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Conserved domains on  [gi|32171186|ref|NP_005736|]
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B-cell receptor-associated protein 31 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-136 4.72e-47

Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This family also contains the Bap29 protein that forms a heterodimer with Bap 31.


:

Pssm-ID: 461673  Cd Length: 137  Bit Score: 152.65  E-value: 4.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186     1 MSLQWTAVATFLYAEVFVVLLLCIPFISPKRwQKIFKSRLVELLVSYGNTFFVVLIVILVLLVIDAVREIRKYDDVTE-- 78
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELEsa 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 32171186    79 KVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAF 136
Cdd:pfam05529  80 KANAHQHPSARMEVQARKFYAQRNLYICGFTLFLSLVLRRTVTLISELATLEAKLEAL 137
Bap31_Bap29_C pfam18035
Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the ...
 193-246 1.23e-11

Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This entry represents the cytoplasmic domain which forms a heterodimeric coiled-coil with Bap29. This Bap29 and Bap31 are homologous to each other and this entry includes both proteins.


:

Pssm-ID: 465623 [Multi-domain]  Cd Length: 52  Bit Score: 58.06  E-value: 1.23e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 32171186   193 DELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQaaVDGPMDKKEE 246
Cdd:pfam18035   1 KEIEKLKKELKKKKSDIEALKKQAEGLQREYDRLSDEHAKLQ--LDEGEDKKDD 52
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 137-238 3.28e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 3.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186 137 KKQAESAsEAAKKYMEENDQLKKGAAVDggKLDVGNAEV-KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQ 215
Cdd:COG1196 206 ERQAEKA-ERYRELKEELKELEAELLLL--KLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282

                        90       100
                ....*....|....*....|...
gi 32171186 216 SEGLTKEYDRLLEEHAKLQAAVD 238
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIA 305
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-136 4.72e-47

Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This family also contains the Bap29 protein that forms a heterodimer with Bap 31.


Pssm-ID: 461673  Cd Length: 137  Bit Score: 152.65  E-value: 4.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186     1 MSLQWTAVATFLYAEVFVVLLLCIPFISPKRwQKIFKSRLVELLVSYGNTFFVVLIVILVLLVIDAVREIRKYDDVTE-- 78
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELEsa 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 32171186    79 KVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAF 136
Cdd:pfam05529  80 KANAHQHPSARMEVQARKFYAQRNLYICGFTLFLSLVLRRTVTLISELATLEAKLEAL 137
Bap31_Bap29_C pfam18035
Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the ...
 193-246 1.23e-11

Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This entry represents the cytoplasmic domain which forms a heterodimeric coiled-coil with Bap29. This Bap29 and Bap31 are homologous to each other and this entry includes both proteins.


Pssm-ID: 465623 [Multi-domain]  Cd Length: 52  Bit Score: 58.06  E-value: 1.23e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 32171186   193 DELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQaaVDGPMDKKEE 246
Cdd:pfam18035   1 KEIEKLKKELKKKKSDIEALKKQAEGLQREYDRLSDEHAKLQ--LDEGEDKKDD 52
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-239 1.80e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186  121 TLISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAE---VKLEEENRSLKA---DLQKLKDE 194
Cdd:COG4913  614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiAELEAELERLDAssdDLAALEEQ 693

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 32171186  195 LASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVDG 239
Cdd:COG4913  694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 122-236 2.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186    122 LISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVK-LEEENRSLKADLQKLKDELASTKQ 200
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRLEELEEQLETLRSKVAQLEL 393

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 32171186    201 KLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAA 236
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 137-238 3.28e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 3.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186 137 KKQAESAsEAAKKYMEENDQLKKGAAVDggKLDVGNAEV-KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQ 215
Cdd:COG1196 206 ERQAEKA-ERYRELKEELKELEAELLLL--KLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282

                        90       100
                ....*....|....*....|...
gi 32171186 216 SEGLTKEYDRLLEEHAKLQAAVD 238
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIA 305
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
134-229 6.78e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.33  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186  134 EAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVK--------LEEENRSLKA----------DLQKLKDEL 195
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrreeieeLEEEIEELRErfgdapvdlgNAEDFLEEL 417

                         90       100       110
                 ....*....|....*....|....*....|....
gi 32171186  196 ASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEE 229
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEA 451
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 187-238 7.21e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.12  E-value: 7.21e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 32171186 187 DLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVD 238
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID 68
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 176-238 9.30e-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: 34.46  E-value: 9.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32171186 176 KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVD 238
Cdd:cd22887   1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLR 63
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-136 4.72e-47

Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This family also contains the Bap29 protein that forms a heterodimer with Bap 31.


Pssm-ID: 461673  Cd Length: 137  Bit Score: 152.65  E-value: 4.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186     1 MSLQWTAVATFLYAEVFVVLLLCIPFISPKRwQKIFKSRLVELLVSYGNTFFVVLIVILVLLVIDAVREIRKYDDVTE-- 78
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELEsa 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 32171186    79 KVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAF 136
Cdd:pfam05529  80 KANAHQHPSARMEVQARKFYAQRNLYICGFTLFLSLVLRRTVTLISELATLEAKLEAL 137
Bap31_Bap29_C pfam18035
Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the ...
 193-246 1.23e-11

Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This entry represents the cytoplasmic domain which forms a heterodimeric coiled-coil with Bap29. This Bap29 and Bap31 are homologous to each other and this entry includes both proteins.


Pssm-ID: 465623 [Multi-domain]  Cd Length: 52  Bit Score: 58.06  E-value: 1.23e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 32171186   193 DELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQaaVDGPMDKKEE 246
Cdd:pfam18035   1 KEIEKLKKELKKKKSDIEALKKQAEGLQREYDRLSDEHAKLQ--LDEGEDKKDD 52
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-239 1.80e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186  121 TLISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAE---VKLEEENRSLKA---DLQKLKDE 194
Cdd:COG4913  614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiAELEAELERLDAssdDLAALEEQ 693

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 32171186  195 LASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVDG 239
Cdd:COG4913  694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 122-236 2.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186    122 LISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVK-LEEENRSLKADLQKLKDELASTKQ 200
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRLEELEEQLETLRSKVAQLEL 393

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 32171186    201 KLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAA 236
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 176-237 2.82e-03

Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.


Pssm-ID: 464008 [Multi-domain]  Cd Length: 177  Bit Score: 37.58  E-value: 2.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32171186   176 KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQSE-----GLTKEYDRLLEEHAKLQAAV 237
Cdd:pfam13870  95 RLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQGGllhvpALLHDYDKTKAEVEEKRKSV 161
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 137-238 3.28e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 3.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186 137 KKQAESAsEAAKKYMEENDQLKKGAAVDggKLDVGNAEV-KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQ 215
Cdd:COG1196 206 ERQAEKA-ERYRELKEELKELEAELLLL--KLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282

                        90       100
                ....*....|....*....|...
gi 32171186 216 SEGLTKEYDRLLEEHAKLQAAVD 238
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIA 305
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
134-229 6.78e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.33  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186  134 EAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVK--------LEEENRSLKA----------DLQKLKDEL 195
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrreeieeLEEEIEELRErfgdapvdlgNAEDFLEEL 417

                         90       100       110
                 ....*....|....*....|....*....|....
gi 32171186  196 ASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEE 229
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEA 451
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 187-238 7.21e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.12  E-value: 7.21e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 32171186 187 DLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVD 238
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID 68
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 176-238 9.30e-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: 34.46  E-value: 9.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32171186 176 KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVD 238
Cdd:cd22887   1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLR 63
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
125-238 9.76e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.20  E-value: 9.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32171186  125 QQATLLASNEAFKKQAESASEAAkkymeENDQLKKGAAVDGGKLDVG---NAEVKLEEENRSLKADLQKLKDELASTKQK 201
Cdd:COG4913  250 QIELLEPIRELAERYAAARERLA-----ELEYLRAALRLWFAQRRLElleAELEELRAELARLEAELERLEARLDALREE 324

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 32171186  202 LEKAENQVL--------AMRKQSEGLTKEYDRLLEEHAKLQAAVD 238
Cdd:COG4913  325 LDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLA 369
 
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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