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Conserved domains on  [gi|74142437|dbj|BAE31972|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

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 ...
1-127 2.96e-74

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 cd07934:

Pssm-ID: 447596  Cd Length: 185  Bit Score: 239.80  E-value: 2.96e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRAHAHSLVGKQCSELGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSK-PQGLTEAERRE 79
Cdd:cd07934  58 LVTHTDPPRVHAHSLVGKHCNESGNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERE 137
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 74142437  80 LEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 127
Cdd:cd07934 138 LEQEAKELKKVMDLSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
134-233 1.68e-59

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


:

Pssm-ID: 238582  Cd Length: 102  Bit Score: 196.77  E-value: 1.68e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 134 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 211
Cdd:cd01177   1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                        90       100
                ....*....|....*....|..
gi 74142437 212 FLQLKRKRGGDVSDSKQFTYYP 233
Cdd:cd01177  81 KIQLKRPSDGERSESVPFTYVP 102
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
680-755 1.82e-32

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: 120.31  E-value: 1.82e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74142437 680 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLLKG 755
Cdd:cd08798   1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
359-612 8.47e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 8.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 359 LAQRSARALLDYGVTADARALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQIAHviyhaqYLGVINLTNHLHQTPLH 438
Cdd:COG0666  19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA------AGADINAKDDGGNTLLH 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 439 LAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARS 518
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG--NLEIVKLLLEAGAD-----VNAQDNDGNTPLHLAAANGN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 519 PECLDLLVDCGAEVEAPERQgGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGA 598
Cdd:COG0666 166 LEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                       250
                ....*....|....
gi 74142437 599 DIHAENEEPLCPLP 612
Cdd:COG0666 244 DLNAKDKDGLTALL 257
 
Name Accession Description Interval E-value
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
1-127 2.96e-74

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: 239.80  E-value: 2.96e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRAHAHSLVGKQCSELGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSK-PQGLTEAERRE 79
Cdd:cd07934  58 LVTHTDPPRVHAHSLVGKHCNESGNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERE 137
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 74142437  80 LEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 127
Cdd:cd07934 138 LEQEAKELKKVMDLSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
134-233 1.68e-59

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


Pssm-ID: 238582  Cd Length: 102  Bit Score: 196.77  E-value: 1.68e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 134 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 211
Cdd:cd01177   1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                        90       100
                ....*....|....*....|..
gi 74142437 212 FLQLKRKRGGDVSDSKQFTYYP 233
Cdd:cd01177  81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
135-234 9.32e-56

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


Pssm-ID: 465045  Cd Length: 102  Bit Score: 186.61  E-value: 9.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   135 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVF 212
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 74142437   213 LQLKRKRGGDVSDSKQFTYYPL 234
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
1-126 1.93e-41

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: 148.99  E-value: 1.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437     1 LVTHSDPPRAHAHSLVGKQCSElGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQrqrlrskpqgLTEAERReL 80
Cdd:pfam00554  56 LVTKDEPHRPHPHSLVGKDCKD-GVCEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-V 123
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 74142437    81 EQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDS 126
Cdd:pfam00554 124 GFEALRQIKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
680-755 1.82e-32

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: 120.31  E-value: 1.82e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74142437 680 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLLKG 755
Cdd:cd08798   1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
359-612 8.47e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 8.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 359 LAQRSARALLDYGVTADARALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQIAHviyhaqYLGVINLTNHLHQTPLH 438
Cdd:COG0666  19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA------AGADINAKDDGGNTLLH 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 439 LAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARS 518
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG--NLEIVKLLLEAGAD-----VNAQDNDGNTPLHLAAANGN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 519 PECLDLLVDCGAEVEAPERQgGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGA 598
Cdd:COG0666 166 LEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                       250
                ....*....|....
gi 74142437 599 DIHAENEEPLCPLP 612
Cdd:COG0666 244 DLNAKDKDGLTALL 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
365-611 5.96e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 5.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  365 RALLDYGVTADARallagqrhllmaqDENGDTPLHLAIIHGQTgvIEQIAHVIYHaqylGV-INLTNHLHQTPLH--LAV 441
Cdd:PHA03095  67 RLLLEAGADVNAP-------------ERCGFTPLHLYLYNATT--LDVIKLLIKA----GAdVNAKDKVGRTPLHvyLSG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  442 ITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAAPELLQALLRSGAHavpqiLHMPDFEGLYPVHlaVHARS--- 518
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLH--HHLQSfkp 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  519 -PECLDLLVDCGAEVEAPERqGGRTALHLATeMEELGLVTHLVTKLHAN--VNARTFAGNTPLHLAAGLGSPTLTRLLLK 595
Cdd:PHA03095 201 rARIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIA 278
                        250
                 ....*....|....*.
gi 74142437  596 AGADIHAENEEPLCPL 611
Cdd:PHA03095 279 LGADINAVSSDGNTPL 294
IPT smart00429
ig-like, plexins, transcription factors;
133-232 1.96e-18

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 80.54  E-value: 1.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437    133 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKMKIERPVTVF 212
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 74142437    213 LQlkrkRGGDV-SDSKQFTYY 232
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
511-604 2.37e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 2.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   511 HLAVHARSPECLDLLVDCGAEVEApERQGGRTALHLATEMEELGLVTHLVTklHANVNARTFaGNTPLHLAAGLGSPTLT 590
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDN-GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 74142437   591 RLLLKAGADIHAEN 604
Cdd:pfam12796  78 KLLLEKGADINVKD 91
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
678-756 1.47e-09

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 55.49  E-value: 1.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437    678 DAALQNLEQLLDGPeAQGSWAELAERLGLRSLV------DTYRKTPSPSGSLLRSYKLAGG---DLVGLLEALSDMGLHE 748
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSEADidqirtEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 74142437    749 GVRLLKGP 756
Cdd:smart00005  81 AVELLRSE 88
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
426-605 7.24e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 56.24  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   426 INLTNHLHQTPLHLAVITGQTR-VVSFLLQVGADPTLldrhGDSALHLA-LRAGAAAPELLQALLRSGAHAVPQILhMPD 503
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAIsLEYVDAVEAILLHLLAAFRKSGPLEL-AND 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   504 ------FEGLYPVHLAVHARSPECLDLLVDCGAEVEApeRQGGRTALhlatEMEELGLVTHlvtklhanvnartfaGNTP 577
Cdd:TIGR00870 120 qytsefTPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFV----KSQGVDSFYH---------------GESP 178
                         170       180
                  ....*....|....*....|....*...
gi 74142437   578 LHLAAGLGSPTLTRLLLKAGADIHAENE 605
Cdd:TIGR00870 179 LNAAACLGSPSIVALLSEDPADILTADS 206
Death pfam00531
Death domain;
682-754 5.66e-07

