NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958643663|ref|XP_038961054|]
View 

tumor susceptibility gene 101 protein isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 187-246 6.44e-29

Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. The core domain of the Vps23 subunit of the heterotrimeric ESCRT-I complex is a helical hairpin sandwiched in a fan-like formation between two other helical hairpins from Vps28 (pfam03997) and Vps37. Vps23 gives ESCRT-I complex its stability.


:

Pssm-ID: 462803 [Multi-domain]  Cd Length: 60  Bit Score: 104.08  E-value: 6.44e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 187 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 246
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-254 8.97e-06

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 8.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  112 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEnndideviip 191
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE---------- 347

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958643663  192 taplykQILNLYAEENAIEDTIFYLGEALRRGVIDLDvflKHVRLLSRKQFQLRALMQKARKT 254
Cdd:TIGR02168  348 ------ELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNE 401
PHA03369 super family cl25753
capsid maturational protease; Provisional
 17-181 6.35e-03

capsid maturational protease; Provisional


The actual alignment was detected with superfamily member PHA03369:

Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 37.67  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  17 VSASYPPYTAAGPPNTSYLPSM---PSGISAYPSGYPP--NPSGYPgcpYPPAGPYPATTSSQYPSQPPVTTAGPSRDGT 91
Cdd:PHA03369  359 VLAAAAKVAVIAAPQTHTGPADrqrPQRPDGIPYSVPArsPMTAYP---PVPQFCGDPGLVSPYNPQSPGTSYGPEPVGP 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  92 ISEDTIRASlisavsdklrwRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELsS 171
Cdd:PHA03369  436 VPPQPTNPY-----------VMPISMANMVYPGHPQEHGHERKRKRGGELKEELIETLKLVKKLKEEQESLAKELEAT-A 503

                         170
                  ....*....|
gi 1958643663 172 ALEKMENQSE 181
Cdd:PHA03369  504 HKSEIKKIAE 513
 
Name Accession Description Interval E-value
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 187-246 6.44e-29

Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. The core domain of the Vps23 subunit of the heterotrimeric ESCRT-I complex is a helical hairpin sandwiched in a fan-like formation between two other helical hairpins from Vps28 (pfam03997) and Vps37. Vps23 gives ESCRT-I complex its stability.


Pssm-ID: 462803 [Multi-domain]  Cd Length: 60  Bit Score: 104.08  E-value: 6.44e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 187 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 246
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-254 8.97e-06

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: 46.59  E-value: 8.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  112 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEnndideviip 191
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE---------- 347

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958643663  192 taplykQILNLYAEENAIEDTIFYLGEALRRGVIDLDvflKHVRLLSRKQFQLRALMQKARKT 254
Cdd:TIGR02168  348 ------ELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNE 401
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 107-163 6.05e-05

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 42.50  E-value: 6.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958643663 107 DKLRWRMKEEMDGAQAE----LNALK-RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLK 163
Cdd:pfam07798  89 EKLKQRLREEITKLKADvrldLNLEKgRIREELKAQELKIQETNNKIDTEIANLRTQIESVK 150
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
112-240 1.09e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 112 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIP 191
Cdd:COG4372    98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958643663 192 TAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRK 240
Cdd:COG4372   178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 121-184 1.95e-04

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: 39.47  E-value: 1.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958643663 121 QAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLkkKDE------ELSSALEKMEN-QSENND 184
Cdd:cd22887     3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL--NDElialqiENNLLEEKLRKlQEENDE 71
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-182 8.86e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 8.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958643663 115 EEMDGAQAELNALKRTEEDLKKG-----HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 182
Cdd:PRK03918  633 EELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
PHA03369 PHA03369
capsid maturational protease; Provisional
 17-181 6.35e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 37.67  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  17 VSASYPPYTAAGPPNTSYLPSM---PSGISAYPSGYPP--NPSGYPgcpYPPAGPYPATTSSQYPSQPPVTTAGPSRDGT 91
Cdd:PHA03369  359 VLAAAAKVAVIAAPQTHTGPADrqrPQRPDGIPYSVPArsPMTAYP---PVPQFCGDPGLVSPYNPQSPGTSYGPEPVGP 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  92 ISEDTIRASlisavsdklrwRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELsS 171
Cdd:PHA03369  436 VPPQPTNPY-----------VMPISMANMVYPGHPQEHGHERKRKRGGELKEELIETLKLVKKLKEEQESLAKELEAT-A 503

                         170
                  ....*....|
gi 1958643663 172 ALEKMENQSE 181
Cdd:PHA03369  504 HKSEIKKIAE 513
 
Name Accession Description Interval E-value
Vps23_core pfam09454
Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from ...
 187-246 6.44e-29

Vps23 core domain; ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. The core domain of the Vps23 subunit of the heterotrimeric ESCRT-I complex is a helical hairpin sandwiched in a fan-like formation between two other helical hairpins from Vps28 (pfam03997) and Vps37. Vps23 gives ESCRT-I complex its stability.


