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Conserved domains on  [gi|1039792749|ref|XP_017168773|]
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E3 ubiquitin-protein ligase TRAIP isoform X2 [Mus musculus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

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
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 4-150 3.58e-06

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   4 STLKKQMKFLEQRQDETKQAREEAHRLKCKMKTMEQIELLLQSQrsEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLK 83
Cdd:COG4942    86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE--DFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792749  84 EARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKLMILQGTLS 150
Cdd:COG4942   164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 4-150 3.58e-06

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: 48.22  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   4 STLKKQMKFLEQRQDETKQAREEAHRLKCKMKTMEQIELLLQSQrsEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLK 83
Cdd:COG4942    86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE--DFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792749  84 EARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKLMILQGTLS 150
Cdd:COG4942   164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 58-142 1.22e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 43.56  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749  58 MGVGQSAVEQLAVYCVSLKKEY-----ENLKEARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSAD 132
Cdd:TIGR04320 216 LGVSISNDGGVTIHFVNFNDSYiadgnKFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQ 295

                          90
                  ....*....|
gi 1039792749 133 QEITSLRKKL 142
Cdd:TIGR04320 296 AALATAQKEL 305
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
13-142 3.98e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749  13 LEQRQDETKQAREEAHRLKCKMKTMEQIELLLQSQRSEVEEMIRDMGVGQSAveqlavycvsLKKEYENLKEARKATGEL 92
Cdd:PRK02224  288 LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA----------HNEEAESLREDADDLEER 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039792749  93 ADRLkkdlvssRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKL 142
Cdd:PRK02224  358 AEEL-------REEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 4-150 3.58e-06

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: 48.22  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   4 STLKKQMKFLEQRQDETKQAREEAHRLKCKMKTMEQIELLLQSQrsEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLK 83
Cdd:COG4942    86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE--DFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792749  84 EARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKLMILQGTLS 150
Cdd:COG4942   164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
13-142 5.98e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 5.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   13 LEQRQDETKQAREEAHRLKCKMKTMEQIELLLQSQRS------EVEEMIRDMgvgQSAVEQLAvycvSLKKEYENLkeaR 86
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaEYSWDEIDV---ASAEREIA----ELEAELERL---D 681

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039792749   87 KATGELAdRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKL 142
Cdd:COG4913    682 ASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4-134 6.09e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 6.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749    4 STLKKQMKFLEQRQDETKQAREEAHRLKckMKTMEQIELL-LQSQRSEVEEMIRDMGVGQSAVEQLavycvslKKEYENL 82
Cdd:COG4913    627 AEAEERLEALEAELDALQERREALQRLA--EYSWDEIDVAsAEREIAELEAELERLDASSDDLAAL-------EEQLEEL 697

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039792749   83 KEARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQE 134
Cdd:COG4913    698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 58-142 1.22e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 43.56  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749  58 MGVGQSAVEQLAVYCVSLKKEY-----ENLKEARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSAD 132
Cdd:TIGR04320 216 LGVSISNDGGVTIHFVNFNDSYiadgnKFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQ 295

                          90
                  ....*....|
gi 1039792749 133 QEITSLRKKL 142
Cdd:TIGR04320 296 AALATAQKEL 305
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-141 1.85e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   11 KFLEQRQDETKQAREEAHRLKCKMKTMEQIELLLQSQRSEVEEMIRdmGVGQSAVEQLAVYCVSLKKEYENLKEARKATG 90
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR--GNGGDRLEQLEREIERLERELEERERRRARLE 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039792749   91 ELADRLKKDLVSSR------------------SKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKK 141
Cdd:COG4913    366 ALLAALGLPLPASAeefaalraeaaallealeEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 74-150 3.66e-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: 42.06  E-value: 3.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792749  74 SLKKEYENLKEARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKLMILQGTLS 150
Cdd:COG4942    31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 6-147 4.55e-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: 41.97  E-value: 4.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749    6 LKKQMKFLE------QRQDETKQAREEAH------RLKCKMKTMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYCV 73
Cdd:TIGR02168  198 LERQLKSLErqaekaERYKELKAELRELElallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039792749   74 SLKKEYENLKEARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKLMILQG 147
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 6-142 4.55e-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: 41.97  E-value: 4.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749    6 LKKQMKFLEQRQDETKQAREEAHRLkckmktMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEA 85
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELESR------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792749   86 RKATGELADRLKKDLVSSRskLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKL 142
Cdd:TIGR02168  423 IEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQAL 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 13-142 6.58e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749  13 LEQRQDETKQAREEAHRLKckmKTMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAvycvslkKEYENLKEARKATGEL 92
Cdd:COG1196   248 LEELEAELEELEAELAELE---AELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIARLEERRRELEER 317

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039792749  93 ADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKL 142
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 84-146 6.62e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 6.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039792749  84 EARKATGELADrLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKLMILQ 146
Cdd:COG3883    17 QIQAKQKELSE-LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
4-150 8.70e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   4 STLKKQMKFLEQRQDETKQAREEahrLKCKMKTMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLK 83
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREE---LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792749  84 EARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKLMILQGTLS 150
Cdd:COG4372   108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-142 8.82e-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: 41.20  E-value: 8.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   13 LEQRQDETKQAREEAHRLKCKMK-TMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKATGE 91
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSeDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039792749   92 LADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQ----------------------KDLQSADQEITSLRKKL 142
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysltleeaealenkieDDEEEARRRLKRLENKI 981
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
13-134 9.09e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 9.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749  13 LEQRQDETKQAREEAHRLKckmKTMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKATGEL 92
Cdd:COG4372    61 LEQLEEELEQARSELEQLE---EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039792749  93 ADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQE 134
Cdd:COG4372   138 IAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-146 1.18e-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: 40.82  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749    4 STLKKQMKFLEQRQDETKQAREEAHR-LKCKMKTMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENL 82
Cdd:TIGR02169  691 SSLQSELRRIENRLDELSQELSDASRkIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039792749   83 KEA----RKATGELADRLkkdlvsSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKLMILQ 146
Cdd:TIGR02169  771 EEDlhklEEALNDLEARL------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 6-142 2.00e-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: 39.14  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   6 LKKQMKFLEQRQDETKQAREEAHRLKckmktmEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVY--CVSLKKEYENLK 83
Cdd:COG1579    36 LEDELAALEARLEAAKTELEDLEKEI------KRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQkeIESLKRRISDLE 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039792749  84 EARKATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKL 142
Cdd:COG1579   110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
13-142 3.98e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749  13 LEQRQDETKQAREEAHRLKCKMKTMEQIELLLQSQRSEVEEMIRDMGVGQSAveqlavycvsLKKEYENLKEARKATGEL 92
Cdd:PRK02224  288 LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA----------HNEEAESLREDADDLEER 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039792749  93 ADRLkkdlvssRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKL 142
Cdd:PRK02224  358 AEEL-------REEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 88-151 4.32e-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: 38.59  E-value: 4.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039792749  88 ATGELADRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKLMILQGTLSL 151
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5-141 5.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   5 TLKKQMKFLEQRQDETKQAREEAHRLKCKMKTMEQIELLLQSQRSEVEEMIRDMGVgqSAVEQLAVYCVSLKKEYENLKE 84
Cdd:PRK03918  529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF--ESVEELEERLKELEPFYNEYLE 606

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039792749  85 ARKATGELADRLKKdlvssrskLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKK 141
Cdd:PRK03918  607 LKDAEKELEREEKE--------LKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
6-147 7.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   6 LKKQMKFLEQRQDETKQAREEAHRLKCKMKTMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYcvslKKEYENLKEA 85
Cdd:PRK03918  226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK----AEEYIKLSEF 301

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039792749  86 RKATGELADRLKKDLVSSRSKLKTLNTELDqaklELRSAQKDLQSADQEITSLRKKLMILQG 147
Cdd:PRK03918  302 YEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEE 359
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 13-140 8.11e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.01  E-value: 8.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   13 LEQRQDETKQAREEAH-RLKCKMKTMEQIELLLQSQRS----------EVEEMIRDMGVGQSAveqlavycvslkkEYEN 81
Cdd:COG3096    989 LRARLEQAEEARREAReQLRQAQAQYSQYNQVLASLKSsrdakqqtlqELEQELEELGVQADA-------------EAEE 1055

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039792749   82 LKEARKatgelaDRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRK 140
Cdd:COG3096   1056 RARIRR------DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 4-141 8.16e-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: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   4 STLKKQMKFLEQRQDETKQAREEAHrlkckmKTMEQIELLLQSQRSEVEEMIRDMGVGQSAVEQLAVYCVS-----LKKE 78
Cdd:COG3883    47 EELNEEYNELQAELEALQAEIDKLQ------AEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSesfsdFLDR 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039792749  79 YENLKEARKATGELADRLKKDlvssRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKK 141
Cdd:COG3883   121 LSALSKIADADADLLEELKAD----KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-142 8.69e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.11  E-value: 8.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039792749   21 KQAREEAHRLKCKMKTMEQIELLLQSQRSEVEEMIRDMgvgQSAVEQLAVYCVSLKKEYE-------NLKEARKATGELA 93
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAELEeleaeleELESRLEELEEQL 381

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1039792749   94 DRLKKDLVSSRSKLKTLNTELDQAKLELRSAQKDLQSADQEITSLRKKL 142
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
 
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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