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Conserved domains on  [gi|568908302|ref|XP_006529278|]
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leucine-rich repeat flightless-interacting protein 1 isoform X30 [Mus musculus]

Protein Classification

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 ...
42-319 4.38e-112

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: 330.12  E-value: 4.38e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   42 MKELERQQKEVEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVE 112
Cdd:pfam09738  20 MRELERQQKEVEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  113 EKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEML 192
Cdd:pfam09738 100 EKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  193 EKHGIILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--K 270
Cdd:pfam09738 180 EKHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskR 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568908302  271 NNKLDLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 319
Cdd:pfam09738 257 NSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
42-319 4.38e-112

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: 330.12  E-value: 4.38e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   42 MKELERQQKEVEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVE 112
Cdd:pfam09738  20 MRELERQQKEVEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  113 EKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEML 192
Cdd:pfam09738 100 EKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  193 EKHGIILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--K 270
Cdd:pfam09738 180 EKHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskR 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568908302  271 NNKLDLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 319
Cdd:pfam09738 257 NSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
125-393 3.52e-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: 42.75  E-value: 3.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   125 LDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKhgiiLNSEIA 204
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----VKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   205 TNGETSDTvndvgYQAPTKITKEELNALKSAgegTLDVRLKKLIDERECLLEQIKKLKGQL-EGRQKNNKLDLLRAedgI 283
Cdd:TIGR02169  762 ELEARIEE-----LEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKE---Y 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   284 LEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSAL 363
Cdd:TIGR02169  831 LE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
                          250       260       270
                   ....*....|....*....|....*....|
gi 568908302   364 DKTEELEVSNGHLVKRLEKMKANRSALLSQ 393
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEE 932
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
244-385 2.42e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  244 LKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTD----------------AHVMDLQRDANRQISDLK 307
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrleqlereierlerelEERERRRARLEALLAALG 372
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568908302  308 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEkieDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 385
Cdd:COG4913   373 LPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
51-286 3.39e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.53  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  51 EVEERPDKDFAEKGSRNMPSLSAA--TLASLGGTSSRRGSGDTSISM----DTEASIREIKDSLAEVEEKYKKAMVSNAQ 124
Cdd:PRK05771  32 HIEDLKEELSNERLRKLRSLLTKLseALDKLRSYLPKLNPLREEKKKvsvkSLEELIKDVEEELEKIEKEIKELEEEISE 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302 125 LDNEKTNFMYQVDTLKdmlleleeqlaesqrQYEEKNKEFEREKHAHSILQFqFAEVKEALrqrEEMLEKHGIILNSEIA 204
Cdd:PRK05771 112 LENEIKELEQEIERLE---------------PWGNFDLDLSLLLGFKYVSVF-VGTVPEDK---LEELKLESDVENVEYI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302 205 TNGETSDTVNDVGYQAPTKITKEELN-----ALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgrQKNNKL-DLLR 278
Cdd:PRK05771 173 STDKGYVYVVVVVLKELSDEVEEELKklgfeRLELEEEGTPSELIREIKEELEEIEKERESLLEELK--ELAKKYlEELL 250

                 ....*...
gi 568908302 279 AEDGILEN 286
Cdd:PRK05771 251 ALYEYLEI 258
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
42-319 4.38e-112

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: 330.12  E-value: 4.38e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   42 MKELERQQKEVEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVE 112
Cdd:pfam09738  20 MRELERQQKEVEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  113 EKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEML 192
Cdd:pfam09738 100 EKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  193 EKHGIILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--K 270
Cdd:pfam09738 180 EKHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskR 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568908302  271 NNKLDLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 319
Cdd:pfam09738 257 NSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
125-393 3.52e-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: 42.75  E-value: 3.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   125 LDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKhgiiLNSEIA 204
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----VKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   205 TNGETSDTvndvgYQAPTKITKEELNALKSAgegTLDVRLKKLIDERECLLEQIKKLKGQL-EGRQKNNKLDLLRAedgI 283
Cdd:TIGR02169  762 ELEARIEE-----LEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKE---Y 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   284 LEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSAL 363
Cdd:TIGR02169  831 LE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
                          250       260       270
                   ....*....|....*....|....*....|
gi 568908302   364 DKTEELEVSNGHLVKRLEKMKANRSALLSQ 393
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
96-369 4.98e-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: 42.35  E-value: 4.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302    96 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQ 175
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   176 FQFAEVKEALRQREEMLEKHGIILNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEgTLDVRLKKLIDERECLL 255
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIE-ELEELIEELESELEALL 879
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   256 EQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqisdLKFKLAKSEQEITALEQNVIRLESQVT-RY 334
Cdd:TIGR02168  880 NERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSeEY 949
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 568908302   335 RSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 369
Cdd:TIGR02168  950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
74-393 5.11e-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: 42.35  E-value: 5.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302    74 ATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 153
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   154 QRQYEEKNKEFEREKHAHSILQFQFA----EVKEALRQREEMLEKHGIiLNSEIATNGETSDTVNDV--GYQAPTKITKE 227
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAqlskELTELEAEIEELEERLEE-AEEELAEAEAEIEELEAQieQLKEELKALRE 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   228 ELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDgilengtdahvmdlqrdANRQISDLK 307
Cdd:TIGR02168  804 ALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-----------------LAAEIEELE 865
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302   308 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANR 387
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLELRLEGLEVRI 938

