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Conserved domains on  [gi|1696059887|ref|XP_029587160|]
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nuclear factor NF-kappa-B p105 subunit-like isoform X1 [Salmo trutta]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13080695)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHD-n super family cl08275
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 40-241 2.80e-129

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).


The actual alignment was detected with superfamily member cd07935:

Pssm-ID: 447596  Cd Length: 202  Bit Score: 387.71  E-value: 2.80e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQCDKG 119
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 120 ICITDLQPKDCSISFPNLGILHVTKKNVSKTLEDRMTEAYRMGYNCGIVIHPEIDTIQGEVRIPRELTDHQRSMICSAAT 199
Cdd:cd07935    81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1696059887 200 KQAKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDSK 241
Cdd:cd07935   161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 248-349 1.73e-60

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: 200.62  E-value: 1.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 248 LKIVRMDRTAGCVTGGEEVYLLCDKVQKDDIQVRFYEDDETGLTWEAFGDFSPTDVHRQFAIVFKTPKYRDLNLQKPTSV 327
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80

                          90       100
                  ....*....|....*....|..
gi 1696059887 328 FVQLKRKSDNETSEPKPFTYHP 349
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
507-755 1.01e-25

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 507 LEARLVDVAERQAEALFHYAVTGDVRYLMAPQRHLMTAQDENGDTGLHLGVIHSQTDAVRSLAQVLSALPGEEVLNMRND 586
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 587 LYQTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQkeggmvgfllRHREVVEL-------VDLPNTAGFC 659
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN----------GNLEIVKLlleagadVNAQDNDGNT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 660 SLHLAVLANSLCSLRDLLVSGGNVEVQERScGRTALHLATELDNVSLAGcLLLEGNADVDCCTYNGSSPLHIAAGRGSVK 739
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         250
                  ....*....|....*.
gi 1696059887 740 LTALLMAAGANPHKEN 755
Cdd:COG0666   234 IVKLLLEAGADLNAKD 249
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 826-897 3.19e-25

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08797:

Pssm-ID: 472698  Cd Length: 76  Bit Score: 99.60  E-value: 3.19e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696059887 826 KRALCQALECQG--GSWESLANTLGLGILNSAFRLSPSPASTLLDSYEVSGGMVKDLLEGLRTVDNSTALTVLQ 897
Cdd:cd08797     2 KQQLYKLLESPDpdKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIE 75
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 723-806 3.55e-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).


The actual alignment was detected with superfamily member cd22193:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 723 YNGSSPLHIAAGRGSVKLTALLMAAGANPHKENfEPLFFREDDcyvdeeeeQDEGYIPGMTPLNMAA---TPEVLEILNG 799
Cdd:cd22193    74 YEGQTALHIAIERRQGDIVALLVENGADVHAHA-KGRFFQPKY--------QGEGFYFGELPLSLAActnQPDIVQYLLE 144


                  ....*..
gi 1696059887 800 KEYKPET 806
Cdd:cd22193   145 NEHQPAD 151
 
Name Accession Description Interval E-value
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
 40-241 2.80e-129

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: 387.71  E-value: 2.80e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQCDKG 119
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 120 ICITDLQPKDCSISFPNLGILHVTKKNVSKTLEDRMTEAYRMGYNCGIVIHPEIDTIQGEVRIPRELTDHQRSMICSAAT 199
Cdd:cd07935    81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1696059887 200 KQAKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDSK 241
Cdd:cd07935   161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 42-240 3.19e-74

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: 241.06  E-value: 3.19e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  42 LQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQCDKGIC 121
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKDGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 122 ITDLQPKDCSISFPNLGILHVTKKNVSKTLEDRMTeayrmgyncgivihpeidtiqgevriprelTDHQRSMICSAATKQ 201
Cdd:pfam00554  81 EVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE------------------------------LNIDPFNVGFEALRQ 130

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1696059887 202 AKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDS 240
Cdd:pfam00554 131 IKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 248-349 1.73e-60

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: 200.62  E-value: 1.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 248 LKIVRMDRTAGCVTGGEEVYLLCDKVQKDDIQVRFYEDDETGLTWEAFGDFSPTDVHRQFAIVFKTPKYRDLNLQKPTSV 327
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80

                          90       100
                  ....*....|....*....|..
gi 1696059887 328 FVQLKRKSDNETSEPKPFTYHP 349
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 249-349 5.11e-57

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 190.85  E-value: 5.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 249 KIVRMDRTAGCVTGGEEVYLLCDKVQKDDIQVRFYEDDETGLTWEAFGDFSPTDVHRQFAIVFKTPKYRDLNLQKPTSVF 328
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80

                          90       100
                  ....*....|....*....|.
gi 1696059887 329 VQLKRKSDNETSEPKPFTYHP 349
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLP 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
507-755 1.01e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 507 LEARLVDVAERQAEALFHYAVTGDVRYLMAPQRHLMTAQDENGDTGLHLGVIHSQTDAVRSLAQVLSALPGEEVLNMRND 586
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 587 LYQTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQkeggmvgfllRHREVVEL-------VDLPNTAGFC 659
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN----------GNLEIVKLlleagadVNAQDNDGNT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 660 SLHLAVLANSLCSLRDLLVSGGNVEVQERScGRTALHLATELDNVSLAGcLLLEGNADVDCCTYNGSSPLHIAAGRGSVK 739
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         250
                  ....*....|....*.
gi 1696059887 740 LTALLMAAGANPHKEN 755
Cdd:COG0666   234 IVKLLLEAGADLNAKD 249
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
 826-897 3.19e-25

