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Conserved domains on  [gi|1147710082|dbj|BAW99773|]
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nonstructural replication protein [Pteropine orthoreovirus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 11467523)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 411-623 6.57e-08

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 6.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 411 NEEIQRLNDEIQLLKAKLSASAEMIKTSSQtpsapskllsrisELTRQNKELLMRQSDFERSGSAqlLSYLEahVCVNAK 490
Cdd:COG3883    50 NEEYNELQAELEALQAEIDKLQAEIAEAEA-------------EIEERREELGERARALYRSGGS--VSYLD--VLLGSE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 491 PFEcELLTKVGLdsmdVTKI--RTEREMNRIRFERRLSSVAIAEL---KPEMDSLKAQIESQQSELEEVIDQclfKDKTI 565
Cdd:COG3883   113 SFS-DFLDRLSA----LSKIadADADLLEELKADKAELEAKKAELeakLAELEALKAELEAAKAELEAQQAE---QEALL 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1147710082 566 ADLESQVTSLKEELRVLSNRAVALNAENHRLSATTKTDVGWATPTDQPVYETPTRLPS 623
Cdd:COG3883   185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
 
Name Accession Description Interval E-value
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 411-623 6.57e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 6.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 411 NEEIQRLNDEIQLLKAKLSASAEMIKTSSQtpsapskllsrisELTRQNKELLMRQSDFERSGSAqlLSYLEahVCVNAK 490
Cdd:COG3883    50 NEEYNELQAELEALQAEIDKLQAEIAEAEA-------------EIEERREELGERARALYRSGGS--VSYLD--VLLGSE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 491 PFEcELLTKVGLdsmdVTKI--RTEREMNRIRFERRLSSVAIAEL---KPEMDSLKAQIESQQSELEEVIDQclfKDKTI 565
Cdd:COG3883   113 SFS-DFLDRLSA----LSKIadADADLLEELKADKAELEAKKAELeakLAELEALKAELEAAKAELEAQQAE---QEALL 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1147710082 566 ADLESQVTSLKEELRVLSNRAVALNAENHRLSATTKTDVGWATPTDQPVYETPTRLPS 623
Cdd:COG3883   185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 413-602 9.55e-06

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: 48.86  E-value: 9.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 413 EIQRLNDEIQLLKAKLSASAEMIKTSSQTPSAPSKLL----SRISELTRQNKELLMRQSDFERSgSAQLLSyleahvcvN 488
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELkskeKELKKLNEEKKELEEKVKDLTKK-ISSLKE--------K 525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 489 AKPFECELLTKVgldsmdvTKIRT-EREMNRIRFERRLSSVA---------IAELKPEMDSLKAQiesqQSELEEVIDQc 558
Cdd:TIGR04523 526 IEKLESEKKEKE-------SKISDlEDELNKDDFELKKENLEkeideknkeIEELKQTQKSLKKK----QEEKQELIDQ- 593

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1147710082 559 lfKDKTIADLESQVTSLKEELRVLSNRAVALNAENHRLSATTKT 602
Cdd:TIGR04523 594 --KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 530-596 7.49e-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: 36.00  E-value: 7.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1147710082 530 IAELKPEMDSLKAQIESQQSELEEvidqclfKDKTIADLESQVTSLKEELRVLSNRAVALNAENHRL 596
Cdd:cd22887    13 LAELEAELASLEEEIKDLEEELKE-------KNKANEILNDELIALQIENNLLEEKLRKLQEENDEL 72
 
Name Accession Description Interval E-value
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 411-623 6.57e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 6.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 411 NEEIQRLNDEIQLLKAKLSASAEMIKTSSQtpsapskllsrisELTRQNKELLMRQSDFERSGSAqlLSYLEahVCVNAK 490
Cdd:COG3883    50 NEEYNELQAELEALQAEIDKLQAEIAEAEA-------------EIEERREELGERARALYRSGGS--VSYLD--VLLGSE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 491 PFEcELLTKVGLdsmdVTKI--RTEREMNRIRFERRLSSVAIAEL---KPEMDSLKAQIESQQSELEEVIDQclfKDKTI 565
Cdd:COG3883   113 SFS-DFLDRLSA----LSKIadADADLLEELKADKAELEAKKAELeakLAELEALKAELEAAKAELEAQQAE---QEALL 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1147710082 566 ADLESQVTSLKEELRVLSNRAVALNAENHRLSATTKTDVGWATPTDQPVYETPTRLPS 623
Cdd:COG3883   185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
412-595 2.12e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 412 EEIQRLNDEIQLLKAKLS-ASAEMIKTSSQtpsapskLLSRISELTRQNKELLMRQSDFERSGSAQLlsyleahvcvnak 490
Cdd:COG4372    38 FELDKLQEELEQLREELEqAREELEQLEEE-------LEQARSELEQLEEELEELNEQLQAAQAELA------------- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 491 pfecelltkvgldsmdvtkiRTEREMNRIRFERRLSSVAIAELKPEMDSLKAQ---IESQQSELEEVIDQclfKDKTIAD 567
Cdd:COG4372    98 --------------------QAQEELESLQEEAEELQEELEELQKERQDLEQQrkqLEAQIAELQSEIAE---REEELKE 154

                         170       180
                  ....*....|....*....|....*...
gi 1147710082 568 LESQVTSLKEELRVLSNRAVALNAENHR 595
Cdd:COG4372   155 LEEQLESLQEELAALEQELQALSEAEAE 182
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 413-602 9.55e-06

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: 48.86  E-value: 9.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 413 EIQRLNDEIQLLKAKLSASAEMIKTSSQTPSAPSKLL----SRISELTRQNKELLMRQSDFERSgSAQLLSyleahvcvN 488
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELkskeKELKKLNEEKKELEEKVKDLTKK-ISSLKE--------K 525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 489 AKPFECELLTKVgldsmdvTKIRT-EREMNRIRFERRLSSVA---------IAELKPEMDSLKAQiesqQSELEEVIDQc 558
Cdd:TIGR04523 526 IEKLESEKKEKE-------SKISDlEDELNKDDFELKKENLEkeideknkeIEELKQTQKSLKKK----QEEKQELIDQ- 593

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1147710082 559 lfKDKTIADLESQVTSLKEELRVLSNRAVALNAENHRLSATTKT 602
Cdd:TIGR04523 594 --KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 411-595 1.40e-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: 45.05  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082  411 NEEIQRLNDEIQLLKAKL-SASAEMIKTSSQTPSAPSKLLSRISELTRQNKELLMRQSDFErSGSAQLLSYLEAHVCVNA 489
Cdd:TIGR02168  294 ANEISRLEQQKQILRERLaNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-SLEAELEELEAELEELES 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082  490 KPFECE-----LLTKVGLDSMDVTKIRTEREMNRIRFER-----------------RLSSVAIAELKPEMDSLKAQIESQ 547
Cdd:TIGR02168  373 RLEELEeqletLRSKVAQLELQIASLNNEIERLEARLERledrrerlqqeieellkKLEEAELKELQAELEELEEELEEL 452

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1147710082  548 QSELEEVIDQCLFKDKTIADLESQVTSLKEELRVLSNRAVALNA--ENHR 595
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlqENLE 502
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
511-601 3.76e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 511 RTEREMNRIRFERRLSSVAIAELKPEMDSLKAQIESQQSELEEVIDQclfkdktIADLESQVTSLKEELRVLSNRAVALN 590
Cdd:COG4372    49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE-------LAQAQEELESLQEEAEELQEELEELQ 121

                          90
                  ....*....|.
gi 1147710082 591 AENHRLSATTK 601
Cdd:COG4372   122 KERQDLEQQRK 132
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 411-599 4.14e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 411 NEEIQRLNDEIQLLKAKLSASAEMIKTSSQTPSAPSKLLS----RISELTRQNKELLMRQSDFERSGSAQ--LLSYLEAH 484
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRaleqELAALEAELAELEKEIAELRAELEAQkeELAELLRA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 485 VCVNAKPFECELLtkvgLDSMDVTK-IRTEREMNRIRFERRLSSVAIAELKPEMDSLKAQIESQQSELEEVIDQCLFKDK 563
Cdd:COG4942   113 LYRLGRQPPLALL----LSPEDFLDaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1147710082 564 TIADLESQ----VTSLKEELRVLSNRAVALNAENHRLSAT 599
Cdd:COG4942   189 ALEALKAErqklLARLEKELAELAAELAELQQEAEELEAL 228
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 501-592 8.31e-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: 42.74  E-value: 8.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082  501 GLDSMDVTKIRTEREMNRIRFERRLSSVAIAELKPEMDSLKAQIESQQSELEEVidqclfkDKTIADLESQVTSLKEELR 580
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-------ANEISRLEQQKQILRERLA 312

                           90
                   ....*....|..
gi 1147710082  581 VLSNRAVALNAE 592
Cdd:TIGR02168  313 NLERQLEELEAQ 324
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
414-599 1.03e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 414 IQRLNDEIQLLKAKLSASAEMI---KTSSQTPSAPSKLLSRISELTRQNKELLMRQSdfERSGSAQLLSYLEAhvcvnak 490
Cdd:COG3206   177 LEFLEEQLPELRKELEEAEAALeefRQKNGLVDLSEEAKLLLQQLSELESQLAEARA--ELAEAEARLAALRA------- 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 491 pfecelltKVGLDSMDVTKIRTEREMNRIRFERRLSSVAIAELK-------PEMDSLKAQIESQQSELEEVIDQclfkdk 563
Cdd:COG3206   248 --------QLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhPDVIALRAQIAALRAQLQQEAQR------ 313

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1147710082 564 TIADLESQVTSLKEELRVLSNRAVALNAENHRLSAT 599
Cdd:COG3206   314 ILASLEAELEALQAREASLQAQLAQLEARLAELPEL 349
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 530-598 2.32e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 530 IAELKPEMDSLKAQIESQQSELEEVIDQCLFKDKTIADLESQVTSLKEELRVLSNRAVALNAE-NHRLSA 598
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARA 94
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 446-598 2.41e-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: 41.20  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082  446 SKLLSRISELTRQNKELLMRQSDfERSGSAQLLSYLEAHVCVNakpfecELLTKVGLDSMDVTKIRTEREMNRIRFERRL 525
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEK-IAELEKALAELRKELEELE------EELEQLRKELEELSRQISALRKDLARLEAEV 742

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1147710082  526 SSVA--IAELKPEMDSLKAQIESQQSELEEVIDQCLFKDKTIADLESQVTSLKEELRVLSNRAVALNAENHRLSA 598
Cdd:TIGR02168  743 EQLEerIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 411-595 3.30e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 411 NEEIQRLNDEIQLLKAKLSASAEMIKTSSQTPSAPSKLLS-RISELTRQNK----ELLMRQSDFERSgsAQLLSYLEAHV 485
Cdd:COG4942    68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAeLLRALYRLGRqpplALLLSPEDFLDA--VRRLQYLKYLA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147710082 486 cvnakPFECELLTKVGLDSMDVTKIRTEREMNRIRFERRLSSV-----AIAELKPEMDSLKAQIESQQSELEEVIDQclf 560
Cdd:COG4942   146 -----PARREQAEELRADLAELAALRAELEAERAELEALLAELeeeraALEALKAERQKLLARLEKELAELAAELAE--- 217

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1147710082 561 KDKTIADLESQVTSLKEELRVLSNRAVALNAENHR 595
Cdd:COG4942   218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 522-592 4.75e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 4.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147710082 522 ERRLSSV--AIAELKPEMDSLKAQIESQQSELEEVIDQCLFKDKTIADLESQVTSLKEELRVLSNRAVALNAE 592
Cdd:COG4942    26 EAELEQLqqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 530-596 7.49e-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: 36.00  E-value: 7.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1147710082 530 IAELKPEMDSLKAQIESQQSELEEvidqclfKDKTIADLESQVTSLKEELRVLSNRAVALNAENHRL 596
Cdd:cd22887    13 LAELEAELASLEEEIKDLEEELKE-------KNKANEILNDELIALQIENNLLEEKLRKLQEENDEL 72
 
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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