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Conserved domains on  [gi|213511508|ref|NP_001132929|]
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B-cell receptor-associated protein 31 isoform a [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 ...
 68-203 7.91e-48

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: 156.88  E-value: 7.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508   68 MSLQWTAVATFLYAEVFVVLLLCIPFISPKRwQKIFKSRLVELLVSYGNTFFVVLIVILVLLVIDAVREIRKYDDVTE-- 145
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELEsa 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 213511508  146 KVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAF 203
Cdd:pfam05529  80 KANAHQHPSARMEVQARKFYAQRNLYICGFTLFLSLVLRRTVTLISELATLEAKLEAL 137
Bap31_Bap29_C pfam18035
Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the ...
 260-313 7.09e-13

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: 62.29  E-value: 7.09e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 213511508  260 DELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQaaVDGPMDKKEE 313
Cdd:pfam18035   1 KEIEKLKKELKKKKSDIEALKKQAEGLQREYDRLSDEHAKLQ--LDEGEDKKDD 52
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 204-305 1.44e-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: 40.31  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508 204 KKQAESAsEAAKKYMEENDQLKKGAAVDggKLDVGNAEV-KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQ 282
Cdd:COG1196  206 ERQAEKA-ERYRELKEELKELEAELLLL--KLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282

                         90       100
                 ....*....|....*....|...
gi 213511508 283 SEGLTKEYDRLLEEHAKLQAAVD 305
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 ...
 68-203 7.91e-48

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: 156.88  E-value: 7.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508   68 MSLQWTAVATFLYAEVFVVLLLCIPFISPKRwQKIFKSRLVELLVSYGNTFFVVLIVILVLLVIDAVREIRKYDDVTE-- 145
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELEsa 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 213511508  146 KVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAF 203
Cdd:pfam05529  80 KANAHQHPSARMEVQARKFYAQRNLYICGFTLFLSLVLRRTVTLISELATLEAKLEAL 137
Bap31_Bap29_C pfam18035
Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the ...
 260-313 7.09e-13

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: 62.29  E-value: 7.09e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 213511508  260 DELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQaaVDGPMDKKEE 313
Cdd:pfam18035   1 KEIEKLKKELKKKKSDIEALKKQAEGLQREYDRLSDEHAKLQ--LDEGEDKKDD 52
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
188-306 9.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508  188 TLISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAE---VKLEEENRSLKA---DLQKLKDE 261
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiAELEAELERLDAssdDLAALEEQ 693

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 213511508  262 LASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVDG 306
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 189-303 1.14e-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: 40.81  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508   189 LISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVK-LEEENRSLKADLQKLKDELASTKQ 267
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRLEELEEQLETLRSKVAQLEL 393

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 213511508   268 KLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAA 303
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 204-305 1.44e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508 204 KKQAESAsEAAKKYMEENDQLKKGAAVDggKLDVGNAEV-KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQ 282
Cdd:COG1196  206 ERQAEKA-ERYRELKEELKELEAELLLL--KLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282

                         90       100
                 ....*....|....*....|...
gi 213511508 283 SEGLTKEYDRLLEEHAKLQAAVD 305
Cdd:COG1196  283 LEEAQAEEYELLAELARLEQDIA 305
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 243-305 1.55e-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: 37.16  E-value: 1.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213511508 243 KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVD 305
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLR 63
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 203-313 2.34e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.70  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508  203 FKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVgnAEVKleeenrslkadLQKLKDELASTKQKLEKAENQvlaMRKQ 282
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNA--YEIK-----------VNKLELELASAKQKFEEIIDN---YQKE 662

                          90       100       110
                  ....*....|....*....|....*....|.
gi 213511508  283 SEGLTKEYDRLLEEHAKLQAAVDGPMDKKEE 313
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKAKAIADEAVKLQKE 693
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
201-296 4.33e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508 201 EAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVK--------LEEENRSLKA----------DLQKLKDEL 262
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrreeieeLEEEIEELRErfgdapvdlgNAEDFLEEL 417

                         90       100       110
                 ....*....|....*....|....*....|....
gi 213511508 263 ASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEE 296
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEA 451
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 254-305 6.61e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 6.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 213511508 254 DLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVD 305
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID 68
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 68-203 7.91e-48

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: 156.88  E-value: 7.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508   68 MSLQWTAVATFLYAEVFVVLLLCIPFISPKRwQKIFKSRLVELLVSYGNTFFVVLIVILVLLVIDAVREIRKYDDVTE-- 145
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELEsa 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 213511508  146 KVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAF 203
Cdd:pfam05529  80 KANAHQHPSARMEVQARKFYAQRNLYICGFTLFLSLVLRRTVTLISELATLEAKLEAL 137
Bap31_Bap29_C pfam18035
Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the ...
 260-313 7.09e-13

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: 62.29  E-value: 7.09e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 213511508  260 DELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQaaVDGPMDKKEE 313
Cdd:pfam18035   1 KEIEKLKKELKKKKSDIEALKKQAEGLQREYDRLSDEHAKLQ--LDEGEDKKDD 52
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 243-305 2.65e-04

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: 41.05  E-value: 2.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 213511508  243 KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQSE-----GLTKEYDRLLEEHAKLQAAVD 305
Cdd:pfam13870  95 RLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQGGllhvpALLHDYDKTKAEVEEKRKSVK 162
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
188-306 9.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508  188 TLISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAE---VKLEEENRSLKA---DLQKLKDE 261
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiAELEAELERLDAssdDLAALEEQ 693

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 213511508  262 LASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVDG 306
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 189-303 1.14e-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: 40.81  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508   189 LISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVK-LEEENRSLKADLQKLKDELASTKQ 267
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRLEELEEQLETLRSKVAQLEL 393

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 213511508   268 KLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAA 303
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 204-305 1.44e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508 204 KKQAESAsEAAKKYMEENDQLKKGAAVDggKLDVGNAEV-KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQ 282
Cdd:COG1196  206 ERQAEKA-ERYRELKEELKELEAELLLL--KLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282

                         90       100
                 ....*....|....*....|...
gi 213511508 283 SEGLTKEYDRLLEEHAKLQAAVD 305
Cdd:COG1196  283 LEEAQAEEYELLAELARLEQDIA 305
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 243-305 1.55e-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: 37.16  E-value: 1.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213511508 243 KLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVD 305
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLR 63
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 203-313 2.34e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.70  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508  203 FKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVgnAEVKleeenrslkadLQKLKDELASTKQKLEKAENQvlaMRKQ 282
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNA--YEIK-----------VNKLELELASAKQKFEEIIDN---YQKE 662

                          90       100       110
                  ....*....|....*....|....*....|.
gi 213511508  283 SEGLTKEYDRLLEEHAKLQAAVDGPMDKKEE 313
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKAKAIADEAVKLQKE 693
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
192-305 4.10e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508  192 QQATLLASNEAFKKQAESASEAAkkymeENDQLKKGAAVDGGKLDVG---NAEVKLEEENRSLKADLQKLKDELASTKQK 268
Cdd:COG4913   250 QIELLEPIRELAERYAAARERLA-----ELEYLRAALRLWFAQRRLElleAELEELRAELARLEAELERLEARLDALREE 324

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 213511508  269 LEKAENQVL--------AMRKQSEGLTKEYDRLLEEHAKLQAAVD 305
Cdd:COG4913   325 LDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLA 369
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
201-296 4.33e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213511508 201 EAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVK--------LEEENRSLKA----------DLQKLKDEL 262
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrreeieeLEEEIEELRErfgdapvdlgNAEDFLEEL 417

                         90       100       110
                 ....*....|....*....|....*....|....
gi 213511508 263 ASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEE 296
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEA 451
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 254-305 6.61e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 6.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 213511508 254 DLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVD 305
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID 68
 
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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