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Conserved domains on  [gi|28849903|ref|NP_789817|]
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pre-mRNA splicing regulator USH1G [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_USH1G cd09586
SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) ...
 388-453 3.69e-34

SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


:

Pssm-ID: 188985  Cd Length: 66  Bit Score: 122.21  E-value: 3.69e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903 388 ETSPLETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQALERP 453
Cdd:cd09586   1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-117 1.81e-27

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 1.81e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   6 HRAARDGYLELLKEATRK--ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:COG0666  92 HAAARNGDLEIVKLLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                        90       100       110
                ....*....|....*....|....*....|....
gi 28849903  84 LVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
CEN_USH1G cd21803
central domain found in usher syndrome type-1G protein; Usher syndrome type-1G protein (USH1G), ...
 296-388 1.84e-25

central domain found in usher syndrome type-1G protein; Usher syndrome type-1G protein (USH1G), also called scaffold protein containing ankyrin repeats and SAM domain (Sans), is an anchoring/scaffolding protein that is part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A, that mediates mechanotransduction in cochlear hair cells. It is required for normal development and maintenance of cochlear hair cell bundles, as well as for normal hearing. USH1G consists of four N-terminal ANK repeats, a central region, and a sterile alpha motif (SAM) followed by a C-terminal type I PDZ binding motif (PBM). This model corresponds to the central region (CEN) of USH1G, which contains the conserved regions CEN1 and CEN2. CEN is directly responsible for binding to the MYO7A MyTH4-FERM tandem.


:

Pssm-ID: 409642  Cd Length: 57  Bit Score: 98.38  E-value: 1.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903 296 EVSTDSGHDSLFTRPGLGTMVFRRNYVSSGLHGLGREDggldgagtprgrlhsspsldddslgsanslqdrscgEELPWD 375
Cdd:cd21803   1 EVSTDSGHDSLFNRPGLGTMVFRRNYVSSGLFGLGRED------------------------------------EELPWD 44

                        90
                ....*....|...
gi 28849903 376 ELDLGLDEDLEPE 388
Cdd:cd21803  45 EVDLGLDDDDEPD 57
 
Name Accession Description Interval E-value
SAM_USH1G cd09586
SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) ...
 388-453 3.69e-34

SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


Pssm-ID: 188985  Cd Length: 66  Bit Score: 122.21  E-value: 3.69e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903 388 ETSPLETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQALERP 453
Cdd:cd09586   1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-117 1.81e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 1.81e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   6 HRAARDGYLELLKEATRK--ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:COG0666  92 HAAARNGDLEIVKLLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                        90       100       110
                ....*....|....*....|....*....|....
gi 28849903  84 LVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
CEN_USH1G cd21803
central domain found in usher syndrome type-1G protein; Usher syndrome type-1G protein (USH1G), ...
 296-388 1.84e-25

central domain found in usher syndrome type-1G protein; Usher syndrome type-1G protein (USH1G), also called scaffold protein containing ankyrin repeats and SAM domain (Sans), is an anchoring/scaffolding protein that is part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A, that mediates mechanotransduction in cochlear hair cells. It is required for normal development and maintenance of cochlear hair cell bundles, as well as for normal hearing. USH1G consists of four N-terminal ANK repeats, a central region, and a sterile alpha motif (SAM) followed by a C-terminal type I PDZ binding motif (PBM). This model corresponds to the central region (CEN) of USH1G, which contains the conserved regions CEN1 and CEN2. CEN is directly responsible for binding to the MYO7A MyTH4-FERM tandem.


Pssm-ID: 409642  Cd Length: 57  Bit Score: 98.38  E-value: 1.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903 296 EVSTDSGHDSLFTRPGLGTMVFRRNYVSSGLHGLGREDggldgagtprgrlhsspsldddslgsanslqdrscgEELPWD 375
Cdd:cd21803   1 EVSTDSGHDSLFNRPGLGTMVFRRNYVSSGLFGLGRED------------------------------------EELPWD 44

                        90
                ....*....|...
gi 28849903 376 ELDLGLDEDLEPE 388
Cdd:cd21803  45 EVDLGLDDDDEPD 57
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-117 7.71e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 7.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903    38 WAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFgANIWCLDNDYhTPLDMAAMKGHMECVRYL 117
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVKLL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 26-127 3.31e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.30  E-value: 3.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   26 NAPDEDGMTPTLWA---------AYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDN 96
Cdd:PTZ00322  67 NLTTEEVIDPVVAHmltvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                         90       100       110
                 ....*....|....*....|....*....|.
gi 28849903   97 DYHTPLDMAAMKGHMECVRYLDSIAAKQSSL 127
Cdd:PTZ00322 147 DGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 395-447 3.50e-08

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 49.96  E-value: 3.50e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28849903   395 FLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAVRRRR 447
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVtLLGHRKKILYAIQRLK 64
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 65-91 9.58e-07

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: 44.89  E-value: 9.58e-07
                           10        20
                   ....*....|....*....|....*..
gi 28849903     65 GNTPLHLAASNGHLHCLSFLVSFGANI 91
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 395-448 1.83e-04

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 39.59  E-value: 1.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903    395 FLASLHMEDFASLLRHEKIDLEALMLCSDL-DLRSISV-PLGPRKKILGAVRRRRQ 448
Cdd:smart00454  12 WLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGItKLGHRKKILKAIQKLKE 67
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 39-117 4.58e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 4.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903  39 AAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAA--SNGHLHC--LSFLVSFGA--NIWCLD----NDYHTPLDMAAMK 108
Cdd:cd22192 143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlqPNKTFACqmYDLILSYDKedDLQPLDlvpnNQGLTPFKLAAKE 222


                ....*....
gi 28849903 109 GHMECVRYL 117
Cdd:cd22192 223 GNIVMFQHL 231
 
Name Accession Description Interval E-value
SAM_USH1G cd09586
SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) ...
 388-453 3.69e-34

SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


Pssm-ID: 188985  Cd Length: 66  Bit Score: 122.21  E-value: 3.69e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903 388 ETSPLETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQALERP 453
Cdd:cd09586   1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 388-453 1.52e-29

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


Pssm-ID: 188916  Cd Length: 66  Bit Score: 109.73  E-value: 1.52e-29
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903 388 ETSPLETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQALERP 453
Cdd:cd09517   1 ETSPLERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPLGPRRKLLNAIAKRKQALENP 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-117 1.81e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 1.81e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   6 HRAARDGYLELLKEATRK--ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:COG0666  92 HAAARNGDLEIVKLLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                        90       100       110
                ....*....|....*....|....*....|....
gi 28849903  84 LVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
CEN_USH1G cd21803
central domain found in usher syndrome type-1G protein; Usher syndrome type-1G protein (USH1G), ...
 296-388 1.84e-25

central domain found in usher syndrome type-1G protein; Usher syndrome type-1G protein (USH1G), also called scaffold protein containing ankyrin repeats and SAM domain (Sans), is an anchoring/scaffolding protein that is part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A, that mediates mechanotransduction in cochlear hair cells. It is required for normal development and maintenance of cochlear hair cell bundles, as well as for normal hearing. USH1G consists of four N-terminal ANK repeats, a central region, and a sterile alpha motif (SAM) followed by a C-terminal type I PDZ binding motif (PBM). This model corresponds to the central region (CEN) of USH1G, which contains the conserved regions CEN1 and CEN2. CEN is directly responsible for binding to the MYO7A MyTH4-FERM tandem.


Pssm-ID: 409642  Cd Length: 57  Bit Score: 98.38  E-value: 1.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903 296 EVSTDSGHDSLFTRPGLGTMVFRRNYVSSGLHGLGREDggldgagtprgrlhsspsldddslgsanslqdrscgEELPWD 375
Cdd:cd21803   1 EVSTDSGHDSLFNRPGLGTMVFRRNYVSSGLFGLGRED------------------------------------EELPWD 44

