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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934     1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSR-PQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934    81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160

                         170       180
                  ....*....|....*....|....*
gi 1019366640 197 FLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07934   161 YLRDSNGSYTLALKPVISDPIHDSK 185

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1019366640 732 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRG 807
Cdd:cd08798     1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934     1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSR-PQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934    81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160

                         170       180
                  ....*....|....*....|....*
gi 1019366640 197 FLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07934   161 YLRDSNGSYTLALKPVISDPIHDSK 185

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80

                          90       100
                  ....*....|....*....|..
gi 1019366640 306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1019366640 732 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRG 807
Cdd:cd08798     1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76

ankyrin-like protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 417 RALLDYGVTADARallagqrhlltaqDENGDTPLHLAIIHGQTsvIEQIVYVIHHAQDlgvVNLTNHLHQTPLH--LAVI 494
Cdd:PHA03095   67 RLLLEAGADVNAP-------------ERCGFTPLHLYLYNATT--LDVIKLLIKAGAD---VNAKDKVGRTPLHvyLSGF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 495 TGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVH---LAVRARsP 571
Cdd:PHA03095  129 NINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLHhhlQSFKPR-A 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 572 ECLDLLVDSGAEVEATERqGGRTALHLATeMEELGLVTHLVTKLRAN--VNARTFAGNTPLHLAAGLGYPTLTRLLLKAG 649
Cdd:PHA03095  203 RIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         250
                  ....*....|....
gi 1019366640 650 ADIHAENEEPLCPL 663
Cdd:PHA03095  281 ADINAVSSDGNTPL 294

Ankyrin repeats (3 copies);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 563 HLAVRARSPECLDLLVDSGAEVEATErQGGRTALHLATEMEELGLVTHLVTKLRANVNARtfaGNTPLHLAAGLGYPTLT 642
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1019366640 643 RLLLKAGADIHAEN 656
Cdd:pfam12796  78 KLLLEKGADINVKD 91

Death domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 734 QNLEQLLDGPEAQG-SWAELAERLGLRSL-VDT----YRQTTSPSGSLLRSYELAGG---DLAGLLEALSDMGLEEGVRL 804
Cdd:pfam00531   2 KQLDRLLDPPPPLGkDWRELARKLGLSENeIDEieseNPRLRSQTYELLRLWEQREGknaTVGTLLEALRKLGRRDAAEK 81

                  ..
gi 1019366640 805 LR 806
Cdd:pfam00531  82 IQ 83

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 446 GDTPLHLAIIHGQtsvIEQIVYVIHHAQDLGVVNLTNHLHQ--TPLHLAVITGQTSVVSFLLRVGADPA-------LLDR 516
Cdd:cd22192    51 GETALHVAALYDN---LEAAVVLMEAAPELVNEPMTSDLYQgeTALHIAVVNQNLNLVRELIARGADVVspratgtFFRP 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 517 HGDSAMH-----LALRAGAGAPELLRALLQSGAPAVPQllhmpDFEGLYPVHLAV----RARSPECLDLLVDSGAE---- 583
Cdd:cd22192   128 GPKNLIYygehpLSFAACVGNEEIVRLLIEHGADIRAQ-----DSLGNTVLHILVlqpnKTFACQMYDLILSYDKEddlq 202

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1019366640 584 -VEATERQGGRTALHLATEMEELGLVTHLVTKLRA 617
Cdd:cd22192   203 pLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRH 237

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934     1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSR-PQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934    81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160

                         170       180
                  ....*....|....*....|....*
gi 1019366640 197 FLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07934   161 YLRDSNGSYTLALKPVISDPIHDSK 185

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640  40 LVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSElGI 119
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKD-GV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 120 CAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQrqrlrsrpqgLTEAEQReLEQEAKELKKVMDLSIVRLRFSAFLR 199
Cdd:pfam00554  80 CEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-VGFEALRQIKDMDLNVVRLCFQAFLP 148

                         170       180
                  ....*....|....*....|.
gi 1019366640 200 ASDGSFSLPLKPVISQPIHDS 220
Cdd:pfam00554 149 DTRGNFTTPLPPVVSNPIYDK 169

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCsEL 117
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHC-ED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGT----MIQKLQR---------------QRLRSRPQGLTEAEQRELEQEA 178
Cdd:cd07935    80 GICTVTAGPKDMVVGFANLGILHVTKKKVFETlearMTEACKKgynpgllvhpelaylQAEGGGDRQLTEREKEIIRQAA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1019366640 179 KELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07935   160 VQQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 229 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80

                          90       100
                  ....*....|....*....|..
gi 1019366640 307 LQLKRKRGGDVSDSKQFTYYPL 328
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYE--DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd00602     1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEkgPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79

