NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|569006534|ref|XP_006526806|]
View 

nuclear factor NF-kappa-B p100 subunit isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
38-221 9.35e-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: 366.53  E-value: 9.35e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 118 GVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSK-PQGLTEAERRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                        170       180
                 ....*....|....*....|....*
gi 569006534 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 3.66e-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: 3.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 569006534 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 6.69e-33

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: 121.47  E-value: 6.69e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006534 774 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLLKG 849
Cdd:cd08798    1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
453-706 4.54e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 4.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 453 LAQRSARALLDYGVTADARALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQIAHviyhaqYLGVINLTNHLHQTPLH 532
Cdd:COG0666   19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA------AGADINAKDDGGNTLLH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 533 LAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARS 612
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG--NLEIVKLLLEAGAD-----VNAQDNDGNTPLHLAAANGN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 613 PECLDLLVDCGAEVEAPERQgGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGA 692
Cdd:COG0666  166 LEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        250
                 ....*....|....
gi 569006534 693 DIHAENEEPLCPLP 706
Cdd:COG0666  244 DLNAKDKDGLTALL 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 9.35e-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: 366.53  E-value: 9.35e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 118 GVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSK-PQGLTEAERRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                        170       180
                 ....*....|....*....|....*
gi 569006534 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 1.61e-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: 257.23  E-value: 1.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534   40 LVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSElGV 119
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKD-GV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  120 CAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQrqrlrskpqgLTEAERReLEQEAKELKKVMDLSIVRLRFSAFLR 199
Cdd:pfam00554  80 CEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-VGFEALRQIKDMDLNVVRLCFQAFLP 148
                         170       180
                  ....*....|....*....|.
gi 569006534  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 3.66e-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: 3.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 569006534 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 1.78e-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: 1.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  229 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 569006534  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 6.69e-33

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: 121.47  E-value: 6.69e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006534 774 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLLKG 849
Cdd:cd08798    1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
453-706 4.54e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 4.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 453 LAQRSARALLDYGVTADARALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQIAHviyhaqYLGVINLTNHLHQTPLH 532
Cdd:COG0666   19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA------AGADINAKDDGGNTLLH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 533 LAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARS 612
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG--NLEIVKLLLEAGAD-----VNAQDNDGNTPLHLAAANGN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 613 PECLDLLVDCGAEVEAPERQgGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGA 692
Cdd:COG0666  166 LEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        250
                 ....*....|....
gi 569006534 693 DIHAENEEPLCPLP 706
Cdd:COG0666  244 DLNAKDKDGLTALL 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
459-705 7.12e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 7.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 459 RALLDYGVTADARallagqrhllmaqDENGDTPLHLAIIHGQTgvIEQIAHVIYHaqylGV-INLTNHLHQTPLH--LAV 535
Cdd:PHA03095  67 RLLLEAGADVNAP-------------ERCGFTPLHLYLYNATT--LDVIKLLIKA----GAdVNAKDKVGRTPLHvyLSG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 536 ITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAAPELLQALLRSGAHavpqiLHMPDFEGLYPVHlaVHARS--- 612
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLH--HHLQSfkp 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 613 -PECLDLLVDCGAEVEAPERqGGRTALHLATeMEELGLVTHLVTKLHAN--VNARTFAGNTPLHLAAGLGSPTLTRLLLK 689
Cdd:PHA03095 201 rARIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIA 278
                        250
                 ....*....|....*.
gi 569006534 690 AGADIHAENEEPLCPL 705
Cdd:PHA03095 279 LGADINAVSSDGNTPL 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 569006534   227 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 569006534   307 LQlkrkRGGDV-SDSKQFTYY 326
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
605-698 1.65e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  605 HLAVHARSPECLDLLVDCGAEVEApERQGGRTALHLATEMEELGLVTHLVTklHANVNARTFaGNTPLHLAAGLGSPTLT 684
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDN-GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 569006534  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 5.46e-10

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: 56.65  E-value: 5.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534   772 DAALQNLEQLLDGPeAQGSWAELAERLGLRSLV------DTYRKTPSPSGSLLRSYKLAGG---DLVGLLEALSDMGLHE 842
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSEADidqirtEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 569006534   843 GVRLLKGP 850
Cdd:smart00005  81 AVELLRSE 88
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
520-699 8.40e-08

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: 56.24  E-value: 8.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  520 INLTNHLHQTPLHLAVITGQTR-VVSFLLQVGADPTLldrhGDSALHLA-LRAGAAAPELLQALLRSGAHAVPQILhMPD 597
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAIsLEYVDAVEAILLHLLAAFRKSGPLEL-AND 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  598 ------FEGLYPVHLAVHARSPECLDLLVDCGAEVEApeRQGGRTALhlatEMEELGLVTHlvtklhanvnartfaGNTP 671
Cdd:TIGR00870 120 qytsefTPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFV----KSQGVDSFYH---------------GESP 178
                         170       180
                  ....*....|....*....|....*...
gi 569006534  672 LHLAAGLGSPTLTRLLLKAGADIHAENE 699
Cdd:TIGR00870 179 LNAAACLGSPSIVALLSEDPADILTADS 206
Death pfam00531
Death domain;
776-848 4.34e-07

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 48.52  E-value: 4.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  776 QNLEQLLDGPEAQG-SWAELAERLGLRSL-VDT----YRKTPSPSGSLLRSYKLAGG---DLVGLLEALSDMGLHEGVRL 846
Cdd:pfam00531   2 KQLDRLLDPPPPLGkDWRELARKLGLSENeIDEieseNPRLRSQTYELLRLWEQREGknaTVGTLLEALRKLGRRDAAEK 81