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: 99.60  E-value: 3.19e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696059887 826 KRALCQALECQG--GSWESLANTLGLGILNSAFRLSPSPASTLLDSYEVSGGMVKDLLEGLRTVDNSTALTVLQ 897
Cdd:cd08797     2 KQQLYKLLESPDpdKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIE 75
IPT smart00429
ig-like, plexins, transcription factors;
247-348 9.29e-14

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.45  E-value: 9.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  247 NLKIVRMDRTAGCVTGGEEVyLLCDKVQKDDIQVRFYEDDetgltWEAFGDFSPTdvhRQFAIVFKTPKYRDLNLQKPTS 326
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEVGV-----GEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71

                           90       100
                   ....*....|....*....|..
gi 1696059887  327 VFvqlKRKSDNETSEPKPFTYH 348
Cdd:smart00429  72 TV---GLRNGGVPSSPQPFTYV 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
661-755 3.76e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 661 LHLAVLANSLCSLRDLLVSGGNVEVQErSCGRTALHLATELDNVSLAGCLLLEGNADVDCctyNGSSPLHIAAGRGSVKL 740
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1696059887 741 TALLMAAGANPHKEN 755
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 606-790 1.86e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 606 ALVLAGADVTLSDRHGNTALHLAtqqkeggMVGFLLRHREVVEL-------VDLPNTAGFCSLHLAVLANSLCSLRDLLV 678
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHLY-------LHYSSEKVKDIVRLlleagadVNAPERCGFTPLHLYLYNATTLDVIKLLI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 679 S-GGNVEVQERsCGRTALH--LATELDNVSLAGcLLLEGNADVDCCTYNGSSPLHI--AAGRGSVKLTALLMAAGANPHK 753
Cdd:PHA03095  105 KaGADVNAKDK-VGRTPLHvyLSGFNINPKVIR-LLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYA 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696059887 754 ENFE--------PLFFREDDCYVdeEEEQDEGYIP------GMTPLNMAAT 790
Cdd:PHA03095  183 VDDRfrsllhhhLQSFKPRARIV--RELIRAGCDPaatdmlGNTPLHSMAT 231
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 590-752 2.07e-06

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: 51.55  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 590 TPLHLAVITQQKEAAEALVL-AGADVTLSDRHGNTALHLATQQKEGGMVGFLLRhrEVVELVDLPNT----AGFCSLHLA 664
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 665 VLANSLCSLRDLLVSGGNVeVQERSCGrTALHLAteldnvslAGCLLlegnadvdcctYNGSSPLHIAAGRGSVKLTALL 744
Cdd:cd22192    97 VVNQNLNLVRELIARGADV-VSPRATG-TFFRPG--------PKNLI-----------YYGEHPLSFAACVGNEEIVRLL 155


                  ....*...
gi 1696059887 745 MAAGANPH 752
Cdd:cd22192   156 IEHGADIR 163
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 521-707 2.12e-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: 45.07  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 521 ALFHYAVTGDVRYLMApqrhLMTAQDENGDTG---LHLGVIHSQtDAVRSLAQVLSALPGEEV-LNMRNDLY-------Q 589
Cdd:TIGR00870  55 ALFVAAIENENLELTE----LLLNLSCRGAVGdtlLHAISLEYV-DAVEAILLHLLAAFRKSGpLELANDQYtseftpgI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 590 TPLHLAVITQQKEAAEALVLAGADVTL--------------SDRHGNTALHLATQQKEGGMVGFLLRHREVVELVD-LPN 654
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADILTADsLGN 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696059887 655 TAgfcsLHLAVLANSL--------CSLRDLLVSGG-------NVEVQERSCGRTALHLATELDNVSLA 707
Cdd:TIGR00870 210 TL----LHLLVMENEFkaeyeelsCQMYNFALSLLdklrdskELEVILNHQGLTPLKLAAKEGRIVLF 273
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 723-806 3.55e-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: 40.93  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 723 YNGSSPLHIAAGRGSVKLTALLMAAGANPHKENfEPLFFREDDcyvdeeeeQDEGYIPGMTPLNMAA---TPEVLEILNG 799
Cdd:cd22193    74 YEGQTALHIAIERRQGDIVALLVENGADVHAHA-KGRFFQPKY--------QGEGFYFGELPLSLAActnQPDIVQYLLE 144


                  ....*..
gi 1696059887 800 KEYKPET 806
Cdd:cd22193   145 NEHQPAD 151
 
Name Accession Description Interval E-value
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
 40-241 2.80e-129

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: 387.71  E-value: 2.80e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQCDKG 119
Cdd:cd07935     1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 120 ICITDLQPKDCSISFPNLGILHVTKKNVSKTLEDRMTEAYRMGYNCGIVIHPEIDTIQGEVRIPRELTDHQRSMICSAAT 199
Cdd:cd07935    81 ICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEGGGDRQLTEREKEIIRQAAV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1696059887 200 KQAKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDSK 241
Cdd:cd07935   161 QQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
 40-241 5.50e-109

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: 334.45  E-value: 5.50e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQCDKG 119
Cdd:cd07883     1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCEDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 120 ICITDLQPKDCSISFPNLGILHVTKKNVSKTLEDRMTEAYRMGYNCGIVIHPEIDTiqgevRIPRELTDHQRSMICSAAT 199
Cdd:cd07883    81 ICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPGDLVHVDAEG-----GGDRQLTDEEQAEIRQKAK 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1696059887 200 KQAKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDSK 241
Cdd:cd07883   156 QQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
 40-241 9.24e-78

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: 251.35  E-value: 9.24e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQCDK- 118
Cdd:cd07934     1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNEs 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 119 GICITDLQPKDCSISFPNLGILHVTKKNVSKTLEDRMTEAYRmgyncgivihpeidtiqgEVRIPRELTDHQRSMICSAA 198
Cdd:cd07934    81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKL------------------RNTGPYKLTEAEERELEQEA 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1696059887 199 TKQAKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDSK 241
Cdd:cd07934   143 KELKKVMDLSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 42-240 3.19e-74

