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Conserved domains on  [gi|48428492|sp|Q9GYV5|]
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RecName: Full=NF-kappa-B essential modulator; AltName: Full=Inhibitor of nuclear factor kappa B kinase subunit gamma; Short=DmIKKgamma; AltName: Full=NEMO homolog

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 230-313 9.50e-25

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


:

Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 96.65  E-value: 9.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 230 FEFVPEYATESKSQELIKKMQLDINELKARDIQKQ---EVIKGLQIQNDIYRRDFEMERADREKNAGEKDQYLMDLRSLQ 306
Cdd:cd09803   1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEadlETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                ....*..
gi 48428492 307 RRNQELI 313
Cdd:cd09803  81 RENQELK 87
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-318 1.82e-05

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 120 EYLALKSTLD--KVNQTMLNYHNLTQQWRQEAADREHQyKEHVKECQAQIAILRVENQELKRDLETKIEQIEgvhtirlK 197
Cdd:COG1196 214 RYRELKEELKelEAELLLLKLRELEAELEELEAELEEL-EAELEELEAELAELEAELEELRLELEELELELE-------E 285

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 198 EQDELRKSVSEKQSLIDNMRVEIDKLKQLnhsfefvpeyatesksQELIKKMQLDINELKARDIQKQEVIKGLQIQNDIY 277
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRREL----------------EERLEELEEELAELEEELEELEEELEELEEELEEA 349

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 48428492 278 RRDFEMERADREKNAGEKDQYLMDLRSLQRRNQELIEALAE 318
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 230-313 9.50e-25

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 96.65  E-value: 9.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 230 FEFVPEYATESKSQELIKKMQLDINELKARDIQKQ---EVIKGLQIQNDIYRRDFEMERADREKNAGEKDQYLMDLRSLQ 306
Cdd:cd09803   1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEadlETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                ....*..
gi 48428492 307 RRNQELI 313
Cdd:cd09803  81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 244-313 9.28e-16

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 72.32  E-value: 9.28e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48428492   244 ELIKKMQLDINELKARDIQKQ---EVIKGLQIQNDIYRRDFEMERADREKNAGEKDQYLMDLRSLQRRNQELI 313
Cdd:pfam16516  28 EALAAKQREIDELKQEIAQKEedlETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQQLK 100
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-318 1.82e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 120 EYLALKSTLD--KVNQTMLNYHNLTQQWRQEAADREHQyKEHVKECQAQIAILRVENQELKRDLETKIEQIEgvhtirlK 197
Cdd:COG1196 214 RYRELKEELKelEAELLLLKLRELEAELEELEAELEEL-EAELEELEAELAELEAELEELRLELEELELELE-------E 285

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 198 EQDELRKSVSEKQSLIDNMRVEIDKLKQLnhsfefvpeyatesksQELIKKMQLDINELKARDIQKQEVIKGLQIQNDIY 277
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRREL----------------EERLEELEEELAELEEELEELEEELEELEEELEEA 349

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 48428492 278 RRDFEMERADREKNAGEKDQYLMDLRSLQRRNQELIEALAE 318
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 146-344 6.16e-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: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492    146 RQ-EAADREHQYKEHVKECQAQIAILRVENQELKRD----------------------LETKIEQIEGVHTIRLKEQDEL 202
Cdd:TIGR02168  207 RQaEKAERYKELKAELRELELALLVLRLEELREELEelqeelkeaeeeleeltaelqeLEEKLEELRLEVSELEEEIEEL 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492    203 RKSVSEKQSLIDNMRVEI----DKLKQLNHSFEFVPEYATESKSQELIKKMQLdiNELKARDIQKQEVIKGLQIQNDiyr 278
Cdd:TIGR02168  287 QKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELAEEL--AELEEKLEELKEELESLEAELE--- 361

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 48428492    279 rDFEMERADREKNAGEKDQYLMDLRSlqRRNQELIEALAESHKASKACSTASPLSSSRSNLREEQR 344
Cdd:TIGR02168  362 -ELEAELEELESRLEELEEQLETLRS--KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 230-313 9.50e-25

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 96.65  E-value: 9.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 230 FEFVPEYATESKSQELIKKMQLDINELKARDIQKQ---EVIKGLQIQNDIYRRDFEMERADREKNAGEKDQYLMDLRSLQ 306
Cdd:cd09803   1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEadlETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                ....*..
gi 48428492 307 RRNQELI 313
Cdd:cd09803  81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 244-313 9.28e-16

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 72.32  E-value: 9.28e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48428492   244 ELIKKMQLDINELKARDIQKQ---EVIKGLQIQNDIYRRDFEMERADREKNAGEKDQYLMDLRSLQRRNQELI 313
Cdd:pfam16516  28 EALAAKQREIDELKQEIAQKEedlETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQQLK 100
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-318 1.82e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 120 EYLALKSTLD--KVNQTMLNYHNLTQQWRQEAADREHQyKEHVKECQAQIAILRVENQELKRDLETKIEQIEgvhtirlK 197
Cdd:COG1196 214 RYRELKEELKelEAELLLLKLRELEAELEELEAELEEL-EAELEELEAELAELEAELEELRLELEELELELE-------E 285

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 198 EQDELRKSVSEKQSLIDNMRVEIDKLKQLnhsfefvpeyatesksQELIKKMQLDINELKARDIQKQEVIKGLQIQNDIY 277
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRREL----------------EERLEELEEELAELEEELEELEEELEELEEELEEA 349

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 48428492 278 RRDFEMERADREKNAGEKDQYLMDLRSLQRRNQELIEALAE 318
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 146-325 1.28e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 146 RQ-EAADREHQYKEHVKECQAQIAILRVENQELKRD-LETKIEQIEGVHTIRLKEQDELRKSVSEKQSLIDNMRVEIDKL 223
Cdd:COG1196 207 RQaEKAERYRELKEELKELEAELLLLKLRELEAELEeLEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 224 KQLnhsfefvpEYATESKSQELIKkmqlDINELKARDIQKQEVIKGLQIQNDIYRRDFEMERADREKNAGEKDQYLMDLR 303
Cdd:COG1196 287 QAE--------EYELLAELARLEQ----DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                       170       180
                ....*....|....*....|..
gi 48428492 304 SLQRRNQELIEALAESHKASKA 325
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAE 376
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
155-261 3.27e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 3.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 155 QYKEHVKECQAQIAILRVENQELKRDLETKIEQIEG----VHTIRLKEQDE----------------LRKSVSEKQSLID 214
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERlereLSEARSEERREirkdreisrldreierLERELEEERERIE 489

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 48428492 215 NMRVEIDKLKQLN---HSFEFVPEYATESKSQELIKKMQlDINELKARDI 261
Cdd:COG2433 490 ELKRKLERLKELWkleHSGELVPVKVVEKFTKEAIRRLE-EEYGLKEGDV 538
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 146-344 6.16e-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: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492    146 RQ-EAADREHQYKEHVKECQAQIAILRVENQELKRD----------------------LETKIEQIEGVHTIRLKEQDEL 202
Cdd:TIGR02168  207 RQaEKAERYKELKAELRELELALLVLRLEELREELEelqeelkeaeeeleeltaelqeLEEKLEELRLEVSELEEEIEEL 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492    203 RKSVSEKQSLIDNMRVEI----DKLKQLNHSFEFVPEYATESKSQELIKKMQLdiNELKARDIQKQEVIKGLQIQNDiyr 278
Cdd:TIGR02168  287 QKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELAEEL--AELEEKLEELKEELESLEAELE--- 361

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 48428492    279 rDFEMERADREKNAGEKDQYLMDLRSlqRRNQELIEALAESHKASKACSTASPLSSSRSNLREEQR 344
Cdd:TIGR02168  362 -ELEAELEELESRLEELEEQLETLRS--KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 148-340 4.35e-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: 38.98  E-value: 4.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 148 EAADREHQYKEHVKECQAQIAILRVENQELKRDLETKIEQIEGVhtirlkeqdeLRKSVSEKQSLIDNMRVEIDKLKQLN 227
Cdd:COG4942  66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL----------LRALYRLGRQPPLALLLSPEDFLDAV 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 228 HSFEFVPEYATESKSQ-ELIKKMQLDINELKARDIQKQEVIKGLQIQNDIYRRDFEMERADR-------EKNAGEKDQYL 299
Cdd:COG4942 136 RRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERqkllarlEKELAELAAEL 215

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 48428492 300 MDLRSLQRRNQELIEALAESHKASKACSTASPLSSSRSNLR 340
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 143-321 7.17e-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: 38.50  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492    143 QQWRQEAADREHQYKEHVKECQAQIAILRVENQELKRDLETKIEQIEGVHTIRLKEQDELRKSVSEKQSLIDNMRVEIDK 222
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492    223 LKQLNHSFEFVPEYATESKSQelIKKMQLDINELKARDIQKQEVIKGLQIQNDIYRRDFEMERADR---EKNAGEKDQYL 299
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAE--IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELrelESKRSELRREL 917

                          170       180       190
                   ....*....|....*....|....*....|...
gi 48428492    300 -----------MDLRSLQRRNQELIEALAESHK 321
Cdd:TIGR02168  918 eelreklaqleLRLEGLEVRIDNLQERLSEEYS 950
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
148-290 8.37e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.58  E-value: 8.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492 148 EAADREHQYKEHVKECQAQIAILRVENQELKRDLETKIEQIEGVHTIRL---KEQDELRKSVSEKQSLIDNMRVEIDKLK 224
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIelyKEADELRKEADELHKEIVEAQEKADELH 229

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 48428492 225 qlnhsfefvpeyatesksqELIKKMQLDINELkardiqkQEVIKGLQIQNDIYRRDFEMERADREK 290
Cdd:COG1340 230 -------------------EEIIELQKELREL-------RKELKKLRKKQRALKREKEKEELEEKA 269
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-320 9.29e-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: 9.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492    140 NLTQQWRQEAADREhQYKEHVKECQAQIAILRVENQELKR---DLETKIEQIEGVHTIRLKEQDELRKSVSEKQSLIDNM 216
Cdd:TIGR02168  744 QLEERIAQLSKELT-ELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48428492    217 RVEIDKLKQLNHSFEFVPEYATESKSQ--ELIKKMQLDINELKARDIQKQEVIKGLQIQNDIYRRDFEMERADREKNAGE 294
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEElsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          170       180
                   ....*....|....*....|....*.
gi 48428492    295 KDQYLMDLRSLQRRNQELIEALAESH 320
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLE 928
 
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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