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 48.13  E-value: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   682 QNLEQLLDGPEAQG-SWAELAERLGLRSL-VDT----YRKTPSPSGSLLRSYKLAGG---DLVGLLEALSDMGLHEGVRL 752
Cdd:pfam00531   2 KQLDRLLDPPPPLGkDWRELARKLGLSENeIDEieseNPRLRSQTYELLRLWEQREGknaTVGTLLEALRKLGRRDAAEK 81

                  ..
gi 74142437   753 LK 754
Cdd:pfam00531  82 IQ 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
420-643 6.75e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 6.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 420 AQYLGVINL--TNHLHQTPLHLAVITGQTRVVSFLL-QVGADPTLLDRHGDSALHLALRAGAAapELLQALLRsgahAVP 496
Cdd:cd22192   2 AQMLDELHLlqQKRISESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNL--EAAVVLME----AAP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 497 QILHMPDFEGLYPvhlavharspecldllvdcgaeveaperqgGRTALHLATEMEELGLVTHLVTKLHANVNART----- 571
Cdd:cd22192  76 ELVNEPMTSDLYQ------------------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtff 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 572 --------FAGNTPLHLAAGLGSPTLTRLLLKAGADIHAE---------------NEEPLCPLPSPSTSgSDSDSEGPER 628
Cdd:cd22192 126 rpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQdslgntvlhilvlqpNKTFACQMYDLILS-YDKEDDLQPL 204
                       250
                ....*....|....*
gi 74142437 629 DTQRNFRGHTPLDLT 643
Cdd:cd22192 205 DLVPNNQGLTPFKLA 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
574-602 8.84e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 8.84e-04
                           10        20
                   ....*....|....*....|....*....
gi 74142437    574 GNTPLHLAAGLGSPTLTRLLLKAGADIHA 602
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
1-127 2.96e-74

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: 239.80  E-value: 2.96e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRAHAHSLVGKQCSELGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSK-PQGLTEAERRE 79
Cdd:cd07934  58 LVTHTDPPRVHAHSLVGKHCNESGNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERE 137
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 74142437  80 LEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 127
Cdd:cd07934 138 LEQEAKELKKVMDLSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
1-127 7.95e-67

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: 220.04  E-value: 7.95e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRAHAHSLVGKQCSElGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSKPQ---------- 70
Cdd:cd07883  58 LVTNSEPPRLHAHSLVGKHCED-GICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPgdlvhvdaeg 136
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74142437  71 ----GLTEAERRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 127
Cdd:cd07883 137 ggdrQLTDEEQAEIRQKAKQQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
134-233 1.68e-59

IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation.


Pssm-ID: 238582  Cd Length: 102  Bit Score: 196.77  E-value: 1.68e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 134 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 211
Cdd:cd01177   1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                        90       100
                ....*....|....*....|..
gi 74142437 212 FLQLKRKRGGDVSDSKQFTYYP 233
Cdd:cd01177  81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
135-234 9.32e-56

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


Pssm-ID: 465045  Cd Length: 102  Bit Score: 186.61  E-value: 9.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   135 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVF 212
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 74142437   213 LQLKRKRGGDVSDSKQFTYYPL 234
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
134-233 7.92e-45

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


Pssm-ID: 238336  Cd Length: 101  Bit Score: 156.29  E-value: 7.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 134 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYE--DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKMKIERPVTV 211
Cdd:cd00602   1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEkgPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79
                        90       100
                ....*....|....*....|..
gi 74142437 212 FLQLKRKRGGDVSDSKQFTYYP 233
Cdd:cd00602  80 PIQLVRPDDRKRSEPLTFTYTP 101
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
1-126 1.93e-41

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: 148.99  E-value: 1.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437     1 LVTHSDPPRAHAHSLVGKQCSElGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQrqrlrskpqgLTEAERReL 80
Cdd:pfam00554  56 LVTKDEPHRPHPHSLVGKDCKD-GVCEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-V 123
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 74142437    81 EQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDS 126
Cdd:pfam00554 124 GFEALRQIKDMDLNVVRLCFQAFLPDTRGNFTTPLPPVVSNPIYDK 169
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
1-127 4.70e-40

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: 145.59  E-value: 4.70e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRAHAHSLVGK-QCSElGVCAVSVGPK-DMTAQFNNLGVLHVTKKNMMEIMIQKLQRQRLRSKpqglteaerr 78
Cdd:cd07827  58 LVTKDDPPKPHPHQLVGKtDCRD-GVCEVRLGPKnNMTASFNNLGIQCVRKKDVEEALGQRIQLGIDPFM---------- 126
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 74142437  79 eLEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 127
Cdd:cd07827 127 -VHKGPEGNASDIDLNRVRLCFQAFIEDSDGGFTLPLPPVLSNPIYDKK 174
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
1-127 1.03e-33

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: 128.47  E-value: 1.03e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRAHAHSLVGKQCsELGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEI----MIQKLQR-------------- 62
Cdd:cd07935  58 LVTNGKNIHLHAHSLVGKHC-EDGICTVTAGPKDMVVGFANLGILHVTKKKVFETlearMTEACKKgynpgllvhpelay 136
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74142437  63 -QRLRSKPQGLTEAERRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 127
Cdd:cd07935 137 lQAEGGGDRQLTEREKEIIRQAAVQQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
680-755 1.82e-32

