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Conserved domains on  [gi|148664246|ref|NP_665872|]
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ankyrin repeat and SAM domain-containing protein 4B [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
 345-410 3.18e-36

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: 127.25  E-value: 3.18e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148664246 345 ATPLEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRRKQVLQQPG 410
Cdd:cd09587    2 ATPLEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQLGPRKKILSAVARRKQVLQQPG 67
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-163 1.38e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   1 MSTRYHQAASDSYLELLKEATKR--DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHA 78
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  79 HCVSFLVNFGANIFALDNDLQTPLDAAASREQNECV-ALLDKAATAqNIMNPKKVTRLKEQAQKNARRQIKECERLQEKH 157
Cdd:COG0666  167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVkLLLEAGADV-NAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245


                 ....*.
gi 148664246 158 QNKMAH 163
Cdd:COG0666  246 NAKDKD 251
CEN_ANKS4B cd21802
central domain found in ankyrin repeat and SAM domain-containing protein 4B; Ankyrin repeat ...
 255-281 2.11e-11

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: 58.67  E-value: 2.11e-11
                         10        20
                 ....*....|....*....|....*..
gi 148664246 255 EEDGSVHHESILNRPGLGSIVFRRNRI 281
Cdd:cd21802    1 EEDGDVQHESIFNRPGLGNIVFRRNRS 27
 
Name Accession Description Interval E-value
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
 345-410 3.18e-36

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: 127.25  E-value: 3.18e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148664246 345 ATPLEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRRKQVLQQPG 410
Cdd:cd09587    2 ATPLEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQLGPRKKILSAVARRKQVLQQPG 67
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-163 1.38e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   1 MSTRYHQAASDSYLELLKEATKR--DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHA 78
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  79 HCVSFLVNFGANIFALDNDLQTPLDAAASREQNECV-ALLDKAATAqNIMNPKKVTRLKEQAQKNARRQIKECERLQEKH 157
Cdd:COG0666  167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVkLLLEAGADV-NAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245


                 ....*.
gi 148664246 158 QNKMAH 163
Cdd:COG0666  246 NAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-121 3.30e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 3.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   38 LAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGAniFALDNDLQTPLDAAASREQNECV-AL 116
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVkLL 80


                  ....*
gi 148664246  117 LDKAA 121
Cdd:pfam12796  81 LEKGA 85
CEN_ANKS4B cd21802
central domain found in ankyrin repeat and SAM domain-containing protein 4B; Ankyrin repeat ...
 255-281 2.11e-11

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: 58.67  E-value: 2.11e-11
                         10        20
                 ....*....|....*....|....*..
gi 148664246 255 EEDGSVHHESILNRPGLGSIVFRRNRI 281
Cdd:cd21802    1 EEDGDVQHESIFNRPGLGNIVFRRNRS 27
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 24-117 7.86e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 7.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  24 DLNLSDEDGMTPTLLA---------AYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFAL 94
Cdd:PTZ00322  65 DHNLTTEEVIDPVVAHmltvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                         90       100
                 ....*....|....*....|...
gi 148664246  95 DNDLQTPLDAAASREQNECVALL 117
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLL 167
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 351-403 9.44e-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: 48.80  E-value: 9.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 148664246  351 FLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQL-GPRKKVLNAINRRK 403
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLlGHRKKILYAIQRLK 64
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 65-93 1.30e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 1.30e-06
                           10        20
                   ....*....|....*....|....*....
gi 148664246    65 GNTPLHFAASNGHAHCVSFLVNFGANIFA 93
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 351-404 7.21e-06

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: 43.44  E-value: 7.21e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148664246   351 FLLSQHLEEFLPIFKREQIDLEALL-LCSDEDLQSIQMQ-LGPRKKVLNAINRRKQ 404
Cdd:smart00454  12 WLESIGLEQYADNFRKNGIDGALLLlLTSEEDLKELGITkLGHRKKILKAIQKLKE 67
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-102 9.64e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 38.07  E-value: 9.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  15 ELLKEATKRDLNLsdedGMTPTLLAAYHGNLEALEIICSRGGD------------PDRCDI--WGNTPLHFAASNGHAHC 80
Cdd:cd22192   76 ELVNEPMTSDLYQ----GETALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyYGEHPLSFAACVGNEEI 151

                         90       100
                 ....*....|....*....|..
gi 148664246  81 VSFLVNFGANIFALDNDLQTPL 102
Cdd:cd22192  152 VRLLIEHGADIRAQDSLGNTVL 173
 
Name Accession Description Interval E-value
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
 345-410 3.18e-36

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: 127.25  E-value: 3.18e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148664246 345 ATPLEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRRKQVLQQPG 410
Cdd:cd09587    2 ATPLEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQLGPRKKILSAVARRKQVLQQPG 67
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 345-409 9.14e-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: 109.73  E-value: 9.14e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148664246 345 ATPLEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRRKQVLQQP 409
Cdd:cd09517    2 TSPLERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPLGPRRKLLNAIAKRKQALENP 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-163 1.38e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   1 MSTRYHQAASDSYLELLKEATKR--DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHA 78
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  79 HCVSFLVNFGANIFALDNDLQTPLDAAASREQNECV-ALLDKAATAqNIMNPKKVTRLKEQAQKNARRQIKECERLQEKH 157
Cdd:COG0666  167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVkLLLEAGADV-NAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245


                 ....*.
gi 148664246 158 QNKMAH 163
Cdd:COG0666  246 NAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-162 1.22e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   3 TRYHQAASDSYLELLKEATKR--DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHC 80
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLEAgaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  81 VSFLVNFGANIFALDNDLQTPLDAAASREQNECVALLDKAATAQNIMNPKKVTRLKEQAQKNARRQIKECERLQEKHQNK 160
Cdd:COG0666  202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281


                 ..
gi 148664246 161 MA 162
Cdd:COG0666  282 LL 283
SAM_USH1G cd09586
SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) ...
 346-409 1.29e-24

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: 96.01  E-value: 1.29e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148664246 346 TPLEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRRKQVLQQP 409
Cdd:cd09586    3 SPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-135 9.40e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 9.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   4 RYHQAASDSYLELLKEATKRDLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSF 83
Cdd:COG0666   59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148664246  84 LVNFGANIFALDNDLQTPLDAAASREQNECV-ALLDKAATAqNIMNPKKVTRL 135
Cdd:COG0666  139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVkLLLEAGADV-NARDNDGETPL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
38-121 3.30e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 3.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   38 LAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGAniFALDNDLQTPLDAAASREQNECV-AL 116
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVkLL 80


                  ....*
gi 148664246  117 LDKAA 121
Cdd:pfam12796  81 LEKGA 85
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-131 3.65e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 3.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   6 HQAASDSYLELLKEATKR--DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSF 83
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAgaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 148664246  84 LVNFGANIFALDNDLQTPLDAAASREQNECVALLDKAATAQNIMNPKK 131
Cdd:COG0666  238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
6-95 2.57e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246    6 HQAASDSYLELLKEATKR--DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGgDPDRCDIwGNTPLHFAASNGHAHCVSF 83
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENgaDANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 148664246   84 LVNFGANIFALD 95
Cdd:pfam12796  80 LLEKGADINVKD 91
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
 357-405 8.60e-14

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: 65.93  E-value: 8.60e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 148664246 357 LEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRRKQV 405
Cdd:cd09585   21 LSEYCDVFEKEKIDLEALALCQERDLKDLGIPLGPRKKILNYIRRRFLL 69
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
 348-403 1.54e-12

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: 62.43  E-value: 1.54e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148664246 348 LEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRRK 403
Cdd:cd09516   12 LEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPMGPRKKLLGFLKDQK 67
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-117 8.49e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 8.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   8 AASDSYLELLKEATKRDLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNF 87
Cdd:COG0666   30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109

                         90       100       110
                 ....*....|....*....|....*....|
gi 148664246  88 GANIFALDNDLQTPLDAAASREQNECVALL 117
Cdd:COG0666  110 GADVNARDKDGETPLHLAAYNGNLEIVKLL 139
CEN_ANKS4B cd21802
central domain found in ankyrin repeat and SAM domain-containing protein 4B; Ankyrin repeat ...
 255-281 2.11e-11

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: 58.67  E-value: 2.11e-11
                         10        20
                 ....*....|....*....|....*..
gi 148664246 255 EEDGSVHHESILNRPGLGSIVFRRNRI 281
Cdd:cd21802    1 EEDGDVQHESIFNRPGLGNIVFRRNRS 27
Ank_4 pfam13637
Ankyrin repeats (many copies);
32-85 6.01e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 6.01e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 148664246   32 GMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLV 85
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 24-117 7.86e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 7.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  24 DLNLSDEDGMTPTLLA---------AYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFAL 94
Cdd:PTZ00322  65 DHNLTTEEVIDPVVAHmltvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                         90       100
                 ....*....|....*....|...
gi 148664246  95 DNDLQTPLDAAASREQNECVALL 117
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLL 167
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 351-401 6.76e-09

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: 51.47  E-value: 6.76e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148664246 351 FLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQ-LGPRKKVLNAINR 401
Cdd:cd09487    5 WLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITsPGHRKKILRAIQR 56
SAM_sec23ip cd09584
SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) ...
 357-402 8.09e-09

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: 51.74  E-value: 8.09e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148664246 357 LEEFLPIFKREQIDLEALLLCSDEDLQSIQMQLGPRKKVLNAINRR 402
Cdd:cd09584   21 LSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPLGPRKKIANFVKEK 66
Ank_4 pfam13637
Ankyrin repeats (many copies);
65-117 8.94e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 8.94e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 148664246   65 GNTPLHFAASNGHAHCVSFLVNFGANIFALDNDLQTPLDAAASREQNECVALL 117
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-117 2.03e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 2.03e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 148664246   69 LHFAASNGHAHCVSFLVNFGANIFALDNDLQTPLDAAASREQNECVALL 117
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
Ank_5 pfam13857
Ankyrin repeats (many copies);
57-105 7.06e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 7.06e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 148664246   57 DPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFALDNDLQTPLDAA 105
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 351-403 9.44e-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: 48.80  E-value: 9.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 148664246  351 FLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQL-GPRKKVLNAINRRK 403
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLlGHRKKILYAIQRLK 64
CEN_USH1G_ANKS4B cd21764
central domain found in usher syndrome type-1G protein, ankyrin repeat and SAM ...
 255-286 1.64e-07

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: 47.46  E-value: 1.64e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 148664246 255 EEDGSVHHESILNRPGLGSIVFRRNRISSPED 286
Cdd:cd21764    1 EESTDSGHESIFNRPGLGNIVFRRNLEELPWD 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
17-72 1.96e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 1.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148664246   17 LKEATKRDLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFA 72
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 3-105 3.53e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.89  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   3 TRYHQAASDSYLELLKEATK--RDLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHC 80
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEygADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         90       100
                 ....*....|....*....|....*
gi 148664246  81 VSFLVNFGANIFALDNDLQTPLDAA 105
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNA 230
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 65-96 4.23e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.13  E-value: 4.23e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 148664246   65 GNTPLHFAA-SNGHAHCVSFLVNFGANIFALDN 96
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 15-125 5.81e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 5.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  15 ELLKEATKRDlnlsDEDGMTPTLLA-AYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFA 93
Cdd:PLN03192 511 DLLGDNGGEH----DDPNMASNLLTvASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                         90       100       110
                 ....*....|....*....|....*....|..
gi 148664246  94 LDNDLQTPLDAAASREQNECVALLDKAATAQN 125
Cdd:PLN03192 587 RDANGNTALWNAISAKHHKIFRILYHFASISD 618
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 65-93 1.30e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 1.30e-06
                           10        20
                   ....*....|....*....|....*....
gi 148664246    65 GNTPLHFAASNGHAHCVSFLVNFGANIFA 93
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 24-98 1.46e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 1.46e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148664246  24 DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFALDNDL 98
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETL 258
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-104 2.79e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  24 DLNLSDEDGMTPTLLAAYHGN-LEALEIICSRGGDPDRCDIWGNTPLHFAASNG--HAHCVSFLVNFGANIFALDNDLQT 100
Cdd:PHA03095  75 DVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMT 154


                 ....
gi 148664246 101 PLDA 104
Cdd:PHA03095 155 PLAV 158
Ank_4 pfam13637
Ankyrin repeats (many copies);
1-49 3.79e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 3.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 148664246    1 MSTRYHQAASDSYLELLKE--ATKRDLNLSDEDGMTPTLLAAYHGNLEALE 49
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLllEKGADINAVDGNGETALHFAASNGNVEVLK 51
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-102 3.80e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.41  E-value: 3.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   6 HQAASDSYLELLKE--ATKRDLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSF 83
Cdd:COG0666  191 HLAAENGHLEIVKLllEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                         90
                 ....*....|....*....
gi 148664246  84 LVNFGANIFALDNDLQTPL 102
Cdd:COG0666  271 LLLALLLLAAALLDLLTLL 289
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 348-401 4.50e-06

SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. SAM is a widespread domain in signaling proteins. In many cases it mediates homo-dimerization/oligomerization.


Pssm-ID: 188918  Cd Length: 64  Bit Score: 44.02  E-value: 4.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148664246 348 LEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQMQL-GPRKKVLNAINR 401
Cdd:cd09519    7 LSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLfGPKRKMTSAIAR 61
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 351-404 7.21e-06

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: 43.44  E-value: 7.21e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 148664246   351 FLLSQHLEEFLPIFKREQIDLEALL-LCSDEDLQSIQMQ-LGPRKKVLNAINRRKQ 404
Cdd:smart00454  12 WLESIGLEQYADNFRKNGIDGALLLlLTSEEDLKELGITkLGHRKKILKAIQKLKE 67
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-142 7.77e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 7.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  30 EDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFALDNDLQTPLDAAASRE 109
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90       100       110
                 ....*....|....*....|....*....|....
gi 148664246 110 QNE-CVALLDKAATAQNIMNPKKVTRLKEQAQKN 142
Cdd:PHA02875 180 DIAiCKMLLDSGANIDYFGKNGCVAALCYAIENN 213
CEN_USH1G cd21803
central domain found in usher syndrome type-1G protein; Usher syndrome type-1G protein (USH1G), ...
 262-283 3.41e-05

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: 41.37  E-value: 3.41e-05
                         10        20
                 ....*....|....*....|..
gi 148664246 262 HESILNRPGLGSIVFRRNRISS 283
Cdd:cd21803    8 HDSLFNRPGLGTMVFRRNYVSS 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 5-121 4.93e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   5 YHQAASDSYLELLKEATKR--DLNLSDEDGMTPTLLAAYHG-NLEALEIICSRGGDPDRCDIWGNTPLHFAAS-NGHAHC 80
Cdd:PHA02876 278 HHASQAPSLSRLVPKLLERgaDVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDI 357

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148664246  81 VSFLVNFGANIFALDNDLQTPLDAAASREQNECV-ALLDKAA 121
Cdd:PHA02876 358 VITLLELGANVNARDYCDKTPIHYAAVRNNVVIInTLLDYGA 399
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 65-91 5.24e-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: 39.93  E-value: 5.24e-05
                          10        20
                  ....*....|....*....|....*..
gi 148664246   65 GNTPLHFAASNGHAHCVSFLVNFGANI 91
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 13-129 5.74e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 5.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  13 YLELLKEATKR--DLNLSDEDGMTptLLAAY----HGNLEALEIICSRGGDPDRC----------------DIWGNTPLH 70
Cdd:PHA03100 120 SYSIVEYLLDNgaNVNIKNSDGEN--LLHLYlesnKIDLKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLH 197

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148664246  71 FAASNGHAHCVSFLVNFGANIFALDNDLQTPLDAAASREQNECVALLDKAATAQNIMNP 129
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
SAM_Scm-like-3MBT3,4 cd09582
SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of ...
 358-399 6.21e-05

SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-3MBT3,4 (Sex comb on midleg, Malignant brain tumor) subfamily proteins (also known as L3mbtl3,4 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are predicted transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain three MBT repeats and Zn finger domain. Murine L3mbtl3 protein of this subfamily is essential for maturation of myeloid progenitor cells during differentiation. Human L3mbtl4 is a potential tumor suppressor gene in breast cancer, while deregulation of L3MBTL3 is associated with neuroblastoma.


Pssm-ID: 188981  Cd Length: 66  Bit Score: 40.72  E-value: 6.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 148664246 358 EEFLPIFKREQIDLEALLLCSDEDLQSI-QMQLGPRKKVLNAI 399
Cdd:cd09582   20 EEHAKVFRDEQIDGEAFLLLTQSDLVKIlGIKLGPALKIYNSI 62
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 357-401 6.78e-05

SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein.


