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Conserved domains on  [gi|117320527|ref|NP_002493|]
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nuclear factor NF-kappa-B p100 subunit isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
38-221 6.70e-122

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: 366.91  E-value: 6.70e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSR-PQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                        170       180
                 ....*....|....*....|....*
gi 117320527 197 FLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07934  161 YLRDSNGSYTLALKPVISDPIHDSK 185
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
228-327 3.63e-59

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: 196.77  E-value: 3.63e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 117320527 306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd01177   81 KIQLKRPSDGERSESVPFTYVP 102
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
774-849 6.42e-36

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: 130.33  E-value: 6.42e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117320527 774 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRG 849
Cdd:cd08798    1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
438-706 1.06e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 438 EMLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIeqivyVIHHAQDL 517
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLV-----ALLLLAAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 518 GVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPD 597
Cdd:COG0666   78 ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA--AYNGNLEIVKLLLEAGAD-----VNAQD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 598 FEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGgRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAG 677
Cdd:COG0666  151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG-ETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
                        250       260
                 ....*....|....*....|....*....
gi 117320527 678 LGYPTLTRLLLKAGADIHAENEEPLCPLP 706
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKDGLTALL 257
 
Name Accession Description Interval E-value
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
38-221 6.70e-122

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: 366.91  E-value: 6.70e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSR-PQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                        170       180
                 ....*....|....*....|....*
gi 117320527 197 FLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07934  161 YLRDSNGSYTLALKPVISDPIHDSK 185
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
40-220 3.91e-80

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: 256.08  E-value: 3.91e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527   40 LVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSElGI 119
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKD-GV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  120 CAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQrqrlrsrpqgLTEAEQReLEQEAKELKKVMDLSIVRLRFSAFLR 199
Cdd:pfam00554  80 CEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-VGFEALRQIKDMDLNVVRLCFQAFLP 148
                         170       180
                  ....*....|....*....|.
gi 117320527  200 ASDGSFSLPLKPVISQPIHDS 220
Cdd:pfam00554 149 DTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
228-327 3.63e-59

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: 196.77  E-value: 3.63e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 117320527 306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd01177   81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
229-328 1.77e-55

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: 186.61  E-value: 1.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  229 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 117320527  307 LQLKRKRGGDVSDSKQFTYYPL 328
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
774-849 6.42e-36

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: 130.33  E-value: 6.42e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117320527 774 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRG 849
Cdd:cd08798    1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
438-706 1.06e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 438 EMLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIeqivyVIHHAQDL 517
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLV-----ALLLLAAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 518 GVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPD 597
Cdd:COG0666   78 ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA--AYNGNLEIVKLLLEAGAD-----VNAQD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 598 FEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGgRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAG 677
Cdd:COG0666  151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG-ETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
                        250       260
                 ....*....|....*....|....*....
gi 117320527 678 LGYPTLTRLLLKAGADIHAENEEPLCPLP 706
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKDGLTALL 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
459-705 4.13e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 4.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 459 RALLDYGVTADARallagqrhlltaqDENGDTPLHLAIIHGQTsvIEQIVYVIHHAQDlgvVNLTNHLHQTPLH--LAVI 536
Cdd:PHA03095  67 RLLLEAGADVNAP-------------ERCGFTPLHLYLYNATT--LDVIKLLIKAGAD---VNAKDKVGRTPLHvyLSGF 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 537 TGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVH---LAVRARsP 613
Cdd:PHA03095 129 NINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLHhhlQSFKPR-A 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 614 ECLDLLVDSGAEVEATERqGGRTALHLATeMEELGLVTHLVTKLRAN--VNARTFAGNTPLHLAAGLGYPTLTRLLLKAG 691
Cdd:PHA03095 203 RIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
                        250
                 ....*....|....
gi 117320527 692 ADIHAENEEPLCPL 705
Cdd:PHA03095 281 ADINAVSSDGNTPL 294
IPT smart00429
ig-like, plexins, transcription factors;
227-326 2.19e-18

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 80.54  E-value: 2.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527   227 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 117320527   307 LQlkrkRGGDV-SDSKQFTYY 326
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
605-698 5.54e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 5.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  605 HLAVRARSPECLDLLVDSGAEVEATErQGGRTALHLATEMEELGLVTHLVTKLRANVNARtfaGNTPLHLAAGLGYPTLT 684
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 117320527  685 RLLLKAGADIHAEN 698
Cdd:pfam12796  78 KLLLEKGADINVKD 91
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
772-850 4.32e-11

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: 59.73  E-value: 4.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527   772 DTALQNLEQLLDGPeAQGSWAELAERLGLRSLV------DTYRQTTSPSGSLLRSYELAGG---DLAGLLEALSDMGLEE 842
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSEADidqirtEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 117320527   843 GVRLLRGP 850
Cdd:smart00005  81 AVELLRSE 88
Death pfam00531
Death domain;
776-848 7.76e-08

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 50.44  E-value: 7.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  776 QNLEQLLDGPEAQG-SWAELAERLGLRSL-VDT----YRQTTSPSGSLLRSYELAGG---DLAGLLEALSDMGLEEGVRL 846
Cdd:pfam00531   2 KQLDRLLDPPPPLGkDWRELARKLGLSENeIDEieseNPRLRSQTYELLRLWEQREGknaTVGTLLEALRKLGRRDAAEK 81

                  ..
gi 117320527  847 LR 848
Cdd:pfam00531  82 IQ 83
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
520-699 3.16e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.85  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  520 VNLTNHLHQTPLHLAVITGQT-SVVSFLLRVGADPALldrhGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPD- 597
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDq 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  598 -----FEGLYPVHLAVRARSPECLDLLVDSGAEVEAteRQGGRTALhlatEMEELGLVTHlvtklranvnartfaGNTPL 672
Cdd:TIGR00870 121 ytsefTPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFV----KSQGVDSFYH---------------GESPL 179
                         170       180
                  ....*....|....*....|....*..
gi 117320527  673 HLAAGLGYPTLTRLLLKAGADIHAENE 699
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADS 206
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
488-659 7.30e-05

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: 46.54  E-value: 7.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 488 GDTPLHLAIIHGQtsvIEQIVYVIHHAQDLGVVNLTNHLHQ--TPLHLAVITGQTSVVSFLLRVGADPA-------LLDR 558
Cdd:cd22192   51 GETALHVAALYDN---LEAAVVLMEAAPELVNEPMTSDLYQgeTALHIAVVNQNLNLVRELIARGADVVspratgtFFRP 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 559 HGDSAMH-----LALRAGAGAPELLRALLQSGAPAVPQllhmpDFEGLYPVHLAV----RARSPECLDLLVDSGAE---- 625
Cdd:cd22192  128 GPKNLIYygehpLSFAACVGNEEIVRLLIEHGADIRAQ-----DSLGNTVLHILVlqpnKTFACQMYDLILSYDKEddlq 202
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 117320527 626 -VEATERQGGRTALHLATEMEELGLVTHLVTKLRA 659
Cdd:cd22192  203 pLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRH 237
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
668-696 9.57e-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: 37.18  E-value: 9.57e-04
                           10        20
                   ....*....|....*....|....*....
gi 117320527   668 GNTPLHLAAGLGYPTLTRLLLKAGADIHA 696
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
38-221 6.70e-122

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: 366.91  E-value: 6.70e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSR-PQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                        170       180
                 ....*....|....*....|....*
gi 117320527 197 FLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07934  161 YLRDSNGSYTLALKPVISDPIHDSK 185
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
38-221 2.55e-117

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: 355.25  E-value: 2.55e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEl 117
Cdd:cd07883    1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCED- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRPQ--------------GLTEAEQRELEQEAKELKK 183
Cdd:cd07883   80 GICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPgdlvhvdaegggdrQLTDEEQAEIRQKAKQQAK 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 117320527 184 VMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07883  160 SMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
40-220 3.91e-80

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: 256.08  E-value: 3.91e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527   40 LVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSElGI 119
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKD-GV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  120 CAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQrqrlrsrpqgLTEAEQReLEQEAKELKKVMDLSIVRLRFSAFLR 199
Cdd:pfam00554  80 CEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-VGFEALRQIKDMDLNVVRLCFQAFLP 148
                         170       180
                  ....*....|....*....|.
gi 117320527  200 ASDGSFSLPLKPVISQPIHDS 220
Cdd:pfam00554 149 DTRGNFTTPLPPVVSNPIYDK 169
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
38-221 5.62e-80

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: 256.14  E-value: 5.62e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGK-QCSE 116
Cdd:cd07827    1 PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPHQLVGKtDCRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 117 lGICAVSVGPK-DMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRpqglteaeqreLEQEAKELKKVMDLSIVRLRFS 195
Cdd:cd07827   81 -GVCEVRLGPKnNMTASFNNLGIQCVRKKDVEEALGQRIQLGIDPFM-----------VHKGPEGNASDIDLNRVRLCFQ 148
                        170       180
                 ....*....|....*....|....*.
gi 117320527 196 AFLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07827  149 AFIEDSDGGFTLPLPPVLSNPIYDKK 174
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
38-221 1.83e-73

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: 239.80  E-value: 1.83e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCsEL 117
Cdd:cd07935    1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHC-ED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGT----MIQKLQR---------------QRLRSRPQGLTEAEQRELEQEA 178
Cdd:cd07935   80 GICTVTAGPKDMVVGFANLGILHVTKKKVFETlearMTEACKKgynpgllvhpelaylQAEGGGDRQLTEREKEIIRQAA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 117320527 179 KELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07935  160 VQQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
228-327 3.63e-59

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: 196.77  E-value: 3.63e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 117320527 306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd01177   81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
229-328 1.77e-55

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: 186.61  E-value: 1.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  229 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 117320527  307 LQLKRKRGGDVSDSKQFTYYPL 328
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
38-221 9.05e-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: 159.19  E-value: 9.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07887    1 PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPHNLVGKEGCKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIqklQRQRLRSRPqglteaeQRELEQEAKELKKVmDLSIVRLRFSAF 197
Cdd:cd07887   81 GVCTKKINPTEMRIVFQKLGIQCVKKKDVEESLK---LREEINVDP-------FRTGFDHKDQINSI-DLNVVRLCFQVF 149
                        170       180
                 ....*....|....*....|....
gi 117320527 198 LRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07887  150 LEDENGRFTVPLPPVVSDPIYDKK 173
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
228-327 1.05e-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: 156.29  E-value: 1.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYE--DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd00602    1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEkgPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79
                         90       100
                 ....*....|....*....|..
gi 117320527 306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd00602   80 PIQLVRPDDRKRSEPLTFTYTP 101
RHD-n_c-Rel cd07933
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ...
38-221 3.98e-42

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: 151.57  E-value: 3.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEl 117
Cdd:cd07933    1 PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPHDLVGKDCRD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRqrlRSRPQGLTEAEQRELEQeakelkkvMDLSIVRLRFSAF 197
Cdd:cd07933   80 GYYEAEFGPERRVLAFQNLGIQCVRRREVKEAIMLRISR---GINPFNVPEEQLLQIEE--------YDLNVVRLCFQIF 148
                        170       180
                 ....*....|....*....|....
gi 117320527 198 LRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07933  149 LPDEHGNYTTALPPIVSNPIYDNR 172
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
38-221 2.28e-40

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: 146.04  E-value: 2.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRgFRFRYGCE-GPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRA-HAHSLVGKQCs 115
Cdd:cd07884    1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQADDNRRKpHVHKLVGKQG- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 116 ELGICAVSVGPK----DMTAQFNNLGVLHVTKKNMMGTMIQklqrqrlrsrpqglteaeqreleqeakelKKVMDLSIVR 191
Cdd:cd07884   79 DDDVCDPHDIEVspegDYVAMFQNMGIIHTAKKNIPEELYK-----------------------------KKNMNLNQVV 129
                        170       180       190
                 ....*....|....*....|....*....|
gi 117320527 192 LRFSAFLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07884  130 LRFQAFAVSANGHLRPICPPVYSNPINNLK 159
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
38-221 1.21e-37

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: 138.46  E-value: 1.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEl 117
Cdd:cd07885    1 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPHELVGKDCKD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQrlrSRPQGLTEAEQREleqeakelkkVMDLSIVRLRFSAF 197
Cdd:cd07885   80 GYYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQRIQTN---NNPFNVPIEEQRA----------DYDLNAVRLCFQVT 146
                        170       180
                 ....*....|....*....|....
gi 117320527 198 LRASDGSFsLPLKPVISQPIHDSK 221
Cdd:cd07885  147 VRDPSGRL-LPLPPVLSQPIYDNR 169
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
774-849 6.42e-36

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: 130.33  E-value: 6.42e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117320527 774 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRG 849
Cdd:cd08798    1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
438-706 1.06e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 438 EMLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIeqivyVIHHAQDL 517
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLV-----ALLLLAAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 518 GVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPD 597
Cdd:COG0666   78 ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA--AYNGNLEIVKLLLEAGAD-----VNAQD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 598 FEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGgRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAG 677
Cdd:COG0666  151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG-ETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAE 228
                        250       260
                 ....*....|....*....|....*....
gi 117320527 678 LGYPTLTRLLLKAGADIHAENEEPLCPLP 706
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKDGLTALL 257
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
38-221 2.99e-33

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


Pssm-ID: 143646  Cd Length: 172  Bit Score: 126.13  E-value: 2.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVD--LVTHSDPPRAHAHSLVGKQCS 115
Cdd:cd07886    1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVTVTvcLVWKDPPHRVHPHGLVGKDCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 116 ElGICAVSVGPKDMTAQ-FNNLGVLHVTKKNMMGTMIQKLQrqrlrsrpQGLT--EAEQRELEQEakelkkvMDLSIVRL 192
Cdd:cd07886   81 N-GICQVTLNPHSSPRHsFSNLGIQCVRKREIEAAIETRLQ--------LNIDpfKAGSLKNHEE-------VDMNVVRL 144
                        170       180
                 ....*....|....*....|....*....
gi 117320527 193 RFSAFLRASDGsFSLPLKPVISQPIHDSK 221
Cdd:cd07886  145 CFQASYRDDDG-RKDCLSPVLSEPIYDKK 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
438-700 5.78e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.30  E-value: 5.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 438 EMLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVyvihhaqDL 517
Cdd:COG0666   37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL-------EA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 518 GV-VNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMP 596
Cdd:COG0666  110 GAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA--AANGNLEIVKLLLEAGAD-----VNAR 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 597 DFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQgGRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAA 676
Cdd:COG0666  183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAA 260
                        250       260
                 ....*....|....*....|....
gi 117320527 677 GLGYPTLTRLLLKAGADIHAENEE 700
Cdd:COG0666  261 AAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
507-705 2.94e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.80  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 507 IVYVIHHAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGA 586
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAA--ALAGDLLVALLLLAAGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 587 PavpqlLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGgRTALHLATEMEELGLVTHLVtKLRANVNARTF 666
Cdd:COG0666   79 D-----INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-ETPLHLAAYNGNLEIVKLLL-EAGADVNAQDN 151
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 117320527 667 AGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
774-848 1.33e-21

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: 89.22  E-value: 1.33e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117320527 774 ALQNLEQLLDGpeaQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLR 848
Cdd:cd08310    1 TRLRLCKLLDV---GKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
459-705 4.13e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 4.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 459 RALLDYGVTADARallagqrhlltaqDENGDTPLHLAIIHGQTsvIEQIVYVIHHAQDlgvVNLTNHLHQTPLH--LAVI 536
Cdd:PHA03095  67 RLLLEAGADVNAP-------------ERCGFTPLHLYLYNATT--LDVIKLLIKAGAD---VNAKDKVGRTPLHvyLSGF 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 537 TGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVH---LAVRARsP 613
Cdd:PHA03095 129 NINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLHhhlQSFKPR-A 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 614 ECLDLLVDSGAEVEATERqGGRTALHLATeMEELGLVTHLVTKLRAN--VNARTFAGNTPLHLAAGLGYPTLTRLLLKAG 691
Cdd:PHA03095 203 RIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
                        250
                 ....*....|....
gi 117320527 692 ADIHAENEEPLCPL 705
Cdd:PHA03095 281 ADINAVSSDGNTPL 294
IPT smart00429
ig-like, plexins, transcription factors;
227-326 2.19e-18

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 80.54  E-value: 2.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527   227 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 117320527   307 LQlkrkRGGDV-SDSKQFTYY 326
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
458-637 2.75e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.16  E-value: 2.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 458 ARALLDYGvtADarallagqrhlLTAQDENGDTPLHLAIIHGQTSVIEQIVyvihhaqDLGV-VNLTNHLHQTPLHLAVI 536
Cdd:COG0666  136 VKLLLEAG--AD-----------VNAQDNDGNTPLHLAAANGNLEIVKLLL-------EAGAdVNARDNDGETPLHLAAE 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 537 TGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPAVPQllhmpDFEGLYPVHLAVRARSPECL 616
Cdd:COG0666  196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLA--AENGNLEIVKLLLEAGADLNAK-----DKDGLTALLLAAAAGAALIV 268
                        170       180
                 ....*....|....*....|.
gi 117320527 617 DLLVDSGAEVEATERQGGRTA 637
Cdd:COG0666  269 KLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
605-698 5.54e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 5.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  605 HLAVRARSPECLDLLVDSGAEVEATErQGGRTALHLATEMEELGLVTHLVTKLRANVNARtfaGNTPLHLAAGLGYPTLT 684
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 117320527  685 RLLLKAGADIHAEN 698
Cdd:pfam12796  78 KLLLEKGADINVKD 91
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
228-327 2.86e-14

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: 69.03  E-value: 2.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKD-DIEVRFYeddengwqAFGDFSPTDVHkQYAIVFRTPPYHkmkIERPVTVF 306
Cdd:cd00102    1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFG--------GGVPCSVLSVS-STAIVCTTPPYA---NPGPGPVE 68
                         90       100
                 ....*....|....*....|.
gi 117320527 307 LQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd00102   69 VTVDRGNGGITSSPLTFTYVP 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
531-629 4.74e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  531 LHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPAVpqllhmpDFEGLYPVHLAVRA 610
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLA--AKNGHLEIVKLLLEHADVNL-------KDNGRTALHYAARS 71
                          90
                  ....*....|....*....
gi 117320527  611 RSPECLDLLVDSGAEVEAT 629
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVK 90
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
776-848 1.35e-11

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: 61.08  E-value: 1.35e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117320527 776 QNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLR 848
Cdd:cd08797    3 QQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIE 75
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
772-850 4.32e-11

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: 59.73  E-value: 4.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527   772 DTALQNLEQLLDGPeAQGSWAELAERLGLRSLV------DTYRQTTSPSGSLLRSYELAGG---DLAGLLEALSDMGLEE 842
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSEADidqirtEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 117320527   843 GVRLLRGP 850
Cdd:smart00005  81 AVELLRSE 88
PHA02878 PHA02878
ankyrin repeat protein; Provisional
539-707 6.60e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 6.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 539 QTSVVSFLLRVGADPALLDRH-GDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSPECLD 617
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYA--TENKDQRLTELLLSYGAN-----VNIPDKTNNSPLHHAVKHYNKPIVH 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 618 LLVDSGAEVEATERQGgRTALHLATEMEELGLVTHLVTKLRANVNAR-TFAGNTPLHLAagLGYPTLTRLLLKAGADIHA 696
Cdd:PHA02878 219 ILLENGASTDARDKCG-NTPLHISVGYCKDYDILKLLLEHGVDVNAKsYILGLTALHSS--IKSERKLKLLLEYGADINS 295
                        170
                 ....*....|.
gi 117320527 697 ENEEPLCPLPS 707
Cdd:PHA02878 296 LNSYKLTPLSS 306
PHA02878 PHA02878
ankyrin repeat protein; Provisional
523-675 9.19e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 9.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 523 TNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGapELLRALLQSGApavpQLLHMpDFEGLY 602
Cdd:PHA02878 164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNK--PIVHILLENGA----STDAR-DKCGNT 236
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117320527 603 PVHLAV-RARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEElglVTHLVTKLRANVNARTFAGNTPLHLA 675
Cdd:PHA02878 237 PLHISVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSER---KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
490-694 9.95e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 9.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 490 TPLHLA--IIHGQTSVIEqIVYVI--HHAQdlgvVNLTNHLHQTPLHLAVIT--GQTSVVSFLLRVGADPALLDRHGDSA 563
Cdd:PHA03100  70 TPLHYLsnIKYNLTDVKE-IVKLLleYGAN----VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 564 MHLALRAGAGAPELLRALLQSGapavpqllhmpdfeglypVHLAVRARspecLDLLVDSGAEVEAT-ERqgGRTALHLAT 642
Cdd:PHA03100 145 LHLYLESNKIDLKILKLLIDKG------------------VDINAKNR----VNYLLSYGVPINIKdVY--GFTPLHYAV 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 117320527 643 EMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADI 694
Cdd:PHA03100 201 YNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
473-557 3.05e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  473 LLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVyvihhaqDLGVVNLTNHlHQTPLHLAVITGQTSVVSFLLRVGAD 552
Cdd:pfam12796  15 LLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-------EHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD 86

                  ....*
gi 117320527  553 PALLD 557
Cdd:pfam12796  87 INVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
485-705 6.30e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 6.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 485 DENGDTPLHLAIihgQTSVIEQIV-YVIHHAQDlgvVNLTNHLHQTPLHLAVITG-QTSVVSFLLRVGADPALLDRHGDS 562
Cdd:PHA02876 270 DDCKNTPLHHAS---QAPSLSRLVpKLLERGAD---VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYIT 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 563 AMHLALRAGAGApELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGrTALHLAT 642
Cdd:PHA02876 344 PLHQASTLDRNK-DIVITLLELGAN-----VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFAL 416
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117320527 643 EMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLG-YPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:PHA02876 417 CGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02874 PHA02874
ankyrin repeat protein; Provisional
480-694 8.75e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 8.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 480 LLTAQDENGDTPLHLAIIHG-QTSVI------EQIVYVIhhaQDLGV-VNLTNHLHQTPLHLAVITGQTSVVSFLLRVGA 551
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNGvDTSILpipcieKDMIKTI---LDCGIdVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 552 DPALLDRHGDSAMHLALRAGAGapELLRALLQSGApavpqLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVeATER 631
Cdd:PHA02874 149 DVNIEDDNGCYPIHIAIKHNFF--DIIKLLLEKGA-----YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKC 220
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117320527 632 QGGRTALHLATeMEELGLVTHLVTKlrANVNARTFAGNTPLHLAagLGYPT---LTRLLLKAGADI 694
Cdd:PHA02874 221 KNGFTPLHNAI-IHNRSAIELLINN--ASINDQDIDGSTPLHHA--INPPCdidIIDILLYHKADI 281
PHA02875 PHA02875
ankyrin repeat protein; Provisional
526-739 8.38e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 8.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 526 LHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALR----------------AGAGAP----ELLRALLQSG 585
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKfrdseaikllmkhgaiPDVKYPdiesELHDAVEEGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 586 APAVPQLLHMPDF-------EGLYPVHLAVRARSPECLDLLVDSGAE--VEATERQggrTALHLATEMEELGLvTHLVTK 656
Cdd:PHA02875  81 VKAVEELLDLGKFaddvfykDGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKF---SPLHLAVMMGDIKG-IELLID 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 657 LRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSD------SEGPEKDTRSSFRG 730
Cdd:PHA02875 157 HKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDivrlfiKRGADCNIMFMIEG 236
                        250
                 ....*....|.
gi 117320527 731 --HTPLDLTCS 739
Cdd:PHA02875 237 eeCTILDMICN 247
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
230-327 2.53e-08

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: 52.49  E-value: 2.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 230 ISRMDKTAGSVRGGDEVYLLCDKVQKDDiEVRFYE---DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:cd01178    4 IEKKSLNSCSVNGGEELFLTGKNFLKDS-KVVFQEkgqDGEAQWEAEATIDKEKSH-QNHLVVEVPPYHNKHVAAPVQVQ 81
                         90       100
                 ....*....|....*....|....
gi 117320527 307 LQL---KRKRggdvSDSKQFTYYP 327
Cdd:cd01178   82 FYVvngKRKR----SQPQTFTYTP 101
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
38-139 2.91e-08

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: 53.82  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  38 PYLVIVEQPKQRgFRFRY---GCEGPSHGGLPGassekgrkTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGK-- 112
Cdd:cd07927    1 YELRIEVQPEPH-HRARYeteGSRGAVKAPSTG--------GFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHRit 71
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 117320527 113 -----QCSELGICAVSV------GPKDMTAQFNNLGVL 139
Cdd:cd07927   72 gktttPCKEKIIGNTKVleiplePKNNMTATIDCAGIL 109
PHA03100 PHA03100
ankyrin repeat protein; Provisional
508-699 5.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 5.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 508 VYVIHHAQDLGVVNLTNHLHQT-PLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGA---PELLRALLQ 583
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVlPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvKEIVKLLLE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 584 SGApavpqLLHMPDFEGLYPVHLAV--RARSPECLDLLVDSGAEVEATERQGGrTALHLATE-------MEELgLVTH-- 652
Cdd:PHA03100  95 YGA-----NVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLEsnkidlkILKL-LIDKgv 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 117320527 653 ---------LVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENE 699
Cdd:PHA03100 168 dinaknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
Death pfam00531
Death domain;
776-848 7.76e-08

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 50.44  E-value: 7.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  776 QNLEQLLDGPEAQG-SWAELAERLGLRSL-VDT----YRQTTSPSGSLLRSYELAGG---DLAGLLEALSDMGLEEGVRL 846
Cdd:pfam00531   2 KQLDRLLDPPPPLGkDWRELARKLGLSENeIDEieseNPRLRSQTYELLRLWEQREGknaTVGTLLEALRKLGRRDAAEK 81

                  ..
gi 117320527  847 LR 848
Cdd:pfam00531  82 IQ 83
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
528-601 1.17e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 528 QTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGapELLRALL-------QSGAPAVPQ--------- 591
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR--EVVQLLSrhsqchfELGANAKPDsftgkppsl 193
                         90
                 ....*....|....*
gi 117320527 592 -----LLHMPDFEGL 601
Cdd:PTZ00322 194 edspiSSHHPDFSAV 208
PHA03095 PHA03095
ankyrin-like protein; Provisional
482-569 1.32e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 482 TAQDENGDTPLHLAIIHGQTSVIEQIVYVIHHAQdlgvVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGD 561
Cdd:PHA03095 216 AATDMLGNTPLHSMATGSSCKRSLVLPLLIAGIS----INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291

                 ....*...
gi 117320527 562 SAMHLALR 569
Cdd:PHA03095 292 TPLSLMVR 299
PHA02875 PHA02875
ankyrin repeat protein; Provisional
489-656 1.47e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 489 DTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNltnhlHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAL 568
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKD-----GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 569 RagAGAPELLRALLQSGApavpqLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELG 648
Cdd:PHA02875 144 M--MGDIKGIELLIDHKA-----CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKID 216

                 ....*...
gi 117320527 649 LVTHLVTK 656
Cdd:PHA02875 217 IVRLFIKR 224
PHA02876 PHA02876
ankyrin repeat protein; Provisional
427-632 6.30e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 6.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 427 SRTPQCEPQAPEMLQRAREYNAR-------LFGLAQ-----RSARALLDYGvtADarallagqrhlLTAQDENGDTPLHl 494
Cdd:PHA02876 281 SQAPSLSRLVPKLLERGADVNAKnikgetpLYLMAKngydtENIRTLIMLG--AD-----------VNAADRLYITPLH- 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 495 aiihgQTSVIEQIVYVIHHAQDLGV-VNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALrAGAG 573
Cdd:PHA02876 347 -----QASTLDRNKDIVITLLELGAnVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL-CGTN 420
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 574 APELLRALLQSGAPAVPQLLHMPDfeglyPVHLAVRAR-SPECLDLLVDSGAEVEATERQ 632
Cdd:PHA02876 421 PYMSVKTLIDRGANVNSKNKDLST-----PLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475
PHA02874 PHA02874
ankyrin repeat protein; Provisional
492-702 6.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 492 LHLAIIHGQTSVIEQIVyvihhAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAG 571
Cdd:PHA02874   5 LRMCIYSGDIEAIEKII-----KNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 572 AGapELLRALLQSGAPAvpQLLHMPDFEGlypvhlavrarspECLDLLVDSGAEVEATERQGgRTALHLATEMEELGLVT 651
Cdd:PHA02874  80 AH--DIIKLLIDNGVDT--SILPIPCIEK-------------DMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIK 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 117320527 652 HLVtKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAEN---EEPL 702
Cdd:PHA02874 142 MLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDnngESPL 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
490-705 1.59e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 490 TPLHLAIIHGQTSVIEqivYVIHHAQDLGVVNlTNHLHqtPLHLAVITGQTSVVSFLLRVGADPALL------------- 556
Cdd:PHA02874  37 TPLIDAIRSGDAKIVE---LFIKHGADINHIN-TKIPH--PLLTAIKIGAHDIIKLLIDNGVDTSILpipciekdmikti 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 557 ----------DRHGDSAMHLALRAGAgaPELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAev 626
Cdd:PHA02874 111 ldcgidvnikDAELKTFLHYAIKKGD--LESIKMLFEYGAD-----VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA-- 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117320527 627 eaterqggrtalhlatemeelglvthlvtklRANVNarTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:PHA02874 182 -------------------------------YANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
556-750 2.79e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 556 LDRHGDSAMHLALRAgagaPELLR---ALLQSGAPavpqlLHMPDFEGLYPVHL-AVRARSPECLDLLVDSGAEVEATER 631
Cdd:PHA02876 269 IDDCKNTPLHHASQA----PSLSRlvpKLLERGAD-----VNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADR 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 632 QGgRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEE-------PLCP 704
Cdd:PHA02876 340 LY-ITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKigtalhfALCG 418
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 117320527 705 lPSPPTSDSDSDSEGPEKDTRSSFRGhTPLDLTCSTK-----VKTLLLNAA 750
Cdd:PHA02876 419 -TNPYMSVKTLIDRGANVNSKNKDLS-TPLHYACKKNckldvIEMLLDNGA 467
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
520-699 3.16e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.85  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  520 VNLTNHLHQTPLHLAVITGQT-SVVSFLLRVGADPALldrhGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPD- 597
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDq 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  598 -----FEGLYPVHLAVRARSPECLDLLVDSGAEVEAteRQGGRTALhlatEMEELGLVTHlvtklranvnartfaGNTPL 672
Cdd:TIGR00870 121 ytsefTPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFV----KSQGVDSFYH---------------GESPL 179
                         170       180
                  ....*....|....*....|....*..
gi 117320527  673 HLAAGLGYPTLTRLLLKAGADIHAENE 699
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADS 206
PHA02878 PHA02878
ankyrin repeat protein; Provisional
491-759 4.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 491 PLHLAIIHGQTSVIEQIVYVIHHaqdlgvVNLTNHLHQTPLHLAVITGQTSVVSFLLRVgadpalldrHGDSAMHLALRA 570
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHN------VNQPDHRDLTPLHIICKEPNKLGMKEMIRS---------INKCSVFYTLVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 571 gagapelLRALLQSGAPAVPQLLHMPDFEGLYPVHLA-VRARS------PECLDLLVDSGAEVEATERQGGRTALHLATE 643
Cdd:PHA02878 105 -------IKDAFNNRNVEIFKIILTNRYKNIQTIDLVyIDKKSkddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 644 MEELGLVTHLVTKlRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSD------S 717
Cdd:PHA02878 178 NKDQRLTELLLSY-GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDilklllE 256
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 117320527 718 EGPEKDTRSSFRGHTPLDLTCSTKVKTLLL-------NAAQNTMEPPLT 759
Cdd:PHA02878 257 HGVDVNAKSYILGLTALHSSIKSERKLKLLleygadiNSLNSYKLTPLS 305
PHA02743 PHA02743
Viral ankyrin protein; Provisional
592-675 6.90e-06

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 47.12  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 592 LLHMPDFEGLYPVHLAV---RARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAG 668
Cdd:PHA02743  49 LLHRYDHHGRQCTHMVAwydRANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQH 128

                 ....*..
gi 117320527 669 NTPLHLA 675
Cdd:PHA02743 129 ETAYHIA 135
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
668-699 8.45e-06

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: 43.05  E-value: 8.45e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 117320527  668 GNTPLHLAAG-LGYPTLTRLLLKAGADIHAENE 699
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
485-628 1.48e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 485 DEN-GDTPLHLAIIHGQTSVIEqivYVIHHAQDLGVVNLTNhlhQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSA 563
Cdd:PHA02878 164 DRHkGNTALHYATENKDQRLTE---LLLSYGANVNIPDKTN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117320527 564 MHLALrAGAGAPELLRALLQSGAPAVPQllhmPDFEGLYPVHLAVraRSPECLDLLVDSGAEVEA 628
Cdd:PHA02878 238 LHISV-GYCKDYDILKLLLEHGVDVNAK----SYILGLTALHSSI--KSERKLKLLLEYGADINS 295
Ank_5 pfam13857
Ankyrin repeats (many copies);
653-705 2.34e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 117320527  653 LVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
488-688 3.47e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  488 GDTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNLTNHLH-------QTPLHLAVITGQTSVVSFLLRVGAD-PA----- 554
Cdd:TIGR00870  82 GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYtseftpgITALHLAAHRQNYEIVKLLLERGASvPAracgd 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  555 --LLDRHGDSAMH----LALRAGAGAPELLRALLQSGAPAVPQ------LLHM----PDFEGLYpvhlavRARSPECLDL 618
Cdd:TIGR00870 162 ffVKSQGVDSFYHgespLNAAACLGSPSIVALLSEDPADILTAdslgntLLHLlvmeNEFKAEY------EELSCQMYNF 235
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  619 LVDSGAeveaterqggrtalHLATEMEelglvthlvtkLRANVNartFAGNTPLHLAAGLGYPTLTRLLL 688
Cdd:TIGR00870 236 ALSLLD--------------KLRDSKE-----------LEVILN---HQGLTPLKLAAKEGRIVLFRLKL 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
488-547 4.66e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527  488 GDTPLHLAIIHGQTSVIEqivYVIHHAQDlgvVNLTNHLHQTPLHLAVITGQTSVVSFLL 547
Cdd:pfam13637   1 ELTALHAAAASGHLELLR---LLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
488-659 7.30e-05

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: 46.54  E-value: 7.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 488 GDTPLHLAIIHGQtsvIEQIVYVIHHAQDLGVVNLTNHLHQ--TPLHLAVITGQTSVVSFLLRVGADPA-------LLDR 558
Cdd:cd22192   51 GETALHVAALYDN---LEAAVVLMEAAPELVNEPMTSDLYQgeTALHIAVVNQNLNLVRELIARGADVVspratgtFFRP 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 559 HGDSAMH-----LALRAGAGAPELLRALLQSGAPAVPQllhmpDFEGLYPVHLAV----RARSPECLDLLVDSGAE---- 625
Cdd:cd22192  128 GPKNLIYygehpLSFAACVGNEEIVRLLIEHGADIRAQ-----DSLGNTVLHILVlqpnKTFACQMYDLILSYDKEddlq 202
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 117320527 626 -VEATERQGGRTALHLATEMEELGLVTHLVTKLRA 659
Cdd:cd22192  203 pLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRH 237
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
534-742 8.99e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 8.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 534 AVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSP 613
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIA--ASKGYEDCVLVLLKHACN-----VHIRDANGNTALWNAISAKHH 604
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 614 ECLDLLVDSGAeveATERQGGRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGAD 693
Cdd:PLN03192 605 KIFRILYHFAS---ISDPHAAGDLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117320527 694 I-HAENEEPLCPL---------------PSPPTSDSDSDSEGPEKDTRSSFRGHTPLDLTCSTKV 742
Cdd:PLN03192 681 VdKANTDDDFSPTelrellqkrelghsiTIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRV 745
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
529-697 1.00e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 529 TPLHLAVITGQTSVVSFLLRV-GADPALLDRHGDSAMHLAlrAGAGAPELLRALLQsgapAVPQLLHMPD----FEGLYP 603
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVA--ALYDNLEAAVVLME----AAPELVNEPMtsdlYQGETA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 604 VHLAVRARSPECLDLLVDSGAEVeATERQGGrtalhlatemeelglvthlvTKLRANVNARTFAGNTPLHLAAGLGYPTL 683
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGADV-VSPRATG--------------------TFFRPGPKNLIYYGEHPLSFAACVGNEEI 151
                        170
                 ....*....|....
gi 117320527 684 TRLLLKAGADIHAE 697
Cdd:cd22192  152 VRLLIEHGADIRAQ 165
Ank_5 pfam13857
Ankyrin repeats (many copies);
513-567 1.00e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 117320527  513 HAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLA 567
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-582 2.20e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 117320527  529 TPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRagAGAPELLRALL 582
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS--NGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
668-696 2.59e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 2.59e-04
                          10        20
                  ....*....|....*....|....*....
gi 117320527  668 GNTPLHLAAGLGYPTLTRLLLKAGADIHA 696
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
528-558 5.88e-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: 38.04  E-value: 5.88e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 117320527  528 QTPLHLAVI-TGQTSVVSFLLRVGADPALLDR 558
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
615-696 6.46e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.59  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 615 CLDLLVDSGAEVEATErqgGRTALHLATEMEELGLVTHLVTKlRANVNART--------------FAGNTPLHLAAGLGY 680
Cdd:cd22194  125 ILDRFINAEYTEEAYE---GQTALNIAIERRQGDIVKLLIAK-GADVNAHAkgvffnpkykhegfYFGETPLALAACTNQ 200
                         90
                 ....*....|....*.
gi 117320527 681 PTLTRLLLKAGADIHA 696
Cdd:cd22194  201 PEIVQLLMEKESTDIT 216
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
776-844 8.22e-04

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: 39.22  E-value: 8.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117320527 776 QNLEQLLDGPEAQGS-WAELAERLGLRSLVDTYRQTTSPSGSLLRSYE---LAGGDLAGLLEALSDMGLEEGV 844
Cdd:cd08799    7 QKLCGSLDAPQTRGNdWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEaqhFPDGNLSRLAAVLEEMGRHETV 79
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
530-609 9.24e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.92  E-value: 9.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 530 PLHLAVITGQTSVVSFLLRVGADPALL---DRHGDSAMHLALRAGAGAPE-------LLRALLQSGAPAVP--QLLHMPD 597
Cdd:cd22197  143 PLSLAACTKQWDVVNYLLENPHQPASLqaqDSLGNTVLHALVMIADNSPEnsalvikMYDGLLQAGARLCPtvQLEEISN 222
                         90
                 ....*....|..
gi 117320527 598 FEGLYPVHLAVR 609
Cdd:cd22197  223 HEGLTPLKLAAK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
560-620 9.46e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 9.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117320527  560 GDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSPECLDLLV 620
Cdd:pfam13637   1 ELTALHAA--AASGHLELLRLLLEKGAD-----INAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
668-696 9.57e-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: 37.18  E-value: 9.57e-04
                           10        20
                   ....*....|....*....|....*....
gi 117320527   668 GNTPLHLAAGLGYPTLTRLLLKAGADIHA 696
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
521-705 1.16e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 521 NLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGApavpQLLHMPDFEG 600
Cdd:PHA02946  66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLVQYGA----KINNSVDEEG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 601 LYPVhLAVRARSPECLDLLVDSGAEVEATERQG-GRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLG 679
Cdd:PHA02946 142 CGPL-LACTDPSERVFKKIMSIGFEARIVDKFGkNHIHRHLMSDNPKASTISWMM-KLGISPSKPDHDGNTPLHIVCSKT 219
                        170       180
                 ....*....|....*....|....*..
gi 117320527 680 YPTLTRL-LLKAGADIHAENEEPLCPL 705
Cdd:PHA02946 220 VKNVDIInLLLPSTDVNKQNKFGDSPL 246
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
634-696 1.20e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.56  E-value: 1.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117320527 634 GRTALHLATEMEELGLVTHLVTKlRANVNART-------------FAGNTPLHLAAGLGYPTLTRLLLKAGADIHA 696
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVEN-GADVSARAtgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPAA 147
PHA03100 PHA03100
ankyrin repeat protein; Provisional
461-552 1.24e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 461 LLDYGVTADARallagqrhlltaqDENGDTPLHLAIIHgqtSVIEQIVYVIHHAQDLGVVNLTNHlhqTPLHLAVITGQT 540
Cdd:PHA03100 178 LLSYGVPINIK-------------DVYGFTPLHYAVYN---NNPEFVKYLLDLGANPNLVNKYGD---TPLHIAILNNNK 238
                         90
                 ....*....|..
gi 117320527 541 SVVSFLLRVGAD 552
Cdd:PHA03100 239 EIFKLLLNNGPS 250
Death_UNC5B cd08802
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ...
782-842 1.88e-03

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: 38.08  E-value: 1.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117320527 782 LDGPEAQGS-WAELAERLGLRSLVDTYRQTTSPSGSLLRSYEL---AGGDLAGLLEALSDMGLEE 842
Cdd:cd08802   13 LDAPNSRGNdWRLLAQKLSMDRYLNYFATKASPTGVILDLWEArhqDDGDLNSLASALEEMGKSE 77
PHA02875 PHA02875
ankyrin repeat protein; Provisional
486-625 2.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 486 ENGDTPLHLAIIhgqTSVIEQIVYVIHHAQDLGVVNLTNHlhqTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMH 565
Cdd:PHA02875 100 KDGMTPLHLATI---LKKLDIMKLLIARGADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117320527 566 LALraGAGAPELLRALLQSGAPavpqllhmPDFEGLYP----VHLAVRARSPECLDLLVDSGAE 625
Cdd:PHA02875 174 IAM--AKGDIAICKMLLDSGAN--------IDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
659-705 2.38e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 2.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 117320527 659 ANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
PHA02736 PHA02736
Viral ankyrin protein; Provisional
604-692 3.16e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320527 604 VHLAVR---ARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGY 680
Cdd:PHA02736  59 VHIVSNpdkADPQEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHD 138
                         90
                 ....*....|..
gi 117320527 681 PTLTRLLLKAGA 692
Cdd:PHA02736 139 AKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
529-553 6.45e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 6.45e-03
                           10        20
                   ....*....|....*....|....*
gi 117320527   529 TPLHLAVITGQTSVVSFLLRVGADP 553
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
527-553 6.58e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 6.58e-03
                          10        20
                  ....*....|....*....|....*..
gi 117320527  527 HQTPLHLAVITGQTSVVSFLLRVGADP 553
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
 
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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