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Conserved domains on  [gi|1907161031|ref|XP_036020774|]
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mismatch repair endonuclease PMS2 isoform X1 [Mus musculus]

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];
86-336 1.75e-43

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 158.97  E-value: 1.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031  86 YEGEKVRGLYEGEGFAVFQGGNTYHGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVYTWPDGSTYEGEVTNGMRN 165
Cdd:COG4642    81 GGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPH 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 166 GFGMFkcgTQP--VSYIGHWCHGKRHGKGSIYYnqegtswyegdwvynikkgwgircyKSGNIYEGQWENNMRHGEGRMR 243
Cdd:COG4642   161 GQGTL---TYAdgDRYEGEFKNGKRHGQGTLTY-------------------------ANGDVYEGEFKNGQRHGQGTYT 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 244 WlttneeytghwekgiQNGFgthtwflkripnsqyplrnEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMT 323
Cdd:COG4642   213 Y---------------ADGD-------------------RYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMT 258

                         250
                  ....*....|...
gi 1907161031 324 FKNGHVYEGLFSN 336
Cdd:COG4642   259 YADGSVYEGEWKN 271
vATP-synt_E super family cl23750
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ...
 782-829 9.31e-04

ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.


The actual alignment was detected with superfamily member pfam01991:

Pssm-ID: 419987 [Multi-domain]  Cd Length: 199  Bit Score: 41.21  E-value: 9.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161031 782 AYKREEMLKEKVKENQLQEAELAQQRQIENEELEARLNIL--REE-------EARKQ 829
Cdd:pfam01991  28 LVQEAEEKIDEIYEKKEKQAEMQKKIIISNAKNEARLKVLeaREEildevfnEAEKK 84
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
86-336 1.75e-43

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 158.97  E-value: 1.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031  86 YEGEKVRGLYEGEGFAVFQGGNTYHGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVYTWPDGSTYEGEVTNGMRN 165
Cdd:COG4642    81 GGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPH 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 166 GFGMFkcgTQP--VSYIGHWCHGKRHGKGSIYYnqegtswyegdwvynikkgwgircyKSGNIYEGQWENNMRHGEGRMR 243
Cdd:COG4642   161 GQGTL---TYAdgDRYEGEFKNGKRHGQGTLTY-------------------------ANGDVYEGEFKNGQRHGQGTYT 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 244 WlttneeytghwekgiQNGFgthtwflkripnsqyplrnEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMT 323
Cdd:COG4642   213 Y---------------ADGD-------------------RYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMT 258

                         250
                  ....*....|...
gi 1907161031 324 FKNGHVYEGLFSN 336
Cdd:COG4642   259 YADGSVYEGEWKN 271
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 106-405 1.42e-28

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 123.02  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 106 GNTYHGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVYTWPDGSTYEGEVTNGMRNGFGMFkCGTQPVSYIGHWCH 185
Cdd:PLN03185    8 GDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTY-TGTDGTTYKGRWRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 186 GKRHGKGsiYYNQEGTSWYEGDWVYNIKKGWGIRCYKSGNIYEGQWENNMRHGEGRMRWlTTNEEYTGHWEKGIQNGFGT 265
Cdd:PLN03185   87 NLKHGLG--YQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTW-VSGDSYEGQWLDGMMHGFGV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 266 HTWflkriPNSQYplrneYIGEFVNGFRHGQGKFYYA-SGAMYEGEWASNKKQGRGRM--TFKNGHVYEGLFSNDHIAQF 342
Cdd:PLN03185  164 YTW-----SDGGC-----YVGTWTRGLKDGKGVFYPAgSRVPAVQEFYLNALRKRGVLpdLRRQNQVLSSHNSEQLSRGV 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907161031 343 fetemdysqSLDRWSDASQRS-RQPRGSSVSAVREpetlRKLDGSESRsVLGTSIELDLTLLLD 405
Cdd:PLN03185  234 ---------SSDKLSKGSLLPlEQSRNRNVSLERR----WSLEVSIEK-VIGHDYSGSSSAVLD 283
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
225-244 5.12e-05

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 40.79  E-value: 5.12e-05
                           10        20
                   ....*....|....*....|
gi 1907161031  225 NIYEGQWENNMRHGEGRMRW 244
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTY 20
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 284-306 6.81e-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: 40.47  E-value: 6.81e-05
                          10        20
                  ....*....|....*....|...
gi 1907161031 284 YIGEFVNGFRHGQGKFYYASGAM 306
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
vATP-synt_E pfam01991
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ...
 782-829 9.31e-04

ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.


