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Conserved domains on  [gi|998701737|ref|XP_015488549|]
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nuclear factor NF-kappa-B p100 subunit isoform X3 [Parus major]

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) ...
45-228 1.14e-123

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: 371.92  E-value: 1.14e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEA 124
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 125 GNCVTIVGPKDMTAQFSNLGVLHVTKKNMMEIMKEKLKQQKMRNRN-HLLTEVELREIELEAKELKKVMDLSIVRLRFTA 203
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTGpYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                        170       180
                 ....*....|....*....|....*
gi 998701737 204 YLRDSSGNFTLALQPVISDPIHDSK 228
Cdd:cd07934  161 YLRDSNGSYTLALKPVISDPIHDSK 185
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
235-334 1.08e-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: 198.31  E-value: 1.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 235 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKPKIDRPVTV 312
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 998701737 313 FLQLKRKRGGDVSDSKQFTYYP 334
Cdd:cd01177   81 KIQLKRPSDGERSESVPFTYVP 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-689 6.29e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 6.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 469 MLLAVQRHLAASQDENGDTPLHLAIIHEQTAVIKQLIDIIVSIpsqqiiNISNNLQQTPLHLAVITKQPQVVQLLLQARA 548
Cdd:COG0666   38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI------NAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 549 DPTLLDRYGNSLLHLALQAGDEEMLRTLLAHlGsATPYllrLPNFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERQs 628
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-G-ADVN---AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND- 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998701737 629 GRTPLHLAVEMENLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
795-870 3.93e-22

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08798:

Pssm-ID: 472698  Cd Length: 76  Bit Score: 91.03  E-value: 3.93e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998701737 795 ALQGLEQLLNQDCSGSDWIELAKRLGLCSLVETYKDTPSPSASLLRSYELAGGSLGGLLEALDSMGLHNAVRMLHK 870
Cdd:cd08798    1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
 
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) ...
45-228 1.14e-123

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: 371.92  E-value: 1.14e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEA 124
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 125 GNCVTIVGPKDMTAQFSNLGVLHVTKKNMMEIMKEKLKQQKMRNRN-HLLTEVELREIELEAKELKKVMDLSIVRLRFTA 203
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTGpYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                        170       180
                 ....*....|....*....|....*
gi 998701737 204 YLRDSSGNFTLALQPVISDPIHDSK 228
Cdd:cd07934  161 YLRDSNGSYTLALKPVISDPIHDSK 185
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
47-227 1.15e-84

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: 268.79  E-value: 1.15e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737   47 LVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEaGN 126
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKD-GV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  127 CVTIVGPKDMTAQFSNLGVLHVTKKNMMEIMKEKLKqqkmrnrnhlLTEVELReIELEAKELKKVMDLSIVRLRFTAYLR 206
Cdd:pfam00554  80 CEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-VGFEALRQIKDMDLNVVRLCFQAFLP 148
                         170       180
                  ....*....|....*....|.
gi 998701737  207 DSSGNFTLALQPVISDPIHDS 227
Cdd:pfam00554 149 DTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
235-334 1.08e-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: 198.31  E-value: 1.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 235 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKPKIDRPVTV 312
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 998701737 313 FLQLKRKRGGDVSDSKQFTYYP 334
Cdd:cd01177   81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
236-334 1.45e-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: 187.00  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  236 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKPKIDRPVTVF 313
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|.
gi 998701737  314 LQLKRKRGGDVSDSKQFTYYP 334
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLP 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-689 6.29e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 6.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 469 MLLAVQRHLAASQDENGDTPLHLAIIHEQTAVIKQLIDIIVSIpsqqiiNISNNLQQTPLHLAVITKQPQVVQLLLQARA 548
Cdd:COG0666   38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI------NAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 549 DPTLLDRYGNSLLHLALQAGDEEMLRTLLAHlGsATPYllrLPNFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERQs 628
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-G-ADVN---AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND- 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998701737 629 GRTPLHLAVEMENLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
795-870 3.93e-22

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: 91.03  E-value: 3.93e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998701737 795 ALQGLEQLLNQDCSGSDWIELAKRLGLCSLVETYKDTPSPSASLLRSYELAGGSLGGLLEALDSMGLHNAVRMLHK 870
Cdd:cd08798    1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
PHA03095 PHA03095
ankyrin-like protein; Provisional
456-691 1.29e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.17  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 456 HALLDYSVTADPRMLLAVqrhLAASQDEN-----GDTPLHLAIIHEQTA-VIKQLIDIIVSIpsqqiiNISNNLQQTPLH 529
Cdd:PHA03095  52 HLYLHYSSEKVKDIVRLL---LEAGADVNapercGFTPLHLYLYNATTLdVIKLLIKAGADV------NAKDKVGRTPLH 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 530 --LAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAG--DEEMLRTLLAHLGSATPyllRLPNFHGLLPVHLAVKA 605
Cdd:PHA03095 123 vyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYA---VDDRFRSLLHHHLQSFK 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 606 KSLACLDLLVRTGADVNAVERqSGRTPLHLAVeMENLNMATHLVKKL--GADINSRTFAGNTPLHLAAGLGSPTLTKLLL 683
Cdd:PHA03095 200 PRARIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLiaGISINARNRYGQTPLHYAAVFNNPRACRRLI 277

                 ....*...
gi 998701737 684 KAGADVLC 691
Cdd:PHA03095 278 ALGADINA 285
IPT smart00429
ig-like, plexins, transcription factors;
234-333 3.68e-18

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 80.16  E-value: 3.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737   234 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKPKIDRPVTVF 313
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 998701737   314 LQlkrkRGGDV-SDSKQFTYY 333
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
600-689 2.39e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  600 HLAVKAKSLACLDLLVRTGADVNaVERQSGRTPLHLAVEMENLNMATHLVKKLGADINSRtfaGNTPLHLAAGLGSPTLT 679
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
                          90
                  ....*....|
gi 998701737  680 KLLLKAGADV 689
Cdd:pfam12796  78 KLLLEKGADI 87
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
517-690 9.32e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 55.86  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  517 INISNNLQQTPLHLAVITKQPQ-VVQLLLQARADPtlldRYGNSLLHLA---LQAGDEEMLRTLLAHLGSATPYLLrlpn 592
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAIsleYVDAVEAILLHLLAAFRKSGPLEL---- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  593 fhgllpvhlaVKAKSLAcldllvrtgadvnavERQSGRTPLHLAVEMENLNMATHLVKKlGADINSRT------------ 660
Cdd:TIGR00870 117 ----------ANDQYTS---------------EFTPGITALHLAAHRQNYEIVKLLLER-GASVPARAcgdffvksqgvd 170
                         170       180       190
                  ....*....|....*....|....*....|..
gi 998701737  661 --FAGNTPLHLAAGLGSPTLTKLLLKAGADVL 690
Cdd:TIGR00870 171 sfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
485-604 5.93e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.09  E-value: 5.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 485 GDTPLHLAIIHEQTAVIKQLIDIIVSIPSQQIINI-----SNNL---QQTPLHLAVITKQPQVVQLLLQARADPTLLDRY 556
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 998701737 557 GNSLLH-LALQAGDE---EMLRTLLA---HLGSATPYllRLPNFHGLLPVHLAVK 604
Cdd:cd22192  169 GNTVLHiLVLQPNKTfacQMYDLILSydkEDDLQPLD--LVPNNQGLTPFKLAAK 221
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
629-657 1.21e-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: 37.18  E-value: 1.21e-03
                           10        20
                   ....*....|....*....|....*....
gi 998701737   629 GRTPLHLAVEMENLNMATHLVKKlGADIN 657
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDK-GADIN 29
 
