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Conserved domains on  [gi|45553319|ref|NP_996187|]
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relish, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 38-224 4.44e-88

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: 276.23  E-value: 4.44e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEKFRFRYKSEMHGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLD--SPHSHQLVVRKDDR 115
Cdd:cd07884   1 PFLRIVEQPVDKFRFRYKSEMHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQADDNrrKPHVHKLVGKQGDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 116 DVCDPHDLHVSKERGYVAQFINMGIIHTAKKYIFEELCKKKqdrlvfqmnrrelshkqlqelhqetereakDMNLNQVRL 195
Cdd:cd07884  81 DVCDPHDIEVSPEGDYVAMFQNMGIIHTAKKNIPEELYKKK------------------------------NMNLNQVVL 130

                       170       180
                ....*....|....*....|....*....
gi 45553319 196 CFEAFKIEDNGAWVPLAPPVYSNAINNRK 224
Cdd:cd07884 131 RFQAFAVSANGHLRPICPPVYSNPINNLK 159
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 231-334 3.98e-52

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: 176.74  E-value: 3.98e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 231 LRIVRLSKPTGGVMGNDELILLVEKVSKKNIKVRFFEEDEDgETVWEAYAKFRESDVHHQYAIVCQTPPYKDKDVDREVN 310
Cdd:cd01177   1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEE-ETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVK 79

                        90       100
                ....*....|....*....|....
gi 45553319 311 VYIELIRPSDDERSfPALPFRYKP 334
Cdd:cd01177  80 VKIQLKRPSDGERS-ESVPFTYVP 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
478-693 8.99e-24

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 8.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 478 IEHALNNYNRDTLLHEVISHKKDKLKLAIQTIQVMNYFNLKDVVNSTLNADGDSALHVACQQDRAHYIRPLLGMGCNPNL 557
Cdd:COG0666  36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 558 KNNAGNTPLHVAVKEEHLSCVESFL-NGVptvqlDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYDrTSISVANTmDGNN 636
Cdd:COG0666 116 RDKDGETPLHLAAYNGNLEIVKLLLeAGA-----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDN-DGET 188

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 45553319 637 ALHMAVLEQSVELLVLILDAQNenltdILQAQNAAGHTPLELAERKANDRVVQLLKN 693
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGA-----DVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
 
Name Accession Description Interval E-value
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 38-224 4.44e-88

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: 276.23  E-value: 4.44e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEKFRFRYKSEMHGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLD--SPHSHQLVVRKDDR 115
Cdd:cd07884   1 PFLRIVEQPVDKFRFRYKSEMHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQADDNrrKPHVHKLVGKQGDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 116 DVCDPHDLHVSKERGYVAQFINMGIIHTAKKYIFEELCKKKqdrlvfqmnrrelshkqlqelhqetereakDMNLNQVRL 195
Cdd:cd07884  81 DVCDPHDIEVSPEGDYVAMFQNMGIIHTAKKNIPEELYKKK------------------------------NMNLNQVVL 130

                       170       180
                ....*....|....*....|....*....
gi 45553319 196 CFEAFKIEDNGAWVPLAPPVYSNAINNRK 224
Cdd:cd07884 131 RFQAFAVSANGHLRPICPPVYSNPINNLK 159
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 40-223 1.16e-64

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: 214.09  E-value: 1.16e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319    40 LRIVEQPVEK-FRFRYKSEmHGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLD-SPHSHQLVVrKDDRDv 117
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCE-GRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPhRPHPHSLVG-KDCKD- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319   118 cDPHDLHVSKERgYVAQFINMGIIHTAKKYIFEELCKkkqdrlvfqmnRRELSHKQLQeLHQETEREAKDMNLNQVRLCF 197
Cdd:pfam00554  78 -GVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKE-----------RIELNIDPFN-VGFEALRQIKDMDLNVVRLCF 143

                         170       180
                  ....*....|....*....|....*.
gi 45553319   198 EAFKIEDNGAWVPLAPPVYSNAINNR 223
Cdd:pfam00554 144 QAFLPDTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 231-334 3.98e-52

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: 176.74  E-value: 3.98e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 231 LRIVRLSKPTGGVMGNDELILLVEKVSKKNIKVRFFEEDEDgETVWEAYAKFRESDVHHQYAIVCQTPPYKDKDVDREVN 310
Cdd:cd01177   1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEE-ETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVK 79

                        90       100
                ....*....|....*....|....
gi 45553319 311 VYIELIRPSDDERSfPALPFRYKP 334
Cdd:cd01177  80 VKIQLKRPSDGERS-ESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 232-335 7.83e-47

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: 161.96  E-value: 7.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319   232 RIVRLSKPTGGVMGNDELILLVEKVSKKNIKVRFFEEDeDGETVWEAYAKFRESDVHHQYAIVCQTPPYKDKDVDREVNV 311
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTV 79

                          90       100
                  ....*....|....*....|....
gi 45553319   312 YIELIRPSDDERSfPALPFRYKPR 335
Cdd:pfam16179  80 NIQLRRPSDKATS-EPQPFTYLPL 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
478-693 8.99e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 8.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 478 IEHALNNYNRDTLLHEVISHKKDKLKLAIQTIQVMNYFNLKDVVNSTLNADGDSALHVACQQDRAHYIRPLLGMGCNPNL 557
Cdd:COG0666  36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 558 KNNAGNTPLHVAVKEEHLSCVESFL-NGVptvqlDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYDrTSISVANTmDGNN 636
Cdd:COG0666 116 RDKDGETPLHLAAYNGNLEIVKLLLeAGA-----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDN-DGET 188

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 45553319 637 ALHMAVLEQSVELLVLILDAQNenltdILQAQNAAGHTPLELAERKANDRVVQLLKN 693
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGA-----DVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
Ank_2 pfam12796
Ankyrin repeats (3 copies);
533-622 1.75e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319   533 LHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLNgvpTVQLDLsltNDDGLTPLHMAIRQNKY 612
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNL---KDNGRTALHYAARSGHL 74

                          90
                  ....*....|
gi 45553319   613 DVAKKLISYD 622
Cdd:pfam12796  75 EIVKLLLEKG 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 467-624 1.08e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  467 KISHHKVEKWFIEHALN----NYNRDTLLHEVISHKKDKLKLAIQTIQVMNYFNLKDVVNSTL---------NADGDSAL 533
Cdd:PHA03100 117 KSNSYSIVEYLLDNGANvnikNSDGENLLHLYLESNKIDLKILKLLIDKGVDINAKNRVNYLLsygvpinikDVYGFTPL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  534 HVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLNGVPTVQL---DLSLTNDDGLTplhmaiRQN 610
Cdd:PHA03100 197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiieTLLYFKDKDLN------TIT 270

                        170
                 ....*....|....
gi 45553319  611 KYDVAKKLISYDRT 624
Cdd:PHA03100 271 KIKMLKKSIMYMFL 284
IPT smart00429
ig-like, plexins, transcription factors;
230-332 4.66e-10

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 57.05  E-value: 4.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319    230 ELRIVRLSKPTGGVMGNDElILLVEKVSKKnIKVRFFEEdedgeTVWEAYAKFRESdvhHQYAIVCQTPPYKDKDVDREV 309
Cdd:smart00429   1 DPVITRISPTSGPVSGGTE-ITLCGKNLKS-ISVVFVEV-----GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPV 70

                           90       100
                   ....*....|....*....|....
gi 45553319    310 N-VYIELirpsdDERSFPALPFRY 332
Cdd:smart00429  71 RtVGLRN-----GGVPSSPQPFTY 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 601-691 1.48e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 601 TPLHMAIRQNKYDVAKKLISYDRTSISVANTMdGNNALHMAVLEQSVELLVLILDAQNENLTDILQAQNAAGHTPLELAE 680
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAL-GETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLYQGETALHIAV 97

                        90
                ....*....|.
gi 45553319 681 RKANDRVVQLL 691
Cdd:cd22192  98 VNQNLNLVREL 108
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 598-624 9.50e-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: 34.49  E-value: 9.50e-03
                           10        20
                   ....*....|....*....|....*..
gi 45553319    598 DGLTPLHMAIRQNKYDVAKKLISYDRT 624
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
RHD-n_Relish cd07884
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ...
 38-224 4.44e-88

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: 276.23  E-value: 4.44e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEKFRFRYKSEMHGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLD--SPHSHQLVVRKDDR 115
Cdd:cd07884   1 PFLRIVEQPVDKFRFRYKSEMHGTHGSLLGERSTSSKKTFPTVKLCNYRGQAVIRCSLYQADDNrrKPHVHKLVGKQGDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 116 DVCDPHDLHVSKERGYVAQFINMGIIHTAKKYIFEELCKKKqdrlvfqmnrrelshkqlqelhqetereakDMNLNQVRL 195
Cdd:cd07884  81 DVCDPHDIEVSPEGDYVAMFQNMGIIHTAKKNIPEELYKKK------------------------------NMNLNQVVL 130

                       170       180
                ....*....|....*....|....*....
gi 45553319 196 CFEAFKIEDNGAWVPLAPPVYSNAINNRK 224
Cdd:cd07884 131 RFQAFAVSANGHLRPICPPVYSNPINNLK 159
RHD-n cd07827
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ...
 38-224 3.48e-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: 229.18  E-value: 3.48e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEK-FRFRYKSEMhGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNL-DSPHSHQLVVRKDDR 115
Cdd:cd07827   1 PYLEITEQPKQRgHRFRYECEG-RSAGSIPGENSTADRKTFPTVKLRNYNGPAKIVVSLVTKDDpPKPHPHQLVGKTDCR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 116 D-VCDPHDLHvskERGYVAQFINMGIIHTAKKYIFEELCKKKQDRLVFQMnrrelshkqlqeLHQETEREAKDMNLNQVR 194
Cdd:cd07827  80 DgVCEVRLGP---KNNMTASFNNLGIQCVRKKDVEEALGQRIQLGIDPFM------------VHKGPEGNASDIDLNRVR 144

