NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119574242|gb|EAW53857|]
View 

chromosome 2 open reading frame 26 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12120816)

ankyrin repeat (ANK) domain-containing protein mediates specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|17176038
SCOP:  4000366

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
302-393 1.11e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242 302 GFTCLHWAAKHGRQELLAMLVnfankhQLPVNIDARTSGGYTALHLAAMHGHVEVVKLLVgAYDADVDIRDYSGKKASQY 381
Cdd:COG0666  153 GNTPLHLAAANGNLEIVKLLL------EAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDL 225

                         90
                 ....*....|..
gi 119574242 382 LSRSIAEEIKNL 393
Cdd:COG0666  226 AAENGNLEIVKL 237
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 5-203 1.48e-03

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242   5 AEWGPEAAL----GPEAVLRF----LAERGGRALHAE-LVQHFRGALGGEPEqrararahfkelVNAVatvrVDPADGAK 75
Cdd:PRK07764 532 AILLPEATVlgvrGDTLVLGFstggLARRFASPGNAEvLVTALAEELGGDWQ------------VEAV----VGPAPGAA 595

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242  76 YvhlkkrfcEGPSEPSGDPPRIQVTAEPEAPDGPAGPEARDRLPDAAAPESLPGQGRELGEGEPPAPAHWPplSAGARRK 155
Cdd:PRK07764 596 G--------GEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVA--VPDASDG 665

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119574242 156 NSRRDVQPLPRTPAPGPSEDLELPPHGCEEADRGSSLVGATAQRPARQ 203
Cdd:PRK07764 666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQ 713
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
302-393 1.11e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242 302 GFTCLHWAAKHGRQELLAMLVnfankhQLPVNIDARTSGGYTALHLAAMHGHVEVVKLLVgAYDADVDIRDYSGKKASQY 381
Cdd:COG0666  153 GNTPLHLAAANGNLEIVKLLL------EAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDL 225

                         90
                 ....*....|..
gi 119574242 382 LSRSIAEEIKNL 393
Cdd:COG0666  226 AAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
272-372 9.16e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 9.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242  272 MLSASDGKWDSLEGLLTCEPGLLVKRDFitGFTCLHWAAKHGRQELLAMLVNFANkhqlpVNIDartSGGYTALHLAAMH 351
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKN--GRTALHLAAKNGHLEIVKLLLEHAD-----VNLK---DNGRTALHYAARS 71

                          90       100
                  ....*....|....*....|.
gi 119574242  352 GHVEVVKLLVgAYDADVDIRD 372
Cdd:pfam12796  72 GHLEIVKLLL-EKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 341-370 4.25e-06

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: 43.35  E-value: 4.25e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 119574242   341 GYTALHLAAMHGHVEVVKLLVGaYDADVDI 370
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD-KGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 273-371 1.41e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242  273 LSASDGKWDSLEGLLtcepgLLVKRDFITGFTCLHWAAK--HGRQELLAMLVNFANKHQLPVN--IDARTSG---GYTAL 345
Cdd:TIGR00870  58 VAAIENENLELTELL-----LNLSCRGAVGDTLLHAISLeyVDAVEAILLHLLAAFRKSGPLElaNDQYTSEftpGITAL 132

                          90       100
                  ....*....|....*....|....*.
gi 119574242  346 HLAAMHGHVEVVKLLVgAYDADVDIR 371
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLL-ERGASVPAR 157
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 332-397 1.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119574242 332 VNIDARTSGGYTALHLAAMHGHVEVVKLLVgAYDADVDIRDYSGKKAsqyLSRSIAEEIKNLVGAL 397
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTP---LHIAILNNNKEIFKLL 244
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 5-203 1.48e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242   5 AEWGPEAAL----GPEAVLRF----LAERGGRALHAE-LVQHFRGALGGEPEqrararahfkelVNAVatvrVDPADGAK 75
Cdd:PRK07764 532 AILLPEATVlgvrGDTLVLGFstggLARRFASPGNAEvLVTALAEELGGDWQ------------VEAV----VGPAPGAA 595

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242  76 YvhlkkrfcEGPSEPSGDPPRIQVTAEPEAPDGPAGPEARDRLPDAAAPESLPGQGRELGEGEPPAPAHWPplSAGARRK 155
Cdd:PRK07764 596 G--------GEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVA--VPDASDG 665

