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Conserved domains on  [gi|1907