                       170       180       190
                ....*....|....*....|....*....|
gi 45553319 195 LCFEAFKIEDNGAWVPLAPPVYSNAINNRK 224
Cdd:cd07827 145 LCFQAFIEDSDGGFTLPLPPVLSNPIYDKK 174
RHD_DNA_bind pfam00554
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ...
 40-223 1.16e-64

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: 214.09  E-value: 1.16e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319    40 LRIVEQPVEK-FRFRYKSEmHGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLD-SPHSHQLVVrKDDRDv 117
Cdd:pfam00554   1 LEIVEQPKQRgMRFRYKCE-GRSAGSIPGESSTRSKKTFPTVQICNYDGPAVIRVSLVTKDEPhRPHPHSLVG-KDCKD- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319   118 cDPHDLHVSKERgYVAQFINMGIIHTAKKYIFEELCKkkqdrlvfqmnRRELSHKQLQeLHQETEREAKDMNLNQVRLCF 197
Cdd:pfam00554  78 -GVCEVELGPED-MVASFQNLGIQCVKKKDVEEALKE-----------RIELNIDPFN-VGFEALRQIKDMDLNVVRLCF 143

                         170       180
                  ....*....|....*....|....*.
gi 45553319   198 EAFKIEDNGAWVPLAPPVYSNAINNR 223
Cdd:pfam00554 144 QAFLPDTRGNFTTPLPPVVSNPIYDK 169
IPT_NFkappaB cd01177
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ...
 231-334 3.98e-52

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: 176.74  E-value: 3.98e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 231 LRIVRLSKPTGGVMGNDELILLVEKVSKKNIKVRFFEEDEDgETVWEAYAKFRESDVHHQYAIVCQTPPYKDKDVDREVN 310
Cdd:cd01177   1 LKICRLDKTSGSVKGGDEVYLLCDKVQKEDIQVRFFEEDEE-ETVWEAFGDFSQTDVHRQYAIVFRTPPYHDPDITEPVK 79

                        90       100
                ....*....|....*....|....
gi 45553319 311 VYIELIRPSDDERSfPALPFRYKP 334
Cdd:cd01177  80 VKIQLKRPSDGERS-ESVPFTYVP 102
RHD_dimer pfam16179
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ...
 232-335 7.83e-47

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: 161.96  E-value: 7.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319   232 RIVRLSKPTGGVMGNDELILLVEKVSKKNIKVRFFEEDeDGETVWEAYAKFRESDVHHQYAIVCQTPPYKDKDVDREVNV 311
Cdd:pfam16179   1 KICRLSLCSGSVTGGEEIILLCEKVLKDDIKVRFYEED-DGQEVWEAEGDFSKTDVHRQVAIVFKTPPYRDPDITEPVTV 79

                          90       100
                  ....*....|....*....|....
gi 45553319   312 YIELIRPSDDERSfPALPFRYKPR 335
Cdd:pfam16179  80 NIQLRRPSDKATS-EPQPFTYLPL 102
IPT_TF cd00602
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ...
 231-334 1.29e-39

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: 141.65  E-value: 1.29e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 231 LRIVRLSKPTGGVMGNDELILLVEKVSKKNIKVRFFEEDEdGETVWEAYAKFRESDVHhQYAIVCQTPPYKDKDVDREVN 310
Cdd:cd00602   1 LPICRVSSLSGSVNGGDEVFLLCDKVNKPDIKVWFGEKGP-GETVWEAEAMFRQEDVR-QVAIVFKTPPYHNKWITRPVQ 78

                        90       100
                ....*....|....*....|....
gi 45553319 311 VYIELIRPSDDERSfPALPFRYKP 334
Cdd:cd00602  79 VPIQLVRPDDRKRS-EPLTFTYTP 101
RHD-n_NFkB cd07883
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ...
 38-224 1.95e-37

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: 139.15  E-value: 1.95e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEK-FRFRYKSEmhG-THGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFqTNLDSP--HSHQLVVRKD 113
Cdd:cd07883   1 PYLEILEQPKQRgFRFRYGCE--GpSHGGLPGASSEKNKKSYPTVKICNYQGPARIVVQLV-TNSEPPrlHAHSLVGKHC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 114 DRDVC----DPHDLhvskergyVAQFINMGIIHTAKKYIFEELCKK--KQDRLVFQMN-----------RRELSHKQLQE 176
Cdd:cd07883  78 EDGICtvqvGPKDM--------TAQFPNLGILHVTKKNVVETLEARllAQCTRGYNPGdlvhvdaegggDRQLTDEEQAE 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 45553319 177 LHQETEREAKDMNLNQVRLCFEAFKIEDNGAWVPLAPPVYSNAINNRK 224
Cdd:cd07883 150 IRQKAKQQAKSMDLSVVRLCFQAFLPDSNGSFTRPLKPVISDAIYDSK 197
RHD-n_NFkB2 cd07934
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ...
 38-224 3.64e-30