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) ...
45-228 1.14e-123

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: 371.92  E-value: 1.14e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEA 124
Cdd:cd07934    1 PYLVIIEQPKQRGFRFRYVCEGPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLVTHTDPPRVHAHSLVGKHCNES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 125 GNCVTIVGPKDMTAQFSNLGVLHVTKKNMMEIMKEKLKQQKMRNRN-HLLTEVELREIELEAKELKKVMDLSIVRLRFTA 203
Cdd:cd07934   81 GNCSVDVGPKDMTAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTGpYKLTEAEERELEQEAKELKKVMDLSIVRLKFTA 160
                        170       180
                 ....*....|....*....|....*
gi 998701737 204 YLRDSSGNFTLALQPVISDPIHDSK 228
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 ...
45-228 2.66e-107

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: 329.44  E-value: 2.66e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEa 124
Cdd:cd07883    1 PYLEILEQPKQRGFRFRYGCEGPSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLVTNSEPPRLHAHSLVGKHCED- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 125 GNCVTIVGPKDMTAQFSNLGVLHVTKKNMMEIMKEKLKQQKMRNRNHL--------------LTEVELREIELEAKELKK 190
Cdd:cd07883   80 GICTVQVGPKDMTAQFPNLGILHVTKKNVVETLEARLLAQCTRGYNPGdlvhvdaegggdrqLTDEEQAEIRQKAKQQAK 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 998701737 191 VMDLSIVRLRFTAYLRDSSGNFTLALQPVISDPIHDSK 228
Cdd:cd07883  160 SMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
47-227 1.15e-84

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: 268.79  E-value: 1.15e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737   47 LVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEaGN 126
Cdd:pfam00554   1 LEIVEQPKQRGMRFRYKCEGRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPHRPHPHSLVGKDCKD-GV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  127 CVTIVGPKDMTAQFSNLGVLHVTKKNMMEIMKEKLKqqkmrnrnhlLTEVELReIELEAKELKKVMDLSIVRLRFTAYLR 206
Cdd:pfam00554  80 CEVELGPEDMVASFQNLGIQCVKKKDVEEALKERIE----------LNIDPFN-VGFEALRQIKDMDLNVVRLCFQAFLP 148
                         170       180
                  ....*....|....*....|.
gi 998701737  207 DSSGNFTLALQPVISDPIHDS 227
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 ...
45-228 5.89e-73

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: 238.64  E-value: 5.89e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCnEA 124
Cdd:cd07935    1 PYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHC-ED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 125 GNCVTIVGPKDMTAQFSNLGVLHVTKKNMMEIMKEKLKQQKMRNRN-------------------HLLTEVELREIELEA 185
Cdd:cd07935   80 GICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACKKGYNpgllvhpelaylqaegggdRQLTEREKEIIRQAA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 998701737 186 KELKKVMDLSIVRLRFTAYLRDSSGNFTLALQPVISDPIHDSK 228
Cdd:cd07935  160 VQQTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
45-228 1.36e-70

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: 231.10  E-value: 1.36e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEA 124
Cdd:cd07827    1 PYLEITEQPKQRGHRFRYECEGRSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDPPKPHPHQLVGKTDCRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 125 GNCVTIVGPK-DMTAQFSNLGVLHVTKKNMMEIMKEklKQQKMRNRNHLltevelreiELEAKELKKVMDLSIVRLRFTA 203
Cdd:cd07827   81 GVCEVRLGPKnNMTASFNNLGIQCVRKKDVEEALGQ--RIQLGIDPFMV---------HKGPEGNASDIDLNRVRLCFQA 149
                        170       180
                 ....*....|....*....|....*
gi 998701737 204 YLRDSSGNFTLALQPVISDPIHDSK 228
Cdd:cd07827  150 FIEDSDGGFTLPLPPVLSNPIYDKK 174
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
235-334 1.08e-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: 198.31  E-value: 1.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 235 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDEN--GWQAFGDFSPTDVHKQYAIVFRTPPYHKPKIDRPVTV 312
Cdd:cd01177    1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEEetVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVKV 80
                         90       100
                 ....*....|....*....|..
gi 998701737 313 FLQLKRKRGGDVSDSKQFTYYP 334
Cdd:cd01177   81 KIQLKRPSDGERSESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
236-334 1.45e-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: 187.00  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  236 KISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDE--NGWQAFGDFSPTDVHKQYAIVFRTPPYHKPKIDRPVTVF 313
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEEDDgqEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTVN 80
                          90       100
                  ....*....|....*....|.
gi 998701737  314 LQLKRKRGGDVSDSKQFTYYP 334
Cdd:pfam16179  81 IQLRRPSDKATSEPQPFTYLP 101
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
235-334 3.08e-45

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


Pssm-ID: 238336  Cd Length: 101  Bit Score: 157.83  E-value: 3.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 235 LKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYE--DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKPKIDRPVTV 312
Cdd:cd00602    1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEkgPGETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQV 79
                         90       100
                 ....*....|....*....|..
gi 998701737 313 FLQLKRKRGGDVSDSKQFTYYP 334
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; ...
45-228 4.64e-45

N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Dorsal and Dif (Dorsal-related immunity factor), and similar proteins. Dorsal and Dif are Rel-like transcription factors, which play roles in mediating innate immunity in Drosophila. They are activated via the Toll pathway. Cytoplasmic Dorsal/Dif are inactivated via forming a complex with Cactus, the Drosophila homologue of mammalian I-kappa B proteins. In response to signals, Cactus is degraded and Dorsal/Dif can be transported into the nucleus, where they act as transcription factors. Dorsal is also an essential gene in establishing the proper dorsal/ventral polarity in the developing embryo.