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: 241.06  E-value: 3.19e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  42 LQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQCDKGIC 121
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKDGVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 122 ITDLQPKDCSISFPNLGILHVTKKNVSKTLEDRMTeayrmgyncgivihpeidtiqgevriprelTDHQRSMICSAATKQ 201
Cdd:pfam00554  81 EVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE------------------------------LNIDPFNVGFEALRQ 130

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1696059887 202 AKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDS 240
Cdd:pfam00554 131 IKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 248-349 1.73e-60

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: 200.62  E-value: 1.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 248 LKIVRMDRTAGCVTGGEEVYLLCDKVQKDDIQVRFYEDDETGLTWEAFGDFSPTDVHRQFAIVFKTPKYRDLNLQKPTSV 327
Cdd:cd01177     1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80

                          90       100
                  ....*....|....*....|..
gi 1696059887 328 FVQLKRKSDNETSEPKPFTYHP 349
Cdd:cd01177    81 KIQLKRPSDGERSESVPFTYVP 102
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 40-241 9.77e-60

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


Pssm-ID: 143640  Cd Length: 174  Bit Score: 201.44  E-value: 9.77e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGK-QCDK 118
Cdd:cd07827     1 PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPHQLVGKtDCRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 119 GICITDLQPK-DCSISFPNLGILHVTKKNVSKTLEDRMteayrmgyNCGIVihpeidtiqgevripreltdhqRSMICSA 197
Cdd:cd07827    81 GVCEVRLGPKnNMTASFNNLGIQCVRKKDVEEALGQRI--------QLGID----------------------PFMVHKG 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1696059887 198 ATKQAKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDSK 241
Cdd:cd07827   131 PEGNASDIDLNRVRLCFQAFIEDSDGGFTLPLPPVLSNPIYDKK 174
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 249-349 5.11e-57

Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 465045  Cd Length: 102  Bit Score: 190.85  E-value: 5.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 249 KIVRMDRTAGCVTGGEEVYLLCDKVQKDDIQVRFYEDDETGLTWEAFGDFSPTDVHRQFAIVFKTPKYRDLNLQKPTSVF 328
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80

                          90       100
                  ....*....|....*....|.
gi 1696059887 329 VQLKRKSDNETSEPKPFTYHP 349
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLP 101
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 248-349 3.17e-46

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: 160.53  E-value: 3.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 248 LKIVRMDRTAGCVTGGEEVYLLCDKVQKDDIQVRFYEDDETGLTWEAFGDFSPTDVHrQFAIVFKTPKYRDLNLQKPTSV 327
Cdd:cd00602     1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEKGPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79

                          90       100
                  ....*....|....*....|..
gi 1696059887 328 FVQLKRKSDNETSEPKPFTYHP 349
Cdd:cd00602    80 PIQLVRPDDRKRSEPLTFTYTP 101
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
 40-241 6.34e-46

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: 162.66  E-value: 6.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQ-CDK 118
Cdd:cd07887     1 PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPHNLVGKEgCKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 119 GICITDLQPKDCSISFPNLGILHVTKKNVSKTL---EDRMTEAYRMGYncgivihpeidtiqgevripreltDHQrsmic 195
Cdd:cd07887    81 GVCTKKINPTEMRIVFQKLGIQCVKKKDVEESLklrEEINVDPFRTGF------------------------DHK----- 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1696059887 196 saatKQAKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDSK 241
Cdd:cd07887   132 ----DQINSIDLNVVRLCFQVFLEDENGRFTVPLPPVVSDPIYDKK 173
RHD-n_c-Rel cd07933
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ...
 40-241 4.80e-43

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: 154.26  E-value: 4.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQCDKG 119
Cdd:cd07933     1 PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPHDLVGKDCRDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 120 ICITDLQPKDCSISFPNLGILHVTKKNVSKTLEDRMTEAyrmgyncgivIHPeidtiqgeVRIPREltdhqrsmicsaAT 199
Cdd:cd07933    81 YYEAEFGPERRVLAFQNLGIQCVRRREVKEAIMLRISRG----------INP--------FNVPEE------------QL 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1696059887 200 KQAKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDSK 241
Cdd:cd07933   131 LQIEEYDLNVVRLCFQIFLPDEHGNYTTALPPIVSNPIYDNR 172
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
 40-241 1.01e-38

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: 141.93  E-value: 1.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGKQCDKG 119
Cdd:cd07885     1 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPHELVGKDCKDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 120 ICITDLQPKDCSISFPNLGILHVTKKNVSKTLEDRmteayrmgyncgivihpeIDTIQGEVRIPREltdhqrsmicsaat 199
Cdd:cd07885    81 YYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQR------------------IQTNNNPFNVPIE-------------- 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1696059887 200 KQAKEMDLSVVRLMFTAFLPDSDGGFSrRLDPVISDPIFDSK 241
Cdd:cd07885   129 EQRADYDLNAVRLCFQVTVRDPSGRLL-PLPPVLSQPIYDNR 169
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
 40-241 1.74e-35

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: 132.68  E-value: 1.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKNRKSYPQVKICNYQGLARV--VVQLVTNSKDAHLHAHSLVGKQCD 117
Cdd:cd07886     1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVtvTVCLVWKDPPHRVHPHGLVGKDCP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 118 KGICITDLQPKDCSI-SFPNLGILHVTKKNVSKTLEDRMTEAyrmgyncgivihpeIDTIQgevripreltdhqrsmicS 196
Cdd:cd07886    81 NGICQVTLNPHSSPRhSFSNLGIQCVRKREIEAAIETRLQLN--------------IDPFK------------------A 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1696059887 197 AATKQAKEMDLSVVRLMFTAFLPDSDgGFSRRLDPVISDPIFDSK 241
Cdd:cd07886   129 GSLKNHEEVDMNVVRLCFQASYRDDD-GRKDCLSPVLSEPIYDKK 172
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 40-241 2.34e-33

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: 126.01  E-value: 2.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  40 PYLQIIEQPKQRgFRFRYGCE-GPSHGGLPGASSEKNRKSYPQVKICNYQGLARVVVQLVT-NSKDAHLHAHSLVGKQCD 117
Cdd:cd07884     1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQaDDNRRKPHVHKLVGKQGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 118 KGIC-ITDLQPK---DCSISFPNLGILHVTKKNvsktledrmteayrmgyncgivihpeidtiqgevrIPRELTdhqrsm 193
Cdd:cd07884    80 DDVCdPHDIEVSpegDYVAMFQNMGIIHTAKKN-----------------------------------IPEELY------ 118

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1696059887 194 icsaatkQAKEMDLSVVRLMFTAFLPDSDGGFSRRLDPVISDPIFDSK 241
Cdd:cd07884   119 -------KKKNMNLNQVVLRFQAFAVSANGHLRPICPPVYSNPINNLK 159
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
507-755 1.01e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 507 LEARLVDVAERQAEALFHYAVTGDVRYLMAPQRHLMTAQDENGDTGLHLGVIHSQTDAVRSLAQVLSALPGEEVLNMRND 586
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 587 LYQTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQkeggmvgfllRHREVVEL-------VDLPNTAGFC 659
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN----------GNLEIVKLlleagadVNAQDNDGNT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 660 SLHLAVLANSLCSLRDLLVSGGNVEVQERScGRTALHLATELDNVSLAGcLLLEGNADVDCCTYNGSSPLHIAAGRGSVK 739
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         250
                  ....*....|....*.
gi 1696059887 740 LTALLMAAGANPHKEN 755
Cdd:COG0666   234 IVKLLLEAGADLNAKD 249
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
 826-897 3.19e-25

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: 99.60  E-value: 3.19e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696059887 826 KRALCQALECQG--GSWESLANTLGLGILNSAFRLSPSPASTLLDSYEVSGGMVKDLLEGLRTVDNSTALTVLQ 897
Cdd:cd08797     2 KQQLYKLLESPDpdKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIE 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
507-755 3.39e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 3.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 507 LEARLVDVAERQAEALFHYAVTGD---VRYLMAPQRHLMTAQDENGDTGLHLGVIHSQTDAVRSLaqvLSAlpGEEVlNM 583
Cdd:COG0666    42 LALLALALADALGALLLLAAALAGdllVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL---LEA--GADV-NA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 584 RNDLYQTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHREVVelvDLPNTAGFCSLHL 663
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV---NARDNDGETPLHL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 664 AVLANSLCSLRDLLVSGGNVEVQERScGRTALHLATELDNVSLAGcLLLEGNADVDCCTYNGSSPLHIAAGRGSVKLTAL 743
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVK-LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                         250
                  ....*....|..
gi 1696059887 744 LMAAGANPHKEN 755
Cdd:COG0666   271 LLLALLLLAAAL 282
IPT smart00429
ig-like, plexins, transcription factors;
247-348 9.29e-14

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 67.45  E-value: 9.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887  247 NLKIVRMDRTAGCVTGGEEVyLLCDKVQKDDIQVRFYEDDetgltWEAFGDFSPTdvhRQFAIVFKTPKYRDLNLQKPTS 326
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEVGV-----GEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVR 71

                           90       100
                   ....*....|....*....|..
gi 1696059887  327 VFvqlKRKSDNETSEPKPFTYH 348
Cdd:smart00429  72 TV---GLRNGGVPSSPQPFTYV 90
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 248-349 1.60e-12

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: 64.02  E-value: 1.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 248 LKIVRMDRTAGCVTGGEEVYLLCDKVQKD-DIQVRFYeddetgltweAFGDFSPTDVHrQFAIVFKTPKYRDLNlqkPTS 326
Cdd:cd00102     1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFG----------GGVPCSVLSVS-STAIVCTTPPYANPG---PGP 66

                          90       100
                  ....*....|....*....|...
gi 1696059887 327 VFVQLKRKSDNETSEPKPFTYHP 349
Cdd:cd00102    67 VEVTVDRGNGGITSSPLTFTYVP 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
661-755 3.76e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 661 LHLAVLANSLCSLRDLLVSGGNVEVQErSCGRTALHLATELDNVSLAGCLLLEGNADVDCctyNGSSPLHIAAGRGSVKL 740
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1696059887 741 TALLMAAGANPHKEN 755
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
 829-897 8.84e-12

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: 61.49  E-value: 8.84e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696059887 829 LCQALEcQGGSWESLANTLGLGILNSAFRLSPSPASTLLDSYEVSGGMVKDLLEGLRTVDNSTALTVLQ 897
Cdd:cd08310     5 LCKLLD-VGKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
 606-790 1.86e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 606 ALVLAGADVTLSDRHGNTALHLAtqqkeggMVGFLLRHREVVEL-------VDLPNTAGFCSLHLAVLANSLCSLRDLLV 678
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHLY-------LHYSSEKVKDIVRLlleagadVNAPERCGFTPLHLYLYNATTLDVIKLLI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 679 S-GGNVEVQERsCGRTALH--LATELDNVSLAGcLLLEGNADVDCCTYNGSSPLHI--AAGRGSVKLTALLMAAGANPHK 753
Cdd:PHA03095  105 KaGADVNAKDK-VGRTPLHvyLSGFNINPKVIR-LLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYA 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696059887 754 ENFE--------PLFFREDDCYVdeEEEQDEGYIP------GMTPLNMAAT 790
Cdd:PHA03095  183 VDDRfrsllhhhLQSFKPRARIV--RELIRAGCDPaatdmlGNTPLHSMAT 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
553-651 2.34e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 553 LHLGVIHSQTDAVRSLaqvlsaLPGEEVLNMRNDLYQTPLHLAVITQQKEAAEALvLAGADVTLSDrHGNTALHLATQQK 632
Cdd:pfam12796   1 LHLAAKNGNLELVKLL------LENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKD-NGRTALHYAARSG 72

                          90
                  ....*....|....*....
gi 1696059887 633 EGGMVGFLLRHREVVELVD 651
Cdd:pfam12796  73 HLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
523-618 2.51e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 523 FHYAVTGD----VRYLMaPQRHLMTAQDENGDTGLHLGVIHSQTDAVRSLAQvlsalpgEEVLNMRNDlYQTPLHLAVIT 598
Cdd:pfam12796   1 LHLAAKNGnlelVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-------HADVNLKDN-GRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 1696059887 599 QQKEAAEALVLAGADVTLSD 618
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
592-686 2.85e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 592 LHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHrEVVELVDLPNTAgfcsLHLAVLANSLC 671
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTA----LHYAARSGHLE 75

                          90
                  ....*....|....*
gi 1696059887 672 SLRDLLVSGGNVEVQ 686
Cdd:pfam12796  76 IVKLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 589-751 3.87e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 589 QTPLHLAVITQQKEAAEALVLAGA---DVTLSDrhGNTALHLATQQKEGGMVGFLLRHREVVelvDLPNTAGFCSLHLAV 665
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADP---DIPNTDKFSPLHLAV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 666 LANSlcslrdllVSGGNVEVQERSCgrtalhlaTELDnvslagclllegnadvDCCtynGSSPLHIAAGRGSVKLTALLM 745
Cdd:PHA02875  144 MMGD--------IKGIELLIDHKAC--------LDIE----------------DCC---GCTPLIIAMAKGDIAICKMLL 188


                  ....*.
gi 1696059887 746 AAGANP 751
Cdd:PHA02875  189 DSGANI 194
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 590-720 5.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 5.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 590 TPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHREVvelVDLPNTAGFCSLHLAVLANS 669
Cdd:PHA02875  104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC---LDIEDCCGCTPLIIAMAKGD 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696059887 670 LCSLRDLLVSGGNVEVQERSCGRTALHLATELDNVSLAGCLLLEGnadVDC 720
Cdd:PHA02875  181 IAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRG---ADC 228
PHA03095 PHA03095
ankyrin-like protein; Provisional
 544-751 6.62e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.19  E-value: 6.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 544 AQDENGDTGLHLGVIHSQTDAVrslAQVLSALpGEEVlNMRNDLYQTPLH--LAVITQQKEAAEALVLAGADVTLSDRHG 621
Cdd:PHA03095   78 APERCGFTPLHLYLYNATTLDV---IKLLIKA-GADV-NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYG 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 622 NTALHLatqqkeggmvgFLLRHREVVELVDLPNTAGfCSLH---------LAVLANSL----CSLRDLLVSGGNVEVQER 688
Cdd:PHA03095  153 MTPLAV-----------LLKSRNANVELLRLLIDAG-ADVYavddrfrslLHHHLQSFkpraRIVRELIRAGCDPAATDM 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696059887 689 ScGRTALH-LATELDNVSLAGCLLLEGNADVDCCTYNGSSPLHIAAGRGSVKLTALLMAAGANP 751
Cdd:PHA03095  221 L-GNTPLHsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI 283
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 581-750 1.95e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 581 LNMRNDLYQTPLHL-----AVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGG--MVGFLLRHREVVELVdlp 653
Cdd:PHA03100   61 INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIK--- 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 654 NTAGFCSLHLAVLAN----SLCSLrdLLVSGGNVEVQER---------------SCGRTALHLATELDNVSLAGcLLLEG 714
Cdd:PHA03100  138 NSDGENLLHLYLESNkidlKILKL--LIDKGVDINAKNRvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVK-YLLDL 214

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1696059887 715 NADVDCCTYNGSSPLHIAAGRGSVKLTALLMAAGAN 750
Cdd:PHA03100  215 GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
512-658 3.35e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.03  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 512 VDVAERQAEALFHYAVTGD----VRYLMA----PqrhlmTAQDENGDTGLHLGVIHSQTDAVRSLaqvLSAlpGEEVlNM 583
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGnleiVKLLLEagadV-----NARDNDGETPLHLAAENGHLEIVKLL---LEA--GADV-NA 214

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696059887 584 RNDLYQTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHREVVELVDLPNTAGF 658
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 581-732 5.27e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 5.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 581 LNMRNDLYQTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLrhrEVVELVDLPNTAGFCS 660
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL---EKGAYANVKDNNGESP 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696059887 661 LHLAVLANSLCSLRDLLVSGGNVEVQERScGRTALHLATeLDNVSLAGclLLEGNADVDCCTYNGSSPLHIA 732
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAI-IHNRSAIE--LLINNASINDQDIDGSTPLHHA 261
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 577-732 5.90e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 5.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 577 GEEVLNMRNDLYQTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHREVvelVDLPNTA 656
Cdd:PHA02878  157 GADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKC 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696059887 657 GFCSLHLAV-LANSLCSLRDLLVSGGNVEVQERSCGRTALHLATELDNVSLagcLLLEGNADVDCCTYNGSSPLHIA 732
Cdd:PHA02878  234 GNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK---LLLEYGADINSLNSYKLTPLSSA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 581-757 1.09e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 581 LNMRNDLYQTPLHL-AVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQqkeggmvgfLLRHREVV----ELVDLPNT 655
Cdd:PHA02876  300 VNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAST---------LDRNKDIVitllELGANVNA 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 656 AGFCS---LHLAVLANSLCSLRDLLVSGGNVEVQERSCGrTALHLATELDNVSLAGCLLLEGNADVDCCTYNGSSPLHIA 732
Cdd:PHA02876  371 RDYCDktpIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449

                         170       180
                  ....*....|....*....|....*.
gi 1696059887 733 AGRG-SVKLTALLMAAGANPHKENFE 757
Cdd:PHA02876  450 CKKNcKLDVIEMLLDNGADVNAINIQ 475
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 589-729 1.48e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 589 QTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHREVVElvdlPNTAGFCsLHLAVLAN 668
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD----PHAAGDL-LCTAAKRN 633

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696059887 669 SLCSLRDLLVSGGNVEVQERScGRTALHLATELDNVSLAGCLLLEGnADVDCC-TYNGSSPL 729
Cdd:PLN03192  634 DLTAMKELLKQGLNVDSEDHQ-GATALQVAMAEDHVDMVRLLIMNG-ADVDKAnTDDDFSPT 693
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 590-752 2.07e-06

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: 51.55  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 590 TPLHLAVITQQKEAAEALVL-AGADVTLSDRHGNTALHLATQQKEGGMVGFLLRhrEVVELVDLPNT----AGFCSLHLA 664
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPMTsdlyQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 665 VLANSLCSLRDLLVSGGNVeVQERSCGrTALHLAteldnvslAGCLLlegnadvdcctYNGSSPLHIAAGRGSVKLTALL 744
Cdd:cd22192    97 VVNQNLNLVRELIARGADV-VSPRATG-TFFRPG--------PKNLI-----------YYGEHPLSFAACVGNEEIVRLL 155


                  ....*...
gi 1696059887 745 MAAGANPH 752
Cdd:cd22192   156 IEHGADIR 163
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 595-745 2.51e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 595 AVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHREVVElVDLPNTAGfcSLHLAVLANSLCSLR 674
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPD-VKYPDIES--ELHDAVEEGDVKAVE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1696059887 675 DLLVSGGNVEVQERSCGRTALHLATELDNVSLAGCLLLEGnADVDCCTYNGSSPLHIAAGRGSVKLTALLM 745
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
 829-884 5.27e-06

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: 45.20  E-value: 5.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1696059887 829 LCQALE--CQGGSWESLANTLGLGILNSAFRLSPSPASTLLDSYEVSGGMVKDLLEGL 884
Cdd:cd08798     5 LEQLLNdtQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEAL 62
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 661-762 5.50e-06

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: 50.01  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 661 LHLAVLANSLCSLRDLLVSGGnVEVQER-SCGRTALHLATELDNVSLAgCLLLEG-----NADVDCCTYNGSSPLHIAAG 734
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPS-CDLFQRgALGETALHVAALYDNLEAA-VVLMEAapelvNEPMTSDLYQGETALHIAVV 98

                          90       100
                  ....*....|....*....|....*...
gi 1696059887 735 RGSVKLTALLMAAGANPHKENFEPLFFR 762
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGTFFR 126
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 250-349 7.05e-06

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: 45.55  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 250 IVRMDRTAGCVTGGEEVYLLCDKVQKDDiQVRFYED-DETGLTWEAFGDFSPTDVHrQFAIVFKTPKYRDLNLQKPTSVF 328
Cdd:cd01178     4 IEKKSLNSCSVNGGEELFLTGKNFLKDS-KVVFQEKgQDGEAQWEAEATIDKEKSH-QNHLVVEVPPYHNKHVAAPVQVQ 81

                          90       100
                  ....*....|....*....|....
gi 1696059887 329 VQL---KRKSdnetSEPKPFTYHP 349
Cdd:cd01178    82 FYVvngKRKR----SQPQTFTYTP 101
Ank_2 pfam12796
Ankyrin repeats (3 copies);
695-797 9.67e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 9.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 695 LHLATELDNVSLAgCLLLEGNADVDCCTYNGSSPLHIAAGRGSVKLTALLMaaganphkenfeplffreDDCYVDEEEEq 774
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL------------------EHADVNLKDN- 60

                          90       100
                  ....*....|....*....|....*.
gi 1696059887 775 degyipGMTPLNMAAT---PEVLEIL 797
Cdd:pfam12796  61 ------GRTALHYAARsghLEIVKLL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 543-651 1.03e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 543 TAQDENGDTGLHLGVIHSQTDavRSL-AQVLSAlpGEEVlNMRNDLYQTPLHLAVITQQKEAAEALVLAGADVTLSDRHG 621
Cdd:PHA03095  216 AATDMLGNTPLHSMATGSSCK--RSLvLPLLIA--GISI-NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290

                          90       100       110
                  ....*....|....*....|....*....|
gi 1696059887 622 NTALHLATQQKEGGMVGFLLRHREVVELVD 651
Cdd:PHA03095  291 NTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 696-779 1.33e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 696 HLATELDNVSLAgcLLLEGNADVDCCTYNGSSPLHIAAGRGSVKLTALLMAAGANPhkenfePLFFREDDCYVDEEEEQD 775
Cdd:PTZ00322   88 QLAASGDAVGAR--ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP------TLLDKDGKTPLELAEENG 159