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119574242 156 NSRRDVQPLPRTPAPGPSEDLELPPHGCEEADRGSSLVGATAQRPARQ 203
Cdd:PRK07764 666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQ 713
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
 18-83 1.99e-03

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


Pssm-ID: 439329  Cd Length: 72  Bit Score: 37.11  E-value: 1.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119574242  18 VLRFLAER-GGRALHAELVQHFRGALGgePEQRARarahFKELVNAVATVRVDPaDGAKYVHLKKRF 83
Cdd:cd22254   12 IRDFLAFQaGGQATTDEIVDHFKDRLP--PEQSAL----FKALLKQICTFERDP-GGRGVWVLKPEF 71
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
302-393 1.11e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242 302 GFTCLHWAAKHGRQELLAMLVnfankhQLPVNIDARTSGGYTALHLAAMHGHVEVVKLLVgAYDADVDIRDYSGKKASQY 381
Cdd:COG0666  153 GNTPLHLAAANGNLEIVKLLL------EAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDL 225

                         90
                 ....*....|..
gi 119574242 382 LSRSIAEEIKNL 393
Cdd:COG0666  226 AAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
272-372 9.16e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 9.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242  272 MLSASDGKWDSLEGLLTCEPGLLVKRDFitGFTCLHWAAKHGRQELLAMLVNFANkhqlpVNIDartSGGYTALHLAAMH 351
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKN--GRTALHLAAKNGHLEIVKLLLEHAD-----VNLK---DNGRTALHYAARS 71

                          90       100
                  ....*....|....*....|.
gi 119574242  352 GHVEVVKLLVgAYDADVDIRD 372
Cdd:pfam12796  72 GHLEIVKLLL-EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
270-375 9.61e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.99  E-value: 9.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242 270 AWMLSASDGKWDSLEGLLtcEPGLLVKRDFITGFTCLHWAAKHGRQELLAMLVnfankhQLPVNIDARTSGGYTALHLAA 349
Cdd:COG0666   90 LLHAAARNGDLEIVKLLL--EAGADVNARDKDGETPLHLAAYNGNLEIVKLLL------EAGADVNAQDNDGNTPLHLAA 161

                         90       100
                 ....*....|....*....|....*.
gi 119574242 350 MHGHVEVVKLLVgAYDADVDIRDYSG 375
Cdd:COG0666  162 ANGNLEIVKLLL-EAGADVNARDNDG 186
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
272-375 1.04e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242 272 MLSASDGKWDSLEGLLTCEPGLLVKRDFITGFTCLHWAAKHGRQELLAMLVnfankhQLPVNIDARTSGGYTALHLAAMH 351
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL------EAGADVNARDKDGETPLHLAAYN 130

                         90       100
                 ....*....|....*....|....
gi 119574242 352 GHVEVVKLLVgAYDADVDIRDYSG 375
Cdd:COG0666  131 GNLEIVKLLL-EAGADVNAQDNDG 153
Ank_4 pfam13637
Ankyrin repeats (many copies);
304-361 3.40e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.22  E-value: 3.40e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 119574242  304 TCLHWAAKHGRQELLAMLvnfankHQLPVNIDARTSGGYTALHLAAMHGHVEVVKLLV 361
Cdd:pfam13637   3 TALHAAAASGHLELLRLL------LEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
306-369 2.28e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 2.28e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119574242  306 LHWAAKHGRQELLAMLVNFankhqlPVNIDARTSGGYTALHLAAMHGHVEVVKLLVGAYDADVD 369
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN------GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK 58
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
302-393 1.08e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242 302 GFTCLHWAAKHGRQELLAMLVNfankhqLPVNIDARTSGGYTALHLAAMHGHVEVVKLLVgAYDADVDIRDYSGKKASQY 381
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLE------AGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLL 258

                         90
                 ....*....|..
gi 119574242 382 LSRSIAEEIKNL 393
Cdd:COG0666  259 AAAAGAALIVKL 270
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 341-372 6.46e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.74  E-value: 6.46e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 119574242  341 GYTALHLAA-MHGHVEVVKLLVgAYDADVDIRD 372
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLL-SKGADVNARD 33
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
281-393 1.26e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.34  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242 281 DSLEGLLTCEPGLLVKRDFITGFTCLHWAAKHGRQELLAMLVNFANkhqlpvNIDARTSGGYTALHLAAMHGHVEVVKLL 360
Cdd:COG0666   33 LLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA------DINAKDDGGNTLLHAAARNGDLEIVKLL 106

