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Conserved domains on  [gi|35040|emb|CAA43715|]
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NF-kB subunit [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
38-221 2.49e-120

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: 363.45  E-value: 2.49e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934   1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSR-PQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934  81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                       170       180
                ....*....|....*....|....*
gi 35040    197 FLRASDGSFSLPLKPVTSQPIHDSK 221
Cdd:cd07934 161 YLRDSNGSYTLALKPVISDPIHDSK 185
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
228-327 4.49e-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: 4.49e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177   1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                        90       100
                ....*....|....*....|..
gi 35040    306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd01177  81 KIQLKRPSDGERSESVPFTYVP 102
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
773-848 5.89e-36

Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the Nuclear Factor-KappaB2 (NF-kB2) precursor protein p100. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). NF-kB2 (or p52) is produced from the processing of the precursor protein p100, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the non-canonical NF-kB pathway. The p100 precursor is cytosolic and interacts with RelB. Upon phosphorylation by IKKalpha, p100 is processed to its 52kDa active, DNA-binding form and the p52/RelB complex is translocated into the nucleus. The non-canonical pathway plays a role in adaptive immunity and lymphorganogenesis. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 176776  Cd Length: 76  Bit Score: 130.33  E-value: 5.89e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35040    773 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRG 848
Cdd:cd08798   1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
440-705 2.60e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    440 LQRAREYNARLFGLAHAAPSPTRLLRHRGRRALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIvyvihhAQDLGVV 519
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLL------LAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    520 NLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEG 599
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA--AYNGNLEIVKLLLEAGAD-----VNAQDNDG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    600 LYPVHLAVRARSPECLDLLVDSGAEVEATERQgGRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLGY 679
Cdd:COG0666 154 NTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGN 231
                       250       260
                ....*....|....*....|....*.
gi 35040    680 PTLTRLLLKAGADIHAENEEPLCPLP 705
Cdd:COG0666 232 LEIVKLLLEAGADLNAKDKDGLTALL 257
 
Name Accession Description Interval E-value
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
38-221 2.49e-120

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: 363.45  E-value: 2.49e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934   1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSR-PQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934  81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                       170       180
                ....*....|....*....|....*
gi 35040    197 FLRASDGSFSLPLKPVTSQPIHDSK 221
Cdd:cd07934 161 YLRDSNGSYTLALKPVISDPIHDSK 185
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
40-220 1.02e-78

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: 253.00  E-value: 1.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040       40 LVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSElGI 119
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKD-GV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      120 CAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQrqrlrsrpqgLTEAEQReLEQEAKELKKVMDLSIVRLRFSAFLR 199
Cdd:pfam00554  80 CEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-VGFEALRQIKDMDLNVVRLCFQAFLP 148
                         170       180
                  ....*....|....*....|.
gi 35040      200 ASDGSFSLPLKPVTSQPIHDS 220
Cdd:pfam00554 149 DTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
228-327 4.49e-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: 4.49e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177   1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                        90       100
                ....*....|....*....|..
gi 35040    306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd01177  81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
229-328 2.09e-55

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


Pssm-ID: 465045  Cd Length: 102  Bit Score: 186.61  E-value: 2.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      229 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 35040      307 LQLKRKRGGDVSDSKQFTYYPL 328
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
773-848 5.89e-36

Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the Nuclear Factor-KappaB2 (NF-kB2) precursor protein p100. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). NF-kB2 (or p52) is produced from the processing of the precursor protein p100, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the non-canonical NF-kB pathway. The p100 precursor is cytosolic and interacts with RelB. Upon phosphorylation by IKKalpha, p100 is processed to its 52kDa active, DNA-binding form and the p52/RelB complex is translocated into the nucleus. The non-canonical pathway plays a role in adaptive immunity and lymphorganogenesis. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176776  Cd Length: 76  Bit Score: 130.33  E-value: 5.89e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35040    773 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRG 848
Cdd:cd08798   1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
440-705 2.60e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    440 LQRAREYNARLFGLAHAAPSPTRLLRHRGRRALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIvyvihhAQDLGVV 519
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLL------LAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    520 NLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEG 599
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA--AYNGNLEIVKLLLEAGAD-----VNAQDNDG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    600 LYPVHLAVRARSPECLDLLVDSGAEVEATERQgGRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLGY 679
Cdd:COG0666 154 NTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGN 231
                       250       260
                ....*....|....*....|....*.
gi 35040    680 PTLTRLLLKAGADIHAENEEPLCPLP 705
Cdd:COG0666 232 LEIVKLLLEAGADLNAKDKDGLTALL 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
470-704 1.76e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.70  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     470 RALL-AGQRhlLTAQDENGDTPLHLAIIHGQTsvIEQIVYVIHHAQDlgvVNLTNHLHQTPLH--LAVITGQTSVVSFLL 546
Cdd:PHA03095  67 RLLLeAGAD--VNAPERCGFTPLHLYLYNATT--LDVIKLLIKAGAD---VNAKDKVGRTPLHvyLSGFNINPKVIRLLL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     547 RVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVH---LAVRARsPECLDLLVDSGA 623
Cdd:PHA03095 140 RKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLHhhlQSFKPR-ARIVRELIRAGC 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     624 EVEATERqGGRTALHLATeMEELGLVTHLVTKLRAN--VNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPL 701
Cdd:PHA03095 214 DPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291

                 ...
gi 35040     702 CPL 704
Cdd:PHA03095 292 TPL 294
IPT smart00429
ig-like, plexins, transcription factors;
227-326 2.28e-18

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 80.54  E-value: 2.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040       227 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 35040       307 LQlkrkRGGDV-SDSKQFTYY 326
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-697 5.76e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      604 HLAVRARSPECLDLLVDSGAEVEATErQGGRTALHLATEMEELGLVTHLVTKLRANVNARtfaGNTPLHLAAGLGYPTLT 683
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 35040      684 RLLLKAGADIHAEN 697
Cdd:pfam12796  78 KLLLEKGADINVKD 91
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
771-849 3.66e-11