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: 117.69  E-value: 3.64e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEK-FRFRYKSEmHGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFqTNLDSP--HSHQLVVRK-D 113
Cdd:cd07934   1 PYLVIIEQPKQRgFRFRYVCE-GPSHGGLPGASSEKGRKTYPTVKICNYVGMARIEVDLV-THTDPPrvHAHSLVGKHcN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 114 DRDVC----DPHDLhvskergyVAQFINMGIIHTAKKYIFEELCKKKQDRLVFQMNRRELSHKQLQELHQETEREAKDMN 189
Cdd:cd07934  79 ESGNCsvdvGPKDM--------TAQFSNLGILHVTKKNMMEILKEKLKRQKLRNTGPYKLTEAEERELEQEAKELKKVMD 150

                       170       180       190
                ....*....|....*....|....*....|....*
gi 45553319 190 LNQVRLCFEAFKIEDNGAWVPLAPPVYSNAINNRK 224
Cdd:cd07934 151 LSIVRLKFTAYLRDSNGSYTLALKPVISDPIHDSK 185
RHD-n_NFkB1 cd07935
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ...
 38-224 3.19e-26

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: 106.90  E-value: 3.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEK-FRFRYKSEmHGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFqTNLDSP--HSHQLVVRKDD 114
Cdd:cd07935   1 PYLQILEQPKQRgFRFRYVCE-GPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLV-TNGKNIhlHAHSLVGKHCE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 115 RDVC----DPHDLHVSkergyvaqFINMGIIHTAKKYIFEELCKKKQDRLVFQMNRRELSHKQLQELHQE-------TER 183
Cdd:cd07935  79 DGICtvtaGPKDMVVG--------FANLGILHVTKKKVFETLEARMTEACKKGYNPGLLVHPELAYLQAEgggdrqlTER 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 45553319 184 E-----------AKDMNLNQVRLCFEAFKIEDNGAWVPLAPPVYSNAINNRK 224
Cdd:cd07935 151 EkeiirqaavqqTKEMDLSVVRLMFTAFLPDSTGGFTRRLEPVVSDAIYDSK 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
478-693 8.99e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 8.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 478 IEHALNNYNRDTLLHEVISHKKDKLKLAIQTIQVMNYFNLKDVVNSTLNADGDSALHVACQQDRAHYIRPLLGMGCNPNL 557
Cdd:COG0666  36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 558 KNNAGNTPLHVAVKEEHLSCVESFL-NGVptvqlDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYDrTSISVANTmDGNN 636
Cdd:COG0666 116 RDKDGETPLHLAAYNGNLEIVKLLLeAGA-----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDN-DGET 188

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 45553319 637 ALHMAVLEQSVELLVLILDAQNenltdILQAQNAAGHTPLELAERKANDRVVQLLKN 693
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGA-----DVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
RHD-n_Dorsal_Dif cd07887
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ...
 38-224 3.34e-23

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: 97.17  E-value: 3.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEK-FRFRYKSEMHGThGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLD-SPHSHQLVVRKD-D 114
Cdd:cd07887   1 PYVRIVEQPTSRaLRFRYECEGRSA-GSIPGANSTSEGKTFPTIQVVNYDGRAVVVVSCVTKDEPfRPHPHNLVGKEGcK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 115 RDVC----DPHDLHVSkergyvaqFINMGiIHTAKKYIFEELCKKKQDRLVFQMnRRELSHKQlqelhqeterEAKDMNL 190
Cdd:cd07887  80 KGVCtkkiNPTEMRIV--------FQKLG-IQCVKKKDVEESLKLREEINVDPF-RTGFDHKD----------QINSIDL 139

                       170       180       190
                ....*....|....*....|....*....|....
gi 45553319 191 NQVRLCFEAFKIEDNGAWVPLAPPVYSNAINNRK 224
Cdd:cd07887 140 NVVRLCFQVFLEDENGRFTVPLPPVVSDPIYDKK 173
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
481-695 3.21e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 3.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 481 ALNNYNRDTLLHEVISHK-KDKLKLAIQtiqvmnyfnLKDVVNSTlNADGDSALHVACQQDRAHYIRPLLGMGCNPNLKN 559
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGdLEIVKLLLE---------AGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 560 NAGNTPLHVAVKEEHLSCVESFL-NGVptvqlDLSLTNDDGLTPLHMAIRQNKYDVAKKLISY--DRTsisvANTMDGNN 636
Cdd:COG0666 151 NDGNTPLHLAAANGNLEIVKLLLeAGA-----DVNARDNDGETPLHLAAENGHLEIVKLLLEAgaDVN----AKDNDGKT 221

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 45553319 637 ALHMAVLEQSVELLVLILDAQNENLTDILQAQNAAGHTPLELAERKANDRVVQLLKNVY 695
Cdd:COG0666 222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
RHD-n_c-Rel cd07933
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ...
 38-223 5.64e-18

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: 82.23  E-value: 5.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEK-FRFRYKSEMHgTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLD-SPHSHQLVvRKDDR 115
Cdd:cd07933   1 PYVEIFEQPRQRgMRFRYKCEGR-SAGSIPGERSTDNNRTYPSIQILNYTGKGKVRITLVTKNEPyKPHPHDLV-GKDCR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 116 DvcDPHDLHVSKERGYVAqFINMGIIHTAKKYIFEELCKkkqdRLVFQMNRRELSHKQLQELhqetereaKDMNLNQVRL 195
Cdd:cd07933  79 D--GYYEAEFGPERRVLA-FQNLGIQCVRRREVKEAIML----RISRGINPFNVPEEQLLQI--------EEYDLNVVRL 143