Pssm-ID: 143647  Cd Length: 173  Bit Score: 159.96  E-value: 4.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEA 124
Cdd:cd07887    1 PYVRIVEQPTSRALRFRYECEGRSAGSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPFRPHPHNLVGKEGCKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 125 GNCVTIVGPKDMTAQFSNLGVLHVTKKNmmeiMKEKLKQQKMRNRNHLLTEVElreielEAKELKKVmDLSIVRLRFTAY 204
Cdd:cd07887   81 GVCTKKINPTEMRIVFQKLGIQCVKKKD----VEESLKLREEINVDPFRTGFD------HKDQINSI-DLNVVRLCFQVF 149
                        170       180
                 ....*....|....*....|....
gi 998701737 205 LRDSSGNFTLALQPVISDPIHDSK 228
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 ...
45-228 2.96e-43

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


Pssm-ID: 143649  Cd Length: 172  Bit Score: 154.65  E-value: 2.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEa 124
Cdd:cd07933    1 PYVEIFEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPYKPHPHDLVGKDCRD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 125 GNCVTIVGPKDMTAQFSNLGVLHVTKKNmmeiMKEKLKQQKMRNRNHL-LTEVELREIEleakelkkVMDLSIVRLRFTA 203
Cdd:cd07933   80 GYYEAEFGPERRVLAFQNLGIQCVRRRE----VKEAIMLRISRGINPFnVPEEQLLQIE--------EYDLNVVRLCFQI 147
                        170       180
                 ....*....|....*....|....*
gi 998701737 204 YLRDSSGNFTLALQPVISDPIHDSK 228
Cdd:cd07933  148 FLPDEHGNYTTALPPIVSNPIYDNR 172
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
45-228 5.76e-37

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: 136.41  E-value: 5.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRgFRFRYGCE-GPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRV-HAHSLVGKQCN 122
Cdd:cd07884    1 PFLRIVEQPVDK-FRFRYKSEmHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQADDNRRKpHVHKLVGKQGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 123 EAGNCVTIVGPK---DMTAQFSNLGVLHVTKKNMMEIMKEklkqqkmrnrnhlltevelreieleakelKKVMDLSIVRL 199
Cdd:cd07884   80 DDVCDPHDIEVSpegDYVAMFQNMGIIHTAKKNIPEELYK-----------------------------KKNMNLNQVVL 130
                        170       180
                 ....*....|....*....|....*....
gi 998701737 200 RFTAYLRDSSGNFTLALQPVISDPIHDSK 228
Cdd:cd07884  131 RFQAFAVSANGHLRPICPPVYSNPINNLK 159
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-689 6.29e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 6.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 469 MLLAVQRHLAASQDENGDTPLHLAIIHEQTAVIKQLIDIIVSIpsqqiiNISNNLQQTPLHLAVITKQPQVVQLLLQARA 548
Cdd:COG0666   38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI------NAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 549 DPTLLDRYGNSLLHLALQAGDEEMLRTLLAHlGsATPYllrLPNFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERQs 628
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-G-ADVN---AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND- 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998701737 629 GRTPLHLAVEMENLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
45-228 3.72e-36

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: 134.61  E-value: 3.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGKQCNEa 124
Cdd:cd07885    1 PYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPHKPHPHELVGKDCKD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 125 GNCVTIVGPKDMTAQFSNLGVLHVTKKNMMEIMKEKLKQQKmrNRNHLLTEvelreieleakELKKVMDLSIVRLRFTAY 204
Cdd:cd07885   80 GYYEAELSPDRCIHSFQNLGIQCVKKRDLEQAVSQRIQTNN--NPFNVPIE-----------EQRADYDLNAVRLCFQVT 146
                        170       180
                 ....*....|....*....|....
gi 998701737 205 LRDSSGNFtLALQPVISDPIHDSK 228
Cdd:cd07885  147 VRDPSGRL-LPLPPVLSQPIYDNR 169
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
45-228 7.25e-34

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: 128.05  E-value: 7.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYTGMARIEVD--LVTHSDPPRVHAHSLVGKQCN 122
Cdd:cd07886    1 PRLLITEQPKQRGMRFRYECEGRSAGSILGESSTEANKTQPAIEIQNCIGLKEVTVTvcLVWKDPPHRVHPHGLVGKDCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 123 EaGNC-VTI---VGPKDmtaQFSNLGVLHVTKKNMMEIMKEKLKQ-----QKMRNRNHlltevelreieleakelkKVMD 193
Cdd:cd07886   81 N-GICqVTLnphSSPRH---SFSNLGIQCVRKREIEAAIETRLQLnidpfKAGSLKNH------------------EEVD 138
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 998701737 194 LSIVRLRFTAYLRDSSGnFTLALQPVISDPIHDSK 228
Cdd:cd07886  139 MNVVRLCFQASYRDDDG-RKDCLSPVLSEPIYDKK 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-695 4.91e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.69  E-value: 4.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 477 LAASQDENGDTPLHLAIIHEQTAVIKQLIDIIVSIPSQQIINISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRY 556
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 557 GNSLLHLALQAGDEEMLRTLLAHLGSatpylLRLPNFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERQsGRTPLHLA 636
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGAD-----VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 998701737 637 VEMENLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADVLCENDE 695
Cdd:COG0666  161 AANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
481-695 3.56e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 3.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 481 QDENGDTPLHLAIIHEQTAVIKQLIDIIVSIpsqqiiNISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSL 560
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADV------NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 561 LHLALQAGDEEMLRTLLAHlgsatpyllrlpnfhgllpvhlavkakslacldllvrtGADVNAVERQsGRTPLHLAVEME 640
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEA--------------------------------------GADVNAKDND-GKTALDLAAENG 230
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 998701737 641 NLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADVLCENDE 695
Cdd:COG0666  231 NLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
795-870 3.93e-22

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: 91.03  E-value: 3.93e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998701737 795 ALQGLEQLLNQDCSGSDWIELAKRLGLCSLVETYKDTPSPSASLLRSYELAGGSLGGLLEALDSMGLHNAVRMLHK 870
Cdd:cd08798    1 TLQRLEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLLRK 76
PHA03095 PHA03095
ankyrin-like protein; Provisional
456-691 1.29e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.17  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 456 HALLDYSVTADPRMLLAVqrhLAASQDEN-----GDTPLHLAIIHEQTA-VIKQLIDIIVSIpsqqiiNISNNLQQTPLH 529
Cdd:PHA03095  52 HLYLHYSSEKVKDIVRLL---LEAGADVNapercGFTPLHLYLYNATTLdVIKLLIKAGADV------NAKDKVGRTPLH 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 530 --LAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAG--DEEMLRTLLAHLGSATPyllRLPNFHGLLPVHLAVKA 605
Cdd:PHA03095 123 vyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYA---VDDRFRSLLHHHLQSFK 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 606 KSLACLDLLVRTGADVNAVERqSGRTPLHLAVeMENLNMATHLVKKL--GADINSRTFAGNTPLHLAAGLGSPTLTKLLL 683
Cdd:PHA03095 200 PRARIVRELIRAGCDPAATDM-LGNTPLHSMA-TGSSCKRSLVLPLLiaGISINARNRYGQTPLHYAAVFNNPRACRRLI 277