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


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 60.12  E-value: 3.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040       771 DTALQNLEQLLDGPeAQGSWAELAERLGLRSLV------DTYRQTTSPSGSLLRSYELAGG---DLAGLLEALSDMGLEE 841
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSEADidqirtEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 35040       842 GVRLLRGP 849
Cdd:smart00005  81 AVELLRSE 88
Death pfam00531
Death domain;
775-847 8.07e-08

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 50.44  E-value: 8.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      775 QNLEQLLDGPEAQG-SWAELAERLGLRSL-VDT----YRQTTSPSGSLLRSYELAGG---DLAGLLEALSDMGLEEGVRL 845
Cdd:pfam00531   2 KQLDRLLDPPPPLGkDWRELARKLGLSENeIDEieseNPRLRSQTYELLRLWEQREGknaTVGTLLEALRKLGRRDAAEK 81

                  ..
gi 35040      846 LR 847
Cdd:pfam00531  82 IQ 83
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
519-698 3.31e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.85  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      519 VNLTNHLHQTPLHLAVITGQT-SVVSFLLRVGADPALldrhGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPD- 596
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDq 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      597 -----FEGLYPVHLAVRARSPECLDLLVDSGAEVEAteRQGGRTALhlatEMEELGLVTHlvtklranvnartfaGNTPL 671
Cdd:TIGR00870 121 ytsefTPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFV----KSQGVDSFYH---------------GESPL 179
                         170       180
                  ....*....|....*....|....*..
gi 35040      672 HLAAGLGYPTLTRLLLKAGADIHAENE 698
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADS 206
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
487-658 7.64e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.54  E-value: 7.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    487 GDTPLHLAIIHGQtsvIEQIVYVIHHAQDLGVVNLTNHLHQ--TPLHLAVITGQTSVVSFLLRVGADPA-------LLDR 557
Cdd:cd22192  51 GETALHVAALYDN---LEAAVVLMEAAPELVNEPMTSDLYQgeTALHIAVVNQNLNLVRELIARGADVVspratgtFFRP 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    558 HGDSAMH-----LALRAGAGAPELLRALLQSGAPAVPQllhmpDFEGLYPVHLAV----RARSPECLDLLVDSGAE---- 624
Cdd:cd22192 128 GPKNLIYygehpLSFAACVGNEEIVRLLIEHGADIRAQ-----DSLGNTVLHILVlqpnKTFACQMYDLILSYDKEddlq 202
                       170       180       190
                ....*....|....*....|....*....|....*
gi 35040    625 -VEATERQGGRTALHLATEMEELGLVTHLVTKLRA 658
Cdd:cd22192 203 pLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRH 237
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
667-695 9.92e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 9.92e-04
                           10        20
                   ....*....|....*....|....*....
gi 35040       667 GNTPLHLAAGLGYPTLTRLLLKAGADIHA 695
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
38-221 2.49e-120

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: 363.45  E-value: 2.49e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07934   1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSR-PQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSA 196
Cdd:cd07934  81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTgPYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                       170       180
                ....*....|....*....|....*
gi 35040    197 FLRASDGSFSLPLKPVTSQPIHDSK 221
Cdd:cd07934 161 YLRDSNGSYTLALKPVISDPIHDSK 185
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
38-221 1.48e-115

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: 351.40  E-value: 1.48e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEl 117
Cdd:cd07883   1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCED- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRPQ--------------GLTEAEQRELEQEAKELKK 183
Cdd:cd07883  80 GICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPgdlvhvdaegggdrQLTDEEQAEIRQKAKQQAK 159
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 35040    184 VMDLSIVRLRFSAFLRASDGSFSLPLKPVTSQPIHDSK 221
Cdd:cd07883 160 SMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
38-221 6.48e-79

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


Pssm-ID: 143640  Cd Length: 174  Bit Score: 253.83  E-value: 6.48e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGK-QCSE 116
Cdd:cd07827   1 PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPHQLVGKtDCRD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    117 lGICAVSVGPK-DMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRpqglteaeqreLEQEAKELKKVMDLSIVRLRFS 195
Cdd:cd07827  81 -GVCEVRLGPKnNMTASFNNLGIQCVRKKDVEEALGQRIQLGIDPFM-----------VHKGPEGNASDIDLNRVRLCFQ 148
                       170       180
                ....*....|....*....|....*.
gi 35040    196 AFLRASDGSFSLPLKPVTSQPIHDSK 221
Cdd:cd07827 149 AFIEDSDGGFTLPLPPVLSNPIYDKK 174
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
40-220 1.02e-78

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: 253.00  E-value: 1.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040       40 LVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSElGI 119
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKD-GV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      120 CAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQrqrlrsrpqgLTEAEQReLEQEAKELKKVMDLSIVRLRFSAFLR 199
Cdd:pfam00554  80 CEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-VGFEALRQIKDMDLNVVRLCFQAFLP 148
                         170       180
                  ....*....|....*....|.
gi 35040      200 ASDGSFSLPLKPVTSQPIHDS 220
Cdd:pfam00554 149 DTRGNFTTPLPPVVSNPIYDK 169
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
38-221 1.49e-72

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: 237.87  E-value: 1.49e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCsEL 117
Cdd:cd07935   1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHC-ED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGT----MIQKLQR---------------QRLRSRPQGLTEAEQRELEQEA 178
Cdd:cd07935  80 GICTVTAGPKDMVVGFANLGILHVTKKKVFETlearMTEACKKgynpgllvhpelaylQAEGGGDRQLTEREKEIIRQAA 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 35040    179 KELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVTSQPIHDSK 221
Cdd:cd07935 160 VQQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
228-327 4.49e-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: 4.49e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd01177   1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                        90       100
                ....*....|....*....|..
gi 35040    306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd01177  81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
229-328 2.09e-55

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


Pssm-ID: 465045  Cd Length: 102  Bit Score: 186.61  E-value: 2.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      229 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|..
gi 35040      307 LQLKRKRGGDVSDSKQFTYYPL 328
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLPL 102
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
228-327 1.12e-44

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


Pssm-ID: 238336  Cd Length: 101  Bit Score: 156.29  E-value: 1.12e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    228 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYE--DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKMKIERPVTV 305
Cdd:cd00602   1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEkgPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79
                        90       100
                ....*....|....*....|..
gi 35040    306 FLQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd00602  80 PIQLVRPDDRKRSEPLTFTYTP 101
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
38-221 4.27e-44

