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Conserved domains on  [gi|519666775|ref|NP_001265535|]
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filensin isoform 3 [Homo sapiens]

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
5-174 8.21e-05

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 44.53  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775    5 LNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQTYISILQQIIHTTPPASI-VTSGMREEKLLTEREVAALR 83
Cdd:pfam00038 108 LRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLdLTSALAEIRAQYEEIAAKNR 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775   84 SQLEEgrevlsHLQAQRVELQAQTTTLEQAIKSAHEcyddEIQLYNEQIETLRKEIEE---TERVLEkssydcRQLAVAQ 160
Cdd:pfam00038 188 EEAEE------WYQSKLEELQQAAARNGDALRSAKE----EITELRRTIQSLEIELQSlkkQKASLE------RQLAETE 251
                         170
                  ....*....|....
gi 519666775  161 QTLKNELDRYHRII 174
Cdd:pfam00038 252 ERYELQLADYQELI 265
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
5-174 8.21e-05

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 44.53  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775    5 LNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQTYISILQQIIHTTPPASI-VTSGMREEKLLTEREVAALR 83
Cdd:pfam00038 108 LRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLdLTSALAEIRAQYEEIAAKNR 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775   84 SQLEEgrevlsHLQAQRVELQAQTTTLEQAIKSAHEcyddEIQLYNEQIETLRKEIEE---TERVLEkssydcRQLAVAQ 160
Cdd:pfam00038 188 EEAEE------WYQSKLEELQQAAARNGDALRSAKE----EITELRRTIQSLEIELQSlkkQKASLE------RQLAETE 251
                         170
                  ....*....|....
gi 519666775  161 QTLKNELDRYHRII 174
Cdd:pfam00038 252 ERYELQLADYQELI 265
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
75-173 2.97e-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: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  75 TEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHEcyddEIQLYNEQIETLRKEIEETERVLEKSSydcR 154
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR----RIRALEQELAALEAELAELEKEIAELR---A 97
                         90
                 ....*....|....*....
gi 519666775 155 QLAVAQQTLKNELDRYHRI 173
Cdd:COG4942   98 ELEAQKEELAELLRALYRL 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-187 4.62e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775     1 MLERLNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKknllEVQTYISILQQIIHTtppASIVTSGMREEKLLTEREVA 80
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAAN---LRERLESLERRIAATERRLE 841
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775    81 ALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHECYD---DEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLA 157
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLRSELEELSEELRELESKRSELRRELEELR 921
                          170       180       190
                   ....*....|....*....|....*....|
gi 519666775   158 VAQQTLKNELDRyhriIEIEGNRLTSAFIE 187
Cdd:TIGR02168  922 EKLAQLELRLEG----LEVRIDNLQERLSE 947
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
69-168 6.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 6.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  69 REEKLLTEReVAALRSQLEEGREVLSHLQAQRvELQAQTTTLEQAIKSAHECYDDEIQLYNEQIETLRKEIEETERVLEK 148
Cdd:PRK02224 199 KEEKDLHER-LNGLESELAELDEEIERYEEQR-EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
                         90       100
                 ....*....|....*....|
gi 519666775 149 SSYDCRQLAVAQQTLKNELD 168
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERD 296
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
5-174 8.21e-05

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 44.53  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775    5 LNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQTYISILQQIIHTTPPASI-VTSGMREEKLLTEREVAALR 83
Cdd:pfam00038 108 LRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLdLTSALAEIRAQYEEIAAKNR 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775   84 SQLEEgrevlsHLQAQRVELQAQTTTLEQAIKSAHEcyddEIQLYNEQIETLRKEIEE---TERVLEkssydcRQLAVAQ 160
Cdd:pfam00038 188 EEAEE------WYQSKLEELQQAAARNGDALRSAKE----EITELRRTIQSLEIELQSlkkQKASLE------RQLAETE 251
                         170
                  ....*....|....
gi 519666775  161 QTLKNELDRYHRII 174
Cdd:pfam00038 252 ERYELQLADYQELI 265
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
75-173 2.97e-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: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  75 TEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHEcyddEIQLYNEQIETLRKEIEETERVLEKSSydcR 154
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR----RIRALEQELAALEAELAELEKEIAELR---A 97
                         90
                 ....*....|....*....
gi 519666775 155 QLAVAQQTLKNELDRYHRI 173
Cdd:COG4942   98 ELEAQKEELAELLRALYRL 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-168 4.47e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775   2 LERLNKEADEALLHnLRLQLEAQFLQDDISAAKDRHKKNLLEVqtyisiLQQIIHTtppASIVTSGMREEKLLTEREVAA 81
Cdd:COG1196  202 LEPLERQAEKAERY-RELKEELKELEAELLLLKLRELEAELEE------LEAELEE---LEAELEELEAELAELEAELEE 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  82 LRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHEcyddEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLAVAQQ 161
Cdd:COG1196  272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEE----RRRELEERLEELEEELAELEEELEELEEELEELEEELE 347