                  ..
gi 569006534  847 LK 848
Cdd:pfam00531  82 IQ 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
514-737 7.81e-07

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: 52.71  E-value: 7.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 514 AQYLGVINL--TNHLHQTPLHLAVITGQTRVVSFLL-QVGADPTLLDRHGDSALHLALRAGAAapELLQALLRsgahAVP 590
Cdd:cd22192    2 AQMLDELHLlqQKRISESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNL--EAAVVLME----AAP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 591 QILHMPDFEGLYPvhlavharspecldllvdcgaeveaperqgGRTALHLATEMEELGLVTHLVTKLHANVNART----- 665
Cdd:cd22192   76 ELVNEPMTSDLYQ------------------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtff 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 666 --------FAGNTPLHLAAGLGSPTLTRLLLKAGADIHAE---------------NEEPLCPLPSPSTSgSDSDSEGPER 722
Cdd:cd22192  126 rpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQdslgntvlhilvlqpNKTFACQMYDLILS-YDKEDDLQPL 204
                        250
                 ....*....|....*
gi 569006534 723 DTQRNFRGHTPLDLT 737
Cdd:cd22192  205 DLVPNNQGLTPFKLA 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
668-696 9.86e-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: 9.86e-04
                           10        20
                   ....*....|....*....|....*....
gi 569006534   668 GNTPLHLAAGLGSPTLTRLLLKAGADIHA 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 9.35e-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: 366.53  E-value: 9.35e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 118 GVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSK-PQGLTEAERRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                        170       180
                 ....*....|....*....|....*
gi 569006534 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 3.15e-116

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: 352.55  E-value: 3.15e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEl 117
Cdd:cd07883    1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCED- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 118 GVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSKPQ--------------GLTEAERRELEQEAKELKK 183
Cdd:cd07883   80 GICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPgdlvhvdaegggdrQLTDEEQAEIRQKAKQQAK 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 569006534 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 1.61e-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: 257.23  E-value: 1.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534   40 LVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSElGV 119
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKD-GV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  120 CAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQrqrlrskpqgLTEAERReLEQEAKELKKVMDLSIVRLRFSAFLR 199
Cdd:pfam00554  80 CEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-VGFEALRQIKDMDLNVVRLCFQAFLP 148
                         170       180
                  ....*....|....*....|.
gi 569006534  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 4.21e-79

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: 253.83  E-value: 4.21e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGK-QCSE 116
Cdd:cd07827    1 PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPHQLVGKtDCRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 117 lGVCAVSVGPK-DMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSKpqglteaerreLEQEAKELKKVMDLSIVRLRFS 195
Cdd:cd07827   81 -GVCEVRLGPKnNMTASFNNLGIQCVRKKDVEEALGQRIQLGIDPFM-----------VHKGPEGNASDIDLNRVRLCFQ 148
                        170       180
                 ....*....|....*....|....*.
gi 569006534 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 1.64e-74

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: 242.49  E-value: 1.64e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCsEL 117
Cdd:cd07935    1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHC-ED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 118 GVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEI----MIQKLQR---------------QRLRSKPQGLTEAERRELEQEA 178
Cdd:cd07935   80 GICTVTAGPKDMVVGFANLGILHVTKKKVFETlearMTEACKKgynpgllvhpelaylQAEGGGDRQLTEREKEIIRQAA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 569006534 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 3.66e-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: 3.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 569006534 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 1.78e-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: 1.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  229 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 569006534  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 4.16e-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: 159.96  E-value: 4.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07887    1 PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPHNLVGKEGCKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 118 GVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIqklQRQRLRSKPqglteaeRRELEQEAKELKKVmDLSIVRLRFSAF 197
Cdd:cd07887   81 GVCTKKINPTEMRIVFQKLGIQCVKKKDVEESLK---LREEINVDP-------FRTGFDHKDQINSI-DLNVVRLCFQVF 149
                        170       180
                 ....*....|....*....|....
gi 569006534 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 569006534 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYE--DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd00602    1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEkgPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79
                         90       100
                 ....*....|....*....|..
gi 569006534 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 9.03e-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: 150.41  E-value: 9.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEl 117
Cdd:cd07933    1 PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPHDLVGKDCRD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 118 GVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRqrlRSKPQGLTEAERRELEQeakelkkvMDLSIVRLRFSAF 197
Cdd:cd07933   80 GYYEAEFGPERRVLAFQNLGIQCVRRREVKEAIMLRISR---GINPFNVPEEQLLQIEE--------YDLNVVRLCFQIF 148
                        170       180
                 ....*....|....*....|....
gi 569006534 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 1.19e-41

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: 149.89  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRgFRFRYGCE-GPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRA-HAHSLVGKQCs 115
Cdd:cd07884    1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQADDNRRKpHVHKLVGKQG- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 116 ELGVCAVSVGPK----DMTAQFNNLGVLHVTKKNMMEIMIQklqrqrlrskpqglteaerreleqeakelKKVMDLSIVR 191
Cdd:cd07884   79 DDDVCDPHDIEVspegDYVAMFQNMGIIHTAKKNIPEELYK-----------------------------KKNMNLNQVV 129
                        170       180       190
                 ....*....|....*....|....*....|
gi 569006534 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 1.16e-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: 138.85  E-value: 1.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEl 117
Cdd:cd07885    1 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPHELVGKDCKD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 118 GVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQrlrSKPQGLTEAERREleqeakelkkVMDLSIVRLRFSAF 197
Cdd:cd07885   80 GYYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQRIQTN---NNPFNVPIEEQRA----------DYDLNAVRLCFQVT 146
                        170       180
                 ....*....|....*....|....
gi 569006534 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 6.69e-33

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: 121.47  E-value: 6.69e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006534 774 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLLKG 849
Cdd:cd08798    1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
38-221 1.02e-32

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: 124.59  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVD--LVTHSDPPRAHAHSLVGKQCS 115
Cdd:cd07886    1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVTVTvcLVWKDPPHRVHPHGLVGKDCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 116 ElGVCAVSVGPKDMTAQ-FNNLGVLHVTKKNMMEIMIQKLQrqrLRSKPqglTEAERRELEQEakelkkvMDLSIVRLRF 194
Cdd:cd07886   81 N-GICQVTLNPHSSPRHsFSNLGIQCVRKREIEAAIETRLQ---LNIDP---FKAGSLKNHEE-------VDMNVVRLCF 146
                        170       180
                 ....*....|....*....|....*..
gi 569006534 195 SAFLRASDGsFSLPLKPVISQPIHDSK 221
Cdd:cd07886  147 QASYRDDDG-RKDCLSPVLSEPIYDKK 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
453-706 4.54e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 4.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 453 LAQRSARALLDYGVTADARALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQIAHviyhaqYLGVINLTNHLHQTPLH 532
Cdd:COG0666   19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA------AGADINAKDDGGNTLLH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 533 LAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARS 612
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG--NLEIVKLLLEAGAD-----VNAQDNDGNTPLHLAAANGN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 613 PECLDLLVDCGAEVEAPERQgGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGA 692
Cdd:COG0666  166 LEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        250
                 ....*....|....
gi 569006534 693 DIHAENEEPLCPLP 706
Cdd:COG0666  244 DLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
436-700 1.86e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 1.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 436 ALDTLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQ-IAHviyha 514
Cdd:COG0666   35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLlLEA----- 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 515 qylGV-INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAHavpqiL 593
Cdd:COG0666  110 ---GAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG--NLEIVKLLLEAGAD-----V 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 594 HMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQgGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLH 673
Cdd:COG0666  180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALL 257
                        250       260
                 ....*....|....*....|....*..
gi 569006534 674 LAAGLGSPTLTRLLLKAGADIHAENEE 700
Cdd:COG0666  258 LAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
480-705 9.33e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 9.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 480 LLMAQDENGDTPLHLAIIHGQTGVIEQIAHVIYHAQYLGVINLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRH 559
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 560 GDSALHLALRAGAAapELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQGgRTALH 639
Cdd:COG0666   87 GNTLLHAAARNGDL--EIVKLLLEAGAD-----VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG-NTPLH 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006534 640 LATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:COG0666  159 LAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
458-670 1.19e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.04  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 458 ARALLDYGVTADARallagqrhllmaqDENGDTPLHLAIIHGQTGVIEQ-IAHviyhaqylGV-INLTNHLHQTPLHLAV 535
Cdd:COG0666  103 VKLLLEAGADVNAR-------------DKDGETPLHLAAYNGNLEIVKLlLEA--------GAdVNAQDNDGNTPLHLAA 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 536 ITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAhavpqILHMPDFEGLYPVHLAVHARSPEC 615
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG--HLEIVKLLLEAGA-----DVNAKDNDGKTALDLAAENGNLEI 234
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569006534 616 LDLLVDCGAEVEAPERQGGrTALHLATEMEELGLVTHLVTKLHANVNARTFAGNT 670
Cdd:COG0666  235 VKLLLEAGADLNAKDKDGL-TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
507-705 1.10e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.18  E-value: 1.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 507 IAHVIYHAQYLGVINLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAAPELLqaLLRSGA 586
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALL--LLAAGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 587 havpqILHMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQGgRTALHLATEMEELGLVTHLVtKLHANVNARTF 666
Cdd:COG0666   79 -----DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-ETPLHLAAYNGNLEIVKLLL-EAGADVNAQDN 151
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 569006534 667 AGNTPLHLAAGLGSPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
774-847 6.62e-20

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: 84.22  E-value: 6.62e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006534 774 ALQNLEQLLDGpeaQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLL 847
Cdd:cd08310    1 TRLRLCKLLDV---GKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELI 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
459-705 7.12e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 7.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 459 RALLDYGVTADARallagqrhllmaqDENGDTPLHLAIIHGQTgvIEQIAHVIYHaqylGV-INLTNHLHQTPLH--LAV 535
Cdd:PHA03095  67 RLLLEAGADVNAP-------------ERCGFTPLHLYLYNATT--LDVIKLLIKA----GAdVNAKDKVGRTPLHvyLSG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 536 ITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAAPELLQALLRSGAHavpqiLHMPDFEGLYPVHlaVHARS--- 612
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLH--HHLQSfkp 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 613 -PECLDLLVDCGAEVEAPERqGGRTALHLATeMEELGLVTHLVTKLHAN--VNARTFAGNTPLHLAAGLGSPTLTRLLLK 689
Cdd:PHA03095 201 rARIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIA 278
                        250
                 ....*....|....*.
gi 569006534 690 AGADIHAENEEPLCPL 705
Cdd:PHA03095 279 LGADINAVSSDGNTPL 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 569006534   227 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 569006534   307 LQlkrkRGGDV-SDSKQFTYY 326
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
605-698 1.65e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  605 HLAVHARSPECLDLLVDCGAEVEApERQGGRTALHLATEMEELGLVTHLVTklHANVNARTFaGNTPLHLAAGLGSPTLT 684
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDN-GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 569006534  685 RLLLKAGADIHAEN 698
Cdd:pfam12796  78 KLLLEKGADINVKD 91
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
228-327 2.87e-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: 2.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKD-DIEVRFYeddengwqAFGDFSPTDVHkQYAIVFRTPPYHkmkIERPVTVF 306
Cdd:cd00102    1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFG--------GGVPCSVLSVS-STAIVCTTPPYA---NPGPGPVE 68
                         90       100
                 ....*....|....*....|.
gi 569006534 307 LQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd00102   69 VTVDRGNGGITSSPLTFTYVP 89
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
776-848 1.73e-12

