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Conserved domains on  [gi|34304383|ref|NP_775748.2|]
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Usher syndrome type-1G protein isoform 1 [Homo sapiens]

Protein Classification

ANK and SAM_USH1G domain-containing protein (domain architecture ID 10079378)

ANK and SAM_USH1G domain-containing protein

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 3.77e-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: 123.75  E-value: 3.77e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34304383 388 ETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQAMERP 453
Cdd:cd09586   1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
6-117 2.73e-31

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


:

Pssm-ID: 238125  Cd Length: 126  Bit Score: 117.48  E-value: 2.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   6 HRAARDGYLELLKEATRK--ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:cd00204  12 HLAASNGHLEVVKLLLENgaDVNAKDNDGRTPLHLAAKNGHLEIVKLLLEKGADVNARDKDGNTPLHLAARNGNLDVVKL 91
                        90       100       110
                ....*....|....*....|....*....|....
gi 34304383  84 LVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:cd00204  92 LLKHGADVNARDKDGRTPLHLAAKNGHLEVVKLL 125
 
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 3.77e-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: 123.75  E-value: 3.77e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34304383 388 ETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQAMERP 453
Cdd:cd09586   1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
6-117 2.73e-31

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


Pssm-ID: 238125  Cd Length: 126  Bit Score: 117.48  E-value: 2.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   6 HRAARDGYLELLKEATRK--ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:cd00204  12 HLAASNGHLEVVKLLLENgaDVNAKDNDGRTPLHLAAKNGHLEIVKLLLEKGADVNARDKDGNTPLHLAARNGNLDVVKL 91
                        90       100       110
                ....*....|....*....|....*....|....
gi 34304383  84 LVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:cd00204  92 LLKHGADVNARDKDGRTPLHLAAKNGHLEVVKLL 125
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-117 1.03e-19

Ankyrin repeats (3 copies);


Pssm-ID: 315466  Cd Length: 92  Bit Score: 84.78  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383    38 WAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFgANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:pfam12796   3 LAAKNGDLELVKLLLEEGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDKNGRTALHYAARSGHLEIVKLL 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-129 8.75e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738  Cd Length: 235  Bit Score: 67.54  E-value: 8.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   1 MNDQYHRAARDGYLELL-KEATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLH 79
Cdd:COG0666  41 LYLELALLPAASLSELLlKLIVDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALNGNPP 120
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34304383  80 -----CLSFLVSFGANIWCL---DNDYHTPLDMAAMKGHMECVRYLDSIAAKQSSLNP 129
Cdd:COG0666 121 egnieVAKLLLEAGADLDVNnlrDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNS 178
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
26-127 2.84e-11

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


Pssm-ID: 140343  Cd Length: 664  Bit Score: 65.30  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   26 NAPDEDGMTPTLWA---------AYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDN 96
Cdd:PTZ00322  67 NLTTEEVIDPVVAHmltvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146
                         90       100       110
                 ....*....|....*....|....*....|.
gi 34304383   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 1.55e-07

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: 306919  Cd Length: 62  Bit Score: 49.54  E-value: 1.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 34304383   395 FLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAVRRRR 447
Cdd:pfam00536   9 WLESIGLGQYIDLFRAGYIDGDTLLLLTEDDLLKLGVtLLGHRKKILYSIQGLK 62
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
65-91 2.90e-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  Cd Length: 30  Bit Score: 45.27  E-value: 2.90e-06
                           10        20
                   ....*....|....*....|....*..
gi 34304383     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 3.60e-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: 3.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 34304383    395 FLASLHMEDFAALLRQEKIDLEALMLCSDL-DLRSISV-PLGPRKKILGAVRRRRQ 448
Cdd:smart00454  12 WLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGItKLGHRKKILKAIQKLKE 67
 
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 3.77e-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: 123.75  E-value: 3.77e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34304383 388 ETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQAMERP 453
Cdd:cd09586   1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
6-117 2.73e-31

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


Pssm-ID: 238125  Cd Length: 126  Bit Score: 117.48  E-value: 2.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   6 HRAARDGYLELLKEATRK--ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:cd00204  12 HLAASNGHLEVVKLLLENgaDVNAKDNDGRTPLHLAAKNGHLEIVKLLLEKGADVNARDKDGNTPLHLAARNGNLDVVKL 91
                        90       100       110
                ....*....|....*....|....*....|....
gi 34304383  84 LVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:cd00204  92 LLKHGADVNARDKDGRTPLHLAAKNGHLEVVKLL 125
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
388-453 7.51e-30

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: 111.66  E-value: 7.51e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34304383 388 ETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQAMERP 453
Cdd:cd09517   1 ETSPLERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPLGPRRKLLNAIAKRKQALENP 66
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
26-117 4.03e-28

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


Pssm-ID: 238125  Cd Length: 126  Bit Score: 108.62  E-value: 4.03e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383  26 NAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMA 105
Cdd:cd00204   1 NARDEDGRTPLHLAASNGHLEVVKLLLENGADVNAKDNDGRTPLHLAAKNGHLEIVKLLLEKGADVNARDKDGNTPLHLA 80
                        90
                ....*....|..
gi 34304383 106 AMKGHMECVRYL 117
Cdd:cd00204  81 ARNGNLDVVKLL 92
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
388-453 1.61e-21

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: 89.12  E-value: 1.61e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34304383 388 ETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQAMERP 453
Cdd:cd09587   1 DATPLEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQLGPRKKILSAVARRKQVLQQP 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-117 1.03e-19

Ankyrin repeats (3 copies);


Pssm-ID: 315466  Cd Length: 92  Bit Score: 84.78  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383    38 WAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFgANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:pfam12796   3 LAAKNGDLELVKLLLEEGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDKNGRTALHYAARSGHLEIVKLL 81
ANK cd00204
ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse ...
6-85 1.85e-17

ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other types of domains. The structural repeat unit contains two antiparallel helices and a beta-hairpin, repeats are stacked in a superhelical arrangement; this alignment contains 4 consecutive repeats.


Pssm-ID: 238125  Cd Length: 126  Bit Score: 79.35  E-value: 1.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   6 HRAARDGYLELLKEATRK--ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:cd00204  45 HLAAKNGHLEIVKLLLEKgaDVNARDKDGNTPLHLAARNGNLDVVKLLLKHGADVNARDKDGRTPLHLAAKNGHLEVVKL 124

                ..
gi 34304383  84 LV 85
Cdd:cd00204 125 LL 126
Ank_2 pfam12796
Ankyrin repeats (3 copies);
6-95 1.42e-15

Ankyrin repeats (3 copies);


Pssm-ID: 315466  Cd Length: 92  Bit Score: 73.22  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383     6 HRAARDGYLELLKE--ATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGgDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:pfam12796   2 HLAAKNGDLELVKLllEEGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDKNGRTALHYAARSGHLEIVKL 80
                          90
                  ....*....|..
gi 34304383    84 LVSFGANIWCLD 95
Cdd:pfam12796  81 LLEKGADINVKD 92
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
383-447 6.14e-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: 70.90  E-value: 6.14e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34304383 383 EDLEPETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRR 447
Cdd:cd09516   3 VEEQEEPLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPMGPRKKLLGFLKDQK 67
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-129 8.75e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738  Cd Length: 235  Bit Score: 67.54  E-value: 8.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   1 MNDQYHRAARDGYLELL-KEATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLH 79
Cdd:COG0666  41 LYLELALLPAASLSELLlKLIVDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALNGNPP 120
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34304383  80 -----CLSFLVSFGANIWCL---DNDYHTPLDMAAMKGHMECVRYLDSIAAKQSSLNP 129
Cdd:COG0666 121 egnieVAKLLLEAGADLDVNnlrDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNS 178
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
389-447 2.70e-12

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: 63.24  E-value: 2.70e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34304383 389 TSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRR 447
Cdd:cd09585   9 TPTLEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGIPLGPRKKILNYIRRRF 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
32-85 3.13e-12

Ankyrin repeats (many copies);