                       170       180
                ....*....|....*....|....*....
gi 45553319 196 CFEAFKIEDNGAWVPLAPPVYSNAI-NNR 223
Cdd:cd07933 144 CFQIFLPDEHGNYTTALPPIVSNPIyDNR 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
481-691 1.20e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 1.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 481 ALNNYNRDTLLHEVISHKKDKLKLAIQTIQVMNYFNLKDVVNSTLNADGDSALHVACQQDRAHYIRPLLGMGCNPNLKNN 560
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 561 AGNTPLHVAVKEEHLSCVESFL-NGVptvqlDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYDrtsisvAN----TMDGN 635
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLeAGA-----DVNARDKDGETPLHLAAYNGNLEIVKLLLEAG------ADvnaqDNDGN 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 45553319 636 NALHMAVLEQSVELLVLILDAqnenlTDILQAQNAAGHTPLELAERKANDRVVQLL 691
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLLEA-----GADVNARDNDGETPLHLAAENGHLEIVKLL 205
RHD-n_RelA cd07885
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ...
 38-223 2.97e-16

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: 77.22  E-value: 2.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEK-FRFRYKSEMHgTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLD-SPHSHQLVvRKDDR 115
Cdd:cd07885   1 PYVEIIEQPKQRgMRFRYKCEGR-SAGSIPGERSTDTTKTHPTIKINNYTGPGRVRISLVTKDPPhKPHPHELV-GKDCK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 116 DVCDPHDLhvSKERGyVAQFINMGIIHTAKKyifeELCKKKQDRLVFQMNrrelshkqlqELHQETEREAKDMNLNQVRL 195
Cdd:cd07885  79 DGYYEAEL--SPDRC-IHSFQNLGIQCVKKR----DLEQAVSQRIQTNNN----------PFNVPIEEQRADYDLNAVRL 141

                       170       180
                ....*....|....*....|....*....
gi 45553319 196 CFEAFKIEDNGAWVPLaPPVYSNAI-NNR 223
Cdd:cd07885 142 CFQVTVRDPSGRLLPL-PPVLSQPIyDNR 169
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
526-671 8.87e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 8.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 526 NADGDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFL-NGVptvqlDLSLTNDDGLTPLH 604
Cdd:COG0666 150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLeAGA-----DVNAKDNDGKTALD 224

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553319 605 MAIRQNKYDVAKKLIsyDRTSISVANTMDGNNALHMAVLEQSVELLVLILDAQNENLTDILQAQNAA 671
Cdd:COG0666 225 LAAENGNLEIVKLLL--EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
533-622 1.75e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319   533 LHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLNgvpTVQLDLsltNDDGLTPLHMAIRQNKY 612
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNL---KDNGRTALHYAARSGHL 74

                          90
                  ....*....|
gi 45553319   613 DVAKKLISYD 622
Cdd:pfam12796  75 EIVKLLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
566-663 1.50e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319   566 LHVAVKEEHLSCVESFLNGVPtvqlDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYdrtsISVANTMDGNNALHMAVLEQ 645
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA----DANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDNGRTALHYAARSG 72

                          90
                  ....*....|....*....
gi 45553319   646 SVELL-VLILDAQNENLTD 663
Cdd:pfam12796  73 HLEIVkLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 467-624 1.08e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  467 KISHHKVEKWFIEHALN----NYNRDTLLHEVISHKKDKLKLAIQTIQVMNYFNLKDVVNSTL---------NADGDSAL 533
Cdd:PHA03100 117 KSNSYSIVEYLLDNGANvnikNSDGENLLHLYLESNKIDLKILKLLIDKGVDINAKNRVNYLLsygvpinikDVYGFTPL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  534 HVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLNGVPTVQL---DLSLTNDDGLTplhmaiRQN 610
Cdd:PHA03100 197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiieTLLYFKDKDLN------TIT 270

                        170
                 ....*....|....
gi 45553319  611 KYDVAKKLISYDRT 624
Cdd:PHA03100 271 KIKMLKKSIMYMFL 284
RHD-n_RelB cd07886
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ...
 38-224 4.18e-10

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: 59.49  E-value: 4.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  38 PQLRIVEQPVEK-FRFRYKSEMHGThGSLNGANSKRTPKTFPEVTLCNYDG---PAVIRCSLFQTNLDSPHSHQLVVRKD 113
Cdd:cd07886   1 PRLLITEQPKQRgMRFRYECEGRSA-GSILGESSTEANKTQPAIEIQNCIGlkeVTVTVCLVWKDPPHRVHPHGLVGKDC 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 114 DRDVC----DPHDlhvskerGYVAQFINMGIihtakkyifeeLCKKKQDRLVFQMNRRELSHKQLQ----ELHQEterea 185
Cdd:cd07886  80 PNGICqvtlNPHS-------SPRHSFSNLGI-----------QCVRKREIEAAIETRLQLNIDPFKagslKNHEE----- 136

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 45553319 186 kdMNLNQVRLCFEAfKIEDNGAWVPLAPPVYSNAINNRK 224
Cdd:cd07886 137 --VDMNVVRLCFQA-SYRDDDGRKDCLSPVLSEPIYDKK 172
IPT smart00429
ig-like, plexins, transcription factors;
230-332 4.66e-10

ig-like, plexins, transcription factors;


Pssm-ID: 214657 [Multi-domain]  Cd Length: 90  Bit Score: 57.05  E-value: 4.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319    230 ELRIVRLSKPTGGVMGNDElILLVEKVSKKnIKVRFFEEdedgeTVWEAYAKFRESdvhHQYAIVCQTPPYKDKDVDREV 309
Cdd:smart00429   1 DPVITRISPTSGPVSGGTE-ITLCGKNLKS-ISVVFVEV-----GVGEAPCTFSPS---SSTAIVCKTPPYHNIPGSVPV 70

                           90       100
                   ....*....|....*....|....
gi 45553319    310 N-VYIELirpsdDERSFPALPFRY 332
Cdd:smart00429  71 RtVGLRN-----GGVPSSPQPFTY 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 528-691 1.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  528 DGDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLngvptvqlDL-SLTND----DGLTP 602
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL--------DLgKFADDvfykDGMTP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  603 LHMAIRQNKYDVAKKLISYdRTSISVANTmDGNNALHMAVLEQSVELLVLILDaqNENLTDIlqaQNAAGHTPLELAERK 682
Cdd:PHA02875 106 LHLATILKKLDIMKLLIAR-GADPDIPNT-DKFSPLHLAVMMGDIKGIELLID--HKACLDI---EDCCGCTPLIIAMAK 178


                 ....*....
gi 45553319  683 ANDRVVQLL 691
Cdd:PHA02875 179 GDIAICKML 187
PHA03095 PHA03095
ankyrin-like protein; Provisional
 508-665 2.22e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  508 TIQVMNYFNLKDVVNSTLNADGDSALHVACQ--QDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKeeHLSCVES----F 581
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSlvlpL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  582 L-NGVptvqlDLSLTNDDGLTPLHMA-IRQNK----------YDVAkkLISYD-RTSISVAnTMDGNNALHMAVLEQ--S 646
Cdd:PHA03095 244 LiAGI-----SINARNRYGQTPLHYAaVFNNPracrrlialgADIN--AVSSDgNTPLSLM-VRNNNGRAVRAALAKnpS 315

                        170
                 ....*....|....*....
gi 45553319  647 VELLVLILDAQNENLTDIL 665
Cdd:PHA03095 316 AETVAATLNTASVAGGDIP 334
IPT cd00102
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ...
 231-334 2.56e-09

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: 54.77  E-value: 2.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 231 LRIVRLSKPTGGVMGNDELILLVEKVSK-KNIKVRFFEEdedgetvweayAKFRESDVHhQYAIVCQTPPYKDKDvdrEV 309
Cdd:cd00102   1 PVITSISPSSGPVSGGTEVTITGSNFGSgSNLRVTFGGG-----------VPCSVLSVS-STAIVCTTPPYANPG---PG 65

                        90       100
                ....*....|....*....|....*
gi 45553319 310 NVYIELIRPSDDERSfPALPFRYKP 334
Cdd:cd00102  66 PVEVTVDRGNGGITS-SPLTFTYVP 89
IPT_NFAT cd01178
IPT domain of the NFAT family of transcription factors. NFAT transcription complexes are a ...
 233-334 1.23e-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: 53.26  E-value: 1.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 233 IVRLSKPTGGVMGNDELILlVEKVSKKNIKVRFFEEDEDGETVWEAYAKFrESDVHHQYAIVCQTPPYKDKDVDREVNVY 312
Cdd:cd01178   4 IEKKSLNSCSVNGGEELFL-TGKNFLKDSKVVFQEKGQDGEAQWEAEATI-DKEKSHQNHLVVEVPPYHNKHVAAPVQVQ 81