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119574242 361 VgAYDADVDIRDYSGKKASQYLSRSIAEEIKNL 393
Cdd:COG0666  107 L-EAGADVNARDKDGETPLHLAAYNGNLEIVKL 138
Ank_5 pfam13857
Ankyrin repeats (many copies);
286-348 2.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 2.25e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119574242  286 LLTCEPGLLVKRDFItGFTCLHWAAKHGRQELLAMLVNFankhqlPVNIDARTSGGYTALHLA 348
Cdd:pfam13857   1 LLEHGPIDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAY------GVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 341-370 4.25e-06

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: 43.35  E-value: 4.25e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 119574242   341 GYTALHLAAMHGHVEVVKLLVGaYDADVDI 370
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD-KGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 341-370 2.21e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 2.21e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 119574242  341 GYTALHLAAMHGHVEVVKLLVgAYDADVDI 370
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLL-ENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
331-381 3.62e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119574242  331 PVNIDARTSGGYTALHLAAMHGHVEVVKLLVgAYDADVDIRDYSGKKASQY 381
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
341-375 1.37e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 119574242  341 GYTALHLAAMHGHVEVVKLLVgAYDADVDIRDYSG 375
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNG 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 273-371 1.41e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242  273 LSASDGKWDSLEGLLtcepgLLVKRDFITGFTCLHWAAK--HGRQELLAMLVNFANKHQLPVN--IDARTSG---GYTAL 345
Cdd:TIGR00870  58 VAAIENENLELTELL-----LNLSCRGAVGDTLLHAISLeyVDAVEAILLHLLAAFRKSGPLElaNDQYTSEftpGITAL 132

                          90       100
                  ....*....|....*....|....*.
gi 119574242  346 HLAAMHGHVEVVKLLVgAYDADVDIR 371
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLL-ERGASVPAR 157
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 332-397 1.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119574242 332 VNIDARTSGGYTALHLAAMHGHVEVVKLLVgAYDADVDIRDYSGKKAsqyLSRSIAEEIKNLVGAL 397
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTP---LHIAILNNNKEIFKLL 244
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 5-203 1.48e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242   5 AEWGPEAAL----GPEAVLRF----LAERGGRALHAE-LVQHFRGALGGEPEqrararahfkelVNAVatvrVDPADGAK 75
Cdd:PRK07764 532 AILLPEATVlgvrGDTLVLGFstggLARRFASPGNAEvLVTALAEELGGDWQ------------VEAV----VGPAPGAA 595

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242  76 YvhlkkrfcEGPSEPSGDPPRIQVTAEPEAPDGPAGPEARDRLPDAAAPESLPGQGRELGEGEPPAPAHWPplSAGARRK 155
Cdd:PRK07764 596 G--------GEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVA--VPDASDG 665

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119574242 156 NSRRDVQPLPRTPAPGPSEDLELPPHGCEEADRGSSLVGATAQRPARQ 203
Cdd:PRK07764 666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQ 713
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
 18-83 1.99e-03

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


Pssm-ID: 439329  Cd Length: 72  Bit Score: 37.11  E-value: 1.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119574242  18 VLRFLAER-GGRALHAELVQHFRGALGgePEQRARarahFKELVNAVATVRVDPaDGAKYVHLKKRF 83
Cdd:cd22254   12 IRDFLAFQaGGQATTDEIVDHFKDRLP--PEQSAL----FKALLKQICTFERDP-GGRGVWVLKPEF 71
PHA03095 PHA03095
ankyrin-like protein; Provisional
 304-383 2.90e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574242 304 TCLHWAAKHGRQELLAMLVNFANkhqlpvnIDARTSGGYTALHLAAMHGHVE-VVKLLVGAyDADVDIRDYSGKKASQ-Y 381
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGAD-------VNAPERCGFTPLHLYLYNATTLdVIKLLIKA-GADVNAKDKVGRTPLHvY 124


                 ..
gi 119574242 382 LS 383
Cdd:PHA03095 125 LS 126
PHA03095 PHA03095
ankyrin-like protein; Provisional
 302-358 9.69e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 9.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119574242 302 GFTCLHWAAKHGRQELLAMLVNfankhqLPVNIDARTSGGYTALHLAAMHGHVEVVK 358
Cdd:PHA03095 257 GQTPLHYAAVFNNPRACRRLIA------LGADINAVSSDGNTPLSLMVRNNNGRAVR 307
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH