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Conserved domains on  [gi|74153511|dbj|BAE43399|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
 437-511 1.35e-41

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: 144.66  E-value: 1.35e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74153511 437 RLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQA 511
Cdd:cd08797   2 KQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-379 1.13e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.30  E-value: 1.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 117 FQDNLFLEKALQLARRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGLISDDII 196
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 197 NMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKsRKAAplIDHPNGEGLNAI 276
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGAD--VNAQDNDGNTPL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 277 HIAVMSNSLPCLLLLVAAGAEVNAQeQKSGRTALHLAVEYDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLA 356
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                       250       260
                ....*....|....*....|...
gi 74153511 357 ALLKAAGADPLVENFEPLYDLDD 379
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLL 258
 
Name Accession Description Interval E-value
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
 437-511 1.35e-41

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: 144.66  E-value: 1.35e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74153511 437 RLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQA 511
Cdd:cd08797   2 KQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-379 1.13e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.30  E-value: 1.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 117 FQDNLFLEKALQLARRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGLISDDII 196
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 197 NMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKsRKAAplIDHPNGEGLNAI 276
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGAD--VNAQDNDGNTPL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 277 HIAVMSNSLPCLLLLVAAGAEVNAQeQKSGRTALHLAVEYDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLA 356
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                       250       260
                ....*....|....*....|...
gi 74153511 357 ALLKAAGADPLVENFEPLYDLDD 379
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
207-301 1.23e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511   207 LHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKAAplidhPNGEGLNAIHIAVMSNSLP 286
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-----LKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*
gi 74153511   287 CLLLLVAAGAEVNAQ 301
Cdd:pfam12796  76 IVKLLLEKGADINVK 90
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 433-512 1.54e-13

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


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 66.28  E-value: 1.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511    433 TEDTRLQLCKLLEIPdPDKNWATLAQKLGLG------ILNNAFRLSPAPSKTLMDNYEVSGG---TIKELMEALQQMGYT 503
Cdd:smart00005   1 PELTRQKLAKLLDHP-LGLDWRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRD 79


                   ....*....
gi 74153511    504 EAIEVIQAA 512
Cdd:smart00005  80 DAVELLRSE 88
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 196-347 1.94e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 1.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  196 INMRN-DLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSrkaAPLIDHPNGEGLN 274
Cdd:PHA02878 160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNT 236

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74153511  275 AIHIAVMS-NSLPCLLLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLagcLLLEGDAHVDSTTYDGTTPLHIA 347
Cdd:PHA02878 237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK---LLLEYGADINSLNSYKLTPLSSA 307
Death pfam00531
Death domain;
437-511 6.22e-11

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 58.92  E-value: 6.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511   437 RLQLCKLLEIPDP-DKNWATLAQKLGLGIL-NNAFRLSPA----PSKTLMDNY---EVSGGTIKELMEALQQMGYTEAIE 507
Cdd:pfam00531   1 RKQLDRLLDPPPPlGKDWRELARKLGLSENeIDEIESENPrlrsQTYELLRLWeqrEGKNATVGTLLEALRKLGRRDAAE 80


                  ....
gi 74153511   508 VIQA 511
Cdd:pfam00531  81 KIQS 84
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 164-353 8.85e-10

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: 61.57  E-value: 8.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 164 GDSVLHLAIIHLHAQLVRDLLEVTSGLISDDiinMRNDLY--QTPLHLAVITKQEDVVEDLLRVGADLSL---------- 231
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPELVNEP---MTSDLYqgETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 232 ----LDRWGNSVLHLAAKEGHDRILSIllksrkaapLIDHpngeglnaihiavmsnslpcllllvaaGAEVNAQEQKsGR 307
Cdd:cd22192 128 gpknLIYYGEHPLSFAACVGNEEIVRL---------LIEH---------------------------GADIRAQDSL-GN 170