                        90       100
                ....*....|....*....|..
gi 45553319 313 IELIRpSDDERSfPALPFRYKP 334
Cdd:cd01178  82 FYVVN-GKRKRS-QPQTFTYTP 101
Ank_4 pfam13637
Ankyrin repeats (many copies);
562-619 1.67e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.67e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45553319   562 GNTPLHVAVKEEHLSCVESFL-NGVptvqlDLSLTNDDGLTPLHMAIRQNKYDVAKKLI 619
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLeKGA-----DINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 483-696 1.67e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  483 NNYNRDTLLHEVISHKK-DKLKLAIQTiqvMNYFNLKDVVNSTLNADGDSALHVAcqQDRAHYIRPLLGMGCNPNLKNNA 561
Cdd:PHA03100  31 SYKKPVLPLYLAKEARNiDVVKILLDN---GADINSSTKNNSTPLHYLSNIKYNL--TDVKEIVKLLLEYGANVNAPDNN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  562 GNTPLHVAV--KEEHLSCVESFL-NGVptvqlDLSLTNDDGLTPLHMAIRQNKYD--VAKKLISY-------DR------ 623
Cdd:PHA03100 106 GITPLLYAIskKSNSYSIVEYLLdNGA-----NVNIKNSDGENLLHLYLESNKIDlkILKLLIDKgvdinakNRvnylls 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553319  624 --TSISVANTMdGNNALHMAVLEQSVELLVLILDAQ-NENLTDILqaqnaaGHTPLELAERKANDRVVQLLKNVYP 696
Cdd:PHA03100 181 ygVPINIKDVY-GFTPLHYAVYNNNPEFVKYLLDLGaNPNLVNKY------GDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 489-642 7.61e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 7.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  489 TLLHEVIshKKDKLKLAIQTIQVMNYFNLKDVvnstlnaDGDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHV 568
Cdd:PHA02874 126 TFLHYAI--KKGDLESIKMLFEYGADVNIEDD-------NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553319  569 AVKEEHLSCVESFLNGVPtvqlDLSLTNDDGLTPLHMAIRQNKyDVAKKLIsyDRTSISVANtMDGNNALHMAV 642
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGN----HIMNKCKNGFTPLHNAIIHNR-SAIELLI--NNASINDQD-IDGSTPLHHAI 262
Ank_2 pfam12796
Ankyrin repeats (3 copies);
525-583 2.05e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45553319   525 LNADGDSALHVACQQDRAHYIRPLLGmGCNPNLKNNaGNTPLHVAVKEEHLSCVESFLN 583
Cdd:pfam12796  26 QDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82
Ank_5 pfam13857
Ankyrin repeats (many copies);
553-606 2.27e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 2.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 45553319   553 CNPNLKNNAGNTPLHVAVKEEHLSCVESFLNGvptvQLDLSLTNDDGLTPLHMA 606
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY----GVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 545-693 5.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 5.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  545 IRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLNgvptVQLDLSLTNDDGLTPLHMAIRQNKYDVAKKLIsyDRT 624
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFE----YGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL--EKG 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553319  625 SISVANTMDGNNALHMAVLEQSVELLVLILDAQNEnltdiLQAQNAAGHTPLELAERKaNDRVVQLLKN 693
Cdd:PHA02874 181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH-----IMNKCKNGFTPLHNAIIH-NRSAIELLIN 243
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 545-621 6.86e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 6.86e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553319  545 IRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLNgvptVQLDLSLTNDDGLTPLHMAIRQNKYDVAKKLISY 621
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE----FGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
RHD-n_NFAT_like cd07927
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ...
 38-111 9.89e-06

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: 46.50  E-value: 9.89e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553319  38 PQLRIVEQPVEKFRFRYKSEmhGTHGSLNGanskRTPKTFPEVTLCNYDGPAVIRCSLFQTN-LDSPHSHQLVVR 111
Cdd:cd07927   1 YELRIEVQPEPHHRARYETE--GSRGAVKA----PSTGGFPTVKLHGYMEPVGLQVFIGTASgRLKPHAFYQVHR 69
PHA03095 PHA03095
ankyrin-like protein; Provisional
 512-687 1.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  512 MNYFN--LKDVVNSTLNAD---------GDSALHV-ACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHV--AVKEEHLSC 577
Cdd:PHA03095  55 LHYSSekVKDIVRLLLEAGadvnapercGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  578 VESFLN-GVptvqlDLSLTNDDGLTPLHMAIRQNKYDVA--KKLISY-----------------------DRTSISVANT 631
Cdd:PHA03095 135 IRLLLRkGA-----DVNALDLYGMTPLAVLLKSRNANVEllRLLIDAgadvyavddrfrsllhhhlqsfkPRARIVRELI 209

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553319  632 ----------MDGNNALH-MAVLEQSVELLVLILDAQNenlTDIlQAQNAAGHTPLELAERKANDRV 687
Cdd:PHA03095 210 ragcdpaatdMLGNTPLHsMATGSSCKRSLVLPLLIAG---ISI-NARNRYGQTPLHYAAVFNNPRA 272
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-579 4.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 45553319   529 GDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVE 579
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 455-619 1.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  455 FEIYkqDRISPIKIS----HHKVEKWFIEH-ALNNYNR---DTLLHEVISHKKDKlklAIQTIQVMNYFnlkdvVNSTLN 526
Cdd:PHA02875  30 FEIY--DGISPIKLAmkfrDSEAIKLLMKHgAIPDVKYpdiESELHDAVEEGDVK---AVEELLDLGKF-----ADDVFY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  527 ADGDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLNGVPTvqldLSLTNDDGLTPLHMA 606
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC----LDIEDCCGCTPLIIA 175

                        170
                 ....*....|...
gi 45553319  607 IRQNKYDVAKKLI 619
Cdd:PHA02875 176 MAKGDIAICKMLL 188
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 601-691 1.48e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 601 TPLHMAIRQNKYDVAKKLISYDRTSISVANTMdGNNALHMAVLEQSVELLVLILDAQNENLTDILQAQNAAGHTPLELAE 680
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAL-GETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLYQGETALHIAV 97

                        90
                ....*....|.
gi 45553319 681 RKANDRVVQLL 691
Cdd:cd22192  98 VNQNLNLVREL 108
Ank_5 pfam13857
Ankyrin repeats (many copies);
524-569 8.77e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 8.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 45553319   524 TLNADGDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVA 569
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 563-654 1.04e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 563 NTPLHVAVKEEHLSCVESFLnGVPTVqlDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYDRTSISVANTMD---GNNALH 639
Cdd:cd22192  18 ESPLLLAAKENDVQAIKKLL-KCPSC--DLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqGETALH 94

                        90
                ....*....|....*
gi 45553319 640 MAVLEQSVELLVLIL 654
Cdd:cd22192  95 IAVVNQNLNLVRELI 109
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 445-621 1.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  445 NRTIkcldDLFEIYKQDRISPIKIshhKVEKWFIEHA--LNNYNRDTL---LHEVISHKKDKLklaiqtiqvMNYFNLKD 519
Cdd:PHA02878 128 IQTI----DLVYIDKKSKDDIIEA---EITKLLLSYGadINMKDRHKGntaLHYATENKDQRL---------TELLLSYG 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  520 VVNSTLNADGDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKE-----------EHLSCVesflNGVPTV 588
Cdd:PHA02878 192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYckdydilklllEHGVDV----NAKSYI 267

                        170       180       190
                 ....*....|....*....|....*....|...
gi 45553319  589 QldlsltnddGLTPLHMAIRQNkyDVAKKLISY 621
Cdd:PHA02878 268 L---------GLTALHSSIKSE--RKLKLLLEY 289
PHA02741 PHA02741
hypothetical protein; Provisional
 558-705 2.23e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.64  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319  558 KNNAGNTPLHVAVKEEHLSCVESFLNGVP--TVQLDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYDRT---SISVANTM 632
Cdd:PHA02741  17 KNSEGENFFHEAARCGCFDIIARFTPFIRgdCHAAALNATDDAGQMCIHIAAEKHEAQLAAEIIDHLIElgaDINAQEML 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553319  633 DGNNALHMAVLEQSVELLVLILDAQNENLTDIlqaqNAAGHTPLELAERKANDRVVQLLKNVYPEKGELAMTW 705
Cdd:PHA02741  97 EGDTALHLAAHRRDHDLAEWLCCQPGIDLHFC----NADNKSPFELAIDNEDVAMMQILREIVATSRGFSNEN 165
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 515-682 2.35e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.38  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 515 FNLKDVVNSTLnadgdsALHVACQQDRAHYiRPLLGMGCNPNLKnnAGNTPLHVAVKEEHLSCVESFLNGVPTVQL---- 590
Cdd:cd22197  56 LNLQDGVNACI------MPLLEIDKDSGNP-KPLVNAQCTDEYY--RGHSALHIAIEKRSLQCVKLLVENGADVHAracg 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 591 DLSLTNDD-----GLTPLHMAIRQNKYDVAKKLIS--YDRTSISVANTMdGNNALHMAVL-----EQSVELLVLILDA-- 656
Cdd:cd22197 127 RFFQKKQGtcfyfGELPLSLAACTKQWDVVNYLLEnpHQPASLQAQDSL-GNTVLHALVMiadnsPENSALVIKMYDGll 205

                       170       180       190
                ....*....|....*....|....*....|...
gi 45553319 657 -------QNENLTDIlqaQNAAGHTPLELAERK 682
Cdd:cd22197 206 qagarlcPTVQLEEI---SNHEGLTPLKLAAKE 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
599-654 3.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 3.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 45553319   599 GLTPLHMAIRQNKYDVAKKLISYdRTSISVANTmDGNNALHMAVLEQSVELLVLIL 654
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK-GADINAVDG-NGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 562-691 3.92e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.63  E-value: 3.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553319 562 GNTPLHVAVKEEHLSCVESFLNGVPTVQldLSLTNDD-----------GLTPLHMAIRQNKYDVAKKLI--SYDRTSISV 628
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENGADVS--ARATGRFfrkspgnlfyfGELPLSLAACTNQEEIVRLLLenGAQPAALEA 150

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553319 629 ANTMdGNNALHMAVL--EQSVEL---------LVLILDAQNENLTDILQAQNAAGHTPLELAERKANDRVVQLL 691
Cdd:cd21882 151 QDSL-GNTVLHALVLqaDNTPENsafvcqmynLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHI 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 528-571 4.03e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 4.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 45553319  528 DGDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVK 571
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
589-641 4.68e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 45553319   589 QLDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYDrtsisVANTM---DGNNALHMA 641
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-----VDLNLkdeEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 598-624 9.50e-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: 34.49  E-value: 9.50e-03
                           10        20
                   ....*....|....*....|....*..
gi 45553319    598 DGLTPLHMAIRQNKYDVAKKLISYDRT 624
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
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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