                        90
                ....*....|...
gi 28849903 376 ELDLGLDEDLEPE 388
Cdd:cd21803  45 EVDLGLDDDDEPD 57
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-149 2.25e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 2.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   6 HRAARDGYLELLKE--ATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:COG0666 125 HLAAYNGNLEIVKLllEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903  84 LVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYLDSIAAKQSSLNPKLVGKLKDKAFREAERRIRE 149
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
 388-453 3.08e-22

SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting Ankyrin Repeat-containing) proteins, also known as ANKS4B, is a protein-protein interaction domain. Proteins of this subfamily have an N-terminal ankyrin repeat region and C-terminal SAM. In mouse epithelial tissues, HARP protein interacts with the PDZ domain of harmonin. This scaffolding complex facilitates signal transduction in epithelia. HARP was found co-expressed with harmonin in a number of epithelial cells including pancreatic ductal epithelium, embryonic epithelia of the lung, kidney, salivary glands, and cochlea.


Pssm-ID: 188986  Cd Length: 67  Bit Score: 89.89  E-value: 3.08e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903 388 ETSPLETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQALERP 453
Cdd:cd09587   1 DATPLEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQLGPRKKILSAVARRKQVLQQP 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-117 1.23e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.64  E-value: 1.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   1 MNDQYHRAARDGYLELLKEATRK--ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHL 78
Cdd:COG0666  54 GALLLLAAALAGDLLVALLLLAAgaDINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 28849903  79 HCLSFLVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:COG0666 134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-117 7.71e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 7.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903    38 WAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFgANIWCLDNDYhTPLDMAAMKGHMECVRYL 117
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVKLL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-123 7.96e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.69  E-value: 7.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   6 HRAARDGYLELLKE--ATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:COG0666 158 HLAAANGNLEIVKLllEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 28849903  84 LVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYLDSIAAK 123
Cdd:COG0666 238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
6-95 2.65e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 2.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903     6 HRAARDGYLELLKE--ATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGgDPDKCDIwGNTPLHLAASNGHLHCLSF 83
Cdd:pfam12796   2 HLAAKNGNLELVKLllENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 28849903    84 LVSFGANIWCLD 95
Cdd:pfam12796  80 LLEKGADINVKD 91
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
 383-447 5.73e-15

SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 interacting protein) subfamily is a potential protein-protein interaction domain. This group of proteins includes Sec23ip and DDHD2 proteins. All of them contain at least two domains: a SAM domain and a predicted metal-binding domain. For mammalian DDHD2 members of this group, phospholipase activity has been demonstrated. Sec23ip proteins of this group interact with Sec23 proteins via an N-terminal proline-rich region. Members of this subfamily are involved in organization of ER/Golgi intermediate compartment.


Pssm-ID: 188915  Cd Length: 69  Bit Score: 69.36  E-value: 5.73e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28849903 383 EDLEPETSPLETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRR 447
Cdd:cd09516   3 VEEQEEPLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPMGPRKKLLGFLKDQK 67
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
 389-447 4.09e-13

SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential protein-protein interaction domain. DDHD2 proteins contain at least two domains:a SAM domain and a predicted metal-binding domain. Phospholipase A1 activity was demonstrated for the mammalian DDHD2 protein. Mutation of the putative catalytic serine resulted in elimination of activity. Unlike SEC23IP, DDHD2 proteins do not have an N-terminal proline-rich region and correspondingly they are not able to interact with Sec23p/Sec24p complex. Overexpression of DDHD2 is the cause of dispersion of ER/Golgi intermediate compartment and dispersion of tethering proteins located in the Golgi region, leading to aggregation in the endoplasmic reticulum.


Pssm-ID: 188984  Cd Length: 69  Bit Score: 64.01  E-value: 4.09e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28849903 389 TSPLETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRR 447
Cdd:cd09585   9 TPTLEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGIPLGPRKKILNYIRRRF 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
32-85 3.16e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 3.16e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28849903    32 GMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLV 85
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
65-117 7.92e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 7.92e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 28849903    65 GNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-117 1.63e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 1.63e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 28849903    69 LHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-117 1.64e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   7 RAARDGYLELLKEATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVS 86
Cdd:COG0666  29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108

                        90       100       110
                ....*....|....*....|....*....|.
gi 28849903  87 FGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:COG0666 109 AGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 26-127 3.31e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.30  E-value: 3.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   26 NAPDEDGMTPTLWA---------AYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDN 96
Cdd:PTZ00322  67 NLTTEEVIDPVVAHmltvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                         90       100       110
                 ....*....|....*....|....*....|.
gi 28849903   97 DYHTPLDMAAMKGHMECVRYLDSIAAKQSSL 127
Cdd:PTZ00322 147 DGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
SAM_sec23ip cd09584
SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) ...
 382-449 1.01e-10

SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) group is a potential protein-protein interaction domain. Sec23ip proteins (also known as p125) contain an N-terminal proline-rich region, a central region containing a SAM domain and a C-terminal region with a predicted metal-binding domain. Sec23ip interacts with Sec23p/Sec24p part of COPII-coated vesicles complex involved in protein transport from the ER to the Golgi apparatus. The proline-rich region plays an essential role in this interaction. Overexpression of Sec23ip leads to disorganization of ER/Golgi intermediate compartment.


Pssm-ID: 188983  Cd Length: 69  Bit Score: 57.52  E-value: 1.01e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28849903 382 DEDLEPETSPLETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQA 449
Cdd:cd09584   2 LNEEEEDVPSLQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPLGPRKKIANFVKEKAAK 69
CEN_USH1G_ANKS4B cd21764
central domain found in usher syndrome type-1G protein, ankyrin repeat and SAM ...
 296-384 2.43e-10

central domain found in usher syndrome type-1G protein, ankyrin repeat and SAM domain-containing protein 4B, and similar proteins; The family includes usher syndrome type-1G protein (USH1G), ankyrin repeat and SAM domain-containing protein 4B (ANKS4B), and similar proteins. USH1G, also called scaffold protein containing ankyrin repeats and SAM domain (Sans), is an anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A, that mediates mechanotransduction in cochlear hair cells. It is required for normal development and maintenance of cochlear hair cell bundles, as well as for normal hearing. ANKS4B, also called Harmonin-interacting ankyrin repeat-containing protein (Harp), is highly expressed in intestine and is essential for intermicrovillar adhesion. As part of the intermicrovillar adhesion complex (IMAC), ANKS4B plays a role in epithelial brush border differentiation, controlling microvilli organization and length. It may be involved in cellular response to endoplasmic reticulum stress. Both USH1G and ANKS4B contain four N-terminal ANK repeats, a central region, and a sterile alpha motif (SAM) followed by a C-terminal type I PDZ binding motif (PBM). This model corresponds to the central region (CEN), which contains the conserved regions CEN1 and CEN2. CEN is directly responsible for USH1G binding to the MYO7A MyTH4-FERM tandem, as well as for ANKS4B binding to the N-terminal MyTH4-FERM-SH3 supramodule of MYO7B.


Pssm-ID: 409640  Cd Length: 41  Bit Score: 55.55  E-value: 2.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903 296 EVSTDSGHDSLFTRPGLGTMVFRRNYvssglhglgredggldgagtprgrlhsspsldddslgsanslqdrscgEELPWD 375
Cdd:cd21764   1 EESTDSGHESIFNRPGLGNIVFRRNL------------------------------------------------EELPWD 32


                ....*....
gi 28849903 376 ELDLGLDED 384
Cdd:cd21764  33 EEELEWDEE 41
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-120 2.87e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.83  E-value: 2.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   25 LNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANI----WCL----DN 96
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIktiiETLlyfkDK 264

                         90       100
                 ....*....|....*....|....
gi 28849903   97 DYHTPLDMAAMKGHMECVRYLDSI 120
Cdd:PHA03100 265 DLNTITKIKMLKKSIMYMFLLDPG 288
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 395-447 3.50e-08

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 49.96  E-value: 3.50e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28849903   395 FLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAVRRRR 447
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVtLLGHRKKILYAIQRLK 64
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 392-445 6.47e-08