Pssm-ID: 188917  Cd Length: 65  Bit Score: 40.63  E-value: 6.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148664246 357 LEEFLPIFKREQIDLEALLLCSDEDLQSIQM-QLGPRKKVLNAINR 401
Cdd:cd09518   17 LEKYQPIFEEQEVDMEAFLTLTDGDLKELGIkTDGPRQQILAAISE 62
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 16-107 1.28e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  16 LLKEATKRDLNLSDEDGMTPTLLAAYHG---NLEALEIICSRGGDPDRCDIWGNTPLHFAASN--GHAHCVSFLVNFGAN 90
Cdd:PHA03100  54 LLDNGADINSSTKNNSTPLHYLSNIKYNltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGAN 133

                         90
                 ....*....|....*..
gi 148664246  91 IFALDNDLQTPLDAAAS 107
Cdd:PHA03100 134 VNIKNSDGENLLHLYLE 150
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-128 1.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  24 DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFALDNDLQTPLD 103
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                         90       100
                 ....*....|....*....|....*
gi 148664246 104 AAASREQNECVALLdkAATAQNIMN 128
Cdd:PHA02874 196 NAAEYGDYACIKLL--IDHGNHIMN 218
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 38-217 2.46e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  38 LAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFALDNDlqtplDAAASREQNEcvaLL 117
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD-----DDFSPTELRE---LL 699

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246 118 DKAATAQNIMNPKKVTRLKEQAqknARRQIKECERLQEKHQNkmahtysKEESGTLSSSKG-TFSRSSPSNASA------ 190
Cdd:PLN03192 700 QKRELGHSITIVDSVPADEPDL---GRDGGSRPGRLQGTSSD-------NQCRPRVSIYKGhPLLRNERCCNEAgklinl 769

                        170       180       190
                 ....*....|....*....|....*....|.
gi 148664246 191 PGTFGSLSKGIKDTFKIKFKK----NKDTAE 217
Cdd:PLN03192 770 PPSLEELKAIAGEKLGFDARKamvtNEEGAE 800
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-118 3.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  10 SDSYLELLKEATKRDlnlsdedgmtptllaayhgNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGA 89
Cdd:PHA02876 142 SIEYMKLIKERIQQD-------------------ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA 202

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148664246  90 --NIFALDnDLQTPLDAAASREQNECVALLD 118
Cdd:PHA02876 203 dvNIIALD-DLSVLECAVDSKNIDTIKAIID 232
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-142 4.36e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.86  E-value: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  14 LELLKEATKRDLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFA 93
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 148664246  94 LDNDLQTPLDAAASREQNECVALLDKAATAQNIMNPKKVTRLKEQAQKN 142
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 348-399 5.41e-04

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 38.04  E-value: 5.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148664246 348 LEVFLLSQHLEEFLPIFKREQIDLEALLLCSDEDLQSIQM-QLGPRKKVLNAI 399
Cdd:cd09521    8 LELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGItQPGDQKKILDAI 60
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-103 6.19e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 6.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  24 DLNLSDEDGMTPtlLAAYHGNLEA----LEIICSRGGDPDRCDIWGNTPLHFAASNGHA--HCVSFLVNFGANIFALDND 97
Cdd:PHA03095 109 DVNAKDKVGRTP--LHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDR 186


                 ....*.
gi 148664246  98 LQTPLD 103
Cdd:PHA03095 187 FRSLLH 192
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 357-399 6.64e-04

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: 37.66  E-value: 6.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 148664246 357 LEEFLPIFKREQIDLEALLLCSDEDLQSIQMQ-LGPRKKVLNAI 399
Cdd:cd09520   16 LEKYIDLFAQQEIDLQTFLTLTDQDLKELGITaFGARRKMLLAI 59
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 24-108 7.41e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  24 DLNLSDED-GMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFALDNDLQTPL 102
Cdd:PHA02878 159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238


                 ....*.
gi 148664246 103 DAAASR 108
Cdd:PHA02878 239 HISVGY 244
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
 351-401 8.07e-04

SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy.


Pssm-ID: 188908  Cd Length: 64  Bit Score: 37.46  E-value: 8.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148664246 351 FLLS-QHLEEFLPIFKREQIDLEALLLCSDEDLQSI-QMQLGPRKKVLNAINR 401
Cdd:cd09509   12 FIKSlDGCAEYAEVFREQEIDGQALLLLTEDDLLKGmGLKLGPALKIYNHIVK 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 24-95 1.34e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148664246  24 DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHCVSFLVNFGANIFALD 95
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-128 1.65e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 1.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148664246  65 GNTPLHFAASNGHAHCVSFLVNFGANIFALDNDLQTPLDAAASREQNECVALLDKAATAQNIMN 128
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 358-403 1.99e-03

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.


Pssm-ID: 188922  Cd Length: 65  Bit Score: 36.50  E-value: 1.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 148664246 358 EEFLPIFKREQIDLEALLLCSDEDLQSIQM-QLGPRKKVLNAINRRK 403
Cdd:cd09523   18 EHYLPVFARHRITMETLSTMTDEDLKKIGIhEIGLRKEILRAAQELL 64
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 3-127 2.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   3 TRYHQAASDSYLELLKEATKR--DLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHAHC 80
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARgaDPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 148664246  81 VSFLVNFGANI-FALDNDLQTPLDAAASREQNECVALLDKAATAQNIM 127
Cdd:PHA02875 184 CKMLLDSGANIdYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIM 231
SAM_Ph1,2,3 cd09577
SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain ...
 354-404 2.91e-03

SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome.


Pssm-ID: 188976  Cd Length: 69  Bit Score: 36.23  E-value: 2.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148664246 354 SQHLEEFlpifKREQIDLEALLLCSDEDLQS-IQMQLGPRKKVLNAINRRKQ 404
Cdd:cd09577   22 SDYAEEF----RAQEIDGQALLLLKEDHLMSaMNIKLGPALKICAKINSLKE 69
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 27-167 4.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.81  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  27 LSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRcdiWGN----TPLHFAASNGHAHCVSFLVNFGANIFALDNDLQTPL 102
Cdd:PHA02884  65 LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNR---YAEeakiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPI 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148664246 103 DaAASREQNECVALLDKAATAQNIM-NPKKVTRLKEQAQKNARRQIKEC--ERLQEKHQNKMAHTYSK 167
Cdd:PHA02884 142 E-LALMICNNFLAFMICDNEISNFYkHPKKILINFDILKILVSHFILQAsnDRLNEKHNKNFNAGYNK 208
PHA02798 PHA02798
ankyrin-like protein; Provisional
 4-145 6.26e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246   4 RYHQAASDSyLELLKEATKR--DLNLSDEDGMTP--TLLA---AYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNG 76
Cdd:PHA02798  42 KYLQRDSPS-TDIVKLFINLgaNVNGLDNEYSTPlcTILSnikDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNG 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148664246  77 HAH---CVSFLVNFGANIFALDND----LQTPLDAAASREQNECVALLDKAATAQNIMNPKKVTRLKEQAQKNARR 145
Cdd:PHA02798 121 YINnleILLFMIENGADTTLLDKDgftmLQVYLQSNHHIDIEIIKLLLEKGVDINTHNNKEKYDTLHCYFKYNIDR 196
PHA02946 PHA02946
ankyin-like protein; Provisional
 26-91 8.52e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.11  E-value: 8.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148664246  26 NLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDRCDIWGNTPLHFAASNGHA--HCVSFLVNFGANI 91
Cdd:PHA02946  66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKI 133
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-106 9.25e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 9.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  24 DLNLSDEDGMTPtlLAAY----------------HG---------NLEALEIIC--------------SRGGDPDRCDIW 64
Cdd:PHA03095 144 DVNALDLYGMTP--LAVLlksrnanvellrllidAGadvyavddrFRSLLHHHLqsfkprarivreliRAGCDPAATDML 221

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 148664246  65 GNTPLHFAASngHAHC----VSFLVNFGANIFALDNDLQTPLDAAA 106
Cdd:PHA03095 222 GNTPLHSMAT--GSSCkrslVLPLLIAGISINARNRYGQTPLHYAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-102 9.64e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 38.07  E-value: 9.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664246  15 ELLKEATKRDLNLsdedGMTPTLLAAYHGNLEALEIICSRGGD------------PDRCDI--WGNTPLHFAASNGHAHC 80
Cdd:cd22192   76 ELVNEPMTSDLYQ----GETALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyYGEHPLSFAACVGNEEI 151

                         90       100
                 ....*....|....*....|..
gi 148664246  81 VSFLVNFGANIFALDNDLQTPL 102
Cdd:cd22192  152 VRLLIEHGADIRAQDSLGNTVL 173
 
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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