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Conserved domains on  [gi|262205531|ref|NP_001160086|]
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radial spoke head 10 homolog B [Bos taurus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
74-337 1.01e-41

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 153.96  E-value: 1.01e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531  74 YEEPVLTKLIVESYEGEKVRGLYEGEGFAIFQGGCTYQGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVFTWPDG 153
Cdd:COG4642   68 GEGGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNG 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 154 STYEGEVVGGMRHGFGMFkcsTQP--VSYIGHWCHGKRHGKGSIYYnqegtswyegdwihnirkgwgircyKSGNIYEGQ 231
Cdd:COG4642  148 DVYEGEFKNGKPHGQGTL---TYAdgDRYEGEFKNGKRHGQGTLTY-------------------------ANGDVYEGE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 232 WENNVRHGEGRMRWlttneeytgqwkhgvQNGlgthtwflkripysqyplrNEYVGEFVNGYRHGHGKFYYASGAMYEGE 311
Cdd:COG4642  200 FKNGQRHGQGTYTY---------------ADG-------------------DRYEGEFKNGKRHGQGTLTYADGDRYEGE 245

                        250       260
                 ....*....|....*....|....*.
gi 262205531 312 WVSNKKHGMGRLTFKNGRVYDGPFSK 337
Cdd:COG4642  246 FKNGKRHGQGTMTYADGSVYEGEWKN 271
Atg16_CCD super family cl46300
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 783-823 2.08e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


The actual alignment was detected with superfamily member cd22887:

Pssm-ID: 480640 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 262205531 783 KHEETLKEKVKEN-RLHNEAMALQrkMENEELEARLNSLREE 823
Cdd:cd22887   29 DLEEELKEKNKANeILNDELIALQ--IENNLLEEKLRKLQEE 68
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
74-337 1.01e-41

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 153.96  E-value: 1.01e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531  74 YEEPVLTKLIVESYEGEKVRGLYEGEGFAIFQGGCTYQGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVFTWPDG 153
Cdd:COG4642   68 GEGGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNG 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 154 STYEGEVVGGMRHGFGMFkcsTQP--VSYIGHWCHGKRHGKGSIYYnqegtswyegdwihnirkgwgircyKSGNIYEGQ 231
Cdd:COG4642  148 DVYEGEFKNGKPHGQGTL---TYAdgDRYEGEFKNGKRHGQGTLTY-------------------------ANGDVYEGE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 232 WENNVRHGEGRMRWlttneeytgqwkhgvQNGlgthtwflkripysqyplrNEYVGEFVNGYRHGHGKFYYASGAMYEGE 311
Cdd:COG4642  200 FKNGQRHGQGTYTY---------------ADG-------------------DRYEGEFKNGKRHGQGTLTYADGDRYEGE 245

                        250       260
                 ....*....|....*....|....*.
gi 262205531 312 WVSNKKHGMGRLTFKNGRVYDGPFSK 337
Cdd:COG4642  246 FKNGKRHGQGTMTYADGSVYEGEWKN 271
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 107-321 1.17e-30

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 129.57  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 107 GCTYQGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVFTWPDGSTYEGEVVGGMRHGFGmfkcstqpvSYIGhwch 186
Cdd:PLN03185   8 GDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSG---------TYTG---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 187 gkrhgkgsiyynqEGTSWYEGDWIHNIRKGWGIRCYKSGNIYEGQWENNVRHGEGRMRWLTTNeEYTGQWKHGVQNGLGT 266
Cdd:PLN03185  75 -------------TDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGN-VYLGDMKGGKMSGKGT 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 262205531 267 HTWFLKripysqyplrNEYVGEFVNGYRHGHGKFYYASGAMYEGEWVSNKKHGMG 321
Cdd:PLN03185 141 LTWVSG----------DSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKG 185
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 110-130 3.25e-05

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 41.24  E-value: 3.25e-05
                          10        20
                  ....*....|....*....|.
gi 262205531  110 YQGMFSEGLMHGQGTYIWADG 130
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
108-129 9.00e-05

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 40.02  E-value: 9.00e-05
                           10        20
                   ....*....|....*....|..
gi 262205531   108 CTYQGMFSEGLMHGQGTYIWAD 129
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 783-823 2.08e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 262205531 783 KHEETLKEKVKEN-RLHNEAMALQrkMENEELEARLNSLREE 823
Cdd:cd22887   29 DLEEELKEKNKANeILNDELIALQ--IENNLLEEKLRKLQEE 68
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
74-337 1.01e-41