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: 63.39  E-value: 1.73e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006534 776 QNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLLK 848
Cdd:cd08797    3 QQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIE 75
Ank_2 pfam12796
Ankyrin repeats (3 copies);
531-628 1.37e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  531 LHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLrsgAHAVPQIlhmpDFEGLYPVHLAVHA 610
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL--EIVKLLL---EHADVNL----KDNGRTALHYAARS 71
                          90
                  ....*....|....*...
gi 569006534  611 RSPECLDLLVDCGAEVEA 628
Cdd:pfam12796  72 GHLEIVKLLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
539-707 2.09e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.21  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 539 QTRVVSFLLQVGADPTLLDRH-GDSALHLAlrAGAAAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSPECLD 617
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYA--TENKDQRLTELLLSYGAN-----VNIPDKTNNSPLHHAVKHYNKPIVH 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 618 LLVDCGAEVEAPERQGgRTALHLATEMEELGLVTHLVTKLHANVNAR-TFAGNTPLHLAagLGSPTLTRLLLKAGADIHA 696
Cdd:PHA02878 219 ILLENGASTDARDKCG-NTPLHISVGYCKDYDILKLLLEHGVDVNAKsYILGLTALHSS--IKSERKLKLLLEYGADINS 295
                        170
                 ....*....|.
gi 569006534 697 ENEEPLCPLPS 707
Cdd:PHA02878 296 LNSYKLTPLSS 306
PHA02878 PHA02878
ankyrin repeat protein; Provisional
523-675 2.77e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 523 TNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRagAAAPELLQALLRSGAHavpqILHMpDFEGLY 602
Cdd:PHA02878 164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK--HYNKPIVHILLENGAS----TDAR-DKCGNT 236
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006534 603 PVHLAV-HARSPECLDLLVDCGAEVEAPERQGGRTALHLATEMEElglVTHLVTKLHANVNARTFAGNTPLHLA 675
Cdd:PHA02878 237 PLHISVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSER---KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
490-694 1.08e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 490 TPLHLA--IIHGQTGVIEqIAHVIYhaQYLGVINLTNHLHQTPLHLAVIT--GQTRVVSFLLQVGADPTLLDRHGDSALH 565
Cdd:PHA03100  70 TPLHYLsnIKYNLTDVKE-IVKLLL--EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLH 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 566 LALRAGAAAPELLQALLRSGA-------------HAVPqiLHMPDFEGLYPVHLAVHARSPECLDLLVDCGAeveaperq 632
Cdd:PHA03100 147 LYLESNKIDLKILKLLIDKGVdinaknrvnyllsYGVP--INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA-------- 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006534 633 ggrtalhlatemeelglvthlvtklhaNVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADI 694
Cdd:PHA03100 217 ---------------------------NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
484-557 2.71e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 2.71e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006534  484 QDENGDTPLHLAIIHGQTGVIEQ-IAHVIyhaqylgvINLTNHlHQTPLHLAVITGQTRVVSFLLQVGADPTLLD 557
Cdd:pfam12796  26 QDKNGRTALHLAAKNGHLEIVKLlLEHAD--------VNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
492-587 3.27e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  492 LHLAIIHGQTGVIEQIahVIYHAQylgvINLTNHLHQTPLHLAVITGQTRVVSFLLQVGAdpTLLDRHGDSALHLALRAG 571
Cdd:pfam12796   1 LHLAAKNGNLELVKLL--LENGAD----ANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSG 72
                          90
                  ....*....|....*.
gi 569006534  572 aaAPELLQALLRSGAH 587
Cdd:pfam12796  73 --HLEIVKLLLEKGAD 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
772-850 5.46e-10