                          90       100
                  ....*....|....*....|..
gi 1019366640 306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd00602    80 PIQLVRPDDRKRSEPLTFTYTP 101

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640  38 PYLVIVEQPKQRgFRFRYGCE-GPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRA-HAHSLVGKQCs 115
Cdd:cd07884     1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQADDNRRKpHVHKLVGKQG- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 116 ELGICAVSVGPK----DMTAQFNNLGVLHVTKKNMMGTMIQklqrqrlrsrpqglteaeqreleqeakelKKVMDLSIVR 191
Cdd:cd07884    79 DDDVCDPHDIEVspegDYVAMFQNMGIIHTAKKNIPEELYK-----------------------------KKNMNLNQVV 129

                         170       180       190
                  ....*....|....*....|....*....|
gi 1019366640 192 LRFSAFLRASDGSFSLPLKPVISQPIHDSK 221
Cdd:cd07884   130 LRFQAFAVSANGHLRPICPPVYSNPINNLK 159

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1019366640 732 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRG 807
Cdd:cd08798     1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640  38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVD--LVTHSDPPRAHAHSLVGKQCS 115
Cdd:cd07886     1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVTVTvcLVWKDPPHRVHPHGLVGKDCP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 116 ElGICAVSVGPKDMTAQ-FNNLGVLHVTKKNMMGTMIQKLQrqrlrsrpQGLT--EAEQRELEQEakelkkvMDLSIVRL 192
Cdd:cd07886    81 N-GICQVTLNPHSSPRHsFSNLGIQCVRKREIEAAIETRLQ--------LNIDpfKAGSLKNHEE-------VDMNVVRL 144

                         170       180
                  ....*....|....*....|....*....
gi 1019366640 193 RFSAFLRASDGsFSLPLKPVISQPIHDSK 221
Cdd:cd07886   145 CFQASYRDDDG-RKDCLSPVLSEPIYDKK 172

Ankyrin repeat [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 465 IVYVIHHAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGA 544
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAA--ALAGDLLVALLLLAAGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 545 PavpqlLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGgRTALHLATEMEELGLVTHLVtKLRANVNARTF 624
Cdd:COG0666    79 D-----INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-ETPLHLAAYNGNLEIVKLLL-EAGADVNAQDN 151

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1019366640 625 AGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPL 663
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190

ankyrin-like protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 417 RALLDYGVTADARallagqrhlltaqDENGDTPLHLAIIHGQTsvIEQIVYVIHHAQDlgvVNLTNHLHQTPLH--LAVI 494
Cdd:PHA03095   67 RLLLEAGADVNAP-------------ERCGFTPLHLYLYNATT--LDVIKLLIKAGAD---VNAKDKVGRTPLHvyLSGF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 495 TGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVH---LAVRARsP 571
Cdd:PHA03095  129 NINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLHhhlQSFKPR-A 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 572 ECLDLLVDSGAEVEATERqGGRTALHLATeMEELGLVTHLVTKLRAN--VNARTFAGNTPLHLAAGLGYPTLTRLLLKAG 649
Cdd:PHA03095  203 RIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         250
                  ....*....|....
gi 1019366640 650 ADIHAENEEPLCPL 663
Cdd:PHA03095  281 ADINAVSSDGNTPL 294

Ankyrin repeat [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 416 ARALLDYGvtADarallagqrhlLTAQDENGDTPLHLAIIHGQTSVIEQIVyvihhaqDLGV-VNLTNHLHQTPLHLAVI 494
Cdd:COG0666   136 VKLLLEAG--AD-----------VNAQDNDGNTPLHLAAANGNLEIVKLLL-------EAGAdVNARDNDGETPLHLAAE 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 495 TGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPAVPQllhmpDFEGLYPVHLAVRARSPECL 574
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLA--AENGNLEIVKLLLEAGADLNAK-----DKDGLTALLLAAAAGAALIV 268

                         170       180
                  ....*....|....*....|.
gi 1019366640 575 DLLVDSGAEVEATERQGGRTA 595
Cdd:COG0666   269 KLLLLALLLLAAALLDLLTLL 289

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019366640 228 LKISRMDKTAGSVRGGDEVYLLCDKVQKD-DIEVRFYeddengwqAFGDFSPTDVHkQYAIVFRTPPYHkmkIERPVTVF 306
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFG--------GGVPCSVLSVS-STAIVCTTPPYA---NPGPGPVE 68

                          90       100
                  ....*....|....*....|.
gi 1019366640 307 LQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd00102    69 VTVDRGNGGITSSPLTFTYVP 89

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1019366640 734 QNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLR 806
Cdd:cd08797     3 QQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIE 75