                 ....*...
gi 998701737 684 KAGADVLC 691
Cdd:PHA03095 278 ALGADINA 285
PHA03100 PHA03100
ankyrin repeat protein; Provisional
487-689 1.45e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.34  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 487 TPLHLAIIHEQTAVIKQLIDIIVSIPSqqiiNISNNLqqTPLHL-----AVITKQPQVVQLLLQARADPTLLDRYGNSLL 561
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINS----STKNNS--TPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 562 HLALQA--GDEEMLRTLLAHlgSATPYLLRlPNFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVER------------- 626
Cdd:PHA03100 111 LYAISKksNSYSIVEYLLDN--GANVNIKN-SDGENLLHLYLESNKIDLKILKLLIDKGVDINAKNRvnyllsygvpini 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 998701737 627 --QSGRTPLHLAVEMENLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:PHA03100 188 kdVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
IPT smart00429
ig-like, plexins, transcription factors;
234-333 3.68e-18

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 80.16  E-value: 3.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737   234 NLKISRMDKTAGSVRGGDEVyLLCDKVQKDDIEVRFYEddeNGWQAFGDFSPTdvhKQYAIVFRTPPYHKPKIDRPVTVF 313
Cdd:smart00429   1 DPVITRISPTSGPVSGGTEI-TLCGKNLKSISVVFVEV---GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPVRTV 73
                           90       100
                   ....*....|....*....|.
gi 998701737   314 LQlkrkRGGDV-SDSKQFTYY 333
Cdd:smart00429  74 GL----RNGGVpSSPQPFTYV 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
600-689 2.39e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  600 HLAVKAKSLACLDLLVRTGADVNaVERQSGRTPLHLAVEMENLNMATHLVKKLGADINSRtfaGNTPLHLAAGLGSPTLT 679
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
                          90
                  ....*....|
gi 998701737  680 KLLLKAGADV 689
Cdd:pfam12796  78 KLLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
542-689 6.80e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.15  E-value: 6.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 542 LLLQARADPTLLDRYGNSLLHLALQAGDEEMLRTLLAHLGSATPYLLRLPNFHGLLPVHLAVKAKSLACLDLLVRTGADV 621
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 998701737 622 NAVERQsGRTPLHLAVEMENLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:COG0666   81 NAKDDG-GNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
235-334 1.12e-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: 70.18  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 235 LKISRMDKTAGSVRGGDEVYLLCDKVQKD-DIEVRFYeddengwqAFGDFSPTDVHkQYAIVFRTPPYHKPkidRPVTVF 313
Cdd:cd00102    1 PVITSISPSSGPVSGGTEVTITGSNFGSGsNLRVTFG--------GGVPCSVLSVS-STAIVCTTPPYANP---GPGPVE 68
                         90       100
                 ....*....|....*....|.
gi 998701737 314 LQLKRKRGGDVSDSKQFTYYP 334
Cdd:cd00102   69 VTVDRGNGGITSSPLTFTYVP 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
528-623 7.78e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 7.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  528 LHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAGDEEMLRTLLAHLGsatpylLRLPNfHGLLPVHLAVKAKS 607
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD------VNLKD-NGRTALHYAARSGH 73
                          90
                  ....*....|....*.
gi 998701737  608 LACLDLLVRTGADVNA 623
Cdd:pfam12796  74 LEIVKLLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
522-670 3.52e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 3.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 522 NLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAGDEEMLRTLLAHlGSATPYLlrlpNFHGLLPVHL 601
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-GASTDAR----DKCGNTPLHI 240
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 602 AV-KAKSLACLDLLVRTGADVNAVERQSGRTPLHLAVEMENlnmATHLVKKLGADINSRTFAGNTPLHLA 670
Cdd:PHA02878 241 SVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSER---KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
486-657 5.35e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.95  E-value: 5.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 486 DTPLHLAIIHEQTAVIKQLIDIivsipSQQIINISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLAL 565
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDL-----GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 566 QAGDEEMLRTLLAHLGSatpylLRLPNFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERQSGRTPLHLAVEMENLNMA 645
Cdd:PHA02875 144 MMGDIKGIELLIDHKAC-----LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIV 218
                        170
                 ....*....|..
gi 998701737 646 THLVKKlGADIN 657
Cdd:PHA02875 219 RLFIKR-GADCN 229
PHA02736 PHA02736
Viral ankyrin protein; Provisional
554-687 5.54e-13

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 67.59  E-value: 5.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 554 DRYGNSLLHLALQAGDEEMLRTLLAHLGSATPYLLRLPNFHGLLPVHLAV---KAKSLACLDLLVRTGADVNAVERQSGR 630
Cdd:PHA02736  14 DIEGENILHYLCRNGGVTDLLAFKNAISDENRYLVLEYNRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERVFGN 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 998701737 631 TPLHLAVEMENLNMATHLVKKLGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGA 687
Cdd:PHA02736  94 TPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02878 PHA02878
ankyrin repeat protein; Provisional
482-689 9.05e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 9.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 482 DENGDTPLHLAIIHEQTAVIKQLIDII--------------------VSIPSQQIINISNNLQQTPL-HLAVITK----Q 536
Cdd:PHA02878  67 DHRDLTPLHIICKEPNKLGMKEMIRSInkcsvfytlvaikdafnnrnVEIFKIILTNRYKNIQTIDLvYIDKKSKddiiE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 537 PQVVQLLLQARADPTLLDRY-GNSLLHLALQAGDEEMLRTLLAHlgSATPyllRLPNFHGLLPVHLAVKAKSLACLDLLV 615
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSY--GANV---NIPDKTNNSPLHHAVKHYNKPIVHILL 221
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998701737 616 RTGADVNAVERqSGRTPLHLAV-EMENLNMATHLVKKlGADINSR-TFAGNTPLHLAagLGSPTLTKLLLKAGADV 689
Cdd:PHA02878 222 ENGASTDARDK-CGNTPLHISVgYCKDYDILKLLLEH-GVDVNAKsYILGLTALHSS--IKSERKLKLLLEYGADI 293
PHA03095 PHA03095
ankyrin-like protein; Provisional
539-689 1.02e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 539 VVQLLLQARADPTLLDRYGNSLLHLALQAG---DEEMLRTLL---AHLGSATPYllrlpnfhGLLPVHLAVK-AKSLACL 611
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLeagADVNAPERC--------GFTPLHLYLYnATTLDVI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 612 DLLVRTGADVNAVERqSGRTPLH--LAVEMENLNMATHLVKKlGADINSRTFAGNTPLHlaAGLGS----PTLTKLLLKA 685
Cdd:PHA03095 101 KLLIKAGADVNAKDK-VGRTPLHvyLSGFNINPKVIRLLLRK-GADVNALDLYGMTPLA--VLLKSrnanVELLRLLIDA 176

                 ....
gi 998701737 686 GADV 689
Cdd:PHA03095 177 GADV 180
PHA02875 PHA02875
ankyrin repeat protein; Provisional
492-689 3.10e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 492 AIIHEQTAVIKQLIDIIVSiPSQQIINisnnlQQTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAGDEE 571
Cdd:PHA02875   9 AILFGELDIARRLLDIGIN-PNFEIYD-----GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 572 MLRTLLAHLGSATPYLLRlpnfHGLLPVHLAVKAKSLACLDLLVRTGADVNaVERQSGRTPLHLAVEMENLNMaTHLVKK 651
Cdd:PHA02875  83 AVEELLDLGKFADDVFYK----DGMTPLHLATILKKLDIMKLLIARGADPD-IPNTDKFSPLHLAVMMGDIKG-IELLID 156
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 998701737 652 LGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:PHA02875 157 HKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
480-554 3.72e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 3.72e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 998701737  480 SQDENGDTPLHLAIIHEQTAVIKQLIDiivsipsQQIINISNNlQQTPLHLAVITKQPQVVQLLLQARADPTLLD 554
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLE-------HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
517-670 7.43e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 7.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 517 INISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAGDEEMLRTLLAHlGSatpyLLRLPNFHGL 596
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GA----YANVKDNNGE 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998701737 597 LPVHLAVKAKSLACLDLLVRTGADVnAVERQSGRTPLHLAVeMENLNMATHLVKKlgADINSRTFAGNTPLHLA 670
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLHNAI-IHNRSAIELLINN--ASINDQDIDGSTPLHHA 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
489-579 8.77e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 8.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  489 LHLAIIHEQTAVIKQLIDIIVSipsqqiINISNNLQQTPLHLAVITKQPQVVQLLLQ-ARADptlLDRYGNSLLHLALQA 567
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD------ANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVN---LKDNGRTALHYAARS 71
                          90
                  ....*....|..
gi 998701737  568 GDEEMLRTLLAH 579
Cdd:pfam12796  72 GHLEIVKLLLEK 83
PHA02875 PHA02875
ankyrin repeat protein; Provisional
483-656 4.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 483 ENGDTPLHLAIIHEQTAVIKQLidiivsIPSQQIINISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLH 562
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLL------IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 563 LALQAGDEEMLRTLLAHlGSATPYLLRLPNFHGLLpvhLAVKAKSLACLDLLVRTGADVNAVERQSGR--TPLHLAVEME 640
Cdd:PHA02875 174 IAMAKGDIAICKMLLDS-GANIDYFGKNGCVAALC---YAIENNKIDIVRLFIKRGADCNIMFMIEGEecTILDMICNMC 249
                        170
                 ....*....|....*.
gi 998701737 641 nLNMATHLVKKLGADI 656
Cdd:PHA02875 250 -TNLESEAIDALIADI 264
PHA02876 PHA02876
ankyrin repeat protein; Provisional
480-689 8.38e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 8.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 480 SQDENGDTPLHLAIiheQTAVIKQLIDIIVSIPSQqiINISNNLQQTPLHL-AVITKQPQVVQLLLQARADPTLLDRYGN 558
Cdd:PHA02876 268 SIDDCKNTPLHHAS---QAPSLSRLVPKLLERGAD--VNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLYI 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 559 SLLHLALQAGDEEMLRTLLAHLGSAtpylLRLPNFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERQSGrTPLHLAVE 638
Cdd:PHA02876 343 TPLHQASTLDRNKDIVITLLELGAN----VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALC 417
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 998701737 639 MENLNMATHLVKKLGADINSRTFAGNTPLHLAAGLG-SPTLTKLLLKAGADV 689
Cdd:PHA02876 418 GTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADV 469
PHA02878 PHA02878
ankyrin repeat protein; Provisional
468-637 1.29e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 468 RMLLAVQRHLAASQDENGDTPLHLAIIHEQTAVIKQLIDIIVSIpsqQIINISNNlqqTPLHLAVITKQPQVVQLLLQAR 547
Cdd:PHA02878 151 KLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANV---NIPDKTNN---SPLHHAVKHYNKPIVHILLENG 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 548 ADPTLLDRYGNSLLHLAL-QAGDEEMLRTLLAHLGS--ATPYLLrlpnfhGLLPVHLAVKAKSLacLDLLVRTGADVNAV 624
Cdd:PHA02878 225 ASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDvnAKSYIL------GLTALHSSIKSERK--LKLLLEYGADINSL 296
                        170
                 ....*....|...
gi 998701737 625 ERQSgRTPLHLAV 637
Cdd:PHA02878 297 NSYK-LTPLSSAV 308
PHA02743 PHA02743
Viral ankyrin protein; Provisional
594-693 1.31e-09

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 57.90  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 594 HGLLPVHLAV---KAKSLACLDLLVRTGADVNAVERQSGRTPLHLAVEMENLNMATHLVKKLGADINSRTFAGNTPLHLA 670
Cdd:PHA02743  56 HGRQCTHMVAwydRANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHETAYHIA 135
                         90       100
                 ....*....|....*....|...
gi 998701737 671 AGLGSPTLTKLLLKAGAdvLCEN 693
Cdd:PHA02743 136 YKMRDRRMMEILRANGA--VCDD 156
PHA02874 PHA02874
ankyrin repeat protein; Provisional
517-693 3.90e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 3.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 517 INISNNLQQTPLHLAVITKQPQVVQLLLQARAD----------P--TLLDRYGNSLLHLALQAG-----------DEEML 573
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADinhintkiphPllTAIKIGAHDIIKLLIDNGvdtsilpipciEKDMI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 574 RTLLAHLGSATPYLLRLPNFhgllpVHLAVKAKSLACLDLLVRTGADVNaVERQSGRTPLHLAVEMENLNMATHLVKKlG 653
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTF-----LHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEK-G 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 998701737 654 ADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADVL--CEN 693
Cdd:PHA02874 181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMnkCKN 222
PHA02876 PHA02876
ankyrin repeat protein; Provisional
497-689 4.85e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 4.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 497 QTAVIKQLIDIIvsipsQQIINISNNLQQTPLHL--AVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAGDEEMLR 574
Cdd:PHA02876 216 ECAVDSKNIDTI-----KAIIDNRSNINKNDLSLlkAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLV 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 575 TLLAHLGSAtpylLRLPNFHGLLPVHLAVK-AKSLACLDLLVRTGADVNAVERQSgRTPLHLAVEMENLNMATHLVKKLG 653
Cdd:PHA02876 291 PKLLERGAD----VNAKNIKGETPLYLMAKnGYDTENIRTLIMLGADVNAADRLY-ITPLHQASTLDRNKDIVITLLELG 365
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 998701737 654 ADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:PHA02876 366 ANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
237-334 1.07e-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: 53.64  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 237 ISRMDKTAGSVRGGDEVYLLCDKVQKDDiEVRFYE---DDENGWQAFGDFSPTDVHkQYAIVFRTPPYHKPKIDRPVTVF 313
Cdd:cd01178    4 IEKKSLNSCSVNGGEELFLTGKNFLKDS-KVVFQEkgqDGEAQWEAEATIDKEKSH-QNHLVVEVPPYHNKHVAAPVQVQ 81
                         90       100
                 ....*....|....*....|....
gi 998701737 314 LQL---KRKRggdvSDSKQFTYYP 334
Cdd:cd01178   82 FYVvngKRKR----SQPQTFTYTP 101
PHA02876 PHA02876
ankyrin repeat protein; Provisional
517-689 1.41e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 517 INISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAGDEEMLRTLLAHLGSATPYLLRLPNfhgl 596
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLK---- 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 597 lpvhlAVKAKSLACLDLLVRTGADVNAVErQSGRTPLHLAVEMENLnmaTHLVKKL---GADINSRTFAGNTPLHLAAGL 673
Cdd:PHA02876 247 -----AIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSL---SRLVPKLlerGADVNAKNIKGETPLYLMAKN 317
                        170
                 ....*....|....*..
gi 998701737 674 GSPTLT-KLLLKAGADV 689
Cdd:PHA02876 318 GYDTENiRTLIMLGADV 334
Ank_4 pfam13637
Ankyrin repeats (many copies);
526-577 4.23e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 998701737  526 TPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAGDEEMLRTLL 577
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
517-690 9.32e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 55.86  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  517 INISNNLQQTPLHLAVITKQPQ-VVQLLLQARADPtlldRYGNSLLHLA---LQAGDEEMLRTLLAHLGSATPYLLrlpn 592
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAIsleYVDAVEAILLHLLAAFRKSGPLEL---- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  593 fhgllpvhlaVKAKSLAcldllvrtgadvnavERQSGRTPLHLAVEMENLNMATHLVKKlGADINSRT------------ 660
Cdd:TIGR00870 117 ----------ANDQYTS---------------EFTPGITALHLAAHRQNYEIVKLLLER-GASVPARAcgdffvksqgvd 170
                         170       180       190
                  ....*....|....*....|....*....|..
gi 998701737  661 --FAGNTPLHLAAGLGSPTLTKLLLKAGADVL 690
Cdd:TIGR00870 171 sfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
PHA03095 PHA03095
ankyrin-like protein; Provisional
478-578 1.47e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 478 AASQDENGDTPLHLAIIHEQTA--VIKQLIDIIVSIpsqqiiNISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDR 555
Cdd:PHA03095 215 PAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISI------NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
                         90       100
                 ....*....|....*....|...
gi 998701737 556 YGNSLLHLALQAGDEEMLRTLLA 578
Cdd:PHA03095 289 DGNTPLSLMVRNNNGRAVRAALA 311
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
795-868 2.55e-07

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: 48.78  E-value: 2.55e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998701737 795 ALQGLEQLLNQDCsgsDWIELAKRLGLCSLVETYKDTPSPSASLLRSYELAGGSLGGLLEALDSMGLHNAVRML 868
Cdd:cd08310    1 TRLRLCKLLDVGK---DWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELI 71
PHA02741 PHA02741
hypothetical protein; Provisional
557-670 2.74e-07

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 51.20  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 557 GNSLLHLALQAGDEEMLRTLLAHL-GSATPYLLRLPNFHGLLPVHLAV----KAKSLACLDLLVRTGADVNAVERQSGRT 631
Cdd:PHA02741  21 GENFFHEAARCGCFDIIARFTPFIrGDCHAAALNATDDAGQMCIHIAAekheAQLAAEIIDHLIELGADINAQEMLEGDT 100
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 998701737 632 PLHLAVEMENLNMATHLVKKLGADINSRTFAGNTPLHLA 670
Cdd:PHA02741 101 ALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
485-604 5.93e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.09  E-value: 5.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 485 GDTPLHLAIIHEQTAVIKQLIDIIVSIPSQQIINI-----SNNL---QQTPLHLAVITKQPQVVQLLLQARADPTLLDRY 556
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 998701737 557 GNSLLH-LALQAGDE---EMLRTLLA---HLGSATPYllRLPNFHGLLPVHLAVK 604
Cdd:cd22192  169 GNTVLHiLVLQPNKTfacQMYDLILSydkEDDLQPLD--LVPNNQGLTPFKLAAK 221
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
45-186 8.64e-07

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: 49.58  E-value: 8.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  45 PYLVIIEQPKQRgFRFRY---GCEGPSHGGLPGassekgrkTYPTVKICNYTGMARIEVDLVTHSDPPRVHAHSLVGK-- 119
Cdd:cd07927    1 YELRIEVQPEPH-HRARYeteGSRGAVKAPSTG--------GFPTVKLHGYMEPVGLQVFIGTASGRLKPHAFYQVHRit 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 120 -----QCNE--AGNCVTIVGPKD----MTAQFSNLGVLHVTKKNmMEIMKEKLKQQKMRNRNHLLTEV-----ELREIEL 183
Cdd:cd07927   72 gktttPCKEkiIGNTKVLEIPLEpknnMTATIDCAGILKLRNAD-IELRKGETDIKKKNTRARLVFRVhipekDGRIVSL 150

                 ...
gi 998701737 184 EAK 186
Cdd:cd07927  151 QTA 153
PHA03100 PHA03100
ankyrin repeat protein; Provisional
484-583 8.72e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 8.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 484 NGDTPLHLAI--IHEQTAVIKQLID--------------IIVSIPsqqiINISNNLQQTPLHLAVITKQPQVVQLLLQAR 547
Cdd:PHA03100 140 DGENLLHLYLesNKIDLKILKLLIDkgvdinaknrvnylLSYGVP----INIKDVYGFTPLHYAVYNNNPEFVKYLLDLG 215
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 998701737 548 ADPTLLDRYGNSLLHLALQAGDEEMLRTLLAHLGSA 583
Cdd:PHA03100 216 ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
633-684 8.85e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 8.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 998701737  633 LHLAVEMENLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLLK 684
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLE 51
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
485-604 1.11e-06

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: 52.45  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 485 GDTPLHLAIIHEQTAVIKQLIDIIVSIPSQ---QIINISNNLQ-----QTPLHLAVITKQPQVVQLLLQARADP-TLLDR 555
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADVNAHakgVFFNPKYKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDiTSQDS 220
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 998701737 556 YGNSLLHLALQAGDE---------EMLRTLLahLGSATPYLLRLPNFHGLLPVHLAVK 604
Cdd:cd22194  221 RGNTVLHALVTVAEDsktqndfvkRMYDMIL--LKSENKNLETIRNNEGLTPLQLAAK 276
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
485-683 1.22e-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: 52.39  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  485 GDTPLHLAIIHEQTAViKQLIDIIVSIPSQQIINISNNLQ--------QTPLHLAVITKQPQVVQLLLQARADptlldry 556
Cdd:TIGR00870  82 GDTLLHAISLEYVDAV-EAILLHLLAAFRKSGPLELANDQytseftpgITALHLAAHRQNYEIVKLLLERGAS------- 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  557 gnsllhLALQAGDEEMLRTllahlgSATPYLlrlpnFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERQsGRTPLHLA 636
Cdd:TIGR00870 154 ------VPARACGDFFVKS------QGVDSF-----YHGESPLNAAACLGSPSIVALLSEDPADILTADSL-GNTLLHLL 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998701737  637 VE-----MENLNMATH---LVKKLGADINS-------RTFAGNTPLHLAAGLGSPTLTKLLL 683
Cdd:TIGR00870 216 VMenefkAEYEELSCQmynFALSLLDKLRDskeleviLNHQGLTPLKLAAKEGRIVLFRLKL 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
525-579 1.30e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 998701737 525 QTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLALQAGDEEMLRTLLAH 579
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
485-651 2.46e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 485 GDTPLHLAIIHEQTAVIKQLIDiivSIPsqQIIN--ISNNLQQ--TPLHLAVITKQPQVVQLLLQARAD----------- 549
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLME---AAP--ELVNepMTSDLYQgeTALHIAVVNQNLNLVRELIARGADvvspratgtff 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 550 ---PTLLDRYGNSLLHLALQAGDEEMLRTLLAHLGSatpylLRLPNFHGLLPVHLAV--KAKSLAC--LDLLV-----RT 617
Cdd:cd22192  126 rpgPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGAD-----IRAQDSLGNTVLHILVlqPNKTFACqmYDLILsydkeDD 200
                        170       180       190
                 ....*....|....*....|....*....|....
gi 998701737 618 GADVNAVERQSGRTPLHLAVEMENLNMATHLVKK 651
Cdd:cd22192  201 LQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
543-763 3.22e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 543 LLQARADPTLLDRYGNSLLHLALQAGDEEMLRTLLAHLGSatpylLRLPNFHGLLPVHLAVKAKSLACLDLLVRTGAdvn 622
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN-----VHIRDANGNTALWNAISAKHHKIFRILYHFAS--- 615
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 623 AVERQSGRTPLHLAVEMENLNMATHLVKkLGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADVLCEN-DEPMSLSS 701
Cdd:PLN03192 616 ISDPHAAGDLLCTAAKRNDLTAMKELLK-QGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPTE 694
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998701737 702 SEASSdtdtdpEEQELAMDLGEPalpaeHSTTSKLSTQGHWQAGQRQRRCHTSLDLTRSQKV 763
Cdd:PLN03192 695 LRELL------QKRELGHSITIV-----DSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRV 745
Ank_5 pfam13857
Ankyrin repeats (many copies);
517-564 4.17e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 4.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 998701737  517 INISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSLLHLA 564
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
613-694 5.12e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 5.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 613 LLVRTGADVNAVErQSGRTPLHLAvemenLNMATHLVKK-------LGADINSRTFAGNTPLHLAAGLGS-PTLTKLLLK 684
Cdd:PHA03095  32 RLLAAGADVNFRG-EYGKTPLHLY-----LHYSSEKVKDivrllleAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
                         90
                 ....*....|
gi 998701737 685 AGADVLCEND 694
Cdd:PHA03095 106 AGADVNAKDK 115
Ank_4 pfam13637
Ankyrin repeats (many copies);
595-645 6.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 6.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 998701737  595 GLLPVHLAVKAKSLACLDLLVRTGADVNAVERQsGRTPLHLAVEMENLNMA 645
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVL 50
PHA03100 PHA03100
ankyrin repeat protein; Provisional
482-556 1.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 1.03e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 998701737 482 DENGDTPLHLAIIHEQTAVIKQLIDiivsipSQQIINISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRY 556
Cdd:PHA03100 189 DVYGFTPLHYAVYNNNPEFVKYLLD------LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
597-689 1.26e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 597 LPVHLAVKAKSLACLDLLVRTgADVNAVERQS-GRTPLHLAVEMENLNMATHLVKKLGADIN----SRTFAGNTPLHLAA 671
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGAlGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97
                         90
                 ....*....|....*...
gi 998701737 672 GLGSPTLTKLLLKAGADV 689
Cdd:cd22192   98 VNQNLNLVRELIARGADV 115
PHA02874 PHA02874
ankyrin repeat protein; Provisional
481-670 1.68e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 481 QDENGDTPLHLAIIHEQTAVIKQLIDIIVSIpsqqiiNISNNLQQTPLHLAVITKQPQVVQLLLQARADPTLLDRYGNSL 560
Cdd:PHA02874 120 KDAELKTFLHYAIKKGDLESIKMLFEYGADV------NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 561 LHLALQAGDEEMLRTLLAHlgsaTPYLLRLPNfHGLLPVHLAVkAKSLACLDLLVrTGADVNaVERQSGRTPLHLAVeme 640
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDH----GNHIMNKCK-NGFTPLHNAI-IHNRSAIELLI-NNASIN-DQDIDGSTPLHHAI--- 262
                        170       180       190
                 ....*....|....*....|....*....|...
gi 998701737 641 NLNMATHLVKKL---GADINSRTFAGNTPLHLA 670
Cdd:PHA02874 263 NPPCDIDIIDILlyhKADISIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
464-647 2.15e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 464 TADPRMLLAVQRHLAASqDENGDTPLHlaiiheQTAVIKQLIDIIVSIPSQQI-INISNNLQQTPLHLAVITKQPQVVQL 542
Cdd:PHA02876 321 TENIRTLIMLGADVNAA-DRLYITPLH------QASTLDRNKDIVITLLELGAnVNARDYCDKTPIHYAAVRNNVVIINT 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 543 LLQARADPTLLDRYGNSLLHLALQAGDEEM-LRTLL---AHLGSATPYLLRlpnfhgllPVHLAVKAK-SLACLDLLVRT 617
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIdrgANVNSKNKDLST--------PLHYACKKNcKLDVIEMLLDN 465
                        170       180       190
                 ....*....|....*....|....*....|.
gi 998701737 618 GADVNAVERQSgRTPLHLAVEMENL-NMATH 647
Cdd:PHA02876 466 GADVNAINIQN-QYPLLIALEYHGIvNILLH 495
Ank_5 pfam13857
Ankyrin repeats (many copies);
613-670 2.92e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 998701737  613 LLVRTGADVNAvERQSGRTPLHLAVEMENLNMATHLVKkLGADINSRTFAGNTPLHLA 670
Cdd:pfam13857   1 LLEHGPIDLNR-LDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
514-692 3.62e-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: 47.31  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 514 QQIINISNnlqqTPLHLAVITKQPQVVQ-LLLQARADPTLLDRYGNSLLHLALQAGDEEMLRTLLahlgSATPYLLRLPN 592
Cdd:cd22192   11 LQQKRISE----SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM----EAAPELVNEPM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 593 ----FHGLLPVHLAVKAKSLACLDLLVRTGADVN------AVERQS-------GRTPLHLAVEMENLNMATHLVKKlGAD 655
Cdd:cd22192   83 tsdlYQGETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGpknliyyGEHPLSFAACVGNEEIVRLLIEH-GAD 161
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 998701737 656 INSRTFAGNTPLHLaaglgsptltkLLLKAGADVLCE 692
Cdd:cd22192  162 IRAQDSLGNTVLHI-----------LVLQPNKTFACQ 187
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
663-694 5.57e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 5.57e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 998701737  663 GNTPLHLAAG-LGSPTLTKLLLKAGADVLCEND 694
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
629-683 5.85e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 5.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 998701737  629 GRTPLHLAVEMENLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLL 683
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
648-695 2.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 998701737  648 LVKKLGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADVLCENDE 695
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
Ank_4 pfam13637
Ankyrin repeats (many copies);
485-544 2.63e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737  485 GDTPLHLAIIHEQTAVIKQLIDiivsipSQQIINISNNLQQTPLHLAVITKQPQVVQLLL 544
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE------KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
543-602 2.94e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998701737  543 LLQAR-ADPTLLDRYGNSLLHLALQAGDEEMLRTLLAHlgsatPYLLRLPNFHGLLPVHLA 602
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-----GVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
653-689 3.80e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 3.80e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 998701737 653 GADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
663-689 4.00e-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: 38.39  E-value: 4.00e-04
                          10        20
                  ....*....|....*....|....*..
gi 998701737  663 GNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
629-689 5.64e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 5.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 998701737 629 GRTPLHLAVEMENLNMATHLVKKlGADINSRT-------------FAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVEN-GADVSARAtgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQP 145
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
485-604 6.09e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 6.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 485 GDTPLHLAIIHEQTAVIKQLIDIIVSIPSQQIINISNNLQQT-------PLHLAVITKQPQVVQLLLQARADPTLL---D 554
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARATGRFFRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALeaqD 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998701737 555 RYGNSLLH-LALQAGDEEMLRTLLAHL----------GSATPYLLRLPNFHGLLPVHLAVK 604
Cdd:cd21882  153 SLGNTVLHaLVLQADNTPENSAFVCQMynlllsygahLDPTQQLEEIPNHQGLTPLKLAAV 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
600-684 6.39e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 600 HLAVKAKSLAcLDLLVRTGADVNAVERQsGRTPLHLAVEMENLNMATHLVkKLGADINSRTFAGNTPLHLAAGLGSPTLT 679
Cdd:PTZ00322  88 QLAASGDAVG-ARILLTGGADPNCRDYD-GRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVV 164