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: 56.65  E-value: 5.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534   772 DAALQNLEQLLDGPeAQGSWAELAERLGLRSLV------DTYRKTPSPSGSLLRSYKLAGG---DLVGLLEALSDMGLHE 842
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSEADidqirtEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 569006534   843 GVRLLKGP 850
Cdd:smart00005  81 AVELLRSE 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
485-705 4.05e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 485 DENGDTPLHLAIihgQTGVIEQIAHVIYHAqylGV-INLTNHLHQTPLHLAVITG-QTRVVSFLLQVGADPTLLDRHGDS 562
Cdd:PHA02876 270 DDCKNTPLHHAS---QAPSLSRLVPKLLER---GAdVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYIT 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 563 ALHLALRAGAAApELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQGGrTALHLAT 642
Cdd:PHA02876 344 PLHQASTLDRNK-DIVITLLELGAN-----VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFAL 416
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006534 643 EMEELGLVTHLVTKLHANVNARTFAGNTPLHLAAGLG-SPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:PHA02876 417 CGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02875 PHA02875
ankyrin repeat protein; Provisional
526-705 6.62e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 6.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 526 LHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAhaVPQIlHMPDFEGlyPVH 605
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDS--EAIKLLMKHGA--IPDV-KYPDIES--ELH 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 606 LAVHARSPECLDLLVDCGAEVEAPERQGGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTR 685
Cdd:PHA02875  74 DAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
                        170       180
                 ....*....|....*....|
gi 569006534 686 LLLKAGADIHAENEEPLCPL 705
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPL 172
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
528-601 8.36e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 8.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 528 QTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLR-------SGAHAVPQIL------- 593
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR--EVVQLLSRhsqchfeLGANAKPDSFtgkppsl 193
                         90
                 ....*....|....*
gi 569006534 594 -------HMPDFEGL 601
Cdd:PTZ00322 194 edspissHHPDFSAV 208
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 569006534 230 ISRMDKTAGSVRGGDEVYLLCDKVQKDDiEVRFYE---DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:cd01178    4 IEKKSLNSCSVNGGEELFLTGKNFLKDS-KVVFQEkgqDGEAQWEAEATIDKEKSH-QNHLVVEVPPYHNKHVAAPVQVQ 81
                         90       100
                 ....*....|....*....|....
gi 569006534 307 LQL---KRKRggdvSDSKQFTYYP 327
Cdd:cd01178   82 FYVvngKRKR----SQPQTFTYTP 101
PHA02874 PHA02874
ankyrin repeat protein; Provisional
520-702 2.68e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 520 INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAHAvpQILHMPDFE 599
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAH--DIIKLLIDNGVDT--SILPIPCIE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 600 GlypvhlavharspECLDLLVDCGAEVEAPERQGgRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLG 679
Cdd:PHA02874 104 K-------------DMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHN 168
                        170       180
                 ....*....|....*....|....*.
gi 569006534 680 SPTLTRLLLKAGADIHAEN---EEPL 702
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDnngESPL 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
520-675 3.36e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 520 INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAHAvpqilHMPDFE 599
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF--DIIKLLLEKGAYA-----NVKDNN 189
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006534 600 GLYPVHLAVHARSPECLDLLVDCGAEVEAPERQgGRTALHLATeMEELGLVTHLVTklHANVNARTFAGNTPLHLA 675
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAI-IHNRSAIELLIN--NASINDQDIDGSTPLHHA 261
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
38-162 4.35e-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: 53.43  E-value: 4.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  38 PYLVIVEQPKQRgFRFRY---GCEGPSHGGLPGassekgrkTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGK-- 112
Cdd:cd07927    1 YELRIEVQPEPH-HRARYeteGSRGAVKAPSTG--------GFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHRit 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006534 113 -----QCSELGVCAVSV------GPKDMTAQFNNLGVLHVTKKNM-MEIMIQKLQRQRLRSK 162
Cdd:cd07927   72 gktttPCKEKIIGNTKVleiplePKNNMTATIDCAGILKLRNADIeLRKGETDIKKKNTRAR 133
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
520-699 8.40e-08

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: 56.24  E-value: 8.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  520 INLTNHLHQTPLHLAVITGQTR-VVSFLLQVGADPTLldrhGDSALHLA-LRAGAAAPELLQALLRSGAHAVPQILhMPD 597
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAIsLEYVDAVEAILLHLLAAFRKSGPLEL-AND 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  598 ------FEGLYPVHLAVHARSPECLDLLVDCGAEVEApeRQGGRTALhlatEMEELGLVTHlvtklhanvnartfaGNTP 671
Cdd:TIGR00870 120 qytsefTPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFV----KSQGVDSFYH---------------GESP 178
                         170       180
                  ....*....|....*....|....*...
gi 569006534  672 LHLAAGLGSPTLTRLLLKAGADIHAENE 699
Cdd:TIGR00870 179 LNAAACLGSPSIVALLSEDPADILTADS 206
PHA02876 PHA02876
ankyrin repeat protein; Provisional
520-716 1.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 520 INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAHAVPQILHMPDfe 599
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI--DTIKAIIDNRSNINKNDLSLLK-- 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 600 glypvhlAVHARSPECLDLLVDCGAEVEAPErQGGRTALHLATEMEELglvTHLVTKL---HANVNARTFAGNTPLHLAA 676
Cdd:PHA02876 247 -------AIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSL---SRLVPKLlerGADVNAKNIKGETPLYLMA 315
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 569006534 677 GLGSPTLT-RLLLKAGADIHAENEEPLCPLPSPSTSGSDSD 716
Cdd:PHA02876 316 KNGYDTENiRTLIMLGADVNAADRLYITPLHQASTLDRNKD 356
Death pfam00531
Death domain;
776-848 4.34e-07

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 48.52  E-value: 4.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  776 QNLEQLLDGPEAQG-SWAELAERLGLRSL-VDT----YRKTPSPSGSLLRSYKLAGG---DLVGLLEALSDMGLHEGVRL 846
Cdd:pfam00531   2 KQLDRLLDPPPPLGkDWRELARKLGLSENeIDEieseNPRLRSQTYELLRLWEQREGknaTVGTLLEALRKLGRRDAAEK 81

                  ..
gi 569006534  847 LK 848
Cdd:pfam00531  82 IQ 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
482-569 5.33e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 5.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 482 MAQDENGDTPLHLAIIHGQtgvieqiAHVIYHAQYL--GV-INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDR 558
Cdd:PHA03095 216 AATDMLGNTPLHSMATGSS-------CKRSLVLPLLiaGIsINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
                         90
                 ....*....|.
gi 569006534 559 HGDSALHLALR 569
Cdd:PHA03095 289 DGNTPLSLMVR 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
514-737 7.81e-07

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: 52.71  E-value: 7.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 514 AQYLGVINL--TNHLHQTPLHLAVITGQTRVVSFLL-QVGADPTLLDRHGDSALHLALRAGAAapELLQALLRsgahAVP 590
Cdd:cd22192    2 AQMLDELHLlqQKRISESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNL--EAAVVLME----AAP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 591 QILHMPDFEGLYPvhlavharspecldllvdcgaeveaperqgGRTALHLATEMEELGLVTHLVTKLHANVNART----- 665
Cdd:cd22192   76 ELVNEPMTSDLYQ------------------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtff 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 666 --------FAGNTPLHLAAGLGSPTLTRLLLKAGADIHAE---------------NEEPLCPLPSPSTSgSDSDSEGPER 722
Cdd:cd22192  126 rpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQdslgntvlhilvlqpNKTFACQMYDLILS-YDKEDDLQPL 204
                        250
                 ....*....|....*
gi 569006534 723 DTQRNFRGHTPLDLT 737
Cdd:cd22192  205 DLVPNNQGLTPFKLA 219
PHA02876 PHA02876
ankyrin repeat protein; Provisional
556-696 9.83e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 9.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 556 LDRHGDSALHLALRAGAAApELLQALLRSGAHavpqiLHMPDFEGLYPVHL-AVHARSPECLDLLVDCGAEVEAPERQGg 634
Cdd:PHA02876 269 IDDCKNTPLHHASQAPSLS-RLVPKLLERGAD-----VNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLY- 341
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006534 635 RTALHLATEMEELGLVTHLVTKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADIHA 696
Cdd:PHA02876 342 ITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403
PHA02878 PHA02878
ankyrin repeat protein; Provisional
471-628 1.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 471 RALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQIahVIYHAQylgvINLTNHLHQTPLHLAVITGQTRVVSFLLQVG 550
Cdd:PHA02878 151 KLLLSYGADINMKDRHKGNTALHYATENKDQRLTELL--LSYGAN----VNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 551 ADPTLLDRHGDSALHLALrAGAAAPELLQALLRSGA--HAVPQILhmpdfeGLYPVHLAVHarSPECLDLLVDCGAEVEA 628
Cdd:PHA02878 225 ASTDARDKCGNTPLHISV-GYCKDYDILKLLLEHGVdvNAKSYIL------GLTALHSSIK--SERKLKLLLEYGADINS 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-582 3.16e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 569006534  529 TPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALL 582
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG--NVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
489-656 3.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 489 DTPLHLAIIHGQTGVIEQ-------IAHVIYHAQylgvinltnhlhQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGD 561
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEElldlgkfADDVFYKDG------------MTPLHLATILKKLDIMKLLIARGADPDIPNTDKF 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 562 SALHLALRAGAAapELLQALLRSGAhavpqILHMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQGGRTALHLA 641
Cdd:PHA02875 137 SPLHLAVMMGDI--KGIELLIDHKA-----CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYA 209
                        170
                 ....*....|....*
gi 569006534 642 TEMEELGLVTHLVTK 656
Cdd:PHA02875 210 IENNKIDIVRLFIKR 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
653-705 6.55e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 569006534  653 LVTKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02946 PHA02946
ankyin-like protein; Provisional
478-705 8.71e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 8.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 478 RHLLMAQDENGDtplhLAIIH---GQTGVIEQIAHVIYHAQYlgVINLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPT 554
Cdd:PHA02946  26 RNMLQAIEPSGN----YHILHaycGIKGLDERFVEELLHRGY--SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 555 LLDRHGDSALHLALRAGAAAPELLQALLRSGAhavpQILHMPDFEGLYPVhLAVHARSPECLDLLVDCGAEVEAPERQG- 633
Cdd:PHA02946 100 ACDKQHKTPLYYLSGTDDEVIERINLLVQYGA----KINNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGk 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006534 634 GRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAglgSPTLTRL----LLKAGADIHAENEEPLCPL 705
Cdd:PHA02946 175 NHIHRHLMSDNPKASTISWMM-KLGISPSKPDHDGNTPLHIVC---SKTVKNVdiinLLLPSTDVNKQNKFGDSPL 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
668-699 1.84e-05

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: 42.28  E-value: 1.84e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 569006534  668 GNTPLHLAAG-LGSPTLTRLLLKAGADIHAENE 699
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
529-699 2.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 529 TPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAA---PELLQALLRSGAhavpqILHMPDFEGLYPVH 605
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvKEIVKLLLEYGA-----NVNAPDNNGITPLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 606 LAV--HARSPECLDLLVDCGAEVEApERQGGRTALHLATE-------MEELgLVTH-----------LVTKLHANVNART 665
Cdd:PHA03100 112 YAIskKSNSYSIVEYLLDNGANVNI-KNSDGENLLHLYLEsnkidlkILKL-LIDKgvdinaknrvnYLLSYGVPINIKD 189
                        170       180       190
                 ....*....|....*....|....*....|....
gi 569006534 666 FAGNTPLHLAAGLGSPTLTRLLLKAGADIHAENE 699
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
Ank_5 pfam13857
Ankyrin repeats (many copies);
520-567 4.36e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 569006534  520 INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLA 567
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
668-696 6.51e-05

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: 40.70  E-value: 6.51e-05
                          10        20
                  ....*....|....*....|....*....
gi 569006534  668 GNTPLHLAAGLGSPTLTRLLLKAGADIHA 696
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02743 PHA02743
Viral ankyrin protein; Provisional
592-692 8.98e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 44.04  E-value: 8.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 592 ILHMPDFEGLYPVHL-AVHARSPECL--DLLVDCGAEVEAPERQGGRTALHLATEMEELGLVTHLVTKLHANVNARTFAG 668
Cdd:PHA02743  49 LLHRYDHHGRQCTHMvAWYDRANAVMkiELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQH 128
                         90       100
                 ....*....|....*....|....
gi 569006534 669 NTPLHLAAGLGSPTLTRLLLKAGA 692
Cdd:PHA02743 129 ETAYHIAYKMRDRRMMEILRANGA 152
PHA02876 PHA02876
ankyrin repeat protein; Provisional
483-628 1.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 483 AQDENGDTPLHlaiihgQTGVIEQIAHVIYHAQYLGV-INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGD 561
Cdd:PHA02876 336 AADRLYITPLH------QASTLDRNKDIVITLLELGAnVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006534 562 SALHLALrAGAAAPELLQALLRSGAHAVPQILHMPDfeglyPVHLAVHAR-SPECLDLLVDCGAEVEA 628
Cdd:PHA02876 410 TALHFAL-CGTNPYMSVKTLIDRGANVNSKNKDLST-----PLHYACKKNcKLDVIEMLLDNGADVNA 471
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
534-742 2.26e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 534 AVITGQTRVVSFLLQVGADPTLLDRHGDSALHLAlrAGAAAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSP 613
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIA--ASKGYEDCVLVLLKHACN-----VHIRDANGNTALWNAISAKHH 604
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 614 ECLDLLVDCGAeveAPERQGGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGAD 693
Cdd:PLN03192 605 KIFRILYHFAS---ISDPHAAGDLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006534 694 I-HAENEEPLCPL---------------PSPSTSGSDSDSEGPERDTQRNFRGHTPLDLTCSTKV 742
Cdd:PLN03192 681 VdKANTDDDFSPTelrellqkrelghsiTIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRV 745
PHA02876 PHA02876
ankyrin repeat protein; Provisional
539-717 2.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 539 QTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSPECLDL 618
Cdd:PHA02876 157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNA--KMVNLLLSYGAD-----VNIIALDDLSVLECAVDSKNIDTIKA 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 619 LVDCGAEVEaperqggRTALHLATEMEELGLVTHLVTKLHA-NVNARTFAGNTPLHLAAGlgSPTLTRL---LLKAGADI 694
Cdd:PHA02876 230 IIDNRSNIN-------KNDLSLLKAIRNEDLETSLLLYDAGfSVNSIDDCKNTPLHHASQ--APSLSRLvpkLLERGADV 300
                        170       180
                 ....*....|....*....|...
gi 569006534 695 HAENEEPLCPLPSPSTSGSDSDS 717
Cdd:PHA02876 301 NAKNIKGETPLYLMAKNGYDTEN 323
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
528-558 2.90e-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: 38.81  E-value: 2.90e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 569006534  528 QTPLHLAVI-TGQTRVVSFLLQVGADPTLLDR 558
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
488-688 3.63e-04

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: 44.30  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  488 GDTPLHLAIIHGQTGVIEQIAHVIYHAQYLGVINLTNHLH-------QTPLHLAVITGQTRVVSFLLQVGAD-------- 552
Cdd:TIGR00870  82 GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYtseftpgITALHLAAHRQNYEIVKLLLERGASvparacgd 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  553 -------PTLLdRHGDSALHLAlrAGAAAPELLQALLRSGAHAVPQ------ILHM----PDFEGLYpvhlavHARSPEC 615
Cdd:TIGR00870 162 ffvksqgVDSF-YHGESPLNAA--ACLGSPSIVALLSEDPADILTAdslgntLLHLlvmeNEFKAEY------EELSCQM 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006534  616 LDLLVDCGAeveaperqggrtalHLATEMEelglvthlvtkLHANVNartFAGNTPLHLAAGLGSPTLTRLLL 688
Cdd:TIGR00870 233 YNFALSLLD--------------KLRDSKE-----------LEVILN---HQGLTPLKLAAKEGRIVLFRLKL 277
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
634-696 4.97e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 4.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006534 634 GRTALHLATEMEELGLVTHLVTK---LHANVNARTFA---------GNTPLHLAAGLGSPTLTRLLLKAGADIHA 696
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENgadVSARATGRFFRkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAA 147
PHA02874 PHA02874
ankyrin repeat protein; Provisional
484-633 5.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 484 QDENGDTPLHLAIIHGQTGVIEQIahvIYHAQYLgviNLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSA 563
Cdd:PHA02874 153 EDDNGCYPIHIAIKHNFFDIIKLL---LEKGAYA---NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006534 564 LHLALRAGAAAPELLqallrsgahAVPQILHMPDFEGLYPVHlavHARSPEC----LDLLVDCGAEVEAPERQG 633
Cdd:PHA02874 227 LHNAIIHNRSAIELL---------INNASINDQDIDGSTPLH---HAINPPCdidiIDILLYHKADISIKDNKG 288
Death_UNC5B cd08802
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ...
782-842 7.00e-04

Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). UNC5B is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5B signaling is involved in the netrin-1-induced proliferation and migration of renal proximal tubular cells. It is also required for vascular patterning during embryonic development, and its activation inhibits sprouting angiogenesis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176780  Cd Length: 84  Bit Score: 39.24  E-value: 7.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006534 782 LDGPEAQGS-WAELAERLGLRSLVDTYRKTPSPSGSLLRSYKL---AGGDLVGLLEALSDMGLHE 842
Cdd:cd08802   13 LDAPNSRGNdWRLLAQKLSMDRYLNYFATKASPTGVILDLWEArhqDDGDLNSLASALEEMGKSE 77
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
615-696 9.34e-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: 42.82  E-value: 9.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 615 CLDLLVDCGAEVEAPErqgGRTALHLATEMEELGLVTHLVTKlHANVNART--------------FAGNTPLHLAAGLGS 680
Cdd:cd22194  125 ILDRFINAEYTEEAYE---GQTALNIAIERRQGDIVKLLIAK-GADVNAHAkgvffnpkykhegfYFGETPLALAACTNQ 200
                         90
                 ....*....|....*.
gi 569006534 681 PTLTRLLLKAGADIHA 696
Cdd:cd22194  201 PEIVQLLMEKESTDIT 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
488-547 9.47e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 9.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534  488 GDTPLHLAIIHGQTGVIEqiahviYHAQYLGVINLTNHLHQTPLHLAVITGQTRVVSFLL 547
Cdd:pfam13637   1 ELTALHAAAASGHLELLR------LLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
668-696 9.86e-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: 9.86e-04
                           10        20
                   ....*....|....*....|....*....
gi 569006534   668 GNTPLHLAAGLGSPTLTRLLLKAGADIHA 696
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
776-844 1.18e-03

Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). UNC5C is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5C plays a critical role in the development of spinal accessory motor neurons. Methylation of the UNC5C gene is associated with early stages of colorectal carcinogenesis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260064  Cd Length: 83  Bit Score: 38.84  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006534 776 QNLEQLLDGPEAQGS-WAELAERLGLRSLVDTYRKTPSPSGSLL---RSYKLAGGDLVGLLEALSDMGLHEGV 844
Cdd:cd08799    7 QKLCGSLDAPQTRGNdWRMLAHKLNLDRYLNYFATKSSPTGVILdlwEAQHFPDGNLSRLAAVLEEMGRHETV 79
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
462-607 1.52e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.15  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 462 LDYGVTADARALL------AGQRHLLMAQDEN----GDTPLHLAI----IHGQTGVIEQIAHViyHAQYLGVINLTN--- 524
Cdd:cd22197   58 LQDGVNACIMPLLeidkdsGNPKPLVNAQCTDeyyrGHSALHIAIekrsLQCVKLLVENGADV--HARACGRFFQKKqgt 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 525 --HLHQTPLHLAVITGQTRVVSFLLQVGADPTLL---DRHGDSALHLALRAGAAAPE-------LLQALLRSGAHAVP-- 590
Cdd:cd22197  136 cfYFGELPLSLAACTKQWDVVNYLLENPHQPASLqaqDSLGNTVLHALVMIADNSPEnsalvikMYDGLLQAGARLCPtv 215
                        170
                 ....*....|....*..
gi 569006534 591 QILHMPDFEGLYPVHLA 607
Cdd:cd22197  216 QLEEISNHEGLTPLKLA 232
PHA02736 PHA02736
Viral ankyrin protein; Provisional
616-692 1.88e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 1.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006534 616 LDLLVDCGAEVEAPERQGGRTALHLATEMEELGLVTHLVTKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGA 692
Cdd:PHA02736  74 LKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
598-673 2.17e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.70  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 598 FEGLYPVHLAVHARSPECLDLLVDCGAEVEA--------PERQG-----GRTALHLATEMEELGLVTHLVTKLH--ANVN 662
Cdd:cd22193   74 YEGQTALHIAIERRQGDIVALLVENGADVHAhakgrffqPKYQGegfyfGELPLSLAACTNQPDIVQYLLENEHqpADIE 153
                         90
                 ....*....|.
gi 569006534 663 ARTFAGNTPLH 673
Cdd:cd22193  154 AQDSRGNTVLH 164
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
488-620 3.23e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 488 GDTPLHLAIIHGQTGVIEQI----AHVIyHAQYLG---VINLTNHLH--QTPLHLAVITGQTRVVSFLLQVGADPTLLDR 558
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELiargADVV-SPRATGtffRPGPKNLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006534 559 HGDSALH-LALRAGAA-APELLQALLRSGAHAVPQIL-HMPDFEGLYPVHLAVHARSPECLDLLV 620
Cdd:cd22192  168 LGNTVLHiLVLQPNKTfACQMYDLILSYDKEDDLQPLdLVPNNQGLTPFKLAAKEGNIVMFQHLV 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
659-705 3.41e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 3.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006534 659 ANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADIHAENEEPLCPL 705
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
529-555 3.76e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.76e-03
                           10        20
                   ....*....|....*....|....*..
gi 569006534   529 TPLHLAVITGQTRVVSFLLQVGADPTL 555
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
530-607 4.04e-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: 41.02  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 530 PLHLAVITGQTRVVSFLLQVGADPTLL---DRHGDSALH-LALRA------GAAAPELLQALLRSGAHAVP--QILHMPD 597
Cdd:cd21882  122 PLSLAACTNQEEIVRLLLENGAQPAALeaqDSLGNTVLHaLVLQAdntpenSAFVCQMYNLLLSYGAHLDPtqQLEEIPN 201
                         90
                 ....*....|
gi 569006534 598 FEGLYPVHLA 607
Cdd:cd21882  202 HQGLTPLKLA 211
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
527-553 4.81e-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: 35.31  E-value: 4.81e-03
                          10        20
                  ....*....|....*....|....*..
gi 569006534  527 HQTPLHLAVITGQTRVVSFLLQVGADP 553
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02875 PHA02875
ankyrin repeat protein; Provisional
486-625 7.72e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 486 ENGDTPLHLAIIHGQTGVIEQIahviyhAQYLGVINLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALH 565
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLL------IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006534 566 LALRAGAAapELLQALLRSGAHavpqilhmPDFEGLYP----VHLAVHARSPECLDLLVDCGAE 625
Cdd:PHA02875 174 IAMAKGDI--AICKMLLDSGAN--------IDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
461-552 9.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006534 461 LLDYGVTADARallagqrhllmaqDENGDTPLHLAIIHgqtgviEQIAHVIYHAQYLGVINLTNHLHQTPLHLAVITGQT 540
Cdd:PHA03100 178 LLSYGVPINIK-------------DVYGFTPLHYAVYN------NNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
                         90
                 ....*....|..
gi 569006534 541 RVVSFLLQVGAD 552
Cdd:PHA03100 239 EIFKLLLNNGPS 250
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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