Pssm-ID: 316185  Cd Length: 54  Bit Score: 62.69  E-value: 3.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 34304383    32 GMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLV 85
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLENGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-117 5.51e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738  Cd Length: 235  Bit Score: 65.23  E-value: 5.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   6 HRAARDGYLELLKEATRK--ELNAPDEDGMTPTLWAAYHGNL-----ESLRLIVSRGGDPDkCDIW----GNTPLHLAAS 74
Cdd:COG0666  78 HSAASKGDDKIVKLLLASgaDVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADLD-VNNLrdedGNTPLHWAAL 156
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 34304383  75 NGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:COG0666 157 NGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLL 199
Ank_4 pfam13637
Ankyrin repeats (many copies);
65-117 1.40e-11

Ankyrin repeats (many copies);


Pssm-ID: 316185  Cd Length: 54  Bit Score: 61.14  E-value: 1.40e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 34304383    65 GNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLENGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
26-127 2.84e-11

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


Pssm-ID: 140343  Cd Length: 664  Bit Score: 65.30  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   26 NAPDEDGMTPTLWA---------AYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDN 96
Cdd:PTZ00322  67 NLTTEEVIDPVVAHmltvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146
                         90       100       110
                 ....*....|....*....|....*....|.
gi 34304383   97 DYHTPLDMAAMKGHMECVRYLDSIAAKQSSL 127
Cdd:PTZ00322 147 DGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-117 6.85e-11

Ankyrin repeats (3 copies);


Pssm-ID: 315466  Cd Length: 92  Bit Score: 59.74  E-value: 6.85e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 34304383    69 LHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKGHMECVRYL 117
Cdd:pfam12796   1 LHLAAKNGDLELVKLLLEEGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
SAM_sec23ip cd09584
SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) ...
382-449 9.56e-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: 55.97  E-value: 9.56e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34304383 382 DEDLEPETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQA 449
Cdd:cd09584   2 LNEEEEDVPSLQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPLGPRKKIANFVKEKAAK 69
PHA03100 PHA03100
ankyrin repeat protein; Provisional
25-120 2.46e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984  Cd Length: 422  Bit Score: 55.83  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   25 LNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANI----WCL----DN 96
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIktiiETLlyfkDK 264
                         90       100
                 ....*....|....*....|....
gi 34304383   97 DYHTPLDMAAMKGHMECVRYLDSI 120
Cdd:PHA03100 265 DLNTITKIKMLKKSIMYMFLLDPG 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-90 3.21e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738  Cd Length: 235  Bit Score: 54.06  E-value: 3.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   5 YHRAARDGYL---------ELLKEATRKE-LNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAAS 74
Cdd:COG0666 110 LHLAALNGNPpegnievakLLLEAGADLDvNNLRDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAK 189
                        90
                ....*....|....*.
gi 34304383  75 NGHLHCLSFLVSFGAN 90
Cdd:COG0666 190 NGRIELVKLLLDKGLH 205
PHA02875 PHA02875
ankyrin repeat protein; Provisional
30-139 1.09e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206  Cd Length: 413  Bit Score: 53.46  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   30 EDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKG 109
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
                         90       100       110
                 ....*....|....*....|....*....|.
gi 34304383  110 HME-CVRYLDSIAakqsslNPKLVGKLKDKA 139
Cdd:PHA02875 180 DIAiCKMLLDSGA------NIDYFGKNGCVA 204
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
395-447 1.55e-07

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: 306919  Cd Length: 62  Bit Score: 49.54  E-value: 1.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 34304383   395 FLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAVRRRR 447
Cdd:pfam00536   9 WLESIGLGQYIDLFRAGYIDGDTLLLLTEDDLLKLGVtLLGHRKKILYSIQGLK 62
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
65-96 3.13e-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: 306522  Cd Length: 33  Bit Score: 48.02  E-value: 3.13e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 34304383    65 GNTPLHLAASNGHLHCLSFLVSFGANIWCLDN 96
Cdd:pfam00023   2 GNTPLHLAAREGNLEIVKLLLSKGADVNARDK 33
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
392-445 3.84e-07

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  Cd Length: 56  Bit Score: 48.39  E-value: 3.84e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 34304383 392 LETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAVRR 445
Cdd:cd09487   2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGItSPGHRKKILRAIQR 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
25-117 4.58e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980  Cd Length: 471  Bit Score: 51.95  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   25 LNAPDEDGMTPTLWAAYHGN-LESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLH--CLSFLVSFGANIWCLDNDYHTP 101
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTP 155
                         90
                 ....*....|....*....
gi 34304383  102 LDmAAMKGH---MECVRYL 117
Cdd:PHA03095 156 LA-VLLKSRnanVELLRLL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
6-105 2.18e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205  Cd Length: 434  Bit Score: 49.58  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383    6 HRAARDGYLELLKE--ATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSF 83
Cdd:PHA02874 129 HYAIKKGDLESIKMlfEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKL 208
                         90       100
                 ....*....|....*....|..
gi 34304383   84 LVSFGANIWCLDNDYHTPLDMA 105
Cdd:PHA02874 209 LIDHGNHIMNKCKNGFTPLHNA 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
65-91 2.90e-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  Cd Length: 30  Bit Score: 45.27  E-value: 2.90e-06
                           10        20
                   ....*....|....*....|....*..
gi 34304383     65 GNTPLHLAASNGHLHCLSFLVSFGANI 91
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
37-135 4.22e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625  Cd Length: 823  Bit Score: 49.10  E-value: 4.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   37 LWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAMKGHMECVRY 116
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609
                         90
                 ....*....|....*....
gi 34304383  117 LDSIAakqSSLNPKLVGKL 135
Cdd:PLN03192 610 LYHFA---SISDPHAAGDL 625
PHA02874 PHA02874
ankyrin repeat protein; Provisional
24-117 4.96e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205  Cd Length: 434  Bit Score: 48.42  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   24 ELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLD 103
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                         90
                 ....*....|....
gi 34304383  104 MAAMKGHMECVRYL 117
Cdd:PHA02874 196 NAAEYGDYACIKLL 209
Ank_4 pfam13637
Ankyrin repeats (many copies);
5-52 2.52e-05

Ankyrin repeats (many copies);


Pssm-ID: 316185  Cd Length: 54  Bit Score: 43.04  E-value: 2.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 34304383     5 YHRAARDGYLELLKE--ATRKELNAPDEDGMTPTLWAAYHGNLESLRLIV 52
Cdd:pfam13637   5 LHAAAASGHLELLRLllENGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
50-105 3.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 316380  Cd Length: 56  Bit Score: 42.74  E-value: 3.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 34304383    50 LIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMA 105
Cdd:pfam13857   1 LLENGPADLNRLDGEGYTPLHLAAKYGALEIVRLLLKRGADLNLKDFRGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
24-131 4.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207  Cd Length: 682  Bit Score: 45.82  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   24 ELNAPDEDGMTPTLWAAYHG-NLESLRLIVSRGGDPDKCDIWGNTPLHLAAS-NGHLHCLSFLVSFGANIWCLDNDYHTP 101
Cdd:PHA02876 299 DVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTP 378
                         90       100       110
                 ....*....|....*....|....*....|
gi 34304383  102 LDMAAMKGHMECVRYLDSIAAKQSSLNPKL 131
Cdd:PHA02876 379 IHYAAVRNNVVIINTLLDYGADIEALSQKI 408
Ank_5 pfam13857
Ankyrin repeats (many copies);
17-72 6.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 316380  Cd Length: 56  Bit Score: 41.97  E-value: 6.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 34304383    17 LKEATRKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLA 72
Cdd:pfam13857   1 LLENGPADLNRLDGEGYTPLHLAAKYGALEIVRLLLKRGADLNLKDFRGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
44-105 1.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984  Cd Length: 422  Bit Score: 43.89  E-value: 1.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34304383   44 NLESLRLIVSRGGDPDKCDIWGNTPLHLAASN--GHLHCLSFLVSFGANIWCLDNDYHTPLDMA 105
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
65-91 1.92e-04

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


Pssm-ID: 316158  Cd Length: 30  Bit Score: 39.96  E-value: 1.92e-04
                          10        20
                  ....*....|....*....|....*..
gi 34304383    65 GNTPLHLAASNGHLHCLSFLVSFGANI 91
Cdd:pfam13606   2 GNTPLHLAARNGRLEVVKLLLELGADI 28
PHA02884 PHA02884
ankyrin repeat protein; Provisional
34-107 3.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212  Cd Length: 300  Bit Score: 42.28  E-value: 3.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34304383   34 TPTLWAAYHGNLESLRLIVSRGGDPDKcdiWGN----TPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMAAM 107
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNR---YAEeakiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
395-448 3.60e-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: 3.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 34304383    395 FLASLHMEDFAALLRQEKIDLEALMLCSDL-DLRSISV-PLGPRKKILGAVRRRRQ 448
Cdd:smart00454  12 WLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGItKLGHRKKILKAIQKLKE 67
PHA02876 PHA02876
ankyrin repeat protein; Provisional
25-106 9.87e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207  Cd Length: 682  Bit Score: 41.59  E-value: 9.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   25 LNAPDEDGMTPTLWAAYHGNLESL-RLIVSRGGDPDKCDIWGNTPLHLAASNGH-LHCLSFLVSFGANIWCLDNDYHTPL 102
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPL 345

                 ....
gi 34304383  103 DMAA 106
Cdd:PHA02876 346 HQAS 349
PHA03100 PHA03100
ankyrin repeat protein; Provisional
42-106 9.92e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984  Cd Length: 422  Bit Score: 41.19  E-value: 9.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   42 HGNLESLRLIVSRGGDPDKC----------------DIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLDMA 105
Cdd:PHA03100 153 KIDLKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232

                 .
gi 34304383  106 A 106
Cdd:PHA03100 233 I 233
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
390-443 1.47e-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: 38.05  E-value: 1.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 34304383 390 SPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAV 443
Cdd:cd09520   5 SDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGItAFGARRKMLLAI 59
PHA02875 PHA02875
ankyrin repeat protein; Provisional
22-104 1.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206  Cd Length: 413  Bit Score: 40.36  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   22 RKELNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGN-TPLHLAASNGHLHCLSFLVSFGAN---IWCLDND 97
Cdd:PHA02875 158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADcniMFMIEGE 237

                 ....*..
gi 34304383   98 YHTPLDM 104
Cdd:PHA02875 238 ECTILDM 244
PHA03095 PHA03095
ankyrin-like protein; Provisional
25-82 4.63e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980  Cd Length: 471  Bit Score: 39.24  E-value: 4.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34304383   25 LNAPDEDGMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLS 82
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
31-62 6.45e-03

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


Pssm-ID: 306522  Cd Length: 33  Bit Score: 35.69  E-value: 6.45e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 34304383    31 DGMTPTLWAAYHGNLESLRLIVSRGGDPDKCD 62
Cdd:pfam00023   1 DGNTPLHLAAREGNLEIVKLLLSKGADVNARD 32
PHA03095 PHA03095
ankyrin-like protein; Provisional
26-147 8.29e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980  Cd Length: 471  Bit Score: 38.08  E-value: 8.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   26 NAPDEDGMTPTLWAAYHGNLESLRLI--VSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPLD 103
Cdd:PHA03095 216 AATDMLGNTPLHSMATGSSCKRSLVLplLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLS 295
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 34304383  104 MAAMKGHMECVRyldsiAAKQSSLNPKLVgklkDKAFREAERRI 147
Cdd:PHA03095 296 LMVRNNNGRAVR-----AALAKNPSAETV----AATLNTASVAG 330
PHA02878 PHA02878
ankyrin repeat protein; Provisional
24-105 8.84e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939  Cd Length: 477  Bit Score: 38.32  E-value: 8.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304383   24 ELNAPDED-GMTPTLWAAYHGNLESLRLIVSRGGDPDKCDIWGNTPLHLAASNGHLHCLSFLVSFGANIWCLDNDYHTPL 102
Cdd:PHA02878 159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                 ...
gi 34304383  103 DMA 105
Cdd:PHA02878 239 HIS 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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