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Conserved domains on  [gi|1958770322|ref|XP_038963825|]
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non-homologous end joining factor IFFO1 isoform X3 [Rattus norvegicus]

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
232-427 5.43e-16

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 78.42  E-value: 5.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 232 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMS 311
Cdd:pfam00038  62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHE 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 312 NNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ------RNCEDVIQMFQ-------------------------- 359
Cdd:pfam00038 142 EEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQyeeiaaKNREEAEEWYQskleelqqaaarngdalrsakeeite 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 360 -----------------QEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKSDMNRHLHEYMEMCSMKRGLDVQME 422
Cdd:pfam00038 222 lrrtiqsleielqslkkQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIA 301

                  ....*
gi 1958770322 423 TCRRL 427
Cdd:pfam00038 302 TYRKL 306
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
232-427 5.43e-16

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 78.42  E-value: 5.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 232 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMS 311
Cdd:pfam00038  62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHE 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 312 NNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ------RNCEDVIQMFQ-------------------------- 359
Cdd:pfam00038 142 EEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQyeeiaaKNREEAEEWYQskleelqqaaarngdalrsakeeite 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 360 -----------------QEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKSDMNRHLHEYMEMCSMKRGLDVQME 422
Cdd:pfam00038 222 lrrtiqsleielqslkkQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIA 301

                  ....*
gi 1958770322 423 TCRRL 427
Cdd:pfam00038 302 TYRKL 306
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
232-410 1.63e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  232 QIDTITPEIRALYNVLAKVKRERDEYKRRWE------EEYTVRIQ-LQERVTELQEEAQEADACQEELAMKVEQLKAELV 304
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAqlskelTELEAEIEeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  305 VFK---GLMSNNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ--RNCEDVI----QMFQQEDSLEKVIKDTESLF 375
Cdd:TIGR02168  800 ALRealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieELSEDIEslaaEIEELEELIEELESELEALL 879
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958770322  376 KTREKEyQETIDQIELELATAKSDMNRHLHEYMEM 410
Cdd:TIGR02168  880 NERASL-EEALALLRSELEELSEELRELESKRSEL 913
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
232-406 2.22e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  232 QIDTITPeIRALYNVLAKVKRERDEYKR-----RWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVF 306
Cdd:COG4913    250 QIELLEP-IRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  307 KGLMSNN-----------LTELDTKIQEKAMKVD--MDICRRIDITAKLCDLAQQRNCEDVIQMFQQEDSLEKVIKDTES 373
Cdd:COG4913    329 EAQIRGNggdrleqlereIERLERELEERERRRArlEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958770322  374 LFKTREKEYQETIDQIELELA---TAKSDMNRHLHE 406
Cdd:COG4913    409 EAEAALRDLRRELRELEAEIAsleRRKSNIPARLLA 444
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
232-427 5.43e-16

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 78.42  E-value: 5.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 232 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMS 311
Cdd:pfam00038  62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHE 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 312 NNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ------RNCEDVIQMFQ-------------------------- 359
Cdd:pfam00038 142 EEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQyeeiaaKNREEAEEWYQskleelqqaaarngdalrsakeeite 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 360 -----------------QEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKSDMNRHLHEYMEMCSMKRGLDVQME 422
Cdd:pfam00038 222 lrrtiqsleielqslkkQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIA 301

                  ....*
gi 1958770322 423 TCRRL 427
Cdd:pfam00038 302 TYRKL 306
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
232-410 1.63e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  232 QIDTITPEIRALYNVLAKVKRERDEYKRRWE------EEYTVRIQ-LQERVTELQEEAQEADACQEELAMKVEQLKAELV 304
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAqlskelTELEAEIEeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  305 VFK---GLMSNNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ--RNCEDVI----QMFQQEDSLEKVIKDTESLF 375
Cdd:TIGR02168  800 ALRealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieELSEDIEslaaEIEELEELIEELESELEALL 879
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958770322  376 KTREKEyQETIDQIELELATAKSDMNRHLHEYMEM 410
Cdd:TIGR02168  880 NERASL-EEALALLRSELEELSEELRELESKRSEL 913
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
232-406 2.22e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  232 QIDTITPeIRALYNVLAKVKRERDEYKR-----RWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVF 306
Cdd:COG4913    250 QIELLEP-IRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  307 KGLMSNN-----------LTELDTKIQEKAMKVD--MDICRRIDITAKLCDLAQQRNCEDVIQMFQQEDSLEKVIKDTES 373
Cdd:COG4913    329 EAQIRGNggdrleqlereIERLERELEERERRRArlEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958770322  374 LFKTREKEYQETIDQIELELA---TAKSDMNRHLHE 406
Cdd:COG4913    409 EAEAALRDLRRELRELEAEIAsleRRKSNIPARLLA 444
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
231-402 3.78e-04