Pssm-ID: 462803 [Multi-domain]  Cd Length: 60  Bit Score: 104.08  E-value: 6.44e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 187 EVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRA 246
Cdd:pfam09454   1 EVVVATTPLSNQLLELVAEDKAIEDTIYLLDKALDRGVIDLDTFLKQVRELAREQFLKRA 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-254 8.97e-06

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: 46.59  E-value: 8.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  112 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEnndideviip 191
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE---------- 347

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958643663  192 taplykQILNLYAEENAIEDTIFYLGEALRRGVIDLDvflKHVRLLSRKQFQLRALMQKARKT 254
Cdd:TIGR02168  348 ------ELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNE 401
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 107-163 6.05e-05

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 42.50  E-value: 6.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958643663 107 DKLRWRMKEEMDGAQAE----LNALK-RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLK 163
Cdd:pfam07798  89 EKLKQRLREEITKLKADvrldLNLEKgRIREELKAQELKIQETNNKIDTEIANLRTQIESVK 150
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-213 7.03e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 7.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 101 LISAVSDKLRWRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMEnqS 180
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK--K 624

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958643663 181 ENNDIDEvIIPTAPLYKQILNLYAEenAIEDTI 213
Cdd:TIGR04523 625 ENEKLSS-IIKNIKSKKNKLKQEVK--QIKETI 654
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
112-240 1.09e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 112 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIP 191
Cdd:COG4372    98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958643663 192 TAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRK 240
Cdd:COG4372   178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-252 1.11e-04

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: 43.12  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  114 KEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIPTA 193
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958643663  194 PLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKAR 252
Cdd:TIGR02168  430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 121-184 1.95e-04

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: 39.47  E-value: 1.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958643663 121 QAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLkkKDE------ELSSALEKMEN-QSENND 184
Cdd:cd22887     3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEIL--NDElialqiENNLLEEKLRKlQEENDE 71
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
99-220 2.47e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  99 ASLISAVSDKLRwRMKEEMDGAQAELNALK-----------RTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDE 167
Cdd:COG4372    23 GILIAALSEQLR-KALFELDKLQEELEQLReeleqareeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958643663 168 ELSSALEKMENQSEnnDIDEVIiptaplyKQILNLYAEENAIEDTIFYLGEAL 220
Cdd:COG4372   102 ELESLQEEAEELQE--ELEELQ-------KERQDLEQQRKQLEAQIAELQSEI 145
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 102-175 6.02e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 6.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958643663 102 ISAVSDKLRwRMKEEMDGAQAELNALKRTEEDLKKghqKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEK 175
Cdd:COG1579   105 ISDLEDEIL-ELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-182 8.86e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 8.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958643663 115 EEMDGAQAELNALKRTEEDLKKG-----HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 182
Cdd:PRK03918  633 EELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
PRK10325 PRK10325
heat shock protein GrpE; Provisional
 112-177 1.07e-03

heat shock protein GrpE; Provisional


Pssm-ID: 182379 [Multi-domain]  Cd Length: 197  Bit Score: 39.27  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958643663 112 RMKEEMDgaqaelNALKRTEEDLKKGHQ-KLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 177
Cdd:PRK10325   64 RVKAEME------NLRRRTELDIEKAHKfALEKFINELLPVIDSLDRALEVADKANPDMSAMVEGIE 124
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 107-240 1.61e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  107 DKLRWRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQsenndID 186
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-----LR 878

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958643663  187 EVIIPTAPLYKQILNLYAEENAIEDtifylgealRRGVIDLDVFLKHVRLLSRK 240
Cdd:TIGR02169  879 DLESRLGDLKKERDELEAQLRELER---------KIEELEAQIEKKRKRLSELK 923
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 114-184 1.99e-03

Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain


Pssm-ID: 238105 [Multi-domain]  Cd Length: 151  Bit Score: 37.65  E-value: 1.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958643663 114 KEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENND 184
Cdd:cd00179    12 RGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSSV 82
PRK12704 PRK12704
phosphodiesterase; Provisional
 114-182 2.45e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 2.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 114 KEEMDGAQAELNALKR-TEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN 182
Cdd:PRK12704   56 KEALLEAKEEIHKLRNeFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
98-253 2.49e-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: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663   98 RASLISAVSDkLRWRMKEeMDGAQAELNALKRTEEDLKKGHQKLEEmvtrLDQEVAEVDKNIELLKKKDEELSSALEKME 177
Cdd:COG4913    646 RREALQRLAE-YSWDEID-VASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLE 719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  178 NQSENndideviiptapLYKQILNLYAEENAIEDTI----FYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARK 253
Cdd:COG4913    720 KELEQ------------AEEELDELQDRLEAAEDLArlelRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 102-176 2.68e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 2.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958643663 102 ISAVSDKLRwRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKM 176
Cdd:COG3883    18 IQAKQKELS-ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 102-213 3.05e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 102 ISAVSDKLRwRMKEEMDGAQA--ELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALE--KME 177
Cdd:COG1579    68 IEEVEARIK-KYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEekKAE 146

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958643663 178 NQSENNDIDeviiptaplyKQILNLYAEENAIEDTI 213
Cdd:COG1579   147 LDEELAELE----------AELEELEAEREELAAKI 172
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 107-190 3.09e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 107 DKLRWRMKEEMDGAQAELNALKRTEEDLKKG-------HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSalEKMENQ 179
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES--EKKEKE 537

                          90
                  ....*....|.
gi 1958643663 180 SENNDIDEVII 190
Cdd:TIGR04523 538 SKISDLEDELN 548
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
112-222 3.22e-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: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  112 RMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEViip 191
Cdd:COG4913    675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL--- 751

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958643663  192 tAPLYKQIL----------NLYAEENAIEDTIFYLGEALRR 222
Cdd:COG4913    752 -EERFAAALgdaverelreNLEERIDALRARLNRAEEELER 791
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 118-189 3.93e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 37.78  E-value: 3.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958643663 118 DGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVA---EVDKNIELLKKKDEELSSALEKMEN--QSENNDIDEVI 189
Cdd:cd21116   112 TSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAvlnALKNQLNSLAEQIDAAIDALEKLSNdwQTLDSDIKELI 188
RPN7 COG5187
26S proteasome regulatory complex component, contains PCI domain [Posttranslational ...
 135-236 5.16e-03

26S proteasome regulatory complex component, contains PCI domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227514 [Multi-domain]  Cd Length: 412  Bit Score: 37.97  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 135 KKGHQKLEEMVTRLDQEVAEvdkniELLKKKDE---ELSSALEKMENQSENNDIDEVIIPTAPLYKQILNLyaeENAIEd 211
Cdd:COG5187    66 EKGNPKTSASVIKFDRGRMN-----TLLKKNEEkieELDERIREKEEDNGETEGSEADRNIAEYYCQIMDI---QNGFE- 136

                          90       100
                  ....*....|....*....|....*...
gi 1958643663 212 tifYLGEALRRGV---IDLDVFLKHVRL 236
Cdd:COG5187   137 ---WMRRLMRDAMstgLKIDVFLCKIRL 161
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
114-177 5.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 5.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958643663 114 KEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKME 177
Cdd:PRK03918  230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
PHA03369 PHA03369
capsid maturational protease; Provisional
 17-181 6.35e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 37.67  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  17 VSASYPPYTAAGPPNTSYLPSM---PSGISAYPSGYPP--NPSGYPgcpYPPAGPYPATTSSQYPSQPPVTTAGPSRDGT 91
Cdd:PHA03369  359 VLAAAAKVAVIAAPQTHTGPADrqrPQRPDGIPYSVPArsPMTAYP---PVPQFCGDPGLVSPYNPQSPGTSYGPEPVGP 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663  92 ISEDTIRASlisavsdklrwRMKEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELsS 171
Cdd:PHA03369  436 VPPQPTNPY-----------VMPISMANMVYPGHPQEHGHERKRKRGGELKEELIETLKLVKKLKEEQESLAKELEAT-A 503

                         170
                  ....*....|
gi 1958643663 172 ALEKMENQSE 181
Cdd:PHA03369  504 HKSEIKKIAE 513
PRK10698 PRK10698
phage shock protein PspA; Provisional
 121-173 8.50e-03

phage shock protein PspA; Provisional


Pssm-ID: 182657 [Multi-domain]  Cd Length: 222  Bit Score: 36.67  E-value: 8.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958643663 121 QAELnALKRTEEDLKKG----HQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSAL 173
Cdd:PRK10698   74 KAEL-ALRKEKEDLARAalieKQKLTDLIATLEHEVTLVDETLARMKKEIGELENKL 129
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 114-213 9.55e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 37.31  E-value: 9.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643663 114 KEEMDGAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSEN--NDIDEV--- 188
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNiqKNIDKIknk 195

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958643663 189 ---------IIPT-----APLYKQILNLYAEENAIEDTI 213
Cdd:TIGR04523 196 llklelllsNLKKkiqknKSLESQISELKKQNNQLKDNI 234
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH