68.93  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 809 KQQLYKLLEAPDPR-KNWSTLAEKLGLGIL-NNAFRLSP----SPSKTLLDNYKI---SGGTVQELLAALRQMDHTEAIE 879
Cdd:pfam00531   1 RKQLDRLLDPPPPLgKDWRELARKLGLSENeIDEIESENprlrSQTYELLRLWEQregKNATVGTLLEALRKLGRRDAAE 80

                  ....*.
gi 1215484311 880 VIEKAL 885
Cdd:pfam00531  81 KIQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
806-884 2.32e-13

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: 66.28  E-value: 2.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  806 ESSKQQLYKLLEAPDPRKnWSTLAEKLGLG------ILNNAFRLSPSPSKTLLDNYKISGG---TVQELLAALRQMDHTE 876
Cdd:smart00005   2 ELTRQKLAKLLDHPLGLD-WRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 1215484311  877 AIEVIEKA 884
Cdd:smart00005  81 AVELLRSE 88
IPT smart00429
ig-like, plexins, transcription factors;
254-355 1.02e-12

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 64.75  E-value: 1.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  254 NLKIVRMDRTAGCVTGGEEIyLLCDKVQKDDIQIRFYEEDenggmWEGFGDFSPTdvhRQFAIVFKTPKYRDVNITKPAS 333
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEVGV-----GEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71
                           90       100
                   ....*....|....*....|..
gi 1215484311  334 VfVQLRRkSDLEtSEPKPFLYY 355
Cdd:smart00429  72 T-VGLRN-GGVP-SSPQPFTYV 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
491-746 1.03e-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: 65.42  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 491 DGLFLekaLQLARRHCSALFDYAVSGDVRmllAAQRHLTAVQDDN------GDNVLHLSIIHLHRELVKNLLEVMPDvny 564
Cdd:cd22192     6 DELHL---LQQKRISESPLLLAAKENDVQ---AIKKLLKCPSCDLfqrgalGETALHVAALYDNLEAAVVLMEAAPE--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 565 tnIIN--MRNDLY--QTPLHLAVITKQAEVVDDLLKAGANVNlldrhgnsvlhLAAAEGddkilSVFLKHQKAssmidLC 640
Cdd:cd22192    77 --LVNepMTSDLYqgETALHIAVVNQNLNLVRELIARGADVV-----------SPRATG-----TFFRPGPKN-----LI 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 641 N-GEglgaiHMVVMA---NSLSCLKLLIAAGVNVNAQEQKsGRTALHLAVEQENLPLAgC----LLLEGDADVDSTTYDg 712
Cdd:cd22192   134 YyGE-----HPLSFAacvGNEEIVRLLIEHGADIRAQDSL-GNTVLHILVLQPNKTFA-CqmydLILSYDKEDDLQPLD- 205
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1215484311 713 ttplHIAAGRGFTKlaavLKAAGADPHVENFEPL 746
Cdd:cd22192   206 ----LVPNNQGLTP----FKLAAKEGNIVMFQHL 231
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
507-733 1.25e-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: 49.31  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 507 SALFDYAVSG---DVRMLLAAQRHLTAVqddnGDNVLHLSIIHLHR---ELVKNLLEVMPDVNYTNIIN--MRNDLY--Q 576
Cdd:TIGR00870  54 SALFVAAIENenlELTELLLNLSCRGAV----GDTLLHAISLEYVDaveAILLHLLAAFRKSGPLELANdqYTSEFTpgI 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 577 TPLHLAVITKQAEVVDDLLKAGANVNlldrhgnsvlhlAAAEGDDkilsvFLKHQKASSmidLCNGEGLGAIHMVVmaNS 656
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVP------------ARACGDF-----FVKSQGVDS---FYHGESPLNAAACL--GS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 657 LSCLKLLIAAGVNVNAQEQKsGRTALHLAVEQ-----ENLPLA-GC--LLLEGDADVDSTT-------YDGTTPLHIAAG 721
Cdd:TIGR00870 188 PSIVALLSEDPADILTADSL-GNTLLHLLVMEnefkaEYEELScQMynFALSLLDKLRDSKelevilnHQGLTPLKLAAK 266
                         250
                  ....*....|..
gi 1215484311 722 RGFTKLAAVLKA 733
Cdd:TIGR00870 267 EGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
577-603 9.42e-04

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: 37.57  E-value: 9.42e-04
                           10        20
                   ....*....|....*....|....*..
gi 1215484311  577 TPLHLAVITKQAEVVDDLLKAGANVNL 603
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
47-248 3.48e-147

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: 435.09  E-value: 3.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFCEDG 126
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 127 VCTVNAGPKDMVVGFANLGILHVTKKKVFETLETRMIDACKKGYNPGLLVHPELGYLQAEGCGDRQLTEREREIIRQAAV 206
Cdd:cd07935    81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1215484311 207 QQTKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSK 248
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 ...
47-248 2.29e-122

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: 370.27  E-value: 2.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFCEDG 126
Cdd:cd07883     1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 127 VCTVNAGPKDMVVGFANLGILHVTKKKVFETLETRMIDACKKGYNPGLLVHPElgylqAEGCGDRQLTEREREIIRQAAV 206
Cdd:cd07883    81 ICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPGDLVHVD-----AEGGGDRQLTDEEQAEIRQKAK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1215484311 207 QQTKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSK 248
Cdd:cd07883   156 QQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
49-247 9.95e-81

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: 259.16  E-value: 9.95e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  49 LQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFCEDGVC 128
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKDGVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 129 TVNAGPKDMVVGFANLGILHVTKKKVFETLETRMidackkgynpgllvhpelgylqaegcgdrQLTEREREiIRQAAVQQ 208
Cdd:pfam00554  81 EVELGPEDMVASFQNLGIQCVKKKDVEEALKERI-----------------------------ELNIDPFN-VGFEALRQ 130
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1215484311 209 TKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDS 247
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) ...
47-248 8.77e-79

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: 254.44  E-value: 8.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFC-ED 125
Cdd:cd07934     1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCnES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 126 GVCTVNAGPKDMVVGFANLGILHVTKKKVFETLETRMIDACKKGYNPGLlvhpelgylqaegcgdrqLTEREREIIRQAA 205
Cdd:cd07934    81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTGPYK------------------LTEAEERELEQEA 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1215484311 206 VQQTKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSK 248
Cdd:cd07934   143 KELKKVMDLSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
47-248 3.55e-62