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: 120.31  E-value: 1.82e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74142437 680 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLLKG 755
Cdd:cd08798   1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
359-612 8.47e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 8.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 359 LAQRSARALLDYGVTADARALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQIAHviyhaqYLGVINLTNHLHQTPLH 438
Cdd:COG0666  19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA------AGADINAKDDGGNTLLH 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 439 LAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARS 518
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG--NLEIVKLLLEAGAD-----VNAQDNDGNTPLHLAAANGN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 519 PECLDLLVDCGAEVEAPERQgGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGA 598
Cdd:COG0666 166 LEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                       250
                ....*....|....
gi 74142437 599 DIHAENEEPLCPLP 612
Cdd:COG0666 244 DLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
342-606 3.78e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 3.78e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 342 ALDTLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQ-IAHviyha 420
Cdd:COG0666  35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLlLEA----- 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 421 qylGV-INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAHavpqiL 499
Cdd:COG0666 110 ---GAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG--NLEIVKLLLEAGAD-----V 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 500 HMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQgGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLH 579
Cdd:COG0666 180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALL 257
                       250       260
                ....*....|....*....|....*..
gi 74142437 580 LAAGLGSPTLTRLLLKAGADIHAENEE 606
Cdd:COG0666 258 LAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
386-611 1.23e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 1.23e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 386 LLMAQDENGDTPLHLAIIHGQTGVIEQIAHVIYHAQYLGVINLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRH 465
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 466 GDSALHLALRAGAAapELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQGgRTALH 545
Cdd:COG0666  87 GNTLLHAAARNGDL--EIVKLLLEAGAD-----VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG-NTPLH 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74142437 546 LATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADIHAENEEPLCPL 611
Cdd:COG0666 159 LAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
364-576 1.93e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.18  E-value: 1.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 364 ARALLDYGVTADARallagqrhllmaqDENGDTPLHLAIIHGQTGVIEQ-IAHviyhaqylGV-INLTNHLHQTPLHLAV 441
Cdd:COG0666 103 VKLLLEAGADVNAR-------------DKDGETPLHLAAYNGNLEIVKLlLEA--------GAdVNAQDNDGNTPLHLAA 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 442 ITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALLRSGAhavpqILHMPDFEGLYPVHLAVHARSPEC 521
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG--HLEIVKLLLEAGA-----DVNAKDNDGKTALDLAAENGNLEI 234
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74142437 522 LDLLVDCGAEVEAPERQGGrTALHLATEMEELGLVTHLVTKLHANVNARTFAGNT 576
Cdd:COG0666 235 VKLLLEAGADLNAKDKDGL-TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
413-611 9.12e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 9.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 413 IAHVIYHAQYLGVINLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAAPELLqaLLRSGA 492
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALL--LLAAGA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 493 havpqILHMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQGgRTALHLATEMEELGLVTHLVtKLHANVNARTF 572
Cdd:COG0666  79 -----DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-ETPLHLAAYNGNLEIVKLLL-EAGADVNAQDN 151
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 74142437 573 AGNTPLHLAAGLGSPTLTRLLLKAGADIHAENEEPLCPL 611
Cdd:COG0666 152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
365-611 5.96e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 5.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  365 RALLDYGVTADARallagqrhllmaqDENGDTPLHLAIIHGQTgvIEQIAHVIYHaqylGV-INLTNHLHQTPLH--LAV 441
Cdd:PHA03095  67 RLLLEAGADVNAP-------------ERCGFTPLHLYLYNATT--LDVIKLLIKA----GAdVNAKDKVGRTPLHvyLSG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  442 ITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAAPELLQALLRSGAHavpqiLHMPDFEGLYPVHlaVHARS--- 518
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLH--HHLQSfkp 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  519 -PECLDLLVDCGAEVEAPERqGGRTALHLATeMEELGLVTHLVTKLHAN--VNARTFAGNTPLHLAAGLGSPTLTRLLLK 595
Cdd:PHA03095 201 rARIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIA 278
                        250
                 ....*....|....*.
gi 74142437  596 AGADIHAENEEPLCPL 611
Cdd:PHA03095 279 LGADINAVSSDGNTPL 294
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
680-753 1.78e-19

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: 83.06  E-value: 1.78e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74142437 680 ALQNLEQLLDGpeaQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLL 753
Cdd:cd08310   1 TRLRLCKLLDV---GKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELI 71
IPT smart00429
ig-like, plexins, transcription factors;
133-232 1.96e-18

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 80.54  E-value: 1.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437    133 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKMKIERPVTVF 212
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 74142437    213 LQlkrkRGGDV-SDSKQFTYY 232
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
2-127 1.00e-17

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: 81.38  E-value: 1.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   2 VTHSDPPRAHAHSLVGKQCSELGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIqklQRQRLRSKPqglteaeRRELE 81
Cdd:cd07887  59 VTKDEPFRPHPHNLVGKEGCKKGVCTKKINPTEMRIVFQKLGIQCVKKKDVEESLK---LREEINVDP-------FRTGF 128
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 74142437  82 QEAKELKKVmDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 127
Cdd:cd07887 129 DHKDQINSI-DLNVVRLCFQVFLEDENGRFTVPLPPVVSDPIYDKK 173
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
1-127 1.87e-17

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: 80.17  E-value: 1.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRA-HAHSLVGKQCsELGVCAVSVGPK----DMTAQFNNLGVLHVTKKNMMEIMIQKlqrqrlrskpqgltea 75
Cdd:cd07884  58 LYQADDNRRKpHVHKLVGKQG-DDDVCDPHDIEVspegDYVAMFQNMGIIHTAKKNIPEELYKK---------------- 120
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 74142437  76 erreleqeakelkKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 127
Cdd:cd07884 121 -------------KNMNLNQVVLRFQAFAVSANGHLRPICPPVYSNPINNLK 159
RHD-n_c-Rel cd07933
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ...
1-127 1.12e-16

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: 78.38  E-value: 1.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRAHAHSLVGKQCSElGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRqrlRSKPQGLTEAERREL 80
Cdd:cd07933  58 LVTKNEPYKPHPHDLVGKDCRD-GYYEAEFGPERRVLAFQNLGIQCVRRREVKEAIMLRISR---GINPFNVPEEQLLQI 133
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 74142437  81 EQeakelkkvMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSK 127
Cdd:cd07933 134 EE--------YDLNVVRLCFQIFLPDEHGNYTTALPPIVSNPIYDNR 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
511-604 2.37e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 2.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   511 HLAVHARSPECLDLLVDCGAEVEApERQGGRTALHLATEMEELGLVTHLVTklHANVNARTFaGNTPLHLAAGLGSPTLT 590
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDN-GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 74142437   591 RLLLKAGADIHAEN 604
Cdd:pfam12796  78 KLLLEKGADINVKD 91
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
134-233 2.55e-14

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


Pssm-ID: 238050 [Multi-domain]  Cd Length: 89  Bit Score: 69.03  E-value: 2.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 134 LKISRMDKTAGSVRGGDEVYLLCDKVQKD-DIEVRFYeddengwqAFGDFSPTDVHkQYAIVFRTPPYHkmkIERPVTVF 212
Cdd:cd00102   1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFG--------GGVPCSVLSVS-STAIVCTTPPYA---NPGPGPVE 68
                        90       100
                ....*....|....*....|.
gi 74142437 213 LQLKRKRGGDVSDSKQFTYYP 233
Cdd:cd00102  69 VTVDRGNGGITSSPLTFTYVP 89
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
682-754 2.37e-12

Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the Nuclear Factor-KappaB1 (NF-kB1) precursor protein p105. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). NF-kB1 (or p50) is produced from the processing of the precursor protein p105, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the classical (or canonical) NF-kB pathway. In the cytosol, p50 forms an inactive complex with RelA (or p65) and the Inhibitor of NF-kB (IkB). Activation is triggered by the phosphorylation and degradation of IkB, resulting in the active DNA-binding p50-RelA dimer to migrate to the nucleus. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260063  Cd Length: 76  Bit Score: 63.00  E-value: 2.37e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74142437 682 QNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRKTPSPSGSLLRSYKLAGGDLVGLLEALSDMGLHEGVRLLK 754
Cdd:cd08797   3 QQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIE 75
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
1-127 2.52e-12

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: 65.66  E-value: 2.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRAHAHSLVGKQCSElGVCAVSVGPKDMTAQFNNLGVLHVTKKNMMEIMIQKLQRQrlrSKPQGLTEAERREl 80
Cdd:cd07885  58 LVTKDPPHKPHPHELVGKDCKD-GYYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQRIQTN---NNPFNVPIEEQRA- 132
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 74142437  81 eqeakelkkVMDLSIVRLRFSAFLRASDGSFsLPLKPVISQPIHDSK 127
Cdd:cd07885 133 ---------DYDLNAVRLCFQVTVRDPSGRL-LPLPPVLSQPIYDNR 169
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
1-127 7.26e-12

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: 64.50  E-value: 7.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   1 LVTHSDPPRAHAHSLVGKQCSElGVCAVSVGPKDMTAQ-FNNLGVLHVTKKNMMEIMIQKLQrqrLRSKPqglTEAERRE 79
Cdd:cd07886  60 LVWKDPPHRVHPHGLVGKDCPN-GICQVTLNPHSSPRHsFSNLGIQCVRKREIEAAIETRLQ---LNIDP---FKAGSLK 132
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 74142437  80 LEQEakelkkvMDLSIVRLRFSAFLRASDGsFSLPLKPVISQPIHDSK 127
Cdd:cd07886 133 NHEE-------VDMNVVRLCFQASYRDDDG-RKDCLSPVLSEPIYDKK 172
PHA02878 PHA02878
ankyrin repeat protein; Provisional
445-613 1.79e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.21  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  445 QTRVVSFLLQVGADPTLLDRH-GDSALHLAlrAGAAAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSPECLD 523
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYA--TENKDQRLTELLLSYGAN-----VNIPDKTNNSPLHHAVKHYNKPIVH 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  524 LLVDCGAEVEAPERQGgRTALHLATEMEELGLVTHLVTKLHANVNAR-TFAGNTPLHLAagLGSPTLTRLLLKAGADIHA 602
Cdd:PHA02878 219 ILLENGASTDARDKCG-NTPLHISVGYCKDYDILKLLLEHGVDVNAKsYILGLTALHSS--IKSERKLKLLLEYGADINS 295
                        170
                 ....*....|.
gi 74142437  603 ENEEPLCPLPS 613
Cdd:PHA02878 296 LNSYKLTPLSS 306
Ank_2 pfam12796
Ankyrin repeats (3 copies);
437-534 1.88e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   437 LHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLrsgAHAVPQIlhmpDFEGLYPVHLAVHA 516
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL--EIVKLLL---EHADVNL----KDNGRTALHYAARS 71
                          90
                  ....*....|....*...
gi 74142437   517 RSPECLDLLVDCGAEVEA 534
Cdd:pfam12796  72 GHLEIVKLLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
429-581 2.37e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  429 TNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRagAAAPELLQALLRSGAHavpqILHMpDFEGLY 508
Cdd:PHA02878 164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK--HYNKPIVHILLENGAS----TDAR-DKCGNT 236
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74142437  509 PVHLAV-HARSPECLDLLVDCGAEVEAPERQGGRTALHLATEMEElglVTHLVTKLHANVNARTFAGNTPLHLA 581
Cdd:PHA02878 237 PLHISVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSER---KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
396-600 9.26e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 9.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  396 TPLHLA--IIHGQTGVIEqIAHVIYhaQYLGVINLTNHLHQTPLHLAVIT--GQTRVVSFLLQVGADPTLLDRHGDSALH 471
Cdd:PHA03100  70 TPLHYLsnIKYNLTDVKE-IVKLLL--EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLH 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  472 LALRAGAAAPELLQALLRSGA-------------HAVPqiLHMPDFEGLYPVHLAVHARSPECLDLLVDCGAeveaperq 538
Cdd:PHA03100 147 LYLESNKIDLKILKLLIDKGVdinaknrvnyllsYGVP--INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA-------- 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74142437  539 ggrtalhlatemeelglvthlvtklhaNVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADI 600
Cdd:PHA03100 217 ---------------------------NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
390-463 3.43e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 3.43e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74142437   390 QDENGDTPLHLAIIHGQTGVIEQ-IAHVIyhaqylgvINLTNHlHQTPLHLAVITGQTRVVSFLLQVGADPTLLD 463
Cdd:pfam12796  26 QDKNGRTALHLAAKNGHLEIVKLlLEHAD--------VNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
398-493 4.56e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   398 LHLAIIHGQTGVIEQIahVIYHAQylgvINLTNHLHQTPLHLAVITGQTRVVSFLLQVGAdpTLLDRHGDSALHLALRAG 477
Cdd:pfam12796   1 LHLAAKNGNLELVKLL--LENGAD----ANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSG 72
                          90
                  ....*....|....*.
gi 74142437   478 aaAPELLQALLRSGAH 493
Cdd:pfam12796  73 --HLEIVKLLLEKGAD 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
678-756 1.47e-09