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 153.96  E-value: 1.01e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531  74 YEEPVLTKLIVESYEGEKVRGLYEGEGFAIFQGGCTYQGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVFTWPDG 153
Cdd:COG4642   68 GEGGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNG 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 154 STYEGEVVGGMRHGFGMFkcsTQP--VSYIGHWCHGKRHGKGSIYYnqegtswyegdwihnirkgwgircyKSGNIYEGQ 231
Cdd:COG4642  148 DVYEGEFKNGKPHGQGTL---TYAdgDRYEGEFKNGKRHGQGTLTY-------------------------ANGDVYEGE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 232 WENNVRHGEGRMRWlttneeytgqwkhgvQNGlgthtwflkripysqyplrNEYVGEFVNGYRHGHGKFYYASGAMYEGE 311
Cdd:COG4642  200 FKNGQRHGQGTYTY---------------ADG-------------------DRYEGEFKNGKRHGQGTLTYADGDRYEGE 245

                        250       260
                 ....*....|....*....|....*.
gi 262205531 312 WVSNKKHGMGRLTFKNGRVYDGPFSK 337
Cdd:COG4642  246 FKNGKRHGQGTMTYADGSVYEGEWKN 271
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
71-355 2.11e-39

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 147.41  E-value: 2.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531  71 TTQYEEPVLTKLIVESYEGEKVRGLYEGEGFAIFQGGCTYQGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVFTW 150
Cdd:COG4642    7 DGAGGGGDATALGGGGEGGLAAAGGEGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEGGVTAAGGGGGGGGGKG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 151 PDGSTYEGEVVGGMRHGFGmFKCSTQPVSYIGhwchgkrhgkgsiYYNQEGTSWYEGDWIHNIRKGWGIRCYKSGNIYEG 230
Cdd:COG4642   87 DGGDGGGGEGGFGGGGGGG-GGKKGGGGGGGG-------------VLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 231 QWENNVRHGEGRMRWlTTNEEYTGQWKHGVQNGLGTHTWflkripysqyPLRNEYVGEFVNGYRHGHGKFYYASGAMYEG 310
Cdd:COG4642  153 EFKNGKPHGQGTLTY-ADGDRYEGEFKNGKRHGQGTLTY----------ANGDVYEGEFKNGQRHGQGTYTYADGDRYEG 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 262205531 311 EWVSNKKHGMGRLTFKNGRVYDGPFSKDHmvafpnLEGE-VMSYPD 355
Cdd:COG4642  222 EFKNGKRHGQGTLTYADGDRYEGEFKNGK------RHGQgTMTYAD 261
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 107-321 1.17e-30

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 129.57  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 107 GCTYQGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVFTWPDGSTYEGEVVGGMRHGFGmfkcstqpvSYIGhwch 186
Cdd:PLN03185   8 GDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSG---------TYTG---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 187 gkrhgkgsiyynqEGTSWYEGDWIHNIRKGWGIRCYKSGNIYEGQWENNVRHGEGRMRWLTTNeEYTGQWKHGVQNGLGT 266
Cdd:PLN03185  75 -------------TDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGN-VYLGDMKGGKMSGKGT 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 262205531 267 HTWFLKripysqyplrNEYVGEFVNGYRHGHGKFYYASGAMYEGEWVSNKKHGMG 321
Cdd:PLN03185 141 LTWVSG----------DSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKG 185
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 87-323 4.15e-21

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 99.14  E-value: 4.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531  87 YEGEKVRGLYEGEGFAIFQGGCTYQGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVFTWPDGSTYEGEVVGGMRH 166
Cdd:PLN03185  34 YEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 167 GFGMFKCSTQPVsYIGHWCHGKRHGKGSIyynqegtSWyegdwihnirkgwgircyKSGNIYEGQWENNVRHGEGRMRWl 246
Cdd:PLN03185 114 GPGKYTWANGNV-YLGDMKGGKMSGKGTL-------TW------------------VSGDSYEGQWLDGMMHGFGVYTW- 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 262205531 247 TTNEEYTGQWKHGVQNGLGTHTWFLKRIPYSQYPLRNEYVGEFVNG--YRHGHGKFYYASGAMYEGewVSNKKHGMGRL 323
Cdd:PLN03185 167 SDGGCYVGTWTRGLKDGKGVFYPAGSRVPAVQEFYLNALRKRGVLPdlRRQNQVLSSHNSEQLSRG--VSSDKLSKGSL 243
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 225-333 1.94e-16

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 84.11  E-value: 1.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 225 GNIYEGQWENNVRHGEGRMRWlTTNEEYTGQWKHGVQNGLGTHTWflkripysqyPLRNEYVGEFVNGYRHGHGKFYYAS 304
Cdd:PLN03185   8 GDFYSGSLLGNVPEGPGKYLW-SDGCMYEGEWRRGMRHGNGKISW----------PSGATYEGEFSGGYMHGSGTYTGTD 76