                  ....
gi 1696059887 776 EGYI 779
Cdd:PTZ00322  160 FREV 163
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 512-665 1.79e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 512 VDVAERQA--EALFHYAVTGD----VRYLMAPQRHL----MTAQDENGDTGLHLGVIHSQTDAVRSL----AQVLSA--- 574
Cdd:cd22192    42 CDLFQRGAlgETALHVAALYDnleaAVVLMEAAPELvnepMTSDLYQGETALHIAVVNQNLNLVRELiargADVVSPrat 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 575 ----LPGEevlnmRNDLY--QTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALH-LATQQ---KEGGMVGFLL--- 641
Cdd:cd22192   122 gtffRPGP-----KNLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQPnktFACQMYDLILsyd 196

                         170       180
                  ....*....|....*....|....
gi 1696059887 642 RHREVVELVDLPNTAGFCSLHLAV 665
Cdd:cd22192   197 KEDDLQPLDLVPNNQGLTPFKLAA 220
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 542-738 2.01e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 542 MTAQDENGDTGLHLGVIHS-QTDAVRSLAQVlsalpGEEVlNMRNDLYQTPLHLA-VITQQKEAAEALVLAGADVTLSDR 619
Cdd:PHA02876  300 VNAKNIKGETPLYLMAKNGyDTENIRTLIML-----GADV-NAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDY 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 620 HGNTALHLATQQKEGGMVGFLLRHREVVELvdLPNTAGfCSLHLAVLA-NSLCSLRDLLVSGGNVEVQERSCGrTALHLA 698
Cdd:PHA02876  374 CDKTPIHYAAVRNNVVIINTLLDYGADIEA--LSQKIG-TALHFALCGtNPYMSVKTLIDRGANVNSKNKDLS-TPLHYA 449

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1696059887 699 TELDNVSLAGCLLLEGNADVDCCTYNGSSPLHIAAGRGSV 738
Cdd:PHA02876  450 CKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI 489
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 589-643 5.32e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1696059887 589 QTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRH 643
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
581-628 6.97e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 6.97e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1696059887 581 LNMRNDLYQTPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLA 628
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
 825-897 1.06e-04

Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in Uncoordinated-5 (UNC-5) homolog family, which includes Unc5A, B, C and D in vertebrates. UNC5 proteins are receptors for secreted netrins (netrin-1, -3 and -4) that are involved in diverse processes like axonal guidance, neuronal migration, blood vessel patterning, and apoptosis. They are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260051  Cd Length: 83  Bit Score: 41.49  E-value: 1.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696059887 825 TKRALCQALECQ---GGSWESLANTLGLGILNSAFRLSPSPASTLLDSYEV---SGGMVKDLLEGLRTVDNSTALTVLQ 897
Cdd:cd08781     5 IRQKLCSLLDPPnarGNDWRLLAQKLSVDRYINYFATKPSPTEVILDLWEArnrDDGALNSLAAILREMGRHDAATILE 83
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 618-749 1.35e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 43.33  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 618 DRHGNTALHLATqqKEGGMVGfLLRHREVVE-----LVDLPNTAGFCSLHLAV---LANSLCSLRDLLVSGGNVEVQERS 689
Cdd:PHA02736   14 DIEGENILHYLC--RNGGVTD-LLAFKNAISdenryLVLEYNRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERV 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 690 CGRTALHLATELDNVSLAGCLLLEGNADVDCCTYNGSSPLHIAAGRGSVKLTALLMAAGA 749
Cdd:PHA02736   91 FGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 599-808 1.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 599 QQKE--AAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHREVVELVDLPntaGFCSLHLAVLANSLCSLRDL 676
Cdd:PHA02876  154 QQDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD---DLSVLECAVDSKNIDTIKAI 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 677 LVSGGNVEvqerscgRTALHLATELDNVSLAGCLLL-EGNADVDCCTYNGSSPLHIAAGRGSV-KLTALLMAAGANPHKE 754
Cdd:PHA02876  231 IDNRSNIN-------KNDLSLLKAIRNEDLETSLLLyDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAK 303

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696059887 755 NFE---PLFFREDDCYVDEE-----------EEQDEGYIpgmTPLNMAATPE--------VLEI---LNGKEYKPETTI 808
Cdd:PHA02876  304 NIKgetPLYLMAKNGYDTENirtlimlgadvNAADRLYI---TPLHQASTLDrnkdivitLLELganVNARDYCDKTPI 379
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 600-732 1.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 600 QKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHREVVELVDLpntAGFCSLHLAVLANSLCSLRDLLVS 679
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD---NGCYPIHIAIKHNFFDIIKLLLEK 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1696059887 680 GGNVEVQERScGRTALHLATELDNVSLAGCLLLEGNADVDCCTyNGSSPLHIA 732
Cdd:PHA02874  180 GAYANVKDNN-GESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNA 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
691-744 1.81e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1696059887 691 GRTALHLATELDNVSLAGcLLLEGNADVDCCTYNGSSPLHIAAGRGSVKLTALL 744
Cdd:pfam13637   1 ELTALHAAAASGHLELLR-LLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 521-707 2.12e-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: 45.07  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 521 ALFHYAVTGDVRYLMApqrhLMTAQDENGDTG---LHLGVIHSQtDAVRSLAQVLSALPGEEV-LNMRNDLY-------Q 589
Cdd:TIGR00870  55 ALFVAAIENENLELTE----LLLNLSCRGAVGdtlLHAISLEYV-DAVEAILLHLLAAFRKSGpLELANDQYtseftpgI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 590 TPLHLAVITQQKEAAEALVLAGADVTL--------------SDRHGNTALHLATQQKEGGMVGFLLRHREVVELVD-LPN 654
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADILTADsLGN 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696059887 655 TAgfcsLHLAVLANSL--------CSLRDLLVSGG-------NVEVQERSCGRTALHLATELDNVSLA 707
Cdd:TIGR00870 210 TL----LHLLVMENEFkaeyeelsCQMYNFALSLLdklrdskELEVILNHQGLTPLKLAAKEGRIVLF 273
Ank_4 pfam13637
Ankyrin repeats (many copies);
590-641 2.43e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1696059887 590 TPLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLL 641
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 580-750 3.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 580 VLNMRNDLYQTPLHL--AVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLRHREVVelVDLPNTAG 657
Cdd:PHA02876  230 IIDNRSNINKNDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGAD--VNAKNIKG 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 658 FCSLHL-AVLANSLCSLRDLLVSGGNVEVQERSCgRTALHLATELDNVSLAGCLLLEGNADVDCCTYNGSSPLHIAAGRG 736
Cdd:PHA02876  308 ETPLYLmAKNGYDTENIRTLIMLGADVNAADRLY-ITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                         170
                  ....*....|....
gi 1696059887 737 SVKLTALLMAAGAN 750
Cdd:PHA02876  387 NVVIINTLLDYGAD 400
PHA02741 PHA02741
hypothetical protein; Provisional
 641-744 1.13e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 40.80  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 641 LRHREVVELVDLPNTAGFCSLHLAVLANS---LCSLRDLLVS-GGNVEVQERSCGRTALHLATELDNVSLAGCLLLEGNA 716
Cdd:PHA02741   44 IRGDCHAAALNATDDAGQMCIHIAAEKHEaqlAAEIIDHLIElGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQPGI 123

