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Conserved domains on  [gi|1907067527|ref|XP_036018321|]
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leucine-rich repeat flightless-interacting protein 1 isoform X23 [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 ...
52-375 1.06e-105

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: 315.87  E-value: 1.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  52 MKELERQQKEtngydgdycgsqslsrrsgrpseygshlnsssrassrassaraspvVEERPDKDFAE---------KGSR 122
Cdd:pfam09738  20 MRELERQQKE----------------------------------------------VEENADRVFDMssssgadtaSGSP 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 123 NMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLEL 202
Cdd:pfam09738  54 TASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEM 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 203 EEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKHGIILNSEIATNGEtsdTVNDVGYQAPTKITK 282
Cdd:pfam09738 134 EESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKHGLVIVPDENTNGE---EENSPADAKRALVSV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 283 EELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQRDANRQIS 360
Cdd:pfam09738 211 EAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQIS 288
                         330
                  ....*....|....*
gi 1907067527 361 DLKFKLAKSEQEITA 375
Cdd:pfam09738 289 DYKFKLQKAEQEITT 303
DUF3450 super family cl26418
Protein of unknown function (DUF3450); This family of proteins are functionally ...
391-450 9.04e-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: 37.60  E-value: 9.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 391 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 450
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 ...
52-375 1.06e-105

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: 315.87  E-value: 1.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  52 MKELERQQKEtngydgdycgsqslsrrsgrpseygshlnsssrassrassaraspvVEERPDKDFAE---------KGSR 122
Cdd:pfam09738  20 MRELERQQKE----------------------------------------------VEENADRVFDMssssgadtaSGSP 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 123 NMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLEL 202
Cdd:pfam09738  54 TASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEM 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 203 EEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKHGIILNSEIATNGEtsdTVNDVGYQAPTKITK 282
Cdd:pfam09738 134 EESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKHGLVIVPDENTNGE---EENSPADAKRALVSV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 283 EELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQRDANRQIS 360
Cdd:pfam09738 211 EAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQIS 288
                         330
                  ....*....|....*
gi 1907067527 361 DLKFKLAKSEQEITA 375
Cdd:pfam09738 289 DYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
181-449 5.68e-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: 45.83  E-value: 5.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  181 LDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKhgiiLNSEIA 260
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----VKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  261 TNGETSDTvndvgYQAPTKITKEELNALKSAgegTLDVRLKKLIDERECLLEQIKKLKGQL-EGRQKNNKLDLLRAedgI 339
Cdd:TIGR02169  762 ELEARIEE-----LEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKE---Y 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  340 LEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSAL 419
Cdd:TIGR02169  831 LE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
                          250       260       270
                   ....*....|....*....|....*....|
gi 1907067527  420 DKTEELEVSNGHLVKRLEKMKANRSALLSQ 449
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEE 932
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
300-441 1.65e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  300 LKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTD----------------AHVMDLQRDANRQISDLK 363
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrleqlereierlerelEERERRRARLEALLAALG 372
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067527  364 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEkieDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 441
Cdd:COG4913    373 LPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
279-450 5.21e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.27  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  279 KITKEELNALKSAGEGTLDVRLKKLIDEREcllEQIKKLKGQL--EGRQKNNKLDLLRA-EDGIlengtdAHVMDLQRDA 355
Cdd:PRK10929    79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLleKSRQAQQEQDRAREiSDSL------SQLPQQQTEA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  356 NRQISDLKFKL--------AKSEQEITALEQNVIRLESQVTRY--------------RSAAENAEKIEDELKAEKRKL-- 411
Cdd:PRK10929   150 RRQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELelaqlsannrqelaRLRSELAKKRSQQLDAYLQALrn 229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907067527  412 ------QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 450
Cdd:PRK10929   230 qlnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
391-450 9.04e-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: 37.60  E-value: 9.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 391 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 450
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 ...
52-375 1.06e-105

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: 315.87  E-value: 1.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  52 MKELERQQKEtngydgdycgsqslsrrsgrpseygshlnsssrassrassaraspvVEERPDKDFAE---------KGSR 122
Cdd:pfam09738  20 MRELERQQKE----------------------------------------------VEENADRVFDMssssgadtaSGSP 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 123 NMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLEL 202
Cdd:pfam09738  54 TASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEM 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 203 EEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKHGIILNSEIATNGEtsdTVNDVGYQAPTKITK 282
Cdd:pfam09738 134 EESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKHGLVIVPDENTNGE---EENSPADAKRALVSV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 283 EELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQRDANRQIS 360
Cdd:pfam09738 211 EAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQIS 288
                         330
                  ....*....|....*
gi 1907067527 361 DLKFKLAKSEQEITA 375
Cdd:pfam09738 289 DYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
181-449 5.68e-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: 45.83  E-value: 5.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  181 LDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKhgiiLNSEIA 260
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----VKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  261 TNGETSDTvndvgYQAPTKITKEELNALKSAgegTLDVRLKKLIDERECLLEQIKKLKGQL-EGRQKNNKLDLLRAedgI 339
Cdd:TIGR02169  762 ELEARIEE-----LEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKE---Y 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  340 LEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSAL 419
Cdd:TIGR02169  831 LE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
                          250       260       270
                   ....*....|....*....|....*....|
gi 1907067527  420 DKTEELEVSNGHLVKRLEKMKANRSALLSQ 449
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
130-449 8.17e-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: 45.05  E-value: 8.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  130 ATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 209
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  210 QRQYEEKNKEFEREKHAHSILQFQFA----EVKEALRQREEMLEKHGIiLNSEIATNGETSDTVNDV--GYQAPTKITKE 283
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAqlskELTELEAEIEELEERLEE-AEEELAEAEAEIEELEAQieQLKEELKALRE 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  284 ELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKldllRAEDGILEngtdahvmdlqrdANRQISDLK 363
Cdd:TIGR02168  804 ALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE----ELSEDIES-------------LAAEIEELE 865
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  364 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANR 443
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLELRLEGLEVRI 938