                         90       100
                 ....*....|....*....|....*....
gi 262205531 305 GAMYEGEWVSNKKHGMGRLTFKNGRVYDG 333
Cdd:PLN03185  77 GTTYKGRWRLNLKHGLGYQRYPNGDVFEG 105
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 280-340 3.21e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 57.54  E-value: 3.21e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262205531 280 PLRNEYVGEFVNGYRHGHGKFYYASGAMYEGEWVSNKKHGMGRLTFKNGRVYDGPFSKDHM 340
Cdd:PLN03185   6 SNGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYM 66
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
154-331 2.49e-06

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 48.53  E-value: 2.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 154 STYEGEVVGGMRHGFGMFKCSTQPVSYIGHWCHGKRHGKGSIYYNQEGTSWYEGDWIHNIRKGWgircYKSGNI-YEGQW 232
Cdd:COG2849   10 SKYLLSLKLKYELGDTLLEKNGYKSGVKEKTEDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTY----YPNGQLkSEGTY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 233 ENNVRHGEGRMRWLTtneeytGQWKhgvqnglgthtwflkripysqyplrneYVGEFVNGYRHGHGKFYYASGA-MYEGE 311
Cdd:COG2849   86 KNGKLEGEWKEYYEN------GKLK---------------------------SEGNYKNGKLHGEWKEYYENGKlKEEGN 132

                        170       180
                 ....*....|....*....|
gi 262205531 312 WVSNKKHGMGRLTFKNGRVY 331
Cdd:COG2849  133 YKNGKKDGVWKYYDENGKLV 152
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 110-130 3.25e-05

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 41.24  E-value: 3.25e-05
                          10        20
                  ....*....|....*....|.
gi 262205531  110 YQGMFSEGLMHGQGTYIWADG 130
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
108-129 9.00e-05

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 40.02  E-value: 9.00e-05
                           10        20
                   ....*....|....*....|..
gi 262205531   108 CTYQGMFSEGLMHGQGTYIWAD 129
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 285-307 1.47e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 39.31  E-value: 1.47e-04
                          10        20
                  ....*....|....*....|...
gi 262205531  285 YVGEFVNGYRHGHGKFYYASGAM 307
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
226-245 1.72e-04

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 39.25  E-value: 1.72e-04
                           10        20
                   ....*....|....*....|
gi 262205531   226 NIYEGQWENNVRHGEGRMRW 245
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTY 20
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
306-327 8.41e-04

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 37.32  E-value: 8.41e-04
                           10        20
                   ....*....|....*....|..
gi 262205531   306 AMYEGEWVSNKKHGMGRLTFKN 327
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 308-328 8.58e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 37.39  E-value: 8.58e-04
                          10        20
                  ....*....|....*....|.
gi 262205531  308 YEGEWVSNKKHGMGRLTFKNG 328
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 783-823 2.08e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 262205531 783 KHEETLKEKVKEN-RLHNEAMALQrkMENEELEARLNSLREE 823
Cdd:cd22887   29 DLEEELKEKNKANeILNDELIALQ--IENNLLEEKLRKLQEE 68
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 133-155 2.57e-03

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 35.85  E-value: 2.57e-03
                          10        20
                  ....*....|....*....|...
gi 262205531  133 YEGDFVKNIPMNHGVFTWPDGST 155
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
283-303 3.07e-03

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 35.78  E-value: 3.07e-03
                           10        20
                   ....*....|....*....|.
gi 262205531   283 NEYVGEFVNGYRHGHGKFYYA 303
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYA 21
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 228-245 4.87e-03

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 35.08  E-value: 4.87e-03
                          10
                  ....*....|....*...
gi 262205531  228 YEGQWENNVRHGEGRMRW 245
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTW 18
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
74-238 6.34e-03

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 38.51  E-value: 6.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531  74 YEEPVLTKLIVESYEGEKVRGLYEGEGFAIFQGGCTYQGMFSEGLMHGQGTYIWADG-LKYEGDFVKNIPmnHGVFT--W 150
Cdd:COG2849   21 ELGDTLLEKNGYKSGVKEKTEDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTYYPNGqLKSEGTYKNGKL--EGEWKeyY 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262205531 151 PDGStyegevvggmrhgfgmfkcstqpVSYIGHWCHGKRHGKgSIYYNQEGTSWYEGDWIHNIRKGWGIRCYKSGNI-YE 229
Cdd:COG2849   99 ENGK-----------------------LKSEGNYKNGKLHGE-WKEYYENGKLKEEGNYKNGKKDGVWKYYDENGKLvKE 154


                 ....*....
gi 262205531 230 GQWENNVRH 238
Cdd:COG2849  155 EEYKNGKKV 163
 
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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