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: 157.26  E-value: 4.27e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEL 117
Cdd:cd07887   1 PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPHNLVGKEGCKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIqklQRQRLRSRPqglteaeQRELEQEAKELKKVmDLSIVRLRFSAF 197
Cdd:cd07887  81 GVCTKKINPTEMRIVFQKLGIQCVKKKDVEESLK---LREEINVDP-------FRTGFDHKDQINSI-DLNVVRLCFQVF 149
                       170       180
                ....*....|....*....|....
gi 35040    198 LRASDGSFSLPLKPVTSQPIHDSK 221
Cdd:cd07887 150 LEDENGRFTVPLPPVVSDPIYDKK 173
RHD-n_c-Rel cd07933
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ...
38-221 3.18e-41

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: 149.25  E-value: 3.18e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEl 117
Cdd:cd07933   1 PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPHDLVGKDCRD- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRqrlRSRPQGLTEAEQRELEQeakelkkvMDLSIVRLRFSAF 197
Cdd:cd07933  80 GYYEAEFGPERRVLAFQNLGIQCVRRREVKEAIMLRISR---GINPFNVPEEQLLQIEE--------YDLNVVRLCFQIF 148
                       170       180
                ....*....|....*....|....
gi 35040    198 LRASDGSFSLPLKPVTSQPIHDSK 221
Cdd:cd07933 149 LPDEHGNYTTALPPIVSNPIYDNR 172
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
38-221 2.92e-40

N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Relish protein, in which the RHD domain co-occurs with C-terminal ankyrin repeats. Family members are sometimes referred to as p110 or p68 (proteolytically processed form). Relish is an NF-kappa B-like transcription factor, which plays a role in mediating innate immunity in Drosophila. It is activated via the Imd (immune deficiency) pathway, which triggers phosphorylation of Relish. IKK-dependent proteolytic cleavage of Relish (which involves Dredd) results in a smaller active form (without the C-terminal ankyrin repeats), which is transported into the nucleus and functions as a transactivator.


Pssm-ID: 143644  Cd Length: 159  Bit Score: 145.65  E-value: 2.92e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRgFRFRYGCE-GPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRA-HAHSLVGKQCs 115
Cdd:cd07884   1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQADDNRRKpHVHKLVGKQG- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    116 ELGICAVSVGPK----DMTAQFNNLGVLHVTKKNMMGTMIQklqrqrlrsrpqglteaeqreleqeakelKKVMDLSIVR 191
Cdd:cd07884  79 DDDVCDPHDIEVspegDYVAMFQNMGIIHTAKKNIPEELYK-----------------------------KKNMNLNQVV 129
                       170       180       190
                ....*....|....*....|....*....|
gi 35040    192 LRFSAFLRASDGSFSLPLKPVTSQPIHDSK 221
Cdd:cd07884 130 LRFQAFAVSANGHLRPICPPVYSNPINNLK 159
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
38-221 8.06e-37

N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD domain of the RelA family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). RelA (also called p65) forms heterodimers with NF-kappa B1 (p50) and B2 (p52). RelA also forms homodimers.


Pssm-ID: 143645  Cd Length: 169  Bit Score: 136.54  E-value: 8.06e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSEl 117
Cdd:cd07885   1 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPHELVGKDCKD- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    118 GICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQrlrSRPQGLTEAEQREleqeakelkkVMDLSIVRLRFSAF 197
Cdd:cd07885  80 GYYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQRIQTN---NNPFNVPIEEQRA----------DYDLNAVRLCFQVT 146
                       170       180
                ....*....|....*....|....
gi 35040    198 LRASDGSFsLPLKPVTSQPIHDSK 221
Cdd:cd07885 147 VRDPSGRL-LPLPPVLSQPIYDNR 169
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
773-848 5.89e-36

Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the Nuclear Factor-KappaB2 (NF-kB2) precursor protein p100. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). NF-kB2 (or p52) is produced from the processing of the precursor protein p100, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the non-canonical NF-kB pathway. The p100 precursor is cytosolic and interacts with RelB. Upon phosphorylation by IKKalpha, p100 is processed to its 52kDa active, DNA-binding form and the p52/RelB complex is translocated into the nucleus. The non-canonical pathway plays a role in adaptive immunity and lymphorganogenesis. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176776  Cd Length: 76  Bit Score: 130.33  E-value: 5.89e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35040    773 ALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRG 848
Cdd:cd08798   1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
440-705 2.60e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    440 LQRAREYNARLFGLAHAAPSPTRLLRHRGRRALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIvyvihhAQDLGVV 519
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLL------LAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    520 NLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEG 599
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA--AYNGNLEIVKLLLEAGAD-----VNAQDNDG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    600 LYPVHLAVRARSPECLDLLVDSGAEVEATERQgGRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLGY 679
Cdd:COG0666 154 NTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGN 231
                       250       260
                ....*....|....*....|....*.
gi 35040    680 PTLTRLLLKAGADIHAENEEPLCPLP 705
Cdd:COG0666 232 LEIVKLLLEAGADLNAKDKDGLTALL 257
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
38-221 1.83e-32

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


Pssm-ID: 143646  Cd Length: 172  Bit Score: 123.82  E-value: 1.83e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVD--LVTHSDPPRAHAHSLVGKQCS 115
Cdd:cd07886   1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVTVTvcLVWKDPPHRVHPHGLVGKDCP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    116 ElGICAVSVGPKDMTAQ-FNNLGVLHVTKKNMMGTMIQKLQrqrlrsrpQGLT--EAEQRELEQEakelkkvMDLSIVRL 192
Cdd:cd07886  81 N-GICQVTLNPHSSPRHsFSNLGIQCVRKREIEAAIETRLQ--------LNIDpfKAGSLKNHEE-------VDMNVVRL 144
                       170       180
                ....*....|....*....|....*....
gi 35040    193 RFSAFLRASDGsFSLPLKPVTSQPIHDSK 221
Cdd:cd07886 145 CFQASYRDDDG-RKDCLSPVLSEPIYDKK 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
470-699 2.49e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 2.49e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    470 RALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVyvihhaqDLGV-VNLTNHLHQTPLHLAVITGQTSVVSFLLRV 548
Cdd:COG0666  70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL-------EAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    549 GADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEAT 628
Cdd:COG0666 143 GADVNAQDNDGNTPLHLA--AANGNLEIVKLLLEAGAD-----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35040    629 ERQgGRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEE 699
Cdd:COG0666 216 DND-GKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
506-704 3.08e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.80  E-value: 3.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    506 IVYVIHHAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGA 585
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAA--ALAGDLLVALLLLAAGA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    586 PavpqlLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGgRTALHLATEMEELGLVTHLVtKLRANVNARTF 665
Cdd:COG0666  79 D-----INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-ETPLHLAAYNGNLEIVKLLL-EAGADVNAQDN 151
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 35040    666 AGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPL 704
Cdd:COG0666 152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
773-847 1.17e-21

Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear Factor-KappaB (NF-kB) precursor proteins. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). Two of these, NF-kB1 and NF-kB2 are produced from the processing of the precursor proteins p105 and p100, respectively. In addition to RHD, p105 and p100 contain ANK repeats and a C-terminal DD. NF-kBs are regulated by the Inhibitor of NF-kB (IkB) Kinase (IKK) complex through classical and non-canonical pathways, which differ in the IKK subunits involved and downstream targets. IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. The precursor proteins p105 and p100 function as IkBs and as NF-kB proteins after being processed by the proteasome. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260024  Cd Length: 72  Bit Score: 89.61  E-value: 1.17e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35040    773 ALQNLEQLLDGpeaQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLR 847
Cdd:cd08310   1 TRLRLCKLLDV---GKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
470-704 1.76e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.70  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     470 RALL-AGQRhlLTAQDENGDTPLHLAIIHGQTsvIEQIVYVIHHAQDlgvVNLTNHLHQTPLH--LAVITGQTSVVSFLL 546
Cdd:PHA03095  67 RLLLeAGAD--VNAPERCGFTPLHLYLYNATT--LDVIKLLIKAGAD---VNAKDKVGRTPLHvyLSGFNINPKVIRLLL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     547 RVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVH---LAVRARsPECLDLLVDSGA 623
Cdd:PHA03095 140 RKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-----VYAVDDRFRSLLHhhlQSFKPR-ARIVRELIRAGC 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     624 EVEATERqGGRTALHLATeMEELGLVTHLVTKLRAN--VNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPL 701
Cdd:PHA03095 214 DPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLIAGisINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291

                 ...
gi 35040     702 CPL 704
Cdd:PHA03095 292 TPL 294
IPT smart00429
ig-like, plexins, transcription factors;
227-326 2.28e-18

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 80.54  E-value: 2.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040       227 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 35040       307 LQlkrkRGGDV-SDSKQFTYY 326
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
482-636 3.64e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 3.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    482 AQDENGDTPLHLAIIHGQTSVIEQIVyvihhaqDLGV-VNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGD 560
Cdd:COG0666 148 AQDNDGNTPLHLAAANGNLEIVKLLL-------EAGAdVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK 220
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35040    561 SAMHLAlrAGAGAPELLRALLQSGAPAVPQllhmpDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGRTA 636
Cdd:COG0666 221 TALDLA--AENGNLEIVKLLLEAGADLNAK-----DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-697 5.76e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      604 HLAVRARSPECLDLLVDSGAEVEATErQGGRTALHLATEMEELGLVTHLVTKLRANVNARtfaGNTPLHLAAGLGYPTLT 683
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 35040      684 RLLLKAGADIHAEN 697
Cdd:pfam12796  78 KLLLEKGADINVKD 91
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
228-327 2.98e-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: 2.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    228 LKISRMDKTAGSVRGGDEVYLLCDKVQKD-DIEVRFYeddengwqAFGDFSPTDVHkQYAIVFRTPPYHkmkIERPVTVF 306
Cdd:cd00102   1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFG--------GGVPCSVLSVS-STAIVCTTPPYA---NPGPGPVE 68
                        90       100
                ....*....|....*....|.
gi 35040    307 LQLKRKRGGDVSDSKQFTYYP 327
Cdd:cd00102  69 VTVDRGNGGITSSPLTFTYVP 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
530-628 4.93e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      530 LHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPAVpqllhmpDFEGLYPVHLAVRA 609
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLA--AKNGHLEIVKLLLEHADVNL-------KDNGRTALHYAARS 71
                          90
                  ....*....|....*....
gi 35040      610 RSPECLDLLVDSGAEVEAT 628
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVK 90
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
775-847 1.17e-11

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


Pssm-ID: 260063  Cd Length: 76  Bit Score: 61.08  E-value: 1.17e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35040    775 QNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLR 847
Cdd:cd08797   3 QQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIE 75
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
771-849 3.66e-11

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


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 60.12  E-value: 3.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040       771 DTALQNLEQLLDGPeAQGSWAELAERLGLRSLV------DTYRQTTSPSGSLLRSYELAGG---DLAGLLEALSDMGLEE 841
Cdd:smart00005   2 ELTRQKLAKLLDHP-LGLDWRELARKLGLSEADidqirtEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDD 80