                   ....*.
gi 568908302   388 SALLSQ 393
Cdd:TIGR02168  939 DNLQER 944
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
244-385 2.42e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  244 LKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTD----------------AHVMDLQRDANRQISDLK 307
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrleqlereierlerelEERERRRARLEALLAALG 372
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568908302  308 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEkieDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 385
Cdd:COG4913   373 LPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
51-286 3.39e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.53  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  51 EVEERPDKDFAEKGSRNMPSLSAA--TLASLGGTSSRRGSGDTSISM----DTEASIREIKDSLAEVEEKYKKAMVSNAQ 124
Cdd:PRK05771  32 HIEDLKEELSNERLRKLRSLLTKLseALDKLRSYLPKLNPLREEKKKvsvkSLEELIKDVEEELEKIEKEIKELEEEISE 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302 125 LDNEKTNFMYQVDTLKdmlleleeqlaesqrQYEEKNKEFEREKHAHSILQFqFAEVKEALrqrEEMLEKHGIILNSEIA 204
Cdd:PRK05771 112 LENEIKELEQEIERLE---------------PWGNFDLDLSLLLGFKYVSVF-VGTVPEDK---LEELKLESDVENVEYI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302 205 TNGETSDTVNDVGYQAPTKITKEELN-----ALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgrQKNNKL-DLLR 278
Cdd:PRK05771 173 STDKGYVYVVVVVLKELSDEVEEELKklgfeRLELEEEGTPSELIREIKEELEEIEKERESLLEELK--ELAKKYlEELL 250

                 ....*...
gi 568908302 279 AEDGILEN 286
Cdd:PRK05771 251 ALYEYLEI 258
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
223-394 5.44e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 5.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302 223 KITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKL------KGQLEGRQKNNKLDLLRAEDGILENGTDAHVMDLQ 296
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaeLARLEQDIARLEERRRELEERLEELEEELAELEEE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302 297 R-DANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGH 375
Cdd:COG1196  332 LeELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
                        170
                 ....*....|....*....
gi 568908302 376 LVKRLEKMKANRSALLSQQ 394
Cdd:COG1196  412 LLERLERLEEELEELEEAL 430
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
154-394 7.29e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302 154 QRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKhgiILNSEIATNGETSDTVNDVGYQAPTKITKEELNALK 233
Cdd:COG1196  259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302 234 SAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENgtDAHVMDLQRDANRQISDLKFKLAKS 313
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEAL 412
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302 314 EQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 393
Cdd:COG1196  413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492

                 .
gi 568908302 394 Q 394
Cdd:COG1196  493 L 493
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
223-394 8.49e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.50  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  223 KITKEELNALKSAGEGTLDVRLKKLIDEREcllEQIKKLKGQL--EGRQKNNKLDLLRA-EDGIlengtdAHVMDLQRDA 299
Cdd:PRK10929   79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLleKSRQAQQEQDRAREiSDSL------SQLPQQQTEA 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908302  300 NRQISDLKFKL--------AKSEQEITALEQNVIRLESQVTRY--------------RSAAENAEKIEDELKAEKRKL-- 355
Cdd:PRK10929  150 RRQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELelaqlsannrqelaRLRSELAKKRSQQLDAYLQALrn 229
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568908302  356 ------QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 394
Cdd:PRK10929  230 qlnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
 
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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