Pssm-ID: 396537 [Multi-domain]  Cd Length: 199  Bit Score: 41.21  E-value: 9.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161031 782 AYKREEMLKEKVKENQLQEAELAQQRQIENEELEARLNIL--REE-------EARKQ 829
Cdd:pfam01991  28 LVQEAEEKIDEIYEKKEKQAEMQKKIIISNAKNEARLKVLeaREEildevfnEAEKK 84
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 784-824 6.12e-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: 36.77  E-value: 6.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907161031 784 KREEMLKEKVKENQLQEAELaQQRQIENEELEARLNILREE 824
Cdd:cd22887    29 DLEEELKEKNKANEILNDEL-IALQIENNLLEEKLRKLQEE 68
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
86-336 1.75e-43

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 158.97  E-value: 1.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031  86 YEGEKVRGLYEGEGFAVFQGGNTYHGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVYTWPDGSTYEGEVTNGMRN 165
Cdd:COG4642    81 GGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPH 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 166 GFGMFkcgTQP--VSYIGHWCHGKRHGKGSIYYnqegtswyegdwvynikkgwgircyKSGNIYEGQWENNMRHGEGRMR 243
Cdd:COG4642   161 GQGTL---TYAdgDRYEGEFKNGKRHGQGTLTY-------------------------ANGDVYEGEFKNGQRHGQGTYT 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 244 WlttneeytghwekgiQNGFgthtwflkripnsqyplrnEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMT 323
Cdd:COG4642   213 Y---------------ADGD-------------------RYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMT 258

                         250
                  ....*....|...
gi 1907161031 324 FKNGHVYEGLFSN 336
Cdd:COG4642   259 YADGSVYEGEWKN 271
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
64-339 5.21e-39

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 146.25  E-value: 5.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031  64 MEQSEEETQYEEPILTKLIVESYEGEKVRGLYEGEGFAVFQGGNTYHGMFSEGLMHGQGTYIWADGLKYEGDFVKNiPMN 143
Cdd:COG4642     1 GGSVAEDGAGGGGDATALGGGGEGGLAAAGGEGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEGGVTAAG-GGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 144 HGVYTWPDGSTYEGEVTNGMRNGFGMFKCGTQPVSYIGhwchgkrhgkgsiYYNQEGTSWYEGDWVYNIKKGWGIRCYKS 223
Cdd:COG4642    80 GGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGG-------------VLEGDDGGGYGGGTADGGRGGGGIYTFPN 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 224 GNIYEGQWENNMRHGEGRMRWlTTNEEYTGHWEKGIQNGFGTHTWflkriPNSqyplrNEYIGEFVNGFRHGQGKFYYAS 303
Cdd:COG4642   147 GDVYEGEFKNGKPHGQGTLTY-ADGDRYEGEFKNGKRHGQGTLTY-----ANG-----DVYEGEFKNGQRHGQGTYTYAD 215

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907161031 304 GAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSNDHI 339
Cdd:COG4642   216 GDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKR 251
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
68-233 9.62e-38

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 142.40  E-value: 9.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031  68 EEETQYEEPILTKLIVESYEGEKVRGLYEGEGFAVFQGGNTYHGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVY 147
Cdd:COG4642   109 KGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTL 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 148 TWPDGSTYEGEVTNGMRNGFGMFKC--GTQpvsYIGHWCHGKRHGKGsIYYNQEGTsWYEGDWVYNIKKGWGIRCYKSGN 225
Cdd:COG4642   189 TYANGDVYEGEFKNGQRHGQGTYTYadGDR---YEGEFKNGKRHGQG-TLTYADGD-RYEGEFKNGKRHGQGTMTYADGS 263


                  ....*...
gi 1907161031 226 IYEGQWEN 233
Cdd:COG4642   264 VYEGEWKN 271
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 106-405 1.42e-28

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 123.02  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 106 GNTYHGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVYTWPDGSTYEGEVTNGMRNGFGMFkCGTQPVSYIGHWCH 185
Cdd:PLN03185    8 GDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTY-TGTDGTTYKGRWRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 186 GKRHGKGsiYYNQEGTSWYEGDWVYNIKKGWGIRCYKSGNIYEGQWENNMRHGEGRMRWlTTNEEYTGHWEKGIQNGFGT 265
Cdd:PLN03185   87 NLKHGLG--YQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTW-VSGDSYEGQWLDGMMHGFGV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 266 HTWflkriPNSQYplrneYIGEFVNGFRHGQGKFYYA-SGAMYEGEWASNKKQGRGRM--TFKNGHVYEGLFSNDHIAQF 342
Cdd:PLN03185  164 YTW-----SDGGC-----YVGTWTRGLKDGKGVFYPAgSRVPAVQEFYLNALRKRGVLpdLRRQNQVLSSHNSEQLSRGV 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907161031 343 fetemdysqSLDRWSDASQRS-RQPRGSSVSAVREpetlRKLDGSESRsVLGTSIELDLTLLLD 405
Cdd:PLN03185  234 ---------SSDKLSKGSLLPlEQSRNRNVSLERR----WSLEVSIEK-VIGHDYSGSSSAVLD 283
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 86-296 7.38e-22

