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Conserved domains on  [gi|1907067521|ref|XP_036018307|]
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leucine-rich repeat flightless-interacting protein 1 isoform X16 [Mus musculus]

Protein Classification

leucine-rich repeat flightless-interacting protein( domain architecture ID 12101455)

leucine-rich repeat flightless-interacting protein (LRRFIP) similar to human LRRFIP2 that may function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
175-442 8.81e-107

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


:

Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 320.88  E-value: 8.81e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 175 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSN 245
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 246 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKHGIILNSE 325
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKHGLVIVPD 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 326 IATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKLDLLRAE 403
Cdd:pfam09738 190 ENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPD 266
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907067521 404 DGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 442
Cdd:pfam09738 267 GFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
DUF3450 super family cl26418
Protein of unknown function (DUF3450); This family of proteins are functionally ...
458-517 8.81e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


The actual alignment was detected with superfamily member pfam11932:

Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 37.98  E-value: 8.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 458 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 517
Cdd:pfam11932  27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
175-442 8.81e-107

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 320.88  E-value: 8.81e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 175 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSN 245
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 246 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKHGIILNSE 325
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKHGLVIVPD 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 326 IATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKLDLLRAE 403
Cdd:pfam09738 190 ENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPD 266
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907067521 404 DGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 442
Cdd:pfam09738 267 GFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
197-516 2.19e-05

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: 47.36  E-value: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  197 ATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 276
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  277 QRQYEEKNKEFER-----EKHAHSILQFQFaEVKEALRQREEMLEKHGIiLNSEIATNGETSDTVNDV--GYQAPTKITK 349
Cdd:TIGR02168  725 SRQISALRKDLARleaevEQLEERIAQLSK-ELTELEAEIEELEERLEE-AEEELAEAEAEIEELEAQieQLKEELKALR 802
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  350 EELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKldllRAEDGILEngtdahvmdlqrdANRQISDL 429
Cdd:TIGR02168  803 EALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE----ELSEDIES-------------LAAEIEEL 864
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  430 KFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKAN 509
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLELRLEGLEVR 937

                   ....*..
gi 1907067521  510 RSALLSQ 516
Cdd:TIGR02168  938 IDNLQER 944
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
362-491 8.31e-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: 41.06  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 362 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 428
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067521 429 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 491
Cdd:COG1579    94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
219-409 5.15e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.53  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 219 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlleleeqlaesqrQYEEKNKEFEREKHAHSILQ 298
Cdd:PRK05771   83 SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE---------------PWGNFDLDLSLLLGFKYVSV 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 299 FqFAEVKEALrqrEEMLEKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELN-----ALKSAGEGTLDVRLKKLIDE 373
Cdd:PRK05771  148 F-VGTVPEDK---LEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKklgfeRLELEEEGTPSELIREIKEE 223
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907067521 374 RECLLEQIKKLKGQLEgrQKNNKL-DLLRAEDGILEN 409
Cdd:PRK05771  224 LEEIEKERESLLEELK--ELAKKYlEELLALYEYLEI 258
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
458-517 8.81e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 37.98  E-value: 8.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 458 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 517
Cdd:pfam11932  27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
175-442 8.81e-107

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 320.88  E-value: 8.81e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 175 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSN 245
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 246 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKHGIILNSE 325
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKHGLVIVPD 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 326 IATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKLDLLRAE 403
Cdd:pfam09738 190 ENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPD 266
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907067521 404 DGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 442
Cdd:pfam09738 267 GFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
197-516 2.19e-05

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: 47.36  E-value: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  197 ATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 276
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  277 QRQYEEKNKEFER-----EKHAHSILQFQFaEVKEALRQREEMLEKHGIiLNSEIATNGETSDTVNDV--GYQAPTKITK 349
Cdd:TIGR02168  725 SRQISALRKDLARleaevEQLEERIAQLSK-ELTELEAEIEELEERLEE-AEEELAEAEAEIEELEAQieQLKEELKALR 802
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  350 EELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKldllRAEDGILEngtdahvmdlqrdANRQISDL 429
Cdd:TIGR02168  803 EALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE----ELSEDIES-------------LAAEIEEL 864
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  430 KFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKAN 509
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLELRLEGLEVR 937

                   ....*..
gi 1907067521  510 RSALLSQ 516
Cdd:TIGR02168  938 IDNLQER 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
225-516 2.57e-05

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: 46.98  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  225 REIKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEV 304
Cdd:TIGR02169  670 RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  305 KEALRQREEMLEKhgiiLNSEIATNGETSDTvndvgYQAPTKITKEELNALKSAgegTLDVRLKKLIDERECLLEQIKKL 384
Cdd:TIGR02169  743 EEDLSSLEQEIEN----VKSELKELEARIEE-----LEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRI 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  385 KGQL-EGRQKNNKLDLLRAedgILEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAEN 463
Cdd:TIGR02169  811 EARLrEIEQKLNRLTLEKE---YLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907067521  464 AEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 516
Cdd:TIGR02169  880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
219-492 4.20e-05

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: 46.59  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  219 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQ 298
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  299 FQFAEVKEALRQREEMLEKHGIILNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEgTLDVRLKKLIDERECLL 378
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIE-ELEELIEELESELEALL 879
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  379 EQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqisdLKFKLAKSEQEITALEQNVIRLESQVT-RY 457
Cdd:TIGR02168  880 NERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSeEY 949
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907067521  458 RSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 492
Cdd:TIGR02168  950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
362-491 8.31e-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: 41.06  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 362 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 428
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067521 429 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 491
Cdd:COG1579    94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
346-517 1.06e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 346 KITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKL------KGQLEGRQKNNKLDLLRAEDGILENGTDAHVMDLQ 419
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaeLARLEQDIARLEERRRELEERLEELEEELAELEEE 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 420 R-DANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGH 498
Cdd:COG1196   332 LeELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
                         170
                  ....*....|....*....
gi 1907067521 499 LVKRLEKMKANRSALLSQQ 517
Cdd:COG1196   412 LLERLERLEEELEELEEAL 430
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
277-517 1.27e-03

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: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 277 QRQYEEKNKEFEREKHAHSILQFQFAEVKEALR---QREEMLEKHGIILNSEIATNGETSDTVNDvgyqapTKITKEELN 353
Cdd:COG1196   259 EAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEE------ELAELEEEL 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 354 ALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENgtDAHVMDLQRDANRQISDLKFKL 433
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAE 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 434 AKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 513
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489

                  ....
gi 1907067521 514 LSQQ 517
Cdd:COG1196   490 AARL 493
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
367-508 1.64e-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: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  367 LKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTD----------------AHVMDLQRDANRQISDLK 430
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrleqlereierlerelEERERRRARLEALLAALG 372
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067521  431 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEkieDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 508
Cdd:COG4913    373 LPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
299-513 3.10e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 299 FQFAEVKEALRQREEMLEKHGIILNSEIATNGETSDTVNDVGYQAPTKI--TKEELNALKsAGEGTLDVRLKKLIDEREC 376
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaaLARRIRALE-QELAALEAELAELEKEIAE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 377 LLEQIKKLKGQLEGR----QKNNKLDLLRaedgILENGTDAhvmdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLES 452
Cdd:COG4942    95 LRAELEAQKEELAELlralYRLGRQPPLA----LLLSPEDF------LDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067521 453 QVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 513
Cdd:COG4942   165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
219-409 5.15e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.53  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 219 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlleleeqlaesqrQYEEKNKEFEREKHAHSILQ 298
Cdd:PRK05771   83 SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE---------------PWGNFDLDLSLLLGFKYVSV 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 299 FqFAEVKEALrqrEEMLEKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELN-----ALKSAGEGTLDVRLKKLIDE 373
Cdd:PRK05771  148 F-VGTVPEDK---LEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKklgfeRLELEEEGTPSELIREIKEE 223
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907067521 374 RECLLEQIKKLKGQLEgrQKNNKL-DLLRAEDGILEN 409
Cdd:PRK05771  224 LEEIEKERESLLEELK--ELAKKYlEELLALYEYLEI 258
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
346-517 5.22e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.65  E-value: 5.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  346 KITKEELNALKSAGEGTLDVRLKKLIDEREcllEQIKKLKGQL--EGRQKNNKLDLLRA-EDGIlengtdAHVMDLQRDA 422
Cdd:PRK10929    79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLleKSRQAQQEQDRAREiSDSL------SQLPQQQTEA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  423 NRQISDLKFKL--------AKSEQEITALEQNVIRLESQVTRY--------------RSAAENAEKIEDELKAEKRKL-- 478
Cdd:PRK10929   150 RRQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELelaqlsannrqelaRLRSELAKKRSQQLDAYLQALrn 229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907067521  479 ------QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 517
Cdd:PRK10929   230 qlnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
353-517 7.80e-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: 39.27  E-value: 7.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  353 NALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEG--RQKNN---KLDLLRAEDGILENGTDAHVMDLQ------RD 421
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEELKEAEEELEEltAELQEleeKLEELRLEVSELEEEIEELQKELYalaneiSR 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521  422 ANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVK 501
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
                          170
                   ....*....|....*.
gi 1907067521  502 RLEKMKANRSALLSQQ 517
Cdd:TIGR02168  380 QLETLRSKVAQLELQI 395
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
458-517 8.81e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 37.98  E-value: 8.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067521 458 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 517
Cdd:pfam11932  27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
 
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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