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: 208.38  E-value: 3.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKF-CED 125
Cdd:cd07827     1 PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPHQLVGKTdCRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 126 GVCTVNAGPK-DMVVGFANLGILHVTKKKVFETLETRMidacKKGYNPGLLVHPELGylqaegcgdrqlterereiirqa 204
Cdd:cd07827    81 GVCEVRLGPKnNMTASFNNLGIQCVRKKDVEEALGQRI----QLGIDPFMVHKGPEG----------------------- 133
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1215484311 205 avqQTKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSK 248
Cdd:cd07827   134 ---NASDIDLNRVRLCFQAFIEDSDGGFTLPLPPVLSNPIYDKK 174
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
255-356 4.79e-61

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: 202.55  E-value: 4.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 255 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEDENGGMWEGFGDFSPTDVHRQFAIVFKTPKYRDVNITKPASV 334
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                          90       100
                  ....*....|....*....|..
gi 1215484311 335 FVQLRRKSDLETSEPKPFLYYP 356
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
256-357 5.05e-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: 191.24  E-value: 5.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 256 KIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEDENGGMWEGFGDFSPTDVHRQFAIVFKTPKYRDVNITKPASVF 335
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 1215484311 336 VQLRRKSDLETSEPKPFLYYPE 357
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 ...
47-248 6.62e-47

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: 165.43  E-value: 6.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFCEDG 126
Cdd:cd07933     1 PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPHDLVGKDCRDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 127 VCTVNAGPKDMVVGFANLGILHVTKKKVFETLETRMIdackKGYNPGllvhpelgylqaeGCGDRQLterereiirqaav 206
Cdd:cd07933    81 YYEAEFGPERRVLAFQNLGIQCVRRREVKEAIMLRIS----RGINPF-------------NVPEEQL------------- 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1215484311 207 QQTKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSK 248
Cdd:cd07933   131 LQIEEYDLNVVRLCFQIFLPDEHGNYTTALPPIVSNPIYDNR 172
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
47-248 2.53e-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: 2.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKF-CED 125
Cdd:cd07887     1 PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPHNLVGKEgCKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 126 GVCTVNAGPKDMVVGFANLGILHVTKKKVFETL---ETRMIDACKKGYNpgllvHPElgylqaegcgdrqlterereiir 202
Cdd:cd07887    81 GVCTKKINPTEMRIVFQKLGIQCVKKKDVEESLklrEEINVDPFRTGFD-----HKD----------------------- 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1215484311 203 qaavqQTKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSK 248
Cdd:cd07887   133 -----QINSIDLNVVRLCFQVFLEDENGRFTVPLPPVVSDPIYDKK 173
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
255-356 1.69e-44

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


Pssm-ID: 238336  Cd Length: 101  Bit Score: 155.52  E-value: 1.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 255 LKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEDENGGMWEGFGDFSPTDVHrQFAIVFKTPKYRDVNITKPASV 334
Cdd:cd00602     1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEKGPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79
                          90       100
                  ....*....|....*....|..
gi 1215484311 335 FVQLRRKSDLETSEPKPFLYYP 356
Cdd:cd00602    80 PIQLVRPDDRKRSEPLTFTYTP 101
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
808-883 7.09e-43

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: 150.06  E-value: 7.09e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 808 SKQQLYKLLEAPDPRKNWSTLAEKLGLGILNNAFRLSPSPSKTLLDNYKISGGTVQELLAALRQMDHTEAIEVIEK 883
Cdd:cd08797     1 VKQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
517-742 2.03e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 2.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 517 DVRMLLAAQRHLTAVQDDNGDNVLHLSIIHLHRELVKNLLEvmpdvNYTNIINMRNDLYQTPLHLAVITKQAEVVDDLLK 596
Cdd:COG0666    34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLL-----AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 597 AGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHqKASsmIDLCNGEGLGAIHMVVMANSLSCLKLLIAAGVNVNAQeQK 676
Cdd:COG0666   109 AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GAD--VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR-DN 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 677 SGRTALHLAVEQENLPLAGcLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGADPHVEN 742
Cdd:COG0666   185 DGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
47-248 5.69e-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: 133.71  E-value: 5.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRgFRFRYVCE-GPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVT-NGKYVHLHAHSLVGKFCE 124
Cdd:cd07884     1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQaDDNRRKPHVHKLVGKQGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 125 DGVCTVNAGPK----DMVVGFANLGILHVTKKKVFETLetrmidaCKKgynpgllvhpelgylqaegcgdrqltererei 200
Cdd:cd07884    80 DDVCDPHDIEVspegDYVAMFQNMGIIHTAKKNIPEEL-------YKK-------------------------------- 120
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1215484311 201 irqaavqqtKEMDLSVVRLMFTAFLPDSNGGFTRRLDPVISDAIYDSK 248
Cdd:cd07884   121 ---------KNMNLNQVVLRFQAFAVSANGHLRPICPPVYSNPINNLK 159
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
47-248 4.95e-35

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


Pssm-ID: 143645  Cd Length: 169  Bit Score: 131.15  E-value: 4.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGKFCEDG 126
Cdd:cd07885     1 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPHELVGKDCKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 127 VCTVNAGPKDMVVGFANLGILHVTKKKVFETLETRMidacKKGYNPgLLVHPElgylqaegcgdrqlterereiirqaav 206
Cdd:cd07885    81 YYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQRI----QTNNNP-FNVPIE--------------------------- 128
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1215484311 207 QQTKEMDLSVVRLMFTAFLPDSNGGFTrRLDPVISDAIYDSK 248
Cdd:cd07885   129 EQRADYDLNAVRLCFQVTVRDPSGRLL-PLPPVLSQPIYDNR 169
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
533-781 4.13e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.77  E-value: 4.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 533 DDNGDNVLHLSIIHLHRELVKNLLEVMPDVNYTNIINMRNDLYQTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVL 612
Cdd:COG0666    12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 613 HLAAAEGDDKILSVFLKHqKASsmIDLCNGEGLGAIHMVVMANSLSCLKLLIAAGVNVNAQEqKSGRTALHLAVEQENLP 692
Cdd:COG0666    92 HAAARNGDLEIVKLLLEA-GAD--VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 693 LAGcLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGADPHVENFEplfdveddvkddddegivpGTTPLDMAA 772
Cdd:COG0666   168 IVK-LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-------------------GKTALDLAA 227

                  ....*....
gi 1215484311 773 SWEVYDILN 781
Cdd:COG0666   228 ENGNLEIVK 236
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
47-248 4.15e-33

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


Pssm-ID: 143646  Cd Length: 172  Bit Score: 125.74  E-value: 4.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  47 PYLQIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKV--IVQLVTNGKYVHLHAHSLVGKFCE 124
Cdd:cd07886     1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVtvTVCLVWKDPPHRVHPHGLVGKDCP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 125 DGVCTV----NAGPKDmvvGFANLGILHVTKKKVFETLETRMidacKKGYNPgllvhpelgyLQAegcGDRQLTErerei 200
Cdd:cd07886    81 NGICQVtlnpHSSPRH---SFSNLGIQCVRKREIEAAIETRL----QLNIDP----------FKA---GSLKNHE----- 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1215484311 201 irqaavqqtkEMDLSVVRLMFTAFLPDSNgGFTRRLDPVISDAIYDSK 248
Cdd:cd07886   136 ----------EVDMNVVRLCFQASYRDDD-GRKDCLSPVLSEPIYDKK 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
556-773 6.56e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 6.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 556 LEVMPDVNYTNIINMRNDLYQTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKASs 635
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 636 mIDLCNGEGLGAIHMVVMANSLSCLKLLIAAGVNVNAQEqKSGRTALHLAVEQENLPLAGcLLLEGDADVDSTTYDGTTP 715
Cdd:COG0666    80 -INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVK-LLLEAGADVNAQDNDGNTP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1215484311 716 LHIAAGRGFTKLAAVLKAAGADPHVENFEplfdveddvkddddegivpGTTPLDMAAS 773
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDND-------------------GETPLHLAAE 195
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
809-882 1.20e-22

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: 92.31  E-value: 1.20e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215484311 809 KQQLYKLLeapDPRKNWSTLAEKLGLGILNNAFRLSPSPSKTLLDNYKISGGTVQELLAALRQMDHTEAIEVIE 882
Cdd:cd08310     2 RLRLCKLL---DVGKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
518-672 2.44e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.85  E-value: 2.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 518 VRMLLAAQrhltA---VQDDNGDNVLHLSIIHLHRELVKNLLEVMPDVNYtniinmRNDLYQTPLHLAVITKQAEVVDDL 594
Cdd:COG0666   136 VKLLLEAG----AdvnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA------RDNDGETPLHLAAENGHLEIVKLL 205
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215484311 595 LKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKAssmIDLCNGEGLGAIHMVVMANSLSCLKLLIAAGVNVNA 672
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
PHA03100 PHA03100
ankyrin repeat protein; Provisional
509-720 5.30e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 5.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 509 LFDYAVSGDVRMLLAAQRHLTAVQDDNGD-------NVLHLSIIHLHRELVKNLLEVMPDVNYTNIINMrndlyqTPLHL 581
Cdd:PHA03100    1 LYSYIVLTKSRIIKVKNIKYIIMEDDLNDysykkpvLPLYLAKEARNIDVVKILLDNGADINSSTKNNS------TPLHY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 582 -----AVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAE--GDDKILSVFLKHQKAssmIDLCNGEGLGAIHMVVMA 654
Cdd:PHA03100   75 lsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGAN---VNIKNSDGENLLHLYLES 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 655 NS--LSCLKLLIAAGVNVNAQEQ---------------KSGRTALHLAVEQENLPLAGcLLLEGDADVDSTTYDGTTPLH 717
Cdd:PHA03100  152 NKidLKILKLLIDKGVDINAKNRvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVK-YLLDLGANPNLVNKYGDTPLH 230

                  ...
gi 1215484311 718 IAA 720
Cdd:PHA03100  231 IAI 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
550-719 1.88e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.31  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 550 ELVKNLLEVMPDVNytniINMRNDLyQTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLK 629
Cdd:PHA02878  148 EITKLLLSYGADIN----MKDRHKG-NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLE 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 630 HQKASSMIDLCngeGLGAIHMVV-MANSLSCLKLLIAAGVNVNAQEQKSGRTALHLAVEQENLPLagcLLLEGDADVDST 708
Cdd:PHA02878  223 NGASTDARDKC---GNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK---LLLEYGADINSL 296
                         170
                  ....*....|.
gi 1215484311 709 TYDGTTPLHIA 719
Cdd:PHA02878  297 NSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
648-742 1.87e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 648 IHMVVMANSLSCLKLLIAAGVNVNAQEQKsGRTALHLAVEQENLPLAGCLLLEGDADVDSttyDGTTPLHIAAGRGFTKL 727
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 1215484311 728 AAVLKAAGADPHVEN 742
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Death pfam00531
Death domain;
809-885 3.01e-14

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 68.93  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 809 KQQLYKLLEAPDPR-KNWSTLAEKLGLGIL-NNAFRLSP----SPSKTLLDNYKI---SGGTVQELLAALRQMDHTEAIE 879
Cdd:pfam00531   1 RKQLDRLLDPPPPLgKDWRELARKLGLSENeIDEIESENprlrSQTYELLRLWEQregKNATVGTLLEALRKLGRRDAAE 80

                  ....*.
gi 1215484311 880 VIEKAL 885
Cdd:pfam00531  81 KIQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
806-884 2.32e-13

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: 66.28  E-value: 2.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  806 ESSKQQLYKLLEAPDPRKnWSTLAEKLGLG------ILNNAFRLSPSPSKTLLDNYKISGG---TVQELLAALRQMDHTE 876
Cdd:smart00005   2 ELTRQKLAKLLDHPLGLD-WRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 1215484311  877 AIEVIEKA 884
Cdd:smart00005  81 AVELLRSE 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
579-673 8.20e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 8.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 579 LHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKASsmidlCNGEGLGAIHMVVMANSLS 658
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-----LKDNGRTALHYAARSGHLE 75
                          90
                  ....*....|....*
gi 1215484311 659 CLKLLIAAGVNVNAQ 673
Cdd:pfam12796  76 IVKLLLEKGADINVK 90
IPT smart00429
ig-like, plexins, transcription factors;
254-355 1.02e-12

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 64.75  E-value: 1.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311  254 NLKIVRMDRTAGCVTGGEEIyLLCDKVQKDDIQIRFYEEDenggmWEGFGDFSPTdvhRQFAIVFKTPKYRDVNITKPAS 333
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEVGV-----GEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71
                           90       100
                   ....*....|....*....|..
gi 1215484311  334 VfVQLRRkSDLEtSEPKPFLYY 355
Cdd:smart00429  72 T-VGLRN-GGVP-SSPQPFTYV 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
534-719 1.34e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.15  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 534 DNGDNVLHLSIIHLHRELVKNLLEVMPDVNytniinMRNDLYQTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLH 613
Cdd:PHA02874   89 DNGVDTSILPIPCIEKDMIKTILDCGIDVN------IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 614 LAAAEGDDKILSVFLKHqkaSSMIDLCNGEGLGAIHMVVMANSLSCLKLLIAAGVNVnAQEQKSGRTALHLAVEQENLPL 693
Cdd:PHA02874  163 IAIKHNFFDIIKLLLEK---GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLHNAIIHNRSAI 238
                         170       180
                  ....*....|....*....|....*.
gi 1215484311 694 AgclLLEGDADVDSTTYDGTTPLHIA 719
Cdd:PHA02874  239 E---LLINNASINDQDIDGSTPLHHA 261
PHA03095 PHA03095
ankyrin-like protein; Provisional
550-739 1.77e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 550 ELVKNLLEVMPDVNYTNIINmrndlyQTPLHLAV---ITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAaaegddkilsv 626
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYG------KTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHLY----------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 627 flkhqkassmidLCNgeglgaihmvvmANSLSCLKLLIAAGVNVNAqEQKSGRTALH--LAVEQENLPLAGcLLLEGDAD 704
Cdd:PHA03095   91 ------------LYN------------ATTLDVIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIR-LLLRKGAD 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1215484311 705 VDSTTYDGTTPLHIaagrgFTK-------LAAVLKAAGADPH 739
Cdd:PHA03095  145 VNALDLYGMTPLAV-----LLKsrnanveLLRLLIDAGADVY 181
PHA03095 PHA03095
ankyrin-like protein; Provisional
518-738 4.43e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.67  E-value: 4.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 518 VRMLLAAQRHLTAVqDDNGDNVLHLSIIHLHRELVKNLLevmpdVNYTNIINMRNDLYQTPLH--LAVITKQAEVVDDLL 595
Cdd:PHA03095   66 VRLLLEAGADVNAP-ERCGFTPLHLYLYNATTLDVIKLL-----IKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 596 KAGANVNLLDRHGNSVLH--LAAAEGDDKILSVFLKHQKASSMIDLCngeGLGAIHmvVMANSL----SCLKLLIAAGVN 669
Cdd:PHA03095  140 RKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDR---FRSLLH--HHLQSFkpraRIVRELIRAGCD 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215484311 670 VNAQEQkSGRTALHLAVEQENL--PLAGCLLLEGdADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGADP 738
Cdd:PHA03095  215 PAATDM-LGNTPLHSMATGSSCkrSLVLPLLIAG-ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI 283
PHA03095 PHA03095
ankyrin-like protein; Provisional
506-716 6.28e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 6.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 506 CSALFDYAVSGD----VRMLLAAQRHLTaVQDDNGDNVLHlsiIHL-----HRELVKNLLEVMPDVNYTNIINMrndlyq 576
Cdd:PHA03095   84 FTPLHLYLYNATtldvIKLLIKAGADVN-AKDKVGRTPLH---VYLsgfniNPKVIRLLLRKGADVNALDLYGM------ 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 577 TPLHLAVITKQA--EVVDDLLKAGANVNLLDRHGNSVLH--LAAAEGDDKILSVFLKHQKASSMIDLcngegLGAIHMVV 652
Cdd:PHA03095  154 TPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDM-----LGNTPLHS 228
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215484311 653 MANSLSCLKL----LIAAGVNVNAQEqKSGRTALHLAVEQENLPLAGCLLLEGdADVDSTTYDGTTPL 716
Cdd:PHA03095  229 MATGSSCKRSlvlpLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALG-ADINAVSSDGNTPL 294
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
255-356 3.01e-11

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


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 60.55  E-value: 3.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 255 LKIVRMDRTAGCVTGGEEIYLLCDKVQKD-DIQIRFYeedenggmweGFGDFSPTDVHrQFAIVFKTPKYRDVNitkPAS 333
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFG----------GGVPCSVLSVS-STAIVCTTPPYANPG---PGP 66
                          90       100
                  ....*....|....*....|...
gi 1215484311 334 VFVQLRRKSDLETSEPKPFLYYP 356
Cdd:cd00102    67 VEVTVDRGNGGITSSPLTFTYVP 89
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
810-883 3.92e-11

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


Pssm-ID: 176776  Cd Length: 76  Bit Score: 59.83  E-value: 3.92e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215484311 810 QQLYKLLEAPDPRKNWSTLAEKLGLGILNNAFRLSPSPSKTLLDNYKISGGTVQELLAALRQMDHTEAIEVIEK 883
Cdd:cd08798     3 QRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
491-746 1.03e-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: 65.42  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 491 DGLFLekaLQLARRHCSALFDYAVSGDVRmllAAQRHLTAVQDDN------GDNVLHLSIIHLHRELVKNLLEVMPDvny 564
Cdd:cd22192     6 DELHL---LQQKRISESPLLLAAKENDVQ---AIKKLLKCPSCDLfqrgalGETALHVAALYDNLEAAVVLMEAAPE--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 565 tnIIN--MRNDLY--QTPLHLAVITKQAEVVDDLLKAGANVNlldrhgnsvlhLAAAEGddkilSVFLKHQKAssmidLC 640
Cdd:cd22192    77 --LVNepMTSDLYqgETALHIAVVNQNLNLVRELIARGADVV-----------SPRATG-----TFFRPGPKN-----LI 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 641 N-GEglgaiHMVVMA---NSLSCLKLLIAAGVNVNAQEQKsGRTALHLAVEQENLPLAgC----LLLEGDADVDSTTYDg 712
Cdd:cd22192   134 YyGE-----HPLSFAacvGNEEIVRLLIEHGADIRAQDSL-GNTVLHILVLQPNKTFA-CqmydLILSYDKEDDLQPLD- 205
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1215484311 713 ttplHIAAGRGFTKlaavLKAAGADPHVENFEPL 746
Cdd:cd22192   206 ----LVPNNQGLTP----FKLAAKEGNIVMFQHL 231
PHA02736 PHA02736
Viral ankyrin protein; Provisional
605-736 4.08e-10

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 59.12  E-value: 4.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 605 DRHGNSVLHLAAAEGDDKILSVFLK--HQKASSMIDLCNGEGLGAIHMVV---MANSLSCLKLLIAAGVNVNAQEQKSGR 679
Cdd:PHA02736   14 DIEGENILHYLCRNGGVTDLLAFKNaiSDENRYLVLEYNRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERVFGN 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1215484311 680 TALHLAVEQENLPLAGCLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGA 736
Cdd:PHA02736   94 TPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
509-605 1.16e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 509 LFDYAVSGDVRM--LLAAQRHLTAVQDDNGDNVLHLSIIHLHRELVKNLLEVMpdvnytnIINMRNDlYQTPLHLAVITK 586
Cdd:pfam12796   1 LHLAAKNGNLELvkLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-------DVNLKDN-GRTALHYAARSG 72
                          90
                  ....*....|....*....
gi 1215484311 587 QAEVVDDLLKAGANVNLLD 605
Cdd:pfam12796  73 HLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
550-743 1.83e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 550 ELVKNLLEvmpdvNYTNIINMRNDLYQTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLK 629
Cdd:PHA02874   15 EAIEKIIK-----NKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 630 hqkassmidlcNGEGLGAIHMVVMANSLscLKLLIAAGVNVNAQEQKSgRTALHLAVEQENLPLAGcLLLEGDADVDSTT 709
Cdd:PHA02874   90 -----------NGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIK-MLFEYGADVNIED 154
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1215484311 710 YDGTTPLHIAAGRGFTKLAAVLKAAGADPHVENF 743
Cdd:PHA02874  155 DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
518-639 2.00e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.97  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 518 VRMLLAAQRHLTAvQDDNGDNVLHLSIIHLHRELVKNLLEVMPDVNytniinMRNDLYQTPLHLAVITKQAEVVDDLLKA 597
Cdd:COG0666   169 VKLLLEAGADVNA-RDNDGETPLHLAAENGHLEIVKLLLEAGADVN------AKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1215484311 598 GANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKASSMIDL 639
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA03095 PHA03095
ankyrin-like protein; Provisional
518-638 2.40e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 518 VRMLLAAQRHLTAVqDDNGDNVLHLSIIH--LHRELVKNLLEVMPDVNYtniinmRNDLYQTPLHLAVITKQAEVVDDLL 595
Cdd:PHA03095  205 VRELIRAGCDPAAT-DMLGNTPLHSMATGssCKRSLVLPLLIAGISINA------RNRYGQTPLHYAAVFNNPRACRRLI 277
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1215484311 596 KAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKASSMID 638
Cdd:PHA03095  278 ALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
PHA02876 PHA02876
ankyrin repeat protein; Provisional
550-721 3.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 550 ELVKNLLEVMPDVNYTNiinmrnDLYQTPLHLA-VITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFL 628
Cdd:PHA02876  322 ENIRTLIMLGADVNAAD------RLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 629 KHqkaSSMIDLCNGEGLGAIHMVVMA-NSLSCLKLLIAAGVNVNAQeQKSGRTALHLAVEQENLPLAGCLLLEGDADVDS 707
Cdd:PHA02876  396 DY---GADIEALSQKIGTALHFALCGtNPYMSVKTLIDRGANVNSK-NKDLSTPLHYACKKNCKLDVIEMLLDNGADVNA 471
                         170
                  ....*....|....
gi 1215484311 708 TTYDGTTPLHIAAG 721
Cdd:PHA02876  472 INIQNQYPLLIALE 485
PHA02874 PHA02874
ankyrin repeat protein; Provisional
531-719 3.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 531 VQDDNGDNVLHLSIIHLHRELVKNLLEVMPDVNYTNIinmrNDLYqtPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNS 610
Cdd:PHA02874  119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD----NGCY--PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 611 VLHLAAAEGDDKILSVFLKHqkASSMIDLCNgEGLGAIHMVVMANSlSCLKLLI-AAGVNVnaqEQKSGRTALHLAVeqe 689
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLIDH--GNHIMNKCK-NGFTPLHNAIIHNR-SAIELLInNASIND---QDIDGSTPLHHAI--- 262
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1215484311 690 NLPlagC------LLLEGDADVDSTTYDGTTPLHIA 719
Cdd:PHA02874  263 NPP---CdidiidILLYHKADISIKDNKGENPIDTA 295
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
807-882 4.31e-09

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: 54.20  E-value: 4.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 807 SSKQQLYKLLEAPDPRKN-WSTLAEKLGLGILNNAFRLSPSPSKTLLDNYKI---SGGTVQELLAALRQMDHTEAIEVIE 882
Cdd:cd08781     4 SIRQKLCSLLDPPNARGNdWRLLAQKLSVDRYINYFATKPSPTEVILDLWEArnrDDGALNSLAAILREMGRHDAATILE 83
PHA02878 PHA02878
ankyrin repeat protein; Provisional
587-746 7.11e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 7.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 587 QAEVVDDLLKAGANVNLLDRH-GNSVLHLAAAEGDDKILSVFLKHQKASSMIDLCNGEGLgaiHMVVMANSLSCLKLLIA 665
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPL---HHAVKHYNKPIVHILLE 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 666 AGVNVNAQEqKSGRTALHLAVEQENLPLAGCLLLEGDADVDSTTY-DGTTPLHIAAgRGFTKLAAVLKaAGADPHVENFE 744
Cdd:PHA02878  223 NGASTDARD-KCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI-KSERKLKLLLE-YGADINSLNSY 299

                  ..
gi 1215484311 745 PL 746
Cdd:PHA02878  300 KL 301
PHA02876 PHA02876
ankyrin repeat protein; Provisional
551-719 8.58e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 8.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 551 LVKNLLEVMPDVNYTNIINmrndlyQTPLHL-AVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLK 629
Cdd:PHA02876  289 LVPKLLERGADVNAKNIKG------ETPLYLmAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLL 362
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 630 HQKAS-SMIDLCNGEglgAIHMVVMANSLSCLKLLIAAGVNVNAQEQKSGrTALHLAVEQENLPLAGCLLLEGDADVDST 708
Cdd:PHA02876  363 ELGANvNARDYCDKT---PIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTNPYMSVKTLIDRGANVNSK 438
                         170
                  ....*....|.
gi 1215484311 709 TYDGTTPLHIA 719
Cdd:PHA02876  439 NKDLSTPLHYA 449
PHA02743 PHA02743
Viral ankyrin protein; Provisional
643-736 1.36e-08

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 55.21  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 643 EGLGAIHMVV---MANSLSCLKLLIAAGVNVNAQEQKSGRTALHLAVEQENLPLAGCLLLEGDADVDSTTYDGTTPLHIA 719
Cdd:PHA02743   56 HGRQCTHMVAwydRANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIA 135
                          90
                  ....*....|....*..
gi 1215484311 720 AGRGFTKLAAVLKAAGA 736
Cdd:PHA02743  136 YKMRDRRMMEILRANGA 152
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
576-716 1.92e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 576 QTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFlkHQKASSMIDLCNGEGLGaihMVVMAN 655
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL--YHFASISDPHAAGDLLC---TAAKRN 633
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215484311 656 SLSCLKLLIAAGVNVNAqEQKSGRTALHLAVEQENLPLAGCLLLEGdADVD-STTYDGTTPL 716
Cdd:PLN03192  634 DLTAMKELLKQGLNVDS-EDHQGATALQVAMAEDHVDMVRLLIMNG-ADVDkANTDDDFSPT 693
PHA02875 PHA02875
ankyrin repeat protein; Provisional
577-701 2.33e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 577 TPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKASSMIDLCNGEGLgaIHMVVMANS 656
Cdd:PHA02875  104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL--IIAMAKGDI 181
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1215484311 657 LSClKLLIAAGVNVNAQEQKSGRTALHLAVEQENLPLAGCLLLEG 701
Cdd:PHA02875  182 AIC-KMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRG 225
PHA03100 PHA03100
ankyrin repeat protein; Provisional
535-640 3.55e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 535 NGDNVLHLSIIHLHREL--VKNLLEVMPDVNYTNIINM----------RNDLYQTPLHLAVITKQAEVVDDLLKAGANVN 602
Cdd:PHA03100  140 DGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNRVNYllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1215484311 603 LLDRHGNSVLHLAAAEGDDKILSVFLKHQKASSMIDLC 640
Cdd:PHA03100  220 LVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02876 PHA02876
ankyrin repeat protein; Provisional
555-737 1.42e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 555 LLEVMPDVNYTNIINMrndlyqTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKAS 634
Cdd:PHA02876  164 LLEGGADVNAKDIYCI------TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 635 SMIDLcngEGLGAIHMVVMANSLsclkLLIAAGVNVNAQEQKSGrTALHLAVEQENLPLAGCLLLEGDADVDSTTYDGTT 714
Cdd:PHA02876  238 NKNDL---SLLKAIRNEDLETSL----LLYDAGFSVNSIDDCKN-TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGET 309
                         170       180
                  ....*....|....*....|....
gi 1215484311 715 PLHIAAGRGF-TKLAAVLKAAGAD 737
Cdd:PHA02876  310 PLYLMAKNGYdTENIRTLIMLGAD 333
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
582-737 1.67e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 582 AVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHqkaSSMIDLCNGEGLGAIHMVVMANSLSCLK 661
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH---ACNVHIRDANGNTALWNAISAKHHKIFR 608
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 662 LLIAAGvnvNAQEQKSGRTALHLAVEQENLPLAGCLLLEGdADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGAD 737
Cdd:PLN03192  609 ILYHFA---SISDPHAAGDLLCTAAKRNDLTAMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
644-698 3.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.71e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1215484311 644 GLGAIHMVVMANSLSCLKLLIAAGVNVNAQEqKSGRTALHLAVEQENLPLAGCLL 698
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
682-781 4.16e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 4.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 682 LHLAVEQENLPLAgCLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLkAAGADPHVENFeplfdveddvkddddegi 761
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN------------------ 60
                          90       100
                  ....*....|....*....|
gi 1215484311 762 vpGTTPLDMAASWEVYDILN 781
Cdd:pfam12796  61 --GRTALHYAARSGHLEIVK 78
PHA02875 PHA02875
ankyrin repeat protein; Provisional
554-738 4.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 554 NLLEVMPDVNYTNIINMRNDLyqTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKA 633
Cdd:PHA02875   16 DIARRLLDIGINPNFEIYDGI--SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 634 SSmiDLCNGEGLGAIHMVVMANSLSCLKLLIAAGVNVNAQEQKSgRTALHLAVEQENLPLAGcLLLEGDADVDSTTYDGT 713
Cdd:PHA02875   94 AD--DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDK-FSPLHLAVMMGDIKGIE-LLIDHKACLDIEDCCGC 169
                         170       180
                  ....*....|....*....|....*
gi 1215484311 714 TPLHIAAGRGFTKLAAVLKAAGADP 738
Cdd:PHA02875  170 TPLIIAMAKGDIAICKMLLDSGANI 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
608-664 1.38e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1215484311 608 GNSVLHLAAAEGDDKILSVFLKHQKassMIDLCNGEGLGAIHMVVMANSLSCLKLLI 664
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA---DINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
507-671 2.60e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 507 SALFDYAVSGDVR---MLLAAQRHLTAVQDDNGDNVLHLSIIHLHRELVKNLLEVMPDVNYTNIINMrndlyqTPLHLAV 583
Cdd:PHA02875   70 SELHDAVEEGDVKaveELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF------SPLHLAV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 584 ITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLkhqKASSMIDLCNGEG-LGAIHMVVMANSLSCLKL 662
Cdd:PHA02875  144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL---DSGANIDYFGKNGcVAALCYAIENNKIDIVRL 220

                  ....*....
gi 1215484311 663 LIAAGVNVN 671
Cdd:PHA02875  221 FIKRGADCN 229
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
808-881 4.31e-06

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: 45.80  E-value: 4.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 808 SKQQLYKLLEAPDPR-KNWSTLAEKLGLG----ILNNAFRLSPSPSKTLLDNYKIS-GGTVQELLAALRQMDHTEAIEVI 881
Cdd:cd08782     2 TRRKLARLLDPPDPMgRDWCLLAVNLGLTdlvaKLDSTSSPLPSPTDRLLQEWTARpPSTIGALLRKLRELGRRDAADFL 81
Ank_4 pfam13637
Ankyrin repeats (many copies);
678-731 5.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1215484311 678 GRTALHLAVEQENLPLAGcLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVL 731
Cdd:pfam13637   1 ELTALHAAAASGHLELLR-LLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
627-781 6.32e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.18  E-value: 6.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 627 FLKHQKASSMIDLCNGEGLGAIHMVVMANSLSCLKLLIAAGVNVNAQEQKSGRTALHLAVEQENLPLAGcLLLEGDADVD 706
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVAL-LLLAAGADIN 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215484311 707 STTYDGTTPLHIAAGRGFTKLAAVLKAAGADPHVENFEplfdveddvkddddegivpGTTPLDMAASWEVYDILN 781
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-------------------GETPLHLAAYNGNLEIVK 137
PHA03100 PHA03100
ankyrin repeat protein; Provisional
531-607 6.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 6.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215484311 531 VQDDNGDNVLHLSIIHLHRELVKNLLEVMPDVNYTNIINmrndlyQTPLHLAVITKQAEVVDDLLKAGANVNLLDRH 607
Cdd:PHA03100  187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG------DTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
507-733 1.25e-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: 49.31  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 507 SALFDYAVSG---DVRMLLAAQRHLTAVqddnGDNVLHLSIIHLHR---ELVKNLLEVMPDVNYTNIIN--MRNDLY--Q 576
Cdd:TIGR00870  54 SALFVAAIENenlELTELLLNLSCRGAV----GDTLLHAISLEYVDaveAILLHLLAAFRKSGPLELANdqYTSEFTpgI 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 577 TPLHLAVITKQAEVVDDLLKAGANVNlldrhgnsvlhlAAAEGDDkilsvFLKHQKASSmidLCNGEGLGAIHMVVmaNS 656
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVP------------ARACGDF-----FVKSQGVDS---FYHGESPLNAAACL--GS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 657 LSCLKLLIAAGVNVNAQEQKsGRTALHLAVEQ-----ENLPLA-GC--LLLEGDADVDSTT-------YDGTTPLHIAAG 721
Cdd:TIGR00870 188 PSIVALLSEDPADILTADSL-GNTLLHLLVMEnefkaEYEELScQMynFALSLLDKLRDSKelevilnHQGLTPLKLAAK 266
                         250
                  ....*....|..
gi 1215484311 722 RGFTKLAAVLKA 733
Cdd:TIGR00870 267 EGRIVLFRLKLA 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
680-738 1.27e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215484311 680 TALH-LAVEQENLPLAG-----CLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGADP 738
Cdd:PTZ00322   77 VVAHmLTVELCQLAASGdavgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
Ank_5 pfam13857
Ankyrin repeats (many copies);
563-615 1.28e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1215484311 563 NYTNIINMRNDLYQTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLA 615
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
563-722 1.96e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 563 NYTNIINMrndLYQTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAE----GDDKILSVFLKHQKASSMI- 637
Cdd:PHA02878   28 NYSTSASL---IPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVa 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 638 --DLCNGEGLGAIHMVVMAN---------------------SLSCLKLLIAAGVNVNAQEQKSGRTALHLAVEQENLPLA 694
Cdd:PHA02878  105 ikDAFNNRNVEIFKIILTNRykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLT 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 695 GCLLLEG--------------------------------DADVDSTTYDGTTPLHIAAGR 722
Cdd:PHA02878  185 ELLLSYGanvnipdktnnsplhhavkhynkpivhillenGASTDARDKCGNTPLHISVGY 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
582-731 2.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 582 AVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKASSMidlcNGEGLGA-IHMVVMANSLSCL 660
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV----KYPDIESeLHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215484311 661 KLLIAAGVNVNAQEQKSGRTALHLAVEQENLPLAGCLLLEGdADVDSTTYDGTTPLHIAAGRGFTKLAAVL 731
Cdd:PHA02875   85 EELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
577-628 2.95e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1215484311 577 TPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFL 628
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02741 PHA02741
hypothetical protein; Provisional
608-732 4.06e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.03  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 608 GNSVLHLAAAEGDDKIL---SVFLKHQKASSMIDLCNGEGLGAIHMVVMAN----SLSCLKLLIAAGVNVNAQEQKSGRT 680
Cdd:PHA02741   21 GENFFHEAARCGCFDIIarfTPFIRGDCHAAALNATDDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEMLEGDT 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1215484311 681 ALHLAVEQENLPLAGCLLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLK 732
Cdd:PHA02741  101 ALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILR 152
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
576-640 1.10e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215484311 576 QTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKASSMIDLC 640
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAN 180
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
536-661 1.25e-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: 45.90  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 536 GDNVLHLSIIHLHRELVKNLLEVMPDVN------YTNIINMRNDLY--QTPLHLAVITKQAEVVDDLL-KAGANVNLLDR 606
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNahakgvFFNPKYKHEGFYfgETPLALAACTNQPEIVQLLMeKESTDITSQDS 220
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215484311 607 HGNSVLHLAAAEGDD---------KILSVFLKHQKASSMIDLCNGEGLGAIHMVVMANSLSCLK 661
Cdd:cd22194   221 RGNTVLHALVTVAEDsktqndfvkRMYDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILK 284
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
47-121 2.46e-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: 2.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215484311  47 PYLQIIEQPKQRgFRFRYVCEGpSHGGLPGASSEknkkSYPQVKICNYVGPAKVIVQLVTNGKYVHLHAHSLVGK 121
Cdd:cd07927     1 YELRIEVQPEPH-HRARYETEG-SRGAVKAPSTG----GFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHR 69
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
576-606 2.82e-04

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: 39.19  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1215484311 576 QTPLHLAVI-TKQAEVVDDLLKAGANVNLLDR 606
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
536-723 3.20e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.49  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 536 GDNVLHLSIIHLHR---ELVKNLLEVMPDV-NYTNIIN--MRNDLY--QTPLHLAVITKQAEVVDDLLKAGANVNlldrh 607
Cdd:cd21882    26 GKTCLHKAALNLNDgvnEAIMLLLEAAPDSgNPKELVNapCTDEFYqgQTALHIAIENRNLNLVRLLVENGADVS----- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 608 gnsvlhlAAAEGDdkilsVFLKHQkassmidlCNGEGLGAIHMVVMA--NSLSCLKLLIAAGVNVNAQEQKS--GRTALH 683
Cdd:cd21882   101 -------ARATGR-----FFRKSP--------GNLFYFGELPLSLAActNQEEIVRLLLENGAQPAALEAQDslGNTVLH 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 684 LAVEQ-----ENLPLAgC----LLLEGDADVDST-------TYDGTTPLHIAAGRG 723
Cdd:cd21882   161 ALVLQadntpENSAFV-CqmynLLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEG 215
Ank_5 pfam13857
Ankyrin repeats (many copies);
663-719 4.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1215484311 663 LIAAG-VNVNAQEQKsGRTALHLAVEQENLPLAgCLLLEGDADVDSTTYDGTTPLHIA 719
Cdd:pfam13857   1 LLEHGpIDLNRLDGE-GYTPLHVAAKYGALEIV-RVLLAYGVDLNLKDEEGLTALDLA 56
Death_UNC5B cd08802
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ...
807-881 4.77e-04

Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). UNC5B is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5B signaling is involved in the netrin-1-induced proliferation and migration of renal proximal tubular cells. It is also required for vascular patterning during embryonic development, and its activation inhibits sprouting angiogenesis. UNC5 proteins 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: 176780  Cd Length: 84  Bit Score: 40.01  E-value: 4.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215484311 807 SSKQQLYKLLEAPDPRKN-WSTLAEKLGLGILNNAFRLSPSPSKTLLDNYKI---SGGTVQELLAALRQMDHTEAIEVI 881
Cdd:cd08802     4 SIRQKICNSLDAPNSRGNdWRLLAQKLSMDRYLNYFATKASPTGVILDLWEArhqDDGDLNSLASALEEMGKSEMLVVM 82
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
673-856 5.63e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 673 QEQKSGRTALHLAVEQENLPLAGC--LLLEGDADVDSTT-----------YDGTTPLHIAAGRGFTKLAAVLKAAGADPH 739
Cdd:cd21882    21 QRGATGKTCLHKAALNLNDGVNEAimLLLEAAPDSGNPKelvnapctdefYQGQTALHIAIENRNLNLVRLLVENGADVS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 740 VENFEPLFdveddvKDDDDEGIVPGTTPLDMAA---SWEVYDILNGKPYTAAAAVSEDLLtqgplrelnesSKQQLYKLL 816
Cdd:cd21882   101 ARATGRFF------RKSPGNLFYFGELPLSLAActnQEEIVRLLLENGAQPAALEAQDSL-----------GNTVLHALV 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1215484311 817 EAPDPRKNWSTLAEKLGLGILNNAFRLSPSPSKTLLDNYK 856
Cdd:cd21882   164 LQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQ 203
PHA02859 PHA02859
ankyrin repeat protein; Provisional
564-723 7.91e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 564 YTNIINMRNDLYQTPLHLAVITKQA--EVVDDLLKAGANVNLLDRHGN-SVLH--LAAAEG-DDKILSVFLkhqKASSMI 637
Cdd:PHA02859   40 WIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNlSALHhyLSFNKNvEPEILKILI---DSGSSI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 638 DLCNGEGLGAIHMvVMAN---SLSCLKLLIAAGVNVnAQEQKSGRTALH----LAVEQEnlpLAGCLLLEGdADVDSTTY 710
Cdd:PHA02859  117 TEEDEDGKNLLHM-YMCNfnvRINVIKLLIDSGVSF-LNKDFDNNNILYsyilFHSDKK---IFDFLTSLG-IDINETNK 190
                         170
                  ....*....|...
gi 1215484311 711 DGTTPLHIAAGRG 723
Cdd:PHA02859  191 SGYNCYDLIKFRN 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
577-603 9.42e-04

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: 37.57  E-value: 9.42e-04
                           10        20
                   ....*....|....*....|....*..
gi 1215484311  577 TPLHLAVITKQAEVVDDLLKAGANVNL 603
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
807-878 1.66e-03

Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). UNC5C is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5C plays a critical role in the development of spinal accessory motor neurons. Methylation of the UNC5C gene is associated with early stages of colorectal carcinogenesis. UNC5 proteins 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: 260064  Cd Length: 83  Bit Score: 38.45  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 807 SSKQQLYKLLEAPDPRKN-WSTLAEKLGLGILNNAFRLSPSPSKTLLDNYK---ISGGTVQELLAALRQMDHTEAI 878
Cdd:cd08799     4 SIRQKLCGSLDAPQTRGNdWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEaqhFPDGNLSRLAAVLEEMGRHETV 79
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
257-356 1.76e-03

IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes mainly involved in cell-cell-interaction.


Pssm-ID: 238583  Cd Length: 101  Bit Score: 38.62  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 257 IVRMDRTAGCVTGGEEIYLLCDKVQKDDiQIRFYEEDENG-GMWEGFGDFSPTDVHrQFAIVFKTPKYRDVNITKPASVF 335
Cdd:cd01178     4 IEKKSLNSCSVNGGEELFLTGKNFLKDS-KVVFQEKGQDGeAQWEAEATIDKEKSH-QNHLVVEVPPYHNKHVAAPVQVQ 81
                          90       100
                  ....*....|....*....|....
gi 1215484311 336 VQL---RRKSdletSEPKPFLYYP 356
Cdd:cd01178    82 FYVvngKRKR----SQPQTFTYTP 101
Death_IRAK cd08309
Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ...
801-881 2.21e-03

Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in Interleukin-1 (IL-1) Receptor-Associated Kinases (IRAK1-4) and similar proteins. IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. All four types are involved in signal transduction involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinase pathways. IRAK1 and IRAK4 are active kinases while IRAK2 and IRAK-M (also called IRAK3) are inactive. In general, IRAKs are expressed ubiquitously, except for IRAK-M which is detected only in macrophages. The insect homologs, Pelle and Tube, are important components of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in the innate immune response. Most members have an N-terminal DD followed by a kinase domain. 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: 260023  Cd Length: 88  Bit Score: 38.10  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 801 LRELNESSKQQLYKLLEAPDPrKNWSTLAEKlglgILNNAFRL---------SPSPSKTLLDNYKISGGTVQELLAALRQ 871
Cdd:cd08309     3 IRNLPPWVLKRLCKVLDALEL-AGWRQLASL----IPYDQTDVrqiesmkqrGQSPTRELLWDWGTQNATVQDLVQLLTQ 77
                          90
                  ....*....|
gi 1215484311 872 MDHTEAIEVI 881
Cdd:cd08309    78 LGLFRAADLI 87
PHA02946 PHA02946
ankyin-like protein; Provisional
569-722 2.72e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 569 NMRNDLYQTPLHLAVITKQAEVVDDLLKAGANVNLLDRHGNSVLHLAAAEGDDKILSVFLKHQKASSMIDLCNGEGLGAI 648
Cdd:PHA02946   66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLVQYGAKINNSVDEEGCGPL 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215484311 649 hMVVMANSLSCLKLLIAAGVNVNAQEqKSGRTALHLAVEQENlPLAGCL--LLEGDADVDSTTYDGTTPLHIAAGR 722
Cdd:PHA02946  146 -LACTDPSERVFKKIMSIGFEARIVD-KFGKNHIHRHLMSDN-PKASTIswMMKLGISPSKPDHDGNTPLHIVCSK 218
PHA03100 PHA03100
ankyrin repeat protein; Provisional
648-737 2.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215484311 648 IHMVVMANSLSCLKLLIAAGVNVNaQEQKSGRTALHL-----AVEQENLPLAgCLLLEGDADVDSTTYDGTTPLHIAAGR 722
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADIN-SSTKNNSTPLHYlsnikYNLTDVKEIV-KLLLEYGANVNAPDNNGITPLLYAISK 116
                          90
                  ....*....|....*..
gi 1215484311 723 GFTKLAAV--LKAAGAD 737
Cdd:PHA03100  117 KSNSYSIVeyLLDNGAN 133
Ank_5 pfam13857
Ankyrin repeats (many copies);
697-771 9.84e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 9.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215484311 697 LLLEGDADVDSTTYDGTTPLHIAAGRGFTKLAAVLKAAGADPHVENFEplfdveddvkddddegivpGTTPLDMA 771
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE-------------------GLTALDLA 56
 
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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