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Conserved domains on  [gi|701341527|ref|XP_009981804|]
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PREDICTED: LOW QUALITY PROTEIN: liprin-alpha-4-like [Tauraco erythrolophus]

Protein Classification

SAM_liprin-alpha1,2,3,4_repeat2 and SAM_liprin-alpha1,2,3,4_repeat3 domain-containing protein( domain architecture ID 10175974)

protein containing domains SAM_liprin-alpha1,2,3,4_repeat1, SAM_liprin-alpha1,2,3,4_repeat2, and SAM_liprin-alpha1,2,3,4_repeat3

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 614-685 1.06e-45

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 157.48  E-value: 1.06e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701341527 614 DVLVWTNDQVIHWIQSIGLREYANNLVESGVHGALLALDENFDHNSLALVLQIPTQNTQARQVLEREFNNLL 685
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 529-594 5.03e-45

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188964  Cd Length: 66  Bit Score: 155.32  E-value: 5.03e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701341527 529 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 594
Cdd:cd09565    1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 414-482 1.76e-39

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188961  Cd Length: 71  Bit Score: 140.01  E-value: 1.76e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701341527 414 FAHWDGPTVVSWLELWVGMPAWF--ACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 482
Cdd:cd09562    1 FALWNGPTVVAWLELWVGMPAWYvaACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 614-685 1.06e-45

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 157.48  E-value: 1.06e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701341527 614 DVLVWTNDQVIHWIQSIGLREYANNLVESGVHGALLALDENFDHNSLALVLQIPTQNTQARQVLEREFNNLL 685
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 529-594 5.03e-45

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 155.32  E-value: 5.03e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701341527 529 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 594
Cdd:cd09565    1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 414-482 1.76e-39

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 140.01  E-value: 1.76e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701341527 414 FAHWDGPTVVSWLELWVGMPAWF--ACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 482
Cdd:cd09562    1 FALWNGPTVVAWLELWVGMPAWYvaACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 528-592 5.99e-15

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: 69.99  E-value: 5.99e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701341527  528 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 592
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 537-592 8.02e-09

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: 52.68  E-value: 8.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 701341527   537 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 592
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 615-686 1.09e-08

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: 52.30  E-value: 1.09e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701341527   615 VLVWTNDQVIHWIQSIGLREYANNLVESGVHGALLALdenfdHNSLALVLQIPTQNTQARQVLEREFNNLLA 686
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLL-----LTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
615-685 3.11e-08

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 50.73  E-value: 3.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701341527  615 VLVWTNDQVIHWIQSIGLREYANNLVESGVHGALLALdeNFDHNSLAlvlQIPTQNTQARQVLEREFNNLL 685
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 414-478 7.25e-08

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: 49.99  E-value: 7.25e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701341527   414 FAHWDGPTVVSWLELWvGMPAWF-ACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 478
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYAdNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 416-478 7.10e-03

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: 35.71  E-value: 7.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701341527  416 HWDGPTVVSWLElWVGMPAW---FacRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 478
Cdd:pfam00536   2 GWSVEDVGEWLE-SIGLGQYidsF--RAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 614-685 1.06e-45

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 157.48  E-value: 1.06e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701341527 614 DVLVWTNDQVIHWIQSIGLREYANNLVESGVHGALLALDENFDHNSLALVLQIPTQNTQARQVLEREFNNLL 685
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 529-594 5.03e-45

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 155.32  E-value: 5.03e-45
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701341527 529 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRL 594
Cdd:cd09565    1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 414-482 1.76e-39

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 140.01  E-value: 1.76e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701341527 414 FAHWDGPTVVSWLELWVGMPAWF--ACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLT 482
Cdd:cd09562    1 FALWNGPTVVAWLELWVGMPAWYvaACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 533-592 6.02e-32

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188894  Cd Length: 60  Bit Score: 118.02  E-value: 6.02e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 701341527 533 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 592
Cdd:cd09495    1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 622-683 1.36e-30

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188895  Cd Length: 62  Bit Score: 114.17  E-value: 1.36e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701341527 622 QVIHWIQSIGLREYANNLVESGVHGALLALDENFDHNSLALVLQIPTQNTQARQVLEREFNN 683
Cdd:cd09496    1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 421-477 4.30e-23

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188893  Cd Length: 58  Bit Score: 92.67  E-value: 4.30e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 701341527 421 TVVSWLELWVGMPAWFA-CRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 477
Cdd:cd09494    1 RVCAWLEDFGLMPMYVIfCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 614-685 1.39e-21

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188969  Cd Length: 72  Bit Score: 89.04  E-value: 1.39e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701341527 614 DVLVWTNDQVIHWIQSIGLREYANNLVESGVHGALLALDENFDHNSLALVLQIPTQNTQARQVLEREFNNLL 685
Cdd:cd09570    1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 614-685 1.74e-17

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188968  Cd Length: 72  Bit Score: 77.50  E-value: 1.74e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701341527 614 DVLVWTNDQVIHWIQSIGLREYANNLVESGVHGALLALDENFDHNSLALVLQIPTQNTQARQVLEREFNNLL 685
Cdd:cd09569    1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 528-592 2.11e-17

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 76.68  E-value: 2.11e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701341527 528 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 592
Cdd:cd09567    1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 528-592 8.23e-17

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 75.04  E-value: 8.23e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701341527 528 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrVHLKMVDSFHRTSLQYGIMCLK 592
Cdd:cd09566    1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDL-LHLKVTSALHHASIRRGIQVLR 63
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 415-477 2.53e-15

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 70.94  E-value: 2.53e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701341527 415 AHWDGPTVVSWLELWVGMPAWF-ACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQE 477
Cdd:cd09564    2 SRWKADMVLAWLEVVMHMPMYSkACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 528-592 5.99e-15

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: 69.99  E-value: 5.99e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701341527  528 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 592
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 537-592 8.02e-09

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: 52.68  E-value: 8.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 701341527   537 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLK 592
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 615-686 1.09e-08

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: 52.30  E-value: 1.09e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701341527   615 VLVWTNDQVIHWIQSIGLREYANNLVESGVHGALLALdenfdHNSLALVLQIPTQNTQARQVLEREFNNLLA 686
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLL-----LTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 414-476 1.28e-08

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 51.84  E-value: 1.28e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701341527 414 FAHWDGPTVVSWLElWVGMPAWF-ACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQ 476
Cdd:cd09563    1 FAEWSTEQVCDWLA-ELGLGQYVdECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
615-685 3.11e-08

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 50.73  E-value: 3.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701341527  615 VLVWTNDQVIHWIQSIGLREYANNLVESGVHGALLALdeNFDHNSLAlvlQIPTQNTQARQVLEREFNNLL 685
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 414-478 7.25e-08

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: 49.99  E-value: 7.25e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701341527   414 FAHWDGPTVVSWLELWvGMPAWF-ACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEM 478
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYAdNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 537-588 6.54e-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 [Multi-domain]  Cd Length: 56  Bit Score: 46.85  E-value: 6.54e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 701341527 537 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRvHLKMVDSFHRTSLQYGI 588
Cdd:cd09487    4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 615-654 3.39e-05

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 42.26  E-value: 3.39e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 701341527 615 VLVWTNDQVIHWIQSIGLREYANNLVESGVHG-ALLALDEN 654
Cdd:cd09512    4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS 44
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
537-592 2.63e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 39.56  E-value: 2.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 701341527  537 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLRvHLKMVDSFHRTSLQYGIMCLK 592
Cdd:pfam07647  11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLK-RLGITSVGHRRKILKKIQELK 66
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 537-581 1.98e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 37.28  E-value: 1.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 701341527 537 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHR 581
Cdd:cd09501   11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 618-649 4.32e-03

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 36.54  E-value: 4.32e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 701341527 618 WTNDQVIHW-IQSIGLREYANNLVESGVHGALL 649
Cdd:cd09504    5 WTVEDTVEWlVNSVELPQYVEAFKENGVDGSAL 37
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 416-478 7.10e-03

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: 35.71  E-value: 7.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701341527  416 HWDGPTVVSWLElWVGMPAW---FacRANVKSGAIMSALSDTEIqREIGISNALHRLKLRLAIQEM 478
Cdd:pfam00536   2 GWSVEDVGEWLE-SIGLGQYidsF--RAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
 
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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