                   ....*...
gi 35040       842 GVRLLRGP 849
Cdd:smart00005  81 AVELLRSE 88
PHA02878 PHA02878
ankyrin repeat protein; Provisional
538-706 6.95e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     538 QTSVVSFLLRVGADPALLDRH-GDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSPECLD 616
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYA--TENKDQRLTELLLSYGAN-----VNIPDKTNNSPLHHAVKHYNKPIVH 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     617 LLVDSGAEVEATERQGgRTALHLATEMEELGLVTHLVTKLRANVNAR-TFAGNTPLHLAagLGYPTLTRLLLKAGADIHA 695
Cdd:PHA02878 219 ILLENGASTDARDKCG-NTPLHISVGYCKDYDILKLLLEHGVDVNAKsYILGLTALHSS--IKSERKLKLLLEYGADINS 295
                        170
                 ....*....|.
gi 35040     696 ENEEPLCPLPS 706
Cdd:PHA02878 296 LNSYKLTPLSS 306
PHA02878 PHA02878
ankyrin repeat protein; Provisional
522-674 9.67e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 9.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     522 TNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGapELLRALLQSGApavpQLLHMpDFEGLY 601
Cdd:PHA02878 164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNK--PIVHILLENGA----STDAR-DKCGNT 236
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 35040     602 PVHLAV-RARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEElglVTHLVTKLRANVNARTFAGNTPLHLA 674
Cdd:PHA02878 237 PLHISVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSER---KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
489-693 1.05e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     489 TPLHLA--IIHGQTSVIEqIVYVI--HHAQdlgvVNLTNHLHQTPLHLAVIT--GQTSVVSFLLRVGADPALLDRHGDSA 562
Cdd:PHA03100  70 TPLHYLsnIKYNLTDVKE-IVKLLleYGAN----VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     563 MHLALRAGAGAPELLRALLQSGapavpqllhmpdfeglypVHLAVRARspecLDLLVDSGAEVEAT-ERqgGRTALHLAT 641
Cdd:PHA03100 145 LHLYLESNKIDLKILKLLIDKG------------------VDINAKNR----VNYLLSYGVPINIKdVY--GFTPLHYAV 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 35040     642 EMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADI 693
Cdd:PHA03100 201 YNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
472-556 3.17e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      472 LLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVyvihhaqDLGVVNLTNHlHQTPLHLAVITGQTSVVSFLLRVGAD 551
Cdd:pfam12796  15 LLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-------EHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD 86

                  ....*
gi 35040      552 PALLD 556
Cdd:pfam12796  87 INVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
484-704 6.63e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 6.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     484 DENGDTPLHLAIihgQTSVIEQIV-YVIHHAQDlgvVNLTNHLHQTPLHLAVITG-QTSVVSFLLRVGADPALLDRHGDS 561
Cdd:PHA02876 270 DDCKNTPLHHAS---QAPSLSRLVpKLLERGAD---VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYIT 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     562 AMHLALRAGAGApELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGrTALHLAT 641
Cdd:PHA02876 344 PLHQASTLDRNK-DIVITLLELGAN-----VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFAL 416
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 35040     642 EMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLG-YPTLTRLLLKAGADIHAENEEPLCPL 704
Cdd:PHA02876 417 CGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02874 PHA02874
ankyrin repeat protein; Provisional
479-693 9.19e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 9.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     479 LLTAQDENGDTPLHLAIIHG-QTSVI------EQIVYVIhhaQDLGV-VNLTNHLHQTPLHLAVITGQTSVVSFLLRVGA 550
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNGvDTSILpipcieKDMIKTI---LDCGIdVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     551 DPALLDRHGDSAMHLALRAGAGapELLRALLQSGApavpqLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVeATER 630
Cdd:PHA02874 149 DVNIEDDNGCYPIHIAIKHNFF--DIIKLLLEKGA-----YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKC 220
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35040     631 QGGRTALHLATeMEELGLVTHLVTKlrANVNARTFAGNTPLHLAagLGYPT---LTRLLLKAGADI 693
Cdd:PHA02874 221 KNGFTPLHNAI-IHNRSAIELLINN--ASINDQDIDGSTPLHHA--INPPCdidIIDILLYHKADI 281
PHA02875 PHA02875
ankyrin repeat protein; Provisional
525-782 5.25e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     525 LHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALR----------------AGAGAP----ELLRALLQSG 584
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKfrdseaikllmkhgaiPDVKYPdiesELHDAVEEGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     585 APAVPQLLHMPDF-------EGLYPVHLAVRARSPECLDLLVDSGAE--VEATERQggrTALHLATEMEELGLvTHLVTK 655
Cdd:PHA02875  81 VKAVEELLDLGKFaddvfykDGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKF---SPLHLAVMMGDIKG-IELLID 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     656 LRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSD------SEGPEKDTRSSFRG 729
Cdd:PHA02875 157 HKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDivrlfiKRGADCNIMFMIEG 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35040     730 --HTPLDLTCS-----------TLVKTLLLNAAQNTMEppltppspAGPGLSLGDTALQNLEQLLD 782
Cdd:PHA02875 237 eeCTILDMICNmctnleseaidALIADIAIRIHKKTIR--------RDEGFKNNMSTIEDKEEFKD 294
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
230-327 2.98e-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: 2.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    230 ISRMDKTAGSVRGGDEVYLLCDKVQKDDiEVRFYE---DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKMKIERPVTVF 306
Cdd:cd01178   4 IEKKSLNSCSVNGGEELFLTGKNFLKDS-KVVFQEkgqDGEAQWEAEATIDKEKSH-QNHLVVEVPPYHNKHVAAPVQVQ 81
                        90       100
                ....*....|....*....|....
gi 35040    307 LQL---KRKRggdvSDSKQFTYYP 327
Cdd:cd01178  82 FYVvngKRKR----SQPQTFTYTP 101
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
38-139 3.67e-08

N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells (NFAT) proteins and similar proteins; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes that are mainly involved in cell-cell interaction. Upon de-phosphorylation of the nuclear localization signal, NFAT enters the nucleus and acts as a transcription factor; its export from the nucleus is triggered by phosphorylation via export kinases. NFATs play important roles in mediating the immune response, and are found in T cells, B Cells, NK cells, mast cells, and monocytes. NFATs are also found in various non-hematopoietic cell types, where they play roles in development. This group also contains the N-terminal RHD sub-domain of the non-calcium regulated tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt.


Pssm-ID: 143648  Cd Length: 161  Bit Score: 53.82  E-value: 3.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     38 PYLVIVEQPKQRgFRFRY---GCEGPSHGGLPGassekgrkTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGK-- 112
Cdd:cd07927   1 YELRIEVQPEPH-HRARYeteGSRGAVKAPSTG--------GFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHRit 71
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 35040    113 -----QCSELGICAVSV------GPKDMTAQFNNLGVL 139
Cdd:cd07927  72 gktttPCKEKIIGNTKVleiplePKNNMTATIDCAGIL 109
PHA03100 PHA03100
ankyrin repeat protein; Provisional
507-698 5.99e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 5.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     507 VYVIHHAQDLGVVNLTNHLHQT-PLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGA---PELLRALLQ 582
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVlPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvKEIVKLLLE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     583 SGApavpqLLHMPDFEGLYPVHLAV--RARSPECLDLLVDSGAEVEATERQGGrTALHLATE-------MEELgLVTH-- 651
Cdd:PHA03100  95 YGA-----NVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLEsnkidlkILKL-LIDKgv 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 35040     652 ---------LVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENE 698
Cdd:PHA03100 168 dinaknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
Death pfam00531
Death domain;
775-847 8.07e-08

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 50.44  E-value: 8.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      775 QNLEQLLDGPEAQG-SWAELAERLGLRSL-VDT----YRQTTSPSGSLLRSYELAGG---DLAGLLEALSDMGLEEGVRL 845
Cdd:pfam00531   2 KQLDRLLDPPPPLGkDWRELARKLGLSENeIDEieseNPRLRSQTYELLRLWEQREGknaTVGTLLEALRKLGRRDAAEK 81

                  ..
gi 35040      846 LR 847
Cdd:pfam00531  82 IQ 83
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
527-600 1.32e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     527 QTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGapELLRALL-------QSGAPAVPQ--------- 590
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR--EVVQLLSrhsqchfELGANAKPDsftgkppsl 193
                         90
                 ....*....|....*
gi 35040     591 -----LLHMPDFEGL 600
Cdd:PTZ00322 194 edspiSSHHPDFSAV 208
PHA03095 PHA03095
ankyrin-like protein; Provisional
481-568 1.39e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     481 TAQDENGDTPLHLAIIHGQTSVIEQIVYVIHHAQdlgvVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGD 560
Cdd:PHA03095 216 AATDMLGNTPLHSMATGSSCKRSLVLPLLIAGIS----INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291

                 ....*...
gi 35040     561 SAMHLALR 568
Cdd:PHA03095 292 TPLSLMVR 299
PHA02875 PHA02875
ankyrin repeat protein; Provisional
488-655 1.54e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     488 DTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNltnhlHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAL 567
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKD-----GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     568 RagAGAPELLRALLQSGApavpqLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELG 647
Cdd:PHA02875 144 M--MGDIKGIELLIDHKA-----CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKID 216

                 ....*...
gi 35040     648 LVTHLVTK 655
Cdd:PHA02875 217 IVRLFIKR 224
PHA02876 PHA02876
ankyrin repeat protein; Provisional
427-631 2.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     427 SRTPQCEPQAPEMLQRAREYNARLFglahAAPSPTRLLRHRG------RRALLAGQRhlLTAQDENGDTPLHlaiihgQT 500
Cdd:PHA02876 281 SQAPSLSRLVPKLLERGADVNAKNI----KGETPLYLMAKNGydteniRTLIMLGAD--VNAADRLYITPLH------QA 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     501 SVIEQIVYVIHHAQDLGV-VNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALrAGAGAPELLRA 579
Cdd:PHA02876 349 STLDRNKDIVITLLELGAnVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL-CGTNPYMSVKT 427
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 35040     580 LLQSGAPAVPQLLHMPDfeglyPVHLAVRAR-SPECLDLLVDSGAEVEATERQ 631
Cdd:PHA02876 428 LIDRGANVNSKNKDLST-----PLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475
PHA02874 PHA02874
ankyrin repeat protein; Provisional
491-701 6.75e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 6.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     491 LHLAIIHGQTSVIEQIVyvihhAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAG 570
Cdd:PHA02874   5 LRMCIYSGDIEAIEKII-----KNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     571 AGapELLRALLQSGAPAvpQLLHMPDFEGlypvhlavrarspECLDLLVDSGAEVEATERQGgRTALHLATEMEELGLVT 650
Cdd:PHA02874  80 AH--DIIKLLIDNGVDT--SILPIPCIEK-------------DMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIK 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 35040     651 HLVtKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAEN---EEPL 701
Cdd:PHA02874 142 MLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDnngESPL 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
489-704 1.66e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     489 TPLHLAIIHGQTSVIEqivYVIHHAQDLGVVNlTNHLHqtPLHLAVITGQTSVVSFLLRVGADPALL------------- 555
Cdd:PHA02874  37 TPLIDAIRSGDAKIVE---LFIKHGADINHIN-TKIPH--PLLTAIKIGAHDIIKLLIDNGVDTSILpipciekdmikti 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     556 ----------DRHGDSAMHLALRAGAgaPELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAev 625
Cdd:PHA02874 111 ldcgidvnikDAELKTFLHYAIKKGD--LESIKMLFEYGAD-----VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA-- 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 35040     626 eaterqggrtalhlatemeelglvthlvtklRANVNarTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPL 704
Cdd:PHA02874 182 -------------------------------YANVK--DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
555-749 2.18e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     555 LDRHGDSAMHLALRAgagaPELLR---ALLQSGAPavpqlLHMPDFEGLYPVHL-AVRARSPECLDLLVDSGAEVEATER 630
Cdd:PHA02876 269 IDDCKNTPLHHASQA----PSLSRlvpKLLERGAD-----VNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADR 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     631 QGgRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEE-------PLCP 703
Cdd:PHA02876 340 LY-ITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKigtalhfALCG 418
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 35040     704 lPSPPTSDSDSDSEGPEKDTRSSFRGhTPLDLTCST-----LVKTLLLNAA 749
Cdd:PHA02876 419 -TNPYMSVKTLIDRGANVNSKNKDLS-TPLHYACKKnckldVIEMLLDNGA 467
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
519-698 3.31e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.85  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      519 VNLTNHLHQTPLHLAVITGQT-SVVSFLLRVGADPALldrhGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPD- 596
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDq 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      597 -----FEGLYPVHLAVRARSPECLDLLVDSGAEVEAteRQGGRTALhlatEMEELGLVTHlvtklranvnartfaGNTPL 671
Cdd:TIGR00870 121 ytsefTPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFV----KSQGVDSFYH---------------GESPL 179
                         170       180
                  ....*....|....*....|....*..
gi 35040      672 HLAAGLGYPTLTRLLLKAGADIHAENE 698
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADS 206
PHA02743 PHA02743
Viral ankyrin protein; Provisional
591-674 6.67e-06

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 47.12  E-value: 6.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     591 LLHMPDFEGLYPVHLAV---RARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAG 667
Cdd:PHA02743  49 LLHRYDHHGRQCTHMVAwydRANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQH 128

                 ....*..
gi 35040     668 NTPLHLA 674
Cdd:PHA02743 129 ETAYHIA 135
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
667-698 7.94e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 7.94e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 35040      667 GNTPLHLAAG-LGYPTLTRLLLKAGADIHAENE 698
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
490-758 1.07e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     490 PLHLAIIHGQTSVIEQIVYVIHHaqdlgvVNLTNHLHQTPLHLAVITGQTSVVSFLLRVgadpalldrHGDSAMHLALRA 569
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHN------VNQPDHRDLTPLHIICKEPNKLGMKEMIRS---------INKCSVFYTLVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     570 gagapelLRALLQSGAPAVPQLLHMPDFEGLYPVHLA-VRARS------PECLDLLVDSGAEVEATERQGGRTALHLATE 642
Cdd:PHA02878 105 -------IKDAFNNRNVEIFKIILTNRYKNIQTIDLVyIDKKSkddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     643 MEELGLVTHLVTKlRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSD------S 716
Cdd:PHA02878 178 NKDQRLTELLLSY-GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDilklllE 256
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 35040     717 EGPEKDTRSSFRGHTPLDLTCSTLVKTLLL-------NAAQNTMEPPLT 758
Cdd:PHA02878 257 HGVDVNAKSYILGLTALHSSIKSERKLKLLleygadiNSLNSYKLTPLS 305
PHA02878 PHA02878
ankyrin repeat protein; Provisional
484-627 1.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     484 DEN-GDTPLHLAIIHGQTSVIEqivYVIHHAQDLGVVNLTNhlhQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSA 562
Cdd:PHA02878 164 DRHkGNTALHYATENKDQRLTE---LLLSYGANVNIPDKTN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35040     563 MHLALrAGAGAPELLRALLQSGAPAVPQllhmPDFEGLYPVHLAVraRSPECLDLLVDSGAEVEA 627
Cdd:PHA02878 238 LHISV-GYCKDYDILKLLLEHGVDVNAK----SYILGLTALHSSI--KSERKLKLLLEYGADINS 295
Ank_5 pfam13857
Ankyrin repeats (many copies);
652-704 2.23e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 35040      652 LVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPL 704
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
487-687 3.64e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      487 GDTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNLTNHLH-------QTPLHLAVITGQTSVVSFLLRVGAD-PA----- 553
Cdd:TIGR00870  82 GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYtseftpgITALHLAAHRQNYEIVKLLLERGASvPAracgd 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      554 --LLDRHGDSAMH----LALRAGAGAPELLRALLQSGAPAVPQ------LLHM----PDFEGLYpvhlavRARSPECLDL 617
Cdd:TIGR00870 162 ffVKSQGVDSFYHgespLNAAACLGSPSIVALLSEDPADILTAdslgntLLHLlvmeNEFKAEY------EELSCQMYNF 235
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      618 LVDSGAeveaterqggrtalHLATEMEelglvthlvtkLRANVNartFAGNTPLHLAAGLGYPTLTRLLL 687
Cdd:TIGR00870 236 ALSLLD--------------KLRDSKE-----------LEVILN---HQGLTPLKLAAKEGRIVLFRLKL 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
487-546 4.84e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040      487 GDTPLHLAIIHGQTSVIEqivYVIHHAQDlgvVNLTNHLHQTPLHLAVITGQTSVVSFLL 546
Cdd:pfam13637   1 ELTALHAAAASGHLELLR---LLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
487-658 7.64e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.54  E-value: 7.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    487 GDTPLHLAIIHGQtsvIEQIVYVIHHAQDLGVVNLTNHLHQ--TPLHLAVITGQTSVVSFLLRVGADPA-------LLDR 557
Cdd:cd22192  51 GETALHVAALYDN---LEAAVVLMEAAPELVNEPMTSDLYQgeTALHIAVVNQNLNLVRELIARGADVVspratgtFFRP 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    558 HGDSAMH-----LALRAGAGAPELLRALLQSGAPAVPQllhmpDFEGLYPVHLAV----RARSPECLDLLVDSGAE---- 624
Cdd:cd22192 128 GPKNLIYygehpLSFAACVGNEEIVRLLIEHGADIRAQ-----DSLGNTVLHILVlqpnKTFACQMYDLILSYDKEddlq 202
                       170       180       190
                ....*....|....*....|....*....|....*
gi 35040    625 -VEATERQGGRTALHLATEMEELGLVTHLVTKLRA 658
Cdd:cd22192 203 pLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRH 237
Ank_5 pfam13857
Ankyrin repeats (many copies);
512-566 9.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 9.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 35040      512 HAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLA 566
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
528-696 1.05e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 1.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    528 TPLHLAVITGQTSVVSFLLRV-GADPALLDRHGDSAMHLAlrAGAGAPELLRALLQsgapAVPQLLHMPD----FEGLYP 602
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVA--ALYDNLEAAVVLME----AAPELVNEPMtsdlYQGETA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    603 VHLAVRARSPECLDLLVDSGAEVeATERQGGrtalhlatemeelglvthlvTKLRANVNARTFAGNTPLHLAAGLGYPTL 682
Cdd:cd22192  93 LHIAVVNQNLNLVRELIARGADV-VSPRATG--------------------TFFRPGPKNLIYYGEHPLSFAACVGNEEI 151
                       170
                ....*....|....
gi 35040    683 TRLLLKAGADIHAE 696
Cdd:cd22192 152 VRLLIEHGADIRAQ 165
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
533-697 1.24e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     533 AVITGQTSVVSFLLRVGADPALLDRHGDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSP 612
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIA--ASKGYEDCVLVLLKHACN-----VHIRDANGNTALWNAISAKHH 604
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     613 ECLDLLVDSGAeveATERQGGRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGAD 692
Cdd:PLN03192 605 KIFRILYHFAS---ISDPHAAGDLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680

                 ....*
gi 35040     693 IHAEN 697
Cdd:PLN03192 681 VDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
528-581 2.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 35040      528 TPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRagAGAPELLRALL 581
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS--NGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
667-695 2.69e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 2.69e-04
                          10        20
                  ....*....|....*....|....*....
gi 35040      667 GNTPLHLAAGLGYPTLTRLLLKAGADIHA 695
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
527-557 5.58e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 5.58e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 35040      527 QTPLHLAVI-TGQTSVVSFLLRVGADPALLDR 557
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
614-695 6.76e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.59  E-value: 6.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    614 CLDLLVDSGAEVEATErqgGRTALHLATEMEELGLVTHLVTKlRANVNART--------------FAGNTPLHLAAGLGY 679
Cdd:cd22194 125 ILDRFINAEYTEEAYE---GQTALNIAIERRQGDIVKLLIAK-GADVNAHAkgvffnpkykhegfYFGETPLALAACTNQ 200
                        90
                ....*....|....*.
gi 35040    680 PTLTRLLLKAGADIHA 695
Cdd:cd22194 201 PEIVQLLMEKESTDIT 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
559-619 9.82e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 9.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35040      559 GDSAMHLAlrAGAGAPELLRALLQSGAPavpqlLHMPDFEGLYPVHLAVRARSPECLDLLV 619
Cdd:pfam13637   1 ELTALHAA--AASGHLELLRLLLEKGAD-----INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
529-608 9.91e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.92  E-value: 9.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040    529 PLHLAVITGQTSVVSFLLRVGADPALL---DRHGDSAMHLALRAGAGAPE-------LLRALLQSGAPAVP--QLLHMPD 596
Cdd:cd22197 143 PLSLAACTKQWDVVNYLLENPHQPASLqaqDSLGNTVLHALVMIADNSPEnsalvikMYDGLLQAGARLCPtvQLEEISN 222
                        90
                ....*....|..
gi 35040    597 FEGLYPVHLAVR 608
Cdd:cd22197 223 HEGLTPLKLAAK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
667-695 9.92e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 9.92e-04
                           10        20
                   ....*....|....*....|....*....
gi 35040       667 GNTPLHLAAGLGYPTLTRLLLKAGADIHA 695
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
775-843 1.10e-03

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


Pssm-ID: 260064  Cd Length: 83  Bit Score: 38.84  E-value: 1.10e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35040    775 QNLEQLLDGPEAQGS-WAELAERLGLRSLVDTYRQTTSPSGSLLRSYE---LAGGDLAGLLEALSDMGLEEGV 843
Cdd:cd08799   7 QKLCGSLDAPQTRGNdWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEaqhFPDGNLSRLAAVLEEMGRHETV 79
PHA02946 PHA02946
ankyin-like protein; Provisional
520-704 1.22e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     520 NLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGApavpQLLHMPDFEG 599
Cdd:PHA02946  66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLVQYGA----KINNSVDEEG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     600 LYPVhLAVRARSPECLDLLVDSGAEVEATERQG-GRTALHLATEMEELGLVTHLVtKLRANVNARTFAGNTPLHLAAGLG 678
Cdd:PHA02946 142 CGPL-LACTDPSERVFKKIMSIGFEARIVDKFGkNHIHRHLMSDNPKASTISWMM-KLGISPSKPDHDGNTPLHIVCSKT 219
                        170       180
                 ....*....|....*....|....*..
gi 35040     679 YPTLTRL-LLKAGADIHAENEEPLCPL 704
Cdd:PHA02946 220 VKNVDIInLLLPSTDVNKQNKFGDSPL 246
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
633-695 1.25e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.56  E-value: 1.25e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35040    633 GRTALHLATEMEELGLVTHLVTKlRANVNART-------------FAGNTPLHLAAGLGYPTLTRLLLKAGADIHA 695
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVEN-GADVSARAtgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPAA 147
Death_UNC5B cd08802
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ...
781-841 1.95e-03

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


Pssm-ID: 176780  Cd Length: 84  Bit Score: 38.08  E-value: 1.95e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35040    781 LDGPEAQGS-WAELAERLGLRSLVDTYRQTTSPSGSLLRSYEL---AGGDLAGLLEALSDMGLEE 841
Cdd:cd08802  13 LDAPNSRGNdWRLLAQKLSMDRYLNYFATKASPTGVILDLWEArhqDDGDLNSLASALEEMGKSE 77
PHA02875 PHA02875
ankyrin repeat protein; Provisional
485-624 2.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     485 ENGDTPLHLAIIhgqTSVIEQIVYVIHHAQDLGVVNLTNHlhqTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMH 564
Cdd:PHA02875 100 KDGMTPLHLATI---LKKLDIMKLLIARGADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 35040     565 LALraGAGAPELLRALLQSGAPavpqllhmPDFEGLYP----VHLAVRARSPECLDLLVDSGAE 624
Cdd:PHA02875 174 IAM--AKGDIAICKMLLDSGAN--------IDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
658-704 2.60e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 2.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 35040     658 ANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPL 704
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
PHA02736 PHA02736
Viral ankyrin protein; Provisional
603-691 3.29e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35040     603 VHLAVR---ARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGY 679
Cdd:PHA02736  59 VHIVSNpdkADPQEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHD 138
                         90
                 ....*....|..
gi 35040     680 PTLTRLLLKAGA 691
Cdd:PHA02736 139 AKMMNILRAKGA 150
PHA03100 PHA03100
ankyrin repeat protein; Provisional
484-551 5.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 5.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 35040     484 DENGDTPLHLAIIHgqtSVIEQIVYVIHHAQDLGVVNLTNHlhqTPLHLAVITGQTSVVSFLLRVGAD 551
Cdd:PHA03100 189 DVYGFTPLHYAVYN---NNPEFVKYLLDLGANPNLVNKYGD---TPLHIAILNNNKEIFKLLLNNGPS 250
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
528-552 6.69e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 6.69e-03
                           10        20
                   ....*....|....*....|....*
gi 35040       528 TPLHLAVITGQTSVVSFLLRVGADP 552
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
526-552 6.83e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 6.83e-03
                          10        20
                  ....*....|....*....|....*..
gi 35040      526 HQTPLHLAVITGQTSVVSFLLRVGADP 552
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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