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 55.49  E-value: 1.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437    678 DAALQNLEQLLDGPeAQGSWAELAERLGLRSLV------DTYRKTPSPSGSLLRSYKLAGG---DLVGLLEALSDMGLHE 748
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSEADidqirtEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 74142437    749 GVRLLKGP 756
Cdd:smart00005  81 AVELLRSE 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
391-611 3.47e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  391 DENGDTPLHLAIihgQTGVIEQIAHVIYHAqylGV-INLTNHLHQTPLHLAVITG-QTRVVSFLLQVGADPTLLDRHGDS 468
Cdd:PHA02876 270 DDCKNTPLHHAS---QAPSLSRLVPKLLER---GAdVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYIT 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  469 ALHLALRAGAAApELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQGGrTALHLAT 548
Cdd:PHA02876 344 PLHQASTLDRNK-DIVITLLELGAN-----VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFAL 416
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74142437  549 EMEELGLVTHLVTKLHANVNARTFAGNTPLHLAAGLG-SPTLTRLLLKAGADIHAENEEPLCPL 611
Cdd:PHA02876 417 CGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02875 PHA02875
ankyrin repeat protein; Provisional
432-611 5.72e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 5.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  432 LHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAhaVPQIlHMPDFEGlyPVH 511
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDS--EAIKLLMKHGA--IPDV-KYPDIES--ELH 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  512 LAVHARSPECLDLLVDCGAEVEAPERQGGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTR 591
Cdd:PHA02875  74 DAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
                        170       180
                 ....*....|....*....|
gi 74142437  592 LLLKAGADIHAENEEPLCPL 611
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPL 172
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
434-507 8.82e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 8.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  434 QTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLR-------SGAHAVPQIL------- 499
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR--EVVQLLSRhsqchfeLGANAKPDSFtgkppsl 193
                         90
                 ....*....|....*
gi 74142437  500 -------HMPDFEGL 507
Cdd:PTZ00322 194 edspissHHPDFSAV 208
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
136-233 2.25e-08

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


Pssm-ID: 238583  Cd Length: 101  Bit Score: 52.49  E-value: 2.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 136 ISRMDKTAGSVRGGDEVYLLCDKVQKDDiEVRFYE---DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKMKIERPVTVF 212
Cdd:cd01178   4 IEKKSLNSCSVNGGEELFLTGKNFLKDS-KVVFQEkgqDGEAQWEAEATIDKEKSH-QNHLVVEVPPYHNKHVAAPVQVQ 81
                        90       100
                ....*....|....*....|....
gi 74142437 213 LQL---KRKRggdvSDSKQFTYYP 233
Cdd:cd01178  82 FYVvngKRKR----SQPQTFTYTP 101
PHA02874 PHA02874
ankyrin repeat protein; Provisional
426-608 2.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  426 INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAHAvpQILHMPDFE 505
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAH--DIIKLLIDNGVDT--SILPIPCIE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  506 GlypvhlavharspECLDLLVDCGAEVEAPERQGgRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLG 585
Cdd:PHA02874 104 K-------------DMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHN 168
                        170       180
                 ....*....|....*....|....*.
gi 74142437  586 SPTLTRLLLKAGADIHAEN---EEPL 608
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDnngESPL 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
426-581 2.90e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 2.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  426 INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAHAvpqilHMPDFE 505
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF--DIIKLLLEKGAYA-----NVKDNN 189
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74142437  506 GLYPVHLAVHARSPECLDLLVDCGAEVEAPERQgGRTALHLATeMEELGLVTHLVTklHANVNARTFAGNTPLHLA 581
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAI-IHNRSAIELLIN--NASINDQDIDGSTPLHHA 261
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
426-605 7.24e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 56.24  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   426 INLTNHLHQTPLHLAVITGQTR-VVSFLLQVGADPTLldrhGDSALHLA-LRAGAAAPELLQALLRSGAHAVPQILhMPD 503
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAIsLEYVDAVEAILLHLLAAFRKSGPLEL-AND 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   504 ------FEGLYPVHLAVHARSPECLDLLVDCGAEVEApeRQGGRTALhlatEMEELGLVTHlvtklhanvnartfaGNTP 577
Cdd:TIGR00870 120 qytsefTPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFV----KSQGVDSFYH---------------GESP 178
                         170       180
                  ....*....|....*....|....*...
gi 74142437   578 LHLAAGLGSPTLTRLLLKAGADIHAENE 605
Cdd:TIGR00870 179 LNAAACLGSPSIVALLSEDPADILTADS 206
PHA02876 PHA02876
ankyrin repeat protein; Provisional
426-622 9.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 9.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  426 INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAHAVPQILHMPDfe 505
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI--DTIKAIIDNRSNINKNDLSLLK-- 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  506 glypvhlAVHARSPECLDLLVDCGAEVEAPErQGGRTALHLATEMEELglvTHLVTKL---HANVNARTFAGNTPLHLAA 582
Cdd:PHA02876 247 -------AIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSL---SRLVPKLlerGADVNAKNIKGETPLYLMA 315
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 74142437  583 GLGSPTLT-RLLLKAGADIHAENEEPLCPLPSPSTSGSDSD 622
Cdd:PHA02876 316 KNGYDTENiRTLIMLGADVNAADRLYITPLHQASTLDRNKD 356
PHA03095 PHA03095
ankyrin-like protein; Provisional
388-475 4.62e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  388 MAQDENGDTPLHLAIIHGQtgvieqiAHVIYHAQYL--GV-INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDR 464
Cdd:PHA03095 216 AATDMLGNTPLHSMATGSS-------CKRSLVLPLLiaGIsINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
                         90
                 ....*....|.
gi 74142437  465 HGDSALHLALR 475
Cdd:PHA03095 289 DGNTPLSLMVR 299
Death pfam00531
Death domain;
682-754 5.66e-07