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: 43.13  E-value: 3.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  231 VQIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELvvfkglm 310
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI------- 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  311 sNNLTELDTKIQEKAMKVDMDICR-RIDITAKLCDLAQ-QRNCEDVI-QMFQQEDSLEKVIKDTESLfktrEKEY---QE 384
Cdd:TIGR02169  402 -NELKRELDRLQEELQRLSEELADlNAAIAGIEAKINElEEEKEDKAlEIKKQEWKLEQLAADLSKY----EQELydlKE 476
                          170
                   ....*....|....*...
gi 1958770322  385 TIDQIELELATAKSDMNR 402
Cdd:TIGR02169  477 EYDRVEKELSKLQRELAE 494
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
232-406 4.18e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 232 QIDTitpEIRALYNVLAKVKRERDEYKRRWEEeytvriqLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMS 311
Cdd:COG1579    14 ELDS---ELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 312 N--NLTELDTKIQEkamkvdmdicrrIDITAKlcdlaQQRNCEDVI-QMFQQEDSLEKVIKDTESLFKTREKEYQETIDQ 388
Cdd:COG1579    84 NvrNNKEYEALQKE------------IESLKR-----RISDLEDEIlELMERIEELEEELAELEAELAELEAELEEKKAE 146
                         170
                  ....*....|....*...
gi 1958770322 389 IELELATAKSDMNRHLHE 406
Cdd:COG1579   147 LDEELAELEAELEELEAE 164
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
225-410 5.37e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.53  E-value: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 225 HPDGVGVQIDTITPEIRALYNVLAKVKRERDEYKRRWEEeytvriqLQERVTELQEEAQEAdacQEELamkvEQLKA--- 301
Cdd:pfam06160 257 ELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPE-------IEDYLEHAEEQNKEL---KEEL----ERVQQsyt 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 302 ----ELVVFKGL------MSNNLTELDTKIQEKAMkvdmdicRRIDITAKLCDLAQQrnCEDViqmfqqEDSLEKVIKDT 371
Cdd:pfam06160 323 lnenELERVRGLekqleeLEKRYDEIVERLEEKEV-------AYSELQEELEEILEQ--LEEI------EEEQEEFKESL 387
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958770322 372 ESLFKTrEKEYQETIDQIELELATAKSDM-NRHL----HEYMEM 410
Cdd:pfam06160 388 QSLRKD-ELEAREKLDEFKLELREIKRLVeKSNLpglpESYLDY 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
232-403 5.62e-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: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  232 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKglms 311
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE---- 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  312 NNLTELDTKIQEKAMKVDmDICRRIDITAklcdlAQQRNCEDVIQmfQQEDSLEKVIKDTESLFKTRE----KEYQETID 387
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVA-QLELQIASLN-----NEIERLEARLE--RLEDRRERLQQEIEELLKKLEeaelKELQAELE 443
                          170
                   ....*....|....*.
gi 1958770322  388 QIELELATAKSDMNRH 403
Cdd:TIGR02168  444 ELEEELEELQEELERL 459
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
246-406 3.38e-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: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  246 VLAKVKRERDEYKRRWEEEYTvriQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLM---SNNLTELDTKIQ 322
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELK---EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalANEISRLEQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322  323 EKAMKVDMDICRRIDITAKLCDLAQQRNC--EDVIQMFQQEDSLEKVIKDTESLFKTREKEYQE---TIDQIELELATAK 397
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDElaEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLR 385

                   ....*....
gi 1958770322  398 SDMNRHLHE 406
Cdd:TIGR02168  386 SKVAQLELQ 394
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
232-390 7.23e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 232 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEaqeadacQEELAMKVEQLKAELvvfkglms 311
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK-------ISSLKEKIEKLESEK-------- 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 312 nnlTELDTKIQEKAMKVDMDicrriDITAKLCDLaqqrncEDVIQMFQQE--------DSLEKVIKDTESLFKTREKEYQ 383
Cdd:TIGR04523 534 ---KEKESKISDLEDELNKD-----DFELKKENL------EKEIDEKNKEieelkqtqKSLKKKQEEKQELIDQKEKEKK 599

                  ....*..
gi 1958770322 384 ETIDQIE 390
Cdd:TIGR04523 600 DLIKEIE 606
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
232-430 8.76e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.97  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 232 QIDTITPEIRALYNVLAKVKRERDEYKRR---WEEE----YTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAElv 304
Cdd:COG1340     2 KTDELSSSLEELEEKIEELREEIEELKEKrdeLNEElkelAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770322 305 vfkglmsnnLTELDTKIQEKAMKVDmdicrriDITAKLCDLAQQRNCEDVIQmfQQEDSLEKVIkDTESLFKTREKEYQE 384
Cdd:COG1340    80 ---------RDELNEKLNELREELD-------ELRKELAELNKAGGSIDKLR--KEIERLEWRQ-QTEVLSPEEEKELVE 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958770322 385 TIDQIELELATAKsDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQ 430
Cdd:COG1340   141 KIKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKE 185
 
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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