                 ....*..
gi 519666775 162 TLKNELD 168
Cdd:COG1196  348 EAEEELE 354
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-160 1.59e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775    2 LERLNKEADEallhnlrLQLEAQFLQDDISAAKDRHKknllEVQTYISILQQIihttppasiVTSGMREEKLL-TEREVA 80
Cdd:COG4913   612 LAALEAELAE-------LEEELAEAEERLEALEAELD----ALQERREALQRL---------AEYSWDEIDVAsAEREIA 671
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775   81 ALRSQ---LEEGREVLSHLQAQRVELQAQTTTLEQAIKSAhecyDDEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLA 157
Cdd:COG4913   672 ELEAElerLDASSDDLAALEEQLEELEAELEELEEELDEL----KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747

                  ...
gi 519666775  158 VAQ 160
Cdd:COG4913   748 RAL 750
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
75-180 2.38e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  75 TEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHECY------DDEIQLYNEQIETLRKEIEETERVLEK 148
Cdd:COG2433  411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEErreirkDREISRLDREIERLERELEEERERIEE 490
                         90       100       110
                 ....*....|....*....|....*....|..
gi 519666775 149 ssydcrqlavaqqtLKNELDRYHRIIEIEGNR 180
Cdd:COG2433  491 --------------LKRKLERLKELWKLEHSG 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-184 3.05e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775   2 LERLNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKKNLLEVQTyisilqqiihttppasivtsgMREEKLLTEREVAA 81
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE---------------------AQAEEYELLAELAR 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  82 LRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHEcyddEIQLYNEQIETLRKEIEETERVLEKSSydcRQLAVAQQ 161
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAE---EALLEAEA 372
                        170       180
                 ....*....|....*....|...
gi 519666775 162 TLKNELDRYHRIIEIEGNRLTSA 184
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAA 395
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
76-169 4.44e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  76 EREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAhecyDDEIQLYNEQIETLRKEIEETERVLEKSSYDCRQ 155
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
                         90
                 ....*....|....
gi 519666775 156 LAVAQQTLKNELDR 169
Cdd:COG1196  314 LEERLEELEEELAE 327
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
18-184 4.46e-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: 39.36  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  18 RLQLEAQFLQDDISAAKDRHKKNLLEVQTY--ISILQQIIHTTPPASIVTSGMREEKLltereVAALRSQLEEGREVLSH 95
Cdd:COG4942   87 ELEKEIAELRAELEAQKEELAELLRALYRLgrQPPLALLLSPEDFLDAVRRLQYLKYL-----APARREQAEELRADLAE 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  96 LQAQRVELQAQTTTLEQAI---KSAHECYDDEIQLYNEQIETLRKEIEETERVLEkssydcrQLAVAQQTLKNELDRYHR 172
Cdd:COG4942  162 LAALRAELEAERAELEALLaelEEERAALEALKAERQKLLARLEKELAELAAELA-------ELQQEAEELEALIARLEA 234
                        170
                 ....*....|..
gi 519666775 173 IIEIEGNRLTSA 184
Cdd:COG4942  235 EAAAAAERTPAA 246
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-187 4.62e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775     1 MLERLNKEADEALLHNLRLQLEAQFLQDDISAAKDRHKknllEVQTYISILQQIIHTtppASIVTSGMREEKLLTEREVA 80
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAAN---LRERLESLERRIAATERRLE 841
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775    81 ALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHECYD---DEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLA 157
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLRSELEELSEELRELESKRSELRRELEELR 921
                          170       180       190
                   ....*....|....*....|....*....|
gi 519666775   158 VAQQTLKNELDRyhriIEIEGNRLTSAFIE 187
Cdd:TIGR02168  922 EKLAQLELRLEG----LEVRIDNLQERLSE 947
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
76-175 4.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775   76 EREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAIKSAHEC-----YDDEIQLYNEQIETLRKEIEEtervLEKSS 150
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswDEIDVASAEREIAELEAELER----LDASS 684
                          90       100
                  ....*....|....*....|....*
gi 519666775  151 YDCRQLAVAQQTLKNELDRYHRIIE 175
Cdd:COG4913   685 DDLAALEEQLEELEAELEELEEELD 709
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
69-168 6.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 6.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775  69 REEKLLTEReVAALRSQLEEGREVLSHLQAQRvELQAQTTTLEQAIKSAHECYDDEIQLYNEQIETLRKEIEETERVLEK 148
Cdd:PRK02224 199 KEEKDLHER-LNGLESELAELDEEIERYEEQR-EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREE 276
                         90       100
                 ....*....|....*....|
gi 519666775 149 SSYDCRQLAVAQQTLKNELD 168
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERD 296
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
18-168 6.39e-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: 39.28  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775    18 RLQLEAQFLQDDISAAKDRhkknLLEVQTYISILQQiihttppasivtsgmreekllterEVAALRSQLEEGREVLSHLQ 97
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLKER----LEELEEDLSSLEQ------------------------EIENVKSELKELEARIEELE 771
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519666775    98 AQRVELQAQTTTLEQAI-KSAHECYDDEIQLYNEQIETLRKEIEETERVLEKSSYDCRQLAVAQQTLKNELD 168
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
69-175 8.35e-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: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519666775   69 REEKLLTEREVAALRSQLEEGREVLSHLQAQRVELQAQTTTLEQAI--KSAHECY-------------DDEIQLYNEQIE 133
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIaeleaelerldasSDDLAALEEQLE 695
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 519666775  134 TLRKEIEETERVLEKSSYDCRQLAVAQQTLKNELDRYHRIIE 175
Cdd:COG4913   696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
 
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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