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 49.16  E-value: 6.47e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28849903 392 LETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAVRR 445
Cdd:cd09487   2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGItSPGHRKKILRAIQR 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-139 1.27e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   30 EDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKG 109
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90       100       110
                 ....*....|....*....|....*....|.
gi 28849903  110 HME-CVRYLDSIAakqsslNPKLVGKLKDKA 139
Cdd:PHA02875 180 DIAiCKMLLDSGA------NIDYFGKNGCVA 204
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-117 5.46e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 5.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   25 LNAPDEDGMTPTLWAAYHGN-LESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLH--CLSFLVSFGANIWCLDNDYHTP 101
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTP 155

                         90
                 ....*....|....*....
gi 28849903  102 LDmAAMKGH---MECVRYL 117
Cdd:PHA03095 156 LA-VLLKSRnanVELLRLL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 65-91 9.58e-07

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: 44.89  E-value: 9.58e-07
                           10        20
                   ....*....|....*....|....*..
gi 28849903     65 GNTPLHLAASNGHLHCLSFLVSFGANI 91
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 6-105 2.55e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903    6 HRAARDGYLELLKE--ATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:PHA02874 129 HYAIKKGDLESIKMlfEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKL 208

                         90       100
                 ....*....|....*....|..
gi 28849903   84 LVSFGANIWCLDNDYHTPLDMA 105
Cdd:PHA02874 209 LIDHGNHIMNKCKNGFTPLHNA 230
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 37-135 5.12e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 5.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   37 LWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKGHMECVRY 116
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609

                         90
                 ....*....|....*....
gi 28849903  117 LDSIAakqSSLNPKLVGKL 135
Cdd:PLN03192 610 LYHFA---SISDPHAAGDL 625
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-102 5.54e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.03  E-value: 5.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   6 HRAARDGYLELLKE--ATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:COG0666 191 HLAAENGHLEIVKLllEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                        90
                ....*....|....*....
gi 28849903  84 LVSFGANIWCLDNDYHTPL 102
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-117 5.81e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   24 ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLD 103
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                         90
                 ....*....|....
gi 28849903  104 MAAMKGHMECVRYL 117
Cdd:PHA02874 196 NAAEYGDYACIKLL 209
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 65-96 7.63e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 7.63e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 28849903    65 GNTPLHLAA-SNGHLHCLSFLVSFGANIWCLDN 96
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
17-72 9.66e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 9.66e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903    17 LKEATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLA 72
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
50-105 1.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903    50 LIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMA 105
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
5-52 2.14e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 28849903     5 YHRAARDGYLELLKE--ATRKELNAPDEDGMTPTLWAAYHGNLESLRLIV 52
Cdd:pfam13637   5 LHAAAASGHLELLRLllEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-131 4.93e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   24 ELNAPDEDGMTPTLWAAYHG-NLESLRLIVSRGGDPDKCDIWGNTPLHLAAS-NGHLHCLSFLVSFGANIWCLDNDYHTP 101
Cdd:PHA02876 299 DVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTP 378

                         90       100       110
                 ....*....|....*....|....*....|
gi 28849903  102 LDMAAMKGHMECVRYLDSIAAKQSSLNPKL 131
Cdd:PHA02876 379 IHYAAVRNNVVIINTLLDYGADIEALSQKI 408
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 65-91 7.03e-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: 39.55  E-value: 7.03e-05
                          10        20
                  ....*....|....*....|....*..
gi 28849903    65 GNTPLHLAASNGHLHCLSFLVSFGANI 91
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
CEN_ANKS4B cd21802
central domain found in ankyrin repeat and SAM domain-containing protein 4B; Ankyrin repeat ...
 303-326 9.24e-05

central domain found in ankyrin repeat and SAM domain-containing protein 4B; Ankyrin repeat and SAM domain-containing protein 4B (ANKS4B), also called Harmonin-interacting ankyrin repeat-containing protein (Harp), is highly expressed in intestine and is essential for intermicrovillar adhesion. As part of the intermicrovillar adhesion complex (IMAC), ANKS4B plays a role in epithelial brush border differentiation, controlling microvilli organization and length. It may be involved in cellular response to endoplasmic reticulum stress. ANKS4B consists of four N-terminal ANK repeats, a central region, and a sterile alpha motif (SAM) followed by a C-terminal type I PDZ binding motif (PBM). This model corresponds to the central region (CEN) of ANKS4B, which contains the conserved regions CEN1 and CEN2. CEN is directly responsible for binding to the N-terminal MyTH4-FERM-SH3 supramodule of MYO7B, with a mechanism highly analogous to the interaction between USH1G and MYO7A.


Pssm-ID: 409641  Cd Length: 46  Bit Score: 39.79  E-value: 9.24e-05
                        10        20
                ....*....|....*....|....
gi 28849903 303 HDSLFTRPGLGTMVFRRNYVSSGL 326
Cdd:cd21802   8 HESIFNRPGLGNIVFRRNRSDDDL 31
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 395-448 1.83e-04

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 39.59  E-value: 1.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 28849903    395 FLASLHMEDFASLLRHEKIDLEALMLCSDL-DLRSISV-PLGPRKKILGAVRRRRQ 448
Cdd:smart00454  12 WLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGItKLGHRKKILKAIQKLKE 67
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 34-107 3.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.28  E-value: 3.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28849903   34 TPTLWAAYHGNLESLRLIVSRGGDPDKcdiWGN----TPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAM 107
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNR---YAEeakiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 39-117 4.58e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 4.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903  39 AAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAA--SNGHLHC--LSFLVSFGA--NIWCLD----NDYHTPLDMAAMK 108
Cdd:cd22192 143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlqPNKTFACqmYDLILSYDKedDLQPLDlvpnNQGLTPFKLAAKE 222


                ....*....
gi 28849903 109 GHMECVRYL 117
Cdd:cd22192 223 GNIVMFQHL 231
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-106 1.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   25 LNAPDEDGMTPTLWAAYHGNLESL-RLIVSRGGDPDKCDIWGNTPLHLAASNGH-LHCLSFLVSFGANIWCLDNDYHTPL 102
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPL 345


                 ....
gi 28849903  103 DMAA 106
Cdd:PHA02876 346 HQAS 349
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 42-106 1.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   42 HGNLESLRLIVSRGGDPDKC----------------DIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMA 105
Cdd:PHA03100 153 KIDLKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232


                 .
gi 28849903  106 A 106
Cdd:PHA03100 233 I 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 22-104 1.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   22 RKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGN-TPLHLAASNGHLHCLSFLVSFGAN---IWCLDND 97
Cdd:PHA02875 158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADcniMFMIEGE 237


                 ....*..
gi 28849903   98 YHTPLDM 104
Cdd:PHA02875 238 ECTILDM 244
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 390-443 2.60e-03

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 36.12  E-value: 2.60e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28849903 390 SPLETFLASLHMEDFASLLRHEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAV 443
Cdd:cd09520   5 SDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGItAFGARRKMLLAI 59
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-117 4.41e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.17  E-value: 4.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903  14 LELLKEATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWC 93
Cdd:COG0666   3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                        90       100
                ....*....|....*....|....
gi 28849903  94 LDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:COG0666  83 KDDGGNTLLHAAARNGDLEIVKLL 106
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 31-60 5.40e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 5.40e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 28849903     31 DGMTPTLWAAYHGNLESLRLIVSRGGDPDK 60
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-82 5.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 5.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 28849903   25 LNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLS 82
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 97-117 8.08e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.72  E-value: 8.08e-03
                           10        20
                   ....*....|....*....|.
gi 28849903     97 DYHTPLDMAAMKGHMECVRYL 117
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLL 21
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-147 9.89e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 9.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28849903   26 NAPDEDGMTPTLWAAYHGNLESLRLI--VSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLD 103
Cdd:PHA03095 216 AATDMLGNTPLHSMATGSSCKRSLVLplLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLS 295

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 28849903  104 MAAMKGHMECVRyldsiAAKQSSLNPKLVgklkDKAFREAERRI 147
Cdd:PHA03095 296 LMVRNNNGRAVR-----AALAKNPSAETV----AATLNTASVAG 330
 
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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