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 101.45  E-value: 7.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031  86 YEGEKVRGLYEGEGFAVFQGGNTYHGMFSEGLMHGQGTYIWADGLKYEGDFVKNIPMNHGVYTWPDGSTYEGEVTNGMRN 165
Cdd:PLN03185   34 YEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 166 GFGMFKCGTQPVsYIGHWCHGKRHGKGSIyynqegtSWyegdwvynikkgwgircyKSGNIYEGQWENNMRHGEGRMRWl 245
Cdd:PLN03185  114 GPGKYTWANGNV-YLGDMKGGKMSGKGTL-------TW------------------VSGDSYEGQWLDGMMHGFGVYTW- 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907161031 246 TTNEEYTGHWEKGIQNGFGTHTWFLKRIPNSQYPLRNEYIGEFVNGFRHGQ 296
Cdd:PLN03185  167 SDGGCYVGTWTRGLKDGKGVFYPAGSRVPAVQEFYLNALRKRGVLPDLRRQ 217
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 271-339 4.28e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 57.15  E-value: 4.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161031 271 KRIPNSQYplrneYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSNDHI 339
Cdd:PLN03185    3 LVLSNGDF-----YSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYM 66
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
153-337 1.33e-05

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


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 46.21  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 153 STYEGEVTNGMRNGFGMFKCGTQPVSYIGHWCHGKRHGKGSIYYNQEGTSWYEGDWVYNIKKGWgircYKSGNI-YEGQW 231
Cdd:COG2849    10 SKYLLSLKLKYELGDTLLEKNGYKSGVKEKTEDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTY----YPNGQLkSEGTY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161031 232 ENNMRHGEgrmrwlttneeYTGHWEKGIQngfgthtwflkripnsqyplrnEYIGEFVNGFRHGQGKFYYASGA-MYEGE 310
Cdd:COG2849    86 KNGKLEGE-----------WKEYYENGKL----------------------KSEGNYKNGKLHGEWKEYYENGKlKEEGN 132

                         170       180
                  ....*....|....*....|....*...
gi 1907161031 311 WASNKKQGRGRMTFKNGH-VYEGLFSND 337
Cdd:COG2849   133 YKNGKKDGVWKYYDENGKlVKEEEYKNG 160
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
225-244 5.12e-05

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 40.79  E-value: 5.12e-05
                           10        20
                   ....*....|....*....|
gi 1907161031  225 NIYEGQWENNMRHGEGRMRW 244
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTY 20
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 284-306 6.81e-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: 40.47  E-value: 6.81e-05
                          10        20
                  ....*....|....*....|...
gi 1907161031 284 YIGEFVNGFRHGQGKFYYASGAM 306
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 109-129 1.02e-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: 40.08  E-value: 1.02e-04
                          10        20
                  ....*....|....*....|.
gi 1907161031 109 YHGMFSEGLMHGQGTYIWADG 129
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
107-128 1.45e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 39.63  E-value: 1.45e-04
                           10        20
                   ....*....|....*....|..
gi 1907161031  107 NTYHGMFSEGLMHGQGTYIWAD 128
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
282-302 5.43e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 37.71  E-value: 5.43e-04
                           10        20
                   ....*....|....*....|.
gi 1907161031  282 NEYIGEFVNGFRHGQGKFYYA 302
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYA 21
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 132-154 9.05e-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: 9.05e-04
                          10        20
                  ....*....|....*....|...
gi 1907161031 132 YEGDFVKNIPMNHGVYTWPDGST 154
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
vATP-synt_E pfam01991
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ...
 782-829 9.31e-04

ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.


Pssm-ID: 396537 [Multi-domain]  Cd Length: 199  Bit Score: 41.21  E-value: 9.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161031 782 AYKREEMLKEKVKENQLQEAELAQQRQIENEELEARLNIL--REE-------EARKQ 829
Cdd:pfam01991  28 LVQEAEEKIDEIYEKKEKQAEMQKKIIISNAKNEARLKVLeaREEildevfnEAEKK 84
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 227-244 1.93e-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: 36.23  E-value: 1.93e-03
                          10
                  ....*....|....*...
gi 1907161031 227 YEGQWENNMRHGEGRMRW 244
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTW 18
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
305-326 4.70e-03

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 35.01  E-value: 4.70e-03
                           10        20
                   ....*....|....*....|..
gi 1907161031  305 AMYEGEWASNKKQGRGRMTFKN 326
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 784-824 6.12e-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: 36.77  E-value: 6.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907161031 784 KREEMLKEKVKENQLQEAELaQQRQIENEELEARLNILREE 824
Cdd:cd22887    29 DLEEELKEKNKANEILNDEL-IALQIENNLLEEKLRKLQEE 68
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 307-329 8.48e-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: 34.31  E-value: 8.48e-03
                          10        20
                  ....*....|....*....|...
gi 1907161031 307 YEGEWASNKKQGRGRMTFKNGHV 329
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
 
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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