                          90       100
                  ....*....|....*....|....*...
gi 1696059887 717 DVDCCTYNGSSPLHIAAGRGSVKLTALL 744
Cdd:PHA02741  124 DLHFCNADNKSPFELAIDNEDVAMMQIL 151
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
 40-114 1.59e-03

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: 40.33  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696059887  40 PYLQIIEQPKQRgFRFRY---GCEGPSHGglpgasseKNRKSYPQVKICNYQGLARVVVQLVTNSKDAHLHAHSLVGK 114
Cdd:cd07927     1 YELRIEVQPEPH-HRARYeteGSRGAVKA--------PSTGGFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHR 69
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 661-759 1.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 661 LHLAVLANSLCSLRDLLVSGGNVEVQERScGRTALHLATELDNVSLAGcLLLEGNADVDCCTYNGSSPLHIAAGRGSVKL 740
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIK-LLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          90       100
                  ....*....|....*....|..
gi 1696059887 741 TALLMAAGANPH---KENFEPL 759
Cdd:PHA02874  206 IKLLIDHGNHIMnkcKNGFTPL 227
PHA02741 PHA02741
hypothetical protein; Provisional
 530-658 2.71e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.64  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 530 DVRYLMAPQRHLMTAQDENGDTGLHLGVIHSQTDAVRSLAQVLSALPGEEVLNMRNDLYQTPLHLAVITQQKEAA----E 605
Cdd:PHA02741    2 ESPHFMTCLEEMIAEKNSEGENFFHEAARCGCFDIIARFTPFIRGDCHAAALNATDDAGQMCIHIAAEKHEAQLAaeiiD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1696059887 606 ALVLAGADVTLSDR-HGNTALHLATQQKEGGMVGFLLRHREV-VELVDLPNTAGF 658
Cdd:PHA02741   82 HLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQPGIdLHFCNADNKSPF 136
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 723-806 3.55e-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: 40.93  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 723 YNGSSPLHIAAGRGSVKLTALLMAAGANPHKENfEPLFFREDDcyvdeeeeQDEGYIPGMTPLNMAA---TPEVLEILNG 799
Cdd:cd22193    74 YEGQTALHIAIERRQGDIVALLVENGADVHAHA-KGRFFQPKY--------QGEGFYFGELPLSLAActnQPDIVQYLLE 144


                  ....*..
gi 1696059887 800 KEYKPET 806
Cdd:cd22193   145 NEHQPAD 151
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 591-750 4.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 591 PLHLAVITQQKEAAEALVLAGADVTLSDRHGNTALHLATQQKEGGMVGFLLR----------HREVVELVDLPNTAGFCS 660
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytLVAIKDAFNNRNVEIFKI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 661 LHLAVLANS-------LCS-----------LRDLLVSGGNVEVQERSCGRTALHLATELDNVSLAGCLLLEGnADVDCCT 722
Cdd:PHA02878  120 ILTNRYKNIqtidlvyIDKkskddiieaeiTKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYG-ANVNIPD 198

                         170       180
                  ....*....|....*....|....*...
gi 1696059887 723 YNGSSPLHIAAGRGSVKLTALLMAAGAN 750
Cdd:PHA02878  199 KTNNSPLHHAVKHYNKPIVHILLENGAS 226
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 724-755 4.37e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 4.37e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1696059887 724 NGSSPLHIAAGR-GSVKLTALLMAAGANPHKEN 755
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 666-749 4.79e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.03  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 666 LANSLCSLRDLLVSGGNVEVQERSCGRTALHLATELDNVSLAGCLLLEGNADVDCCTYNGSSPLHIAAGRGSVKLTALLM 745
Cdd:PHA02743   69 RANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIAYKMRDRRMMEILR 148


                  ....
gi 1696059887 746 AAGA 749
Cdd:PHA02743  149 ANGA 152
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 660-760 5.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.42  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696059887 660 SLHLAVLANSLCSLRDLLVSGGNVeVQERSCGRTALHLAT-----ELDNVSLAgCLLLEGNADVDCCTYNGSSPLHIAAG 734
Cdd:PHA03100   38 PLYLAKEARNIDVVKILLDNGADI-NSSTKNNSTPLHYLSnikynLTDVKEIV-KLLLEYGANVNAPDNNGITPLLYAIS 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 1696059887 735 R--GSVKLTALLMAAGA--NPHKENFEPLF 760
Cdd:PHA03100  116 KksNSYSIVEYLLDNGAnvNIKNSDGENLL 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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