                 ....*
gi 998701737 680 KLLLK 684
Cdd:PTZ00322 165 QLLSR 169
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
525-555 9.34e-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: 37.65  E-value: 9.34e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 998701737  525 QTPLHLAVI-TKQPQVVQLLLQARADPTLLDR 555
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
576-636 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998701737  576 LLAHlgsaTPYLLRLPNFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERqSGRTPLHLA 636
Cdd:pfam13857   1 LLEH----GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
629-657 1.21e-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: 37.18  E-value: 1.21e-03
                           10        20
                   ....*....|....*....|....*....
gi 998701737   629 GRTPLHLAVEMENLNMATHLVKKlGADIN 657
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDK-GADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
549-638 1.55e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 549 DPTLLDRYGNSLLHLAlQAGDEEMLRTLLAhlGSATPyllRLPNFHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERQs 628
Cdd:PTZ00322  75 DPVVAHMLTVELCQLA-ASGDAVGARILLT--GGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD- 147
                         90
                 ....*....|
gi 998701737 629 GRTPLHLAVE 638
Cdd:PTZ00322 148 GKTPLELAEE 157
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
563-668 1.62e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.09  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 563 LALQAGDEEMLRTLLAhLGSATPYLLRLPN-------FHGLLPVHLAVKAKSLACLDLLVRTGADVNAVERQS------- 628
Cdd:cd22193   38 LNLNPGTNDTIRILLD-IAEKTDNLKRFINaeytdeyYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyq 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 998701737 629 ------GRTPLHLAVEMENLNMATHLVKK--LGADINSRTFAGNTPLH 668
Cdd:cd22193  117 gegfyfGELPLSLAACTNQPDIVQYLLENehQPADIEAQDSRGNTVLH 164
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
629-660 1.67e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 998701737  629 GRTPLHLAVEME-NLNMATHLVKKlGADINSRT 660
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSK-GADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
637-689 2.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 2.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 998701737 637 VEMENLNMATHLVKKlGADINSRTFAGNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:PHA02876 153 IQQDELLIAEMLLEG-GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADV 204
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
663-689 3.34e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.34e-03
                           10        20
                   ....*....|....*....|....*..
gi 998701737   663 GNTPLHLAAGLGSPTLTKLLLKAGADV 689
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
526-552 3.91e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.91e-03
                           10        20
                   ....*....|....*....|....*..
gi 998701737   526 TPLHLAVITKQPQVVQLLLQARADPTL 552
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
478-604 4.37e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.61  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 478 AASQDE--NGDTPLHLAIIHEQTAVIKQLIDIIVSIPS-------QQIINISNNLQQTPLHLAVITKQPQVVQLLLQARA 548
Cdd:cd22197   85 AQCTDEyyRGHSALHIAIEKRSLQCVKLLVENGADVHAracgrffQKKQGTCFYFGELPLSLAACTKQWDVVNYLLENPH 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 549 DPTLL---DRYGNSLLH-LALQAGDEEMLRTLLAHLGSA----------TPYLLRLPNFHGLLPVHLAVK 604
Cdd:cd22197  165 QPASLqaqDSLGNTVLHaLVMIADNSPENSALVIKMYDGllqagarlcpTVQLEEISNHEGLTPLKLAAK 234
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
797-878 5.00e-03

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: 36.81  E-value: 5.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 797 QGLEQLLNQDCSGSDWIELAKRLGLCSLVETYKDTPSPSASLLRSYELAGGSLGGllealdsmgLHNAVRMLHKTEALEK 876
Cdd:cd08797    3 QQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRE---------LLAALRQMGYTEAIEV 73

                 ..
gi 998701737 877 LQ 878
Cdd:cd08797   74 IE 75
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
485-604 6.36e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998701737 485 GDTPLHLAIIHEQTAVIKQLIDIIVSIPSQQIINISNNLQQ--------TPLHLAVITKQPQVVQLLLQ---ARADPTLL 553
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGRFFQPKYQgegfyfgeLPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998701737 554 DRYGNSLLHLALQAGDE---------EMLRTLLAHLGSATPY--LLRLPNFHGLLPVHLAVK 604
Cdd:cd22193  156 DSRGNTVLHALVTVADNtkentkfvtRMYDMILIRGAKLCPTveLEEIRNNDGLTPLQLAAK 217
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
484-511 6.84e-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: 6.84e-03
                           10        20
                   ....*....|....*....|....*...
gi 998701737   484 NGDTPLHLAIIHEQTAVIKQLIDIIVSI 511
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 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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