                   ....*.
gi 1907067527  444 SALLSQ 449
Cdd:TIGR02168  939 DNLQER 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
152-425 1.05e-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: 45.05  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  152 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQ 231
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  232 FQFAEVKEALRQREEMLEKHGIILNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEgTLDVRLKKLIDERECLL 311
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIE-ELEELIEELESELEALL 879
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  312 EQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqisdLKFKLAKSEQEITALEQNVIRLESQVT-RY 390
Cdd:TIGR02168  880 NERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSeEY 949
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907067527  391 RSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 425
Cdd:TIGR02168  950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
300-441 1.65e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  300 LKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTD----------------AHVMDLQRDANRQISDLK 363
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrleqlereierlerelEERERRRARLEALLAALG 372
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067527  364 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEkieDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 441
Cdd:COG4913    373 LPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
279-450 1.88e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 279 KITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKL------KGQLEGRQKNNKLDLLRAEDGILENGTDAHVMDLQ 352
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaeLARLEQDIARLEERRRELEERLEELEEELAELEEE 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 353 R-DANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGH 431
Cdd:COG1196   332 LeELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
                         170
                  ....*....|....*....
gi 1907067527 432 LVKRLEKMKANRSALLSQQ 450
Cdd:COG1196   412 LLERLERLEEELEELEEAL 430
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
295-424 2.67e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 295 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 361
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067527 362 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 424
Cdd:COG1579    94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
210-450 2.74e-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: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 210 QRQYEEKNKEFEREKHAHSILQFQFAEVKEALR---QREEMLEKHGIILNSEIATNGETSDTVNDvgyqapTKITKEELN 286
Cdd:COG1196   259 EAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEE------ELAELEEEL 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 287 ALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENgtDAHVMDLQRDANRQISDLKFKL 366
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAE 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 367 AKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 446
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489

                  ....
gi 1907067527 447 LSQQ 450
Cdd:COG1196   490 AARL 493
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
279-450 5.21e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.27  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  279 KITKEELNALKSAGEGTLDVRLKKLIDEREcllEQIKKLKGQL--EGRQKNNKLDLLRA-EDGIlengtdAHVMDLQRDA 355
Cdd:PRK10929    79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLleKSRQAQQEQDRAREiSDSL------SQLPQQQTEA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527  356 NRQISDLKFKL--------AKSEQEITALEQNVIRLESQVTRY--------------RSAAENAEKIEDELKAEKRKL-- 411
Cdd:PRK10929   150 RRQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELelaqlsannrqelaRLRSELAKKRSQQLDAYLQALrn 229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907067527  412 ------QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 450
Cdd:PRK10929   230 qlnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
152-342 5.77e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 152 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlleleeqlaesqrQYEEKNKEFEREKHAHSILQ 231
Cdd:PRK05771   83 SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE---------------PWGNFDLDLSLLLGFKYVSV 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 232 FqFAEVKEALrqrEEMLEKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELN-----ALKSAGEGTLDVRLKKLIDE 306
Cdd:PRK05771  148 F-VGTVPEDK---LEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKklgfeRLELEEEGTPSELIREIKEE 223
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907067527 307 RECLLEQIKKLKGQLEgrQKNNKL-DLLRAEDGILEN 342
Cdd:PRK05771  224 LEEIEKERESLLEELK--ELAKKYlEELLALYEYLEI 258
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
232-446 6.29e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 232 FQFAEVKEALRQREEMLEKHGIILNSEIATNGETSDTVNDVGYQAPTKI--TKEELNALKsAGEGTLDVRLKKLIDEREC 309
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaaLARRIRALE-QELAALEAELAELEKEIAE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 310 LLEQIKKLKGQLEGR----QKNNKLDLLRaedgILENGTDAhvmdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLES 385
Cdd:COG4942    95 LRAELEAQKEELAELlralYRLGRQPPLA----LLLSPEDF------LDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067527 386 QVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 446
Cdd:COG4942   165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
391-450 9.04e-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: 37.60  E-value: 9.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067527 391 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 450
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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