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 74153511 308 TALHLAVEYDNISLAgC----LLLEGDAHVDS------TTYDGTTPLHIAAGRGST 353
Cdd:cd22192 171 TVLHILVLQPNKTFA-CqmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNI 225
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 196-300 1.12e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511   196 INMRNDLYQTPLHLAVItkqEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHD---RILSILLKSRKAAPLIDHPNGE- 271
Cdd:TIGR00870  45 INCPDRLGRSALFVAAI---ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDaveAILLHLLAAFRKSGPLELANDQy 121

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 74153511   272 ------GLNAIHIAVMSNSLPCLLLLVAAGAEVNA 300
Cdd:TIGR00870 122 tseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
 
Name Accession Description Interval E-value
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
 437-511 1.35e-41

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: 144.66  E-value: 1.35e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74153511 437 RLQLCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQA 511
Cdd:cd08797   2 KQQLYKLLESPDPDKNWATLAQKLGLGILNNAFRLSPSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIEE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-379 1.13e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.30  E-value: 1.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 117 FQDNLFLEKALQLARRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSGLISDDII 196
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 197 NMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKsRKAAplIDHPNGEGLNAI 276
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGAD--VNAQDNDGNTPL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 277 HIAVMSNSLPCLLLLVAAGAEVNAQeQKSGRTALHLAVEYDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLA 356
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNAR-DNDGETPLHLAAENGHLEIVK-LLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                       250       260
                ....*....|....*....|...
gi 74153511 357 ALLKAAGADPLVENFEPLYDLDD 379
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-365 6.84e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 6.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 102 IALASTMEDKEQDMGFQDNLFLEKALQLARRHANALFDYAvtgDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVR 181
Cdd:COG0666  28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDL---LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 182 DLLEvtsgliSDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKsRKA 261
Cdd:COG0666 105 LLLE------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGA 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 262 AplIDHPNGEGLNAIHIAVMSNSLPCLLLLVAAGAEVNAQeQKSGRTALHLAVEYDNISLAGcLLLEGDAHVDSTTYDGT 341
Cdd:COG0666 178 D--VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVK-LLLEAGADLNAKDKDGL 253

                       250       260
                ....*....|....*....|....
gi 74153511 342 TPLHIAAGRGSTRLAALLKAAGAD 365
Cdd:COG0666 254 TALLLAAAAGAALIVKLLLLALLL 277
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
 436-510 7.96e-26

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: 100.78  E-value: 7.96e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74153511 436 TRLQLCKLLeipDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVIQ 510
Cdd:cd08310   1 TRLRLCKLL---DVGKDWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
159-300 2.68e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.61  E-value: 2.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 159 VQDENGDSVLHLAIIHLHAQLVRDLLEvtsgliSDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNS 238
Cdd:COG0666 148 AQDNDGNTPLHLAAANGNLEIVKLLLE------AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74153511 239 VLHLAAKEGHDRILSILLKSRKAaplIDHPNGEGLNAIHIAVMSNSLPCLLLLVAAGAEVNA 300
Cdd:COG0666 222 ALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
207-301 1.23e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511   207 LHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKAAplidhPNGEGLNAIHIAVMSNSLP 286
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-----LKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*
gi 74153511   287 CLLLLVAAGAEVNAQ 301
Cdd:pfam12796  76 IVKLLLEKGADINVK 90
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 433-512 1.54e-13

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


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 66.28  E-value: 1.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511    433 TEDTRLQLCKLLEIPdPDKNWATLAQKLGLG------ILNNAFRLSPAPSKTLMDNYEVSGG---TIKELMEALQQMGYT 503
Cdd:smart00005   1 PELTRQKLAKLLDHP-LGLDWRELARKLGLSeadidqIRTEAPRDLAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRD 79


                   ....*....
gi 74153511    504 EAIEVIQAA 512
Cdd:smart00005  80 DAVELLRSE 88
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 196-347 1.94e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 1.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  196 INMRN-DLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSrkaAPLIDHPNGEGLN 274
Cdd:PHA02878 160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNT 236

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74153511  275 AIHIAVMS-NSLPCLLLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLagcLLLEGDAHVDSTTYDGTTPLHIA 347
Cdd:PHA02878 237 PLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK---LLLEYGADINSLNSYKLTPLSSA 307
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
 440-509 6.05e-13

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: 64.07  E-value: 6.05e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 440 LCKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTIKELMEALQQMGYTEAIEVI 509
Cdd:cd08798   5 LEQLLNDTQTDVPWMELAERLGLQSLVDTYKPTQSPPGSLLRSYELAGGPLQGLIEALQDMGLREGVRLL 74
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-352 6.12e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 6.12e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74153511   276 IHIAVMSNSLPCLLLLVAAGAEVNAQEQKsGRTALHLAVEYDNISLAGCLLLEGDAHVDSttyDGTTPLHIAAGRGS 352
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGH 73
Death pfam00531
Death domain;
437-511 6.22e-11

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 58.92  E-value: 6.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511   437 RLQLCKLLEIPDP-DKNWATLAQKLGLGIL-NNAFRLSPA----PSKTLMDNY---EVSGGTIKELMEALQQMGYTEAIE 507
Cdd:pfam00531   1 RKQLDRLLDPPPPlGKDWRELARKLGLSENeIDEIESENPrlrsQTYELLRLWeqrEGKNATVGTLLEALRKLGRRDAAE 80


                  ....
gi 74153511   508 VIQA 511
Cdd:pfam00531  81 KIQS 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 196-348 2.14e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.15  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  196 INMRNDLYQTPLHL-----AVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAA--KEGHDRILSILLKSRKAaplIDHP 268
Cdd:PHA03100  61 INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGAN---VNIK 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  269 NGEGLNAIHIAVMSNS--LPCLLLLVAAGAEVNAQEQ---------------KSGRTALHLAVEYDNISLAGcLLLEGDA 331
Cdd:PHA03100 138 NSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVK-YLLDLGA 216

                        170
                 ....*....|....*..
gi 74153511  332 HVDSTTYDGTTPLHIAA 348
Cdd:PHA03100 217 NPNLVNKYGDTPLHIAI 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 164-353 8.85e-10

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: 61.57  E-value: 8.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 164 GDSVLHLAIIHLHAQLVRDLLEVTSGLISDDiinMRNDLY--QTPLHLAVITKQEDVVEDLLRVGADLSL---------- 231
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPELVNEP---MTSDLYqgETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 232 ----LDRWGNSVLHLAAKEGHDRILSIllksrkaapLIDHpngeglnaihiavmsnslpcllllvaaGAEVNAQEQKsGR 307
Cdd:cd22192 128 gpknLIYYGEHPLSFAACVGNEEIVRL---------LIEH---------------------------GADIRAQDSL-GN 170

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 74153511 308 TALHLAVEYDNISLAgC----LLLEGDAHVDS------TTYDGTTPLHIAAGRGST 353
Cdd:cd22192 171 TVLHILVLQPNKTFA-CqmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNI 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 196-347 2.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  196 INMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKAAPLIDHpNGEglNA 275
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN-NGE--SP 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74153511  276 IHIAVMSNSLPCLLLLVAAGAEVnAQEQKSGRTALHLAVEYDNISLAgclLLEGDAHVDSTTYDGTTPLHIA 347
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLHNAIIHNRSAIE---LLINNASINDQDIDGSTPLHHA 261
PHA03095 PHA03095
ankyrin-like protein; Provisional
 159-344 3.08e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 3.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  159 VQDENGDSVLHlaiIHL-----HAQLVRDLLEVTSGlisddiINMRNDLYQTPLHLAVITKQEDV--VEDLLRVGADLSL 231
Cdd:PHA03095 112 AKDKVGRTPLH---VYLsgfniNPKVIRLLLRKGAD------VNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  232 LDRWGNSVLHLAAKEGHDR--ILSILLKSRKAAPLIdhpNGEGLNAIHIAVMSNSLPCLLL--LVAAGAEVNAQEqKSGR 307
Cdd:PHA03095 183 VDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAAT---DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARN-RYGQ 258

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 74153511  308 TALHLAVEYDNISLAGCLLLEGdAHVDSTTYDGTTPL 344
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALG-ADINAVSSDGNTPL 294
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
 432-510 7.39e-09

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


Pssm-ID: 260051  Cd Length: 83  Bit Score: 52.66  E-value: 7.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 432 LTEDTRLQLCKLLEIPDPDKN-WATLAQKLGLGILNNAFRLSPAPSKTLMDNYEV---SGGTIKELMEALQQMGYTEAIE 507
Cdd:cd08781   1 LPYSIRQKLCSLLDPPNARGNdWRLLAQKLSVDRYINYFATKPSPTEVILDLWEArnrDDGALNSLAAILREMGRHDAAT 80


                ...
gi 74153511 508 VIQ 510
Cdd:cd08781  81 ILE 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
159-273 1.87e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 1.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 159 VQDENGDSVLHLAIIHLHAQLVRDLLEvtsgliSDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNS 238
Cdd:COG0666 181 ARDNDGETPLHLAAENGHLEIVKLLLE------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254

                        90       100       110
                ....*....|....*....|....*....|....*
gi 74153511 239 VLHLAAKEGHDRILSILLKSRKAAPLIDHPNGEGL 273
Cdd:COG0666 255 ALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 165-329 4.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 4.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  165 DSVLHLAIIHLHAQLVRDLLEvtSGLISDDIINMRNDlyqTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAA 244
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLD--LGKFADDVFYKDGM---TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  245 KEGHDRILSILLKSRKAAPLIDhpnGEGLNAIHIAVMSNSLPCLLLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLAGC 324
Cdd:PHA02875 144 MMGDIKGIELLIDHKACLDIED---CCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRL 220


                 ....*
gi 74153511  325 LLLEG 329
Cdd:PHA02875 221 FIKRG 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 132-347 5.47e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 5.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  132 RHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLhlAIIHLHAQLVRDLLEVTSGLISDDI------------INMR 199
Cdd:PHA02876 192 KMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK--AIIDNRSNINKNDLSLLKAIRNEDLetslllydagfsVNSI 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  200 NDLYQTPLHLAVITKQ-EDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHD----RILSILLKSRKAA------PL---- 264
Cdd:PHA02876 270 DDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDteniRTLIMLGADVNAAdrlyitPLhqas 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  265 -IDHPN---------GEGLNA--------IHIAVMSNSLPCLLLLVAAGAEVNAQEQKSGrTALHLAVEYDNISLAGCLL 326
Cdd:PHA02876 350 tLDRNKdivitllelGANVNArdycdktpIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTNPYMSVKTL 428

                        250       260
                 ....*....|....*....|.
gi 74153511  327 LEGDAHVDSTTYDGTTPLHIA 347
Cdd:PHA02876 429 IDRGANVNSKNKDLSTPLHYA 449
PHA03095 PHA03095
ankyrin-like protein; Provisional
 196-346 6.76e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 6.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  196 INMRNDLYQtplhlaVITKQEDV----VEDLLRVGADLSLLDRWGNSVLHLAAKEGHD---RILSILLksrKAAPLIDHP 268
Cdd:PHA03095   9 IIMEAALYD------YLLNASNVtveeVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLL---EAGADVNAP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  269 NGEGLNAIHIAVMSNS-LPCLLLLVAAGAEVNAqEQKSGRTALH-----LAVEYDNISlagcLLLEGDAHVDSTTYDGTT 342
Cdd:PHA03095  80 ERCGFTPLHLYLYNATtLDVIKLLIKAGADVNA-KDKVGRTPLHvylsgFNINPKVIR----LLLRKGADVNALDLYGMT 154


                 ....
gi 74153511  343 PLHI 346
Cdd:PHA03095 155 PLAV 158
Ank_2 pfam12796
Ankyrin repeats (3 copies);
159-233 7.81e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 7.81e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74153511   159 VQDENGDSVLHLAIIHLHAQLVRDLLEVtsglisdDIINMRNDlYQTPLHLAVITKQEDVVEDLLRVGADLSLLD 233
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLEH-------ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
168-258 9.04e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 9.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511   168 LHLAIIHLHAQLVRDLLEVTSGlisddiINMRNDLYQTPLHLAVITKQEDVVEDLLRVgADLSLLDRwGNSVLHLAAKEG 247
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD------ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72

                          90
                  ....*....|.
gi 74153511   248 HDRILSILLKS 258
Cdd:pfam12796  73 HLEIVKLLLEK 83
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 233-354 1.07e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 51.42  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  233 DRWGNSVLHLAAKEGHdriLSILLKSRKAAP-----LIDHPNGEGLNAIHIAV---MSNSLPCLLLLVAAGAEVNAQEQK 304
Cdd:PHA02736  14 DIEGENILHYLCRNGG---VTDLLAFKNAISdenryLVLEYNRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERV 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 74153511  305 SGRTALHLAVEYDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTR 354
Cdd:PHA02736  91 FGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAK 140
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 204-344 1.13e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  204 QTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLK-SRKAAPlidHPNGEGLNaihIAVMS 282
Cdd:PLN03192 559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfASISDP---HAAGDLLC---TAAKR 632

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74153511  283 NSLPCLLLLVAAGAEVNAqEQKSGRTALHLAVEYDNISLAGCLLLEGDAHVDSTTYDGTTPL 344
Cdd:PLN03192 633 NDLTAMKELLKQGLNVDS-EDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPT 693
PHA03095 PHA03095
ankyrin-like protein; Provisional
 131-354 1.99e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  131 RRHANALFDYAVTGDVKMLLAVQRHLTAVQDEN-----GDSVLHL---AIIHLHAQLVRDLLEVTSglisddIINMRNDL 202
Cdd:PHA03095   9 IIMEAALYDYLLNASNVTVEEVRRLLAAGADVNfrgeyGKTPLHLylhYSSEKVKDIVRLLLEAGA------DVNAPERC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  203 YQTPLHLAVITKQ-EDVVEDLLRVGADLSLLDRWGNSVLH--LAAKEGHDRILSILLksRKAAPLIDHpNGEGLNAIHIA 279
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLL--RKGADVNAL-DLYGMTPLAVL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  280 VMSN--SLPCLLLLVAAGAEVNAQEQkSGRTALHLAVEY--------DNISLAGCL------------------------ 325
Cdd:PHA03095 160 LKSRnaNVELLRLLIDAGADVYAVDD-RFRSLLHHHLQSfkprarivRELIRAGCDpaatdmlgntplhsmatgssckrs 238

                        250       260       270
                 ....*....|....*....|....*....|...
gi 74153511  326 ----LLEGDAHVDSTTYDGTTPLHIAAGRGSTR 354
Cdd:PHA03095 239 lvlpLLIAGISINARNRYGQTPLHYAAVFNNPR 271
PHA03095 PHA03095
ankyrin-like protein; Provisional
 133-296 2.82e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  133 HANALFDYAvtGDVKMLLAVQRHLTAVqDENGDSVLHLAIIH--LHAQLVRDLLEvtSGLIsddiINMRNDLYQTPLHLA 210
Cdd:PHA03095 194 HLQSFKPRA--RIVRELIRAGCDPAAT-DMLGNTPLHSMATGssCKRSLVLPLLI--AGIS----INARNRYGQTPLHYA 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  211 VITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKAAPLIDHPNGEGLNAIHIAVMSNSLPCLLL 290
Cdd:PHA03095 265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDATRLCVAK 344


                 ....*.
gi 74153511  291 LVAAGA 296
Cdd:PHA03095 345 VVLRGA 350
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-326 7.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 7.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74153511   272 GLNAIHIAVMSNSLPCLLLLVAAGAEVNAQEqKSGRTALHLAVEYDNISLAGCLL 326
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
236-292 7.44e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 7.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 74153511   236 GNSVLHLAAKEGHDRILSILLKSRkaaPLIDHPNGEGLNAIHIAVMSNSLPCLLLLV 292
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG---ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 190-266 3.78e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 3.78e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74153511  190 LISDDI-INMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKAAPLID 266
Cdd:PHA03100 178 LLSYGVpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 137-299 8.52e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 8.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  137 LFDYAVTGDVK---MLLAVQRHLTAVQDENGDSVLHLAIIHLHAQLVRDLLEVTSgliSDDIINMRNdlyQTPLHLAVIT 213
Cdd:PHA02875  72 LHDAVEEGDVKaveELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDK---FSPLHLAVMM 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  214 KQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSrKAAPLIDHPNGEgLNAIHIAVMSNSLPCLLLLVA 293
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS-GANIDYFGKNGC-VAALCYAIENNKIDIVRLFIK 223


                 ....*.
gi 74153511  294 AGAEVN 299
Cdd:PHA02875 224 RGADCN 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
205-256 9.45e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 9.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 74153511   205 TPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILL 256
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 196-300 1.12e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511   196 INMRNDLYQTPLHLAVItkqEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHD---RILSILLKSRKAAPLIDHPNGE- 271
Cdd:TIGR00870  45 INCPDRLGRSALFVAAI---ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDaveAILLHLLAAFRKSGPLELANDQy 121

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 74153511   272 ------GLNAIHIAVMSNSLPCLLLLVAAGAEVNA 300
Cdd:TIGR00870 122 tseftpGITALHLAAHRQNYEIVKLLLERGASVPA 156
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 184-351 1.35e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  184 LEVTSGLISD--DIINMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKA 261
Cdd:PHA02874  14 IEAIEKIIKNkgNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  262 APLIDHP--NGEGLNAI------------------HIAVMSNSLPCLLLLVAAGAEVNAqEQKSGRTALHLAVEYDNISL 321
Cdd:PHA02874  94 TSILPIPciEKDMIKTIldcgidvnikdaelktflHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDI 172

                        170       180       190
                 ....*....|....*....|....*....|
gi 74153511  322 AGcLLLEGDAHVDSTTYDGTTPLHIAAGRG 351
Cdd:PHA02874 173 IK-LLLEKGAYANVKDNNGESPLHNAAEYG 201
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 266-347 1.82e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 45.19  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  266 DHpngEGLNAIHIAV---MSNSLPCLLLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLAGCLLLEGDAHVDSTTYDGTT 342
Cdd:PHA02743  54 DH---HGRQCTHMVAwydRANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGAINYQHET 130


                 ....*
gi 74153511  343 PLHIA 347
Cdd:PHA02743 131 AYHIA 135
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 436-509 3.31e-05

Death domain found in death-associated protein kinase 1; Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. 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: 260052  Cd Length: 82  Bit Score: 42.33  E-value: 3.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 436 TRLQLCKLLEIPDP-DKNWATLAQKLGLG----ILNNAFRLSPAPSKTLMD---NYEVSggTIKELMEALQQMGYTEAIE 507
Cdd:cd08782   2 TRRKLARLLDPPDPmGRDWCLLAVNLGLTdlvaKLDSTSSPLPSPTDRLLQewtARPPS--TIGALLRKLRELGRRDAAD 79


                ..
gi 74153511 508 VI 509
Cdd:cd08782  80 FL 81
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 161-351 4.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  161 DENGDSVLHLAIIHLHAQlvRDLLEVTSGLISDDI-INMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSV 239
Cdd:PHA02876 137 DKINESIEYMKLIKERIQ--QDELLIAEMLLEGGAdVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSV 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  240 LHLAAKEGHDRILSILLKSRKAaplIDHPNGEGLNAIHiavmSNSLPCLLLLVAAGAEVNAQEQKSgRTALHLAVEYDNI 319
Cdd:PHA02876 215 LECAVDSKNIDTIKAIIDNRSN---INKNDLSLLKAIR----NEDLETSLLLYDAGFSVNSIDDCK-NTPLHHASQAPSL 286

                        170       180       190
                 ....*....|....*....|....*....|..
gi 74153511  320 SLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRG 351
Cdd:PHA02876 287 SRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 146-234 4.82e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  146 VKMLLAVQRHLTAVqDENGDSVLHLAIIHLHAQLVRDLLEVTSGlisddiINMRNDLYQTPLHLAVITKQEDVVEDLLRV 225
Cdd:PHA03100 175 VNYLLSYGVPINIK-DVYGFTPLHYAVYNNNPEFVKYLLDLGAN------PNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247


                 ....*....
gi 74153511  226 GADLSLLDR 234
Cdd:PHA03100 248 GPSIKTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-353 5.11e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 5.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 74153511   310 LHLAVEYDNISLAgCLLLEGDAHVDSTTYDGTTPLHIAAGRGST 353
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHL 43
PHA02741 PHA02741
hypothetical protein; Provisional
 236-347 5.87e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 43.88  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  236 GNSVLHLAAKEGHDRIL---SILLKSRKAAPLIDHPNGEGLNAIHIAVMSN----SLPCLLLLVAAGAEVNAQEQKSGRT 308
Cdd:PHA02741  21 GENFFHEAARCGCFDIIarfTPFIRGDCHAAALNATDDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEMLEGDT 100

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 74153511  309 ALHLAVEYDNISLAGCLLLEGDAHVDSTTYDGTTPLHIA 347
Cdd:PHA02741 101 ALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 236-346 6.15e-05

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: 46.03  E-value: 6.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 236 GNSVLHLAAKEGHDRILSILLKSRKAAPLIDHPNG-----------EGLNAIHIAVMSNSLPCLLLLVAAGAEVNAQE-- 302
Cdd:cd21882  26 GKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 74153511 303 ---QKSGRTALHLAvEYDnISLAGC--------LLLEGDAHVDSTTYD---GTTPLHI 346
Cdd:cd21882 106 rffRKSPGNLFYFG-ELP-LSLAACtnqeeivrLLLENGAQPAALEAQdslGNTVLHA 161
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 204-257 1.07e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 74153511  204 QTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLK 257
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Death_UNC5B cd08802
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ...
 437-509 1.10e-04

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


Pssm-ID: 176780  Cd Length: 84  Bit Score: 41.16  E-value: 1.10e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74153511 437 RLQLCKLLEIPDPDKN-WATLAQKLGLGILNNAFRLSPAPSKTLMDNYEV---SGGTIKELMEALQQMGYTEAIEVI 509
Cdd:cd08802   6 RQKICNSLDAPNSRGNdWRLLAQKLSMDRYLNYFATKASPTGVILDLWEArhqDDGDLNSLASALEEMGKSEMLVVM 82
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 206-347 2.06e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  206 PLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKE----GHDRILSILLKSRKAAPLIDHPNGEGLNAIHIAVM 281
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  282 ------------------------SNSLPCLLLLVAAGAEVNAQEQKSGRTALHLAVEYDNISLAGCLLLEGdAHVDSTT 337
Cdd:PHA02878 120 iltnrykniqtidlvyidkkskddIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYG-ANVNIPD 198

                        170
                 ....*....|
gi 74153511  338 YDGTTPLHIA 347
Cdd:PHA02878 199 KTNNSPLHHA 208
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 164-279 2.22e-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: 44.10  E-value: 2.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 164 GDSVLHLAIIHLHAQLVRDLLE----VTSGLISDDI-INMRNDLY--QTPLHLAVITKQEDVVEDLLRVGAD---LSLLD 233
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVEngadVSARATGRFFrKSPGNLFYfgELPLSLAACTNQEEIVRLLLENGAQpaaLEAQD 152

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 74153511 234 RWGNSVLHLA-------------AKEGHDRILSILLKSRKAAPLIDHPNGEGLNAIHIA 279
Cdd:cd21882 153 SLGNTVLHALvlqadntpensafVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLA 211
Ank_5 pfam13857
Ankyrin repeats (many copies);
264-313 2.57e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 74153511   264 LIDHPNGEGLNAIHIAVMSNSLPCLLLLVAAGAEVNAQEqKSGRTALHLA 313
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
306-354 3.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 3.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 74153511   306 GRTALHLAVEYDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGSTR 354
Cdd:pfam13637   1 ELTALHAAAASGHLELLR-LLLEKGADINAVDGNGETALHFAASNGNVE 48
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 164-279 6.77e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.76  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511   164 GDSVLHLAIIHLHAQLVRDLLEvtSG------------LISDdiinMRNDLY--QTPLHLAVITKQEDVVEDLLRVGADL 229
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLE--RGasvparacgdffVKSQ----GVDSFYhgESPLNAAACLGSPSIVALLSEDPADI 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74153511   230 SLLDRWGNSVLHLAAKEGHDR-------------ILSILLKSRKAAPLIDHPNGEGLNAIHIA 279
Cdd:TIGR00870 202 LTADSLGNTLLHLLVMENEFKaeyeelscqmynfALSLLDKLRDSKELEVILNHQGLTPLKLA 264
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 205-353 1.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  205 TPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKAAPliDHPNGEGLNAIHIAVMSNS 284
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKDGMTPLHLATILKK 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74153511  285 LPCLLLLVAAGAEVNAQEQKSgRTALHLAVEYDNISLAGcLLLEGDAHVDSTTYDGTTPLHIAAGRGST 353
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDK-FSPLHLAVMMGDIKGIE-LLIDHKACLDIEDCCGCTPLIIAMAKGDI 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 139-245 1.42e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511  139 DYAVtgdVKMLLAVQRHLTaVQDENGDSVLHLAIIHlhaqlVRDLLEVtsgLISDDIINMRNDLYQTPLHLAVITK-QED 217
Cdd:PHA02874 202 DYAC---IKLLIDHGNHIM-NKCKNGFTPLHNAIIH-----NRSAIEL---LINNASINDQDIDGSTPLHHAINPPcDID 269

                         90       100
                 ....*....|....*....|....*...
gi 74153511  218 VVEDLLRVGADLSLLDRWGNSVLHLAAK 245
Cdd:PHA02874 270 IIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_5 pfam13857
Ankyrin repeats (many copies);
196-243 1.88e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 1.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 74153511   196 INMRNDLYQTPLHLAVITKQEDVVEDLLRVGADLSLLDRWGNSVLHLA 243
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
290-347 2.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 2.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 74153511   290 LLVAAGAEVNAQEQKsGRTALHLAVEYDNISLAgCLLLEGDAHVDSTTYDGTTPLHIA 347
Cdd:pfam13857   1 LLEHGPIDLNRLDGE-GYTPLHVAAKYGALEIV-RVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
164-223 2.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 2.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511   164 GDSVLHLAIIHLHAQLVRDLLEvtSGLIsddiINMRNDLYQTPLHLAVITKQEDVVEDLL 223
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE--KGAD----INAVDGNGETALHFAASNGNVEVLKLLL 54
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
 437-506 3.00e-03

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


Pssm-ID: 260064  Cd Length: 83  Bit Score: 36.91  E-value: 3.00e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74153511 437 RLQLCKLLEIPDPDKN-WATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVS---GGTIKELMEALQQMGYTEAI 506
Cdd:cd08799   6 RQKLCGSLDAPQTRGNdWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEAQhfpDGNLSRLAAVLEEMGRHETV 79
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 164-279 4.28e-03

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: 40.13  E-value: 4.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74153511 164 GDSVLHLAIIHLHAQLVRDLLEVTSGL---ISDDIIN--MRNDLY---QTPLHLAVITKQEDVVEDLL-RVGADLSLLDR 234
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVnahAKGVFFNpkYKHEGFyfgETPLALAACTNQPEIVQLLMeKESTDITSQDS 220

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 74153511 235 WGNSVLHLAAKEGHD---------RILSILLKSRKAAPLIDHPNGEGLNAIHIA 279
Cdd:cd22194 221 RGNTVLHALVTVAEDsktqndfvkRMYDMILLKSENKNLETIRNNEGLTPLQLA 274
Ank_5 pfam13857
Ankyrin repeats (many copies);
227-279 7.84e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 7.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 74153511   227 ADLSLLDRWGNSVLHLAAKEGHDRILSILLKSRKAAPLidhPNGEGLNAIHIA 279
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL---KDEEGLTALDLA 56
 
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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