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 48.13  E-value: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   682 QNLEQLLDGPEAQG-SWAELAERLGLRSL-VDT----YRKTPSPSGSLLRSYKLAGG---DLVGLLEALSDMGLHEGVRL 752
Cdd:pfam00531   2 KQLDRLLDPPPPLGkDWRELARKLGLSENeIDEieseNPRLRSQTYELLRLWEQREGknaTVGTLLEALRKLGRRDAAEK 81

                  ..
gi 74142437   753 LK 754
Cdd:pfam00531  82 IQ 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
420-643 6.75e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 6.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 420 AQYLGVINL--TNHLHQTPLHLAVITGQTRVVSFLL-QVGADPTLLDRHGDSALHLALRAGAAapELLQALLRsgahAVP 496
Cdd:cd22192   2 AQMLDELHLlqQKRISESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNL--EAAVVLME----AAP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 497 QILHMPDFEGLYPvhlavharspecldllvdcgaeveaperqgGRTALHLATEMEELGLVTHLVTKLHANVNART----- 571
Cdd:cd22192  76 ELVNEPMTSDLYQ------------------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtff 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 572 --------FAGNTPLHLAAGLGSPTLTRLLLKAGADIHAE---------------NEEPLCPLPSPSTSgSDSDSEGPER 628
Cdd:cd22192 126 rpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQdslgntvlhilvlqpNKTFACQMYDLILS-YDKEDDLQPL 204
                       250
                ....*....|....*
gi 74142437 629 DTQRNFRGHTPLDLT 643
Cdd:cd22192 205 DLVPNNQGLTPFKLA 219
PHA02876 PHA02876
ankyrin repeat protein; Provisional
462-602 8.51e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 8.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  462 LDRHGDSALHLALRAGAAApELLQALLRSGAHavpqiLHMPDFEGLYPVHL-AVHARSPECLDLLVDCGAEVEAPERQGg 540
Cdd:PHA02876 269 IDDCKNTPLHHASQAPSLS-RLVPKLLERGAD-----VNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLY- 341
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74142437  541 RTALHLATEMEELGLVTHLVTKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADIHA 602
Cdd:PHA02876 342 ITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403
PHA02878 PHA02878
ankyrin repeat protein; Provisional
377-534 1.03e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  377 RALLAGQRHLLMAQDENGDTPLHLAIIHGQTGVIEQIahVIYHAQylgvINLTNHLHQTPLHLAVITGQTRVVSFLLQVG 456
Cdd:PHA02878 151 KLLLSYGADINMKDRHKGNTALHYATENKDQRLTELL--LSYGAN----VNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  457 ADPTLLDRHGDSALHLALrAGAAAPELLQALLRSGA--HAVPQILhmpdfeGLYPVHLAVHarSPECLDLLVDCGAEVEA 534
Cdd:PHA02878 225 ASTDARDKCGNTPLHISV-GYCKDYDILKLLLEHGVdvNAKSYIL------GLTALHSSIK--SERKLKLLLEYGADINS 295
PHA02875 PHA02875
ankyrin repeat protein; Provisional
395-562 3.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  395 DTPLHLAIIHGQTGVIEQ-------IAHVIYHAQylgvinltnhlhQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGD 467
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEElldlgkfADDVFYKDG------------MTPLHLATILKKLDIMKLLIARGADPDIPNTDKF 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  468 SALHLALRAGAAapELLQALLRSGAhavpqILHMPDFEGLYPVHLAVHARSPECLDLLVDCGAEVEAPERQGGRTALHLA 547
Cdd:PHA02875 137 SPLHLAVMMGDI--KGIELLIDHKA-----CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYA 209
                        170
                 ....*....|....*
gi 74142437  548 TEMEELGLVTHLVTK 562
Cdd:PHA02875 210 IENNKIDIVRLFIKR 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
435-488 5.85e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 5.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 74142437   435 TPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGaaAPELLQALL 488
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG--NVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
384-611 7.57e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 7.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  384 RHLLMAQDENGDtplhLAIIH---GQTGVIEQIAHVIYHAQYlgVINLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPT 460
Cdd:PHA02946  26 RNMLQAIEPSGN----YHILHaycGIKGLDERFVEELLHRGY--SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  461 LLDRHGDSALHLALRAGAAAPELLQALLRSGAhavpQILHMPDFEGLYPVhLAVHARSPECLDLLVDCGAEVEAPERQG- 539
Cdd:PHA02946 100 ACDKQHKTPLYYLSGTDDEVIERINLLVQYGA----KINNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGk 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74142437  540 GRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAglgSPTLTRL----LLKAGADIHAENEEPLCPL 611
Cdd:PHA02946 175 NHIHRHLMSDNPKASTISWMM-KLGISPSKPDHDGNTPLHIVC---SKTVKNVdiinLLLPSTDVNKQNKFGDSPL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
559-611 9.47e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 9.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 74142437   559 LVTKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADIHAENEEPLCPL 611
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
435-605 2.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  435 TPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAA---PELLQALLRSGAhavpqILHMPDFEGLYPVH 511
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvKEIVKLLLEYGA-----NVNAPDNNGITPLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  512 LAV--HARSPECLDLLVDCGAEVEApERQGGRTALHLATE-------MEELgLVTH-----------LVTKLHANVNART 571
Cdd:PHA03100 112 YAIskKSNSYSIVEYLLDNGANVNI-KNSDGENLLHLYLEsnkidlkILKL-LIDKgvdinaknrvnYLLSYGVPINIKD 189
                        170       180       190
                 ....*....|....*....|....*....|....
gi 74142437  572 FAGNTPLHLAAGLGSPTLTRLLLKAGADIHAENE 605
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
574-605 2.88e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 2.88e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 74142437   574 GNTPLHLAAG-LGSPTLTRLLLKAGADIHAENE 605
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
426-473 6.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 6.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 74142437   426 INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALHLA 473
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
574-602 6.44e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 6.44e-05
                          10        20
                  ....*....|....*....|....*....
gi 74142437   574 GNTPLHLAAGLGSPTLTRLLLKAGADIHA 602
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02743 PHA02743
Viral ankyrin protein; Provisional
498-598 1.06e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 43.65  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  498 ILHMPDFEGLYPVHL-AVHARSPECL--DLLVDCGAEVEAPERQGGRTALHLATEMEELGLVTHLVTKLHANVNARTFAG 574
Cdd:PHA02743  49 LLHRYDHHGRQCTHMvAWYDRANAVMkiELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQH 128
                         90       100
                 ....*....|....*....|....
gi 74142437  575 NTPLHLAAGLGSPTLTRLLLKAGA 598
Cdd:PHA02743 129 ETAYHIAYKMRDRRMMEILRANGA 152
PHA02876 PHA02876
ankyrin repeat protein; Provisional
389-534 1.21e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  389 AQDENGDTPLHlaiihgQTGVIEQIAHVIYHAQYLGV-INLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGD 467
Cdd:PHA02876 336 AADRLYITPLH------QASTLDRNKDIVITLLELGAnVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74142437  468 SALHLALrAGAAAPELLQALLRSGAHAVPQILHMPDfeglyPVHLAVHAR-SPECLDLLVDCGAEVEA 534
Cdd:PHA02876 410 TALHFAL-CGTNPYMSVKTLIDRGANVNSKNKDLST-----PLHYACKKNcKLDVIEMLLDNGADVNA 471
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
440-648 1.97e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  440 AVITGQTRVVSFLLQVGADPTLLDRHGDSALHLAlrAGAAAPELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSP 519
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIA--ASKGYEDCVLVLLKHACN-----VHIRDANGNTALWNAISAKHH 604
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  520 ECLDLLVDCGAeveAPERQGGRTALHLATEMEELGLVTHLVtKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGAD 599
Cdd:PLN03192 605 KIFRILYHFAS---ISDPHAAGDLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74142437  600 I-HAENEEPLCPL---------------PSPSTSGSDSDSEGPERDTQRNFRGHTPLDLTCSTKV 648
Cdd:PLN03192 681 VdKANTDDDFSPTelrellqkrelghsiTIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRV 745
PHA02876 PHA02876
ankyrin repeat protein; Provisional
445-623 2.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  445 QTRVVSFLLQVGADPTLLDRHGDSALHLALRAGAAapELLQALLRSGAHavpqiLHMPDFEGLYPVHLAVHARSPECLDL 524
Cdd:PHA02876 157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNA--KMVNLLLSYGAD-----VNIIALDDLSVLECAVDSKNIDTIKA 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  525 LVDCGAEVEaperqggRTALHLATEMEELGLVTHLVTKLHA-NVNARTFAGNTPLHLAAGlgSPTLTRL---LLKAGADI 600
Cdd:PHA02876 230 IIDNRSNIN-------KNDLSLLKAIRNEDLETSLLLYDAGfSVNSIDDCKNTPLHHASQ--APSLSRLvpkLLERGADV 300
                        170       180
                 ....*....|....*....|...
gi 74142437  601 HAENEEPLCPLPSPSTSGSDSDS 623
Cdd:PHA02876 301 NAKNIKGETPLYLMAKNGYDTEN 323
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
394-594 3.16e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.30  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   394 GDTPLHLAIIHGQTGVIEQIAHVIYHAQYLGVINLTNHLH-------QTPLHLAVITGQTRVVSFLLQVGAD-------- 458
Cdd:TIGR00870  82 GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYtseftpgITALHLAAHRQNYEIVKLLLERGASvparacgd 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   459 -------PTLLdRHGDSALHLAlrAGAAAPELLQALLRSGAHAVPQ------ILHM----PDFEGLYpvhlavHARSPEC 521
Cdd:TIGR00870 162 ffvksqgVDSF-YHGESPLNAA--ACLGSPSIVALLSEDPADILTAdslgntLLHLlvmeNEFKAEY------EELSCQM 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74142437   522 LDLLVDCGAeveaperqggrtalHLATEMEelglvthlvtkLHANVNartFAGNTPLHLAAGLGSPTLTRLLL 594
Cdd:TIGR00870 233 YNFALSLLD--------------KLRDSKE-----------LEVILN---HQGLTPLKLAAKEGRIVLFRLKL 277
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
540-602 4.33e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 4.33e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74142437 540 GRTALHLATEMEELGLVTHLVTK---LHANVNARTFA---------GNTPLHLAAGLGSPTLTRLLLKAGADIHA 602
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENgadVSARATGRFFRkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAA 147
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
434-464 4.37e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 4.37e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 74142437   434 QTPLHLAVI-TGQTRVVSFLLQVGADPTLLDR 464
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02874 PHA02874
ankyrin repeat protein; Provisional
390-539 4.87e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  390 QDENGDTPLHLAIIHGQTGVIEQIahvIYHAQYLgviNLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSA 469
Cdd:PHA02874 153 EDDNGCYPIHIAIKHNFFDIIKLL---LEKGAYA---NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74142437  470 LHLALRAGAAAPELLqallrsgahAVPQILHMPDFEGLYPVHlavHARSPEC----LDLLVDCGAEVEAPERQG 539
Cdd:PHA02874 227 LHNAIIHNRSAIELL---------INNASINDQDIDGSTPLH---HAINPPCdidiIDILLYHKADISIKDNKG 288
Death_UNC5B cd08802
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ...
688-748 6.24e-04

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


Pssm-ID: 176780  Cd Length: 84  Bit Score: 39.24  E-value: 6.24e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74142437 688 LDGPEAQGS-WAELAERLGLRSLVDTYRKTPSPSGSLLRSYKL---AGGDLVGLLEALSDMGLHE 748
Cdd:cd08802  13 LDAPNSRGNdWRLLAQKLSMDRYLNYFATKASPTGVILDLWEArhqDDGDLNSLASALEEMGKSE 77
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
521-602 8.15e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.82  E-value: 8.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 521 CLDLLVDCGAEVEAPErqgGRTALHLATEMEELGLVTHLVTKlHANVNART--------------FAGNTPLHLAAGLGS 586
Cdd:cd22194 125 ILDRFINAEYTEEAYE---GQTALNIAIERRQGDIVKLLIAK-GADVNAHAkgvffnpkykhegfYFGETPLALAACTNQ 200
                        90
                ....*....|....*.
gi 74142437 587 PTLTRLLLKAGADIHA 602
Cdd:cd22194 201 PEIVQLLMEKESTDIT 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
574-602 8.84e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 8.84e-04
                           10        20
                   ....*....|....*....|....*....
gi 74142437    574 GNTPLHLAAGLGSPTLTRLLLKAGADIHA 602
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
682-750 1.39e-03

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


Pssm-ID: 260064  Cd Length: 83  Bit Score: 38.45  E-value: 1.39e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74142437 682 QNLEQLLDGPEAQGS-WAELAERLGLRSLVDTYRKTPSPSGSLL---RSYKLAGGDLVGLLEALSDMGLHEGV 750
Cdd:cd08799   7 QKLCGSLDAPQTRGNdWRMLAHKLNLDRYLNYFATKSSPTGVILdlwEAQHFPDGNLSRLAAVLEEMGRHETV 79
Ank_4 pfam13637
Ankyrin repeats (many copies);
394-453 1.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437   394 GDTPLHLAIIHGQTGVIEqiahviYHAQYLGVINLTNHLHQTPLHLAVITGQTRVVSFLL 453
Cdd:pfam13637   1 ELTALHAAAASGHLELLR------LLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02736 PHA02736
Viral ankyrin protein; Provisional
522-598 1.66e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 1.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74142437  522 LDLLVDCGAEVEAPERQGGRTALHLATEMEELGLVTHLVTKLHANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGA 598
Cdd:PHA02736  74 LKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
368-513 1.69e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.76  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 368 LDYGVTADARALL------AGQRHLLMAQDEN----GDTPLHLAI----IHGQTGVIEQIAHViyHAQYLGVINLTN--- 430
Cdd:cd22197  58 LQDGVNACIMPLLeidkdsGNPKPLVNAQCTDeyyrGHSALHIAIekrsLQCVKLLVENGADV--HARACGRFFQKKqgt 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 431 --HLHQTPLHLAVITGQTRVVSFLLQVGADPTLL---DRHGDSALHLALRAGAAAPE-------LLQALLRSGAHAVP-- 496
Cdd:cd22197 136 cfYFGELPLSLAACTKQWDVVNYLLENPHQPASLqaqDSLGNTVLHALVMIADNSPEnsalvikMYDGLLQAGARLCPtv 215
                       170
                ....*....|....*..
gi 74142437 497 QILHMPDFEGLYPVHLA 513
Cdd:cd22197 216 QLEEISNHEGLTPLKLA 232
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
504-579 1.90e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.70  E-value: 1.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 504 FEGLYPVHLAVHARSPECLDLLVDCGAEVEA--------PERQG-----GRTALHLATEMEELGLVTHLVTKLH--ANVN 568
Cdd:cd22193  74 YEGQTALHIAIERRQGDIVALLVENGADVHAhakgrffqPKYQGegfyfGELPLSLAACTNQPDIVQYLLENEHqpADIE 153
                        90
                ....*....|.
gi 74142437 569 ARTFAGNTPLH 579
Cdd:cd22193 154 AQDSRGNTVLH 164
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
394-526 2.83e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 2.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 394 GDTPLHLAIIHGQTGVIEQI----AHVIyHAQYLG---VINLTNHLH--QTPLHLAVITGQTRVVSFLLQVGADPTLLDR 464
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELiargADVV-SPRATGtffRPGPKNLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74142437 465 HGDSALH-LALRAGAA-APELLQALLRSGAHAVPQIL-HMPDFEGLYPVHLAVHARSPECLDLLV 526
Cdd:cd22192 168 LGNTVLHiLVLQPNKTfACQMYDLILSYDKEDDLQPLdLVPNNQGLTPFKLAAKEGNIVMFQHLV 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
565-611 3.33e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 3.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 74142437  565 ANVNARTFAGNTPLHLAAGLGSPTLTRLLLKAGADIHAENEEPLCPL 611
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
435-461 3.37e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.37e-03
                           10        20
                   ....*....|....*....|....*..
gi 74142437    435 TPLHLAVITGQTRVVSFLLQVGADPTL 461
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
436-513 3.53e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.02  E-value: 3.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437 436 PLHLAVITGQTRVVSFLLQVGADPTLL---DRHGDSALH-LALRA------GAAAPELLQALLRSGAHAVP--QILHMPD 503
Cdd:cd21882 122 PLSLAACTNQEEIVRLLLENGAQPAALeaqDSLGNTVLHaLVLQAdntpenSAFVCQMYNLLLSYGAHLDPtqQLEEIPN 201
                        90
                ....*....|
gi 74142437 504 FEGLYPVHLA 513
Cdd:cd21882 202 HQGLTPLKLA 211
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
433-459 4.62e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 4.62e-03
                          10        20
                  ....*....|....*....|....*..
gi 74142437   433 HQTPLHLAVITGQTRVVSFLLQVGADP 459
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02875 PHA02875
ankyrin repeat protein; Provisional
392-531 6.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 6.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  392 ENGDTPLHLAIIHGQTGVIEQIahviyhAQYLGVINLTNHLHQTPLHLAVITGQTRVVSFLLQVGADPTLLDRHGDSALH 471
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLL------IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74142437  472 LALRAGAAapELLQALLRSGAHavpqilhmPDFEGLYP----VHLAVHARSPECLDLLVDCGAE 531
Cdd:PHA02875 174 IAMAKGDI--AICKMLLDSGAN--------IDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
367-458 8.58e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 8.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74142437  367 LLDYGVTADARallagqrhllmaqDENGDTPLHLAIIHgqtgviEQIAHVIYHAQYLGVINLTNHLHQTPLHLAVITGQT 446
Cdd:PHA03100 178 LLSYGVPINIK-------------DVYGFTPLHYAVYN------NNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
                         90
                 ....*....|..
gi 74142437  447 RVVSFLLQVGAD 458
Cdd:PHA03100 239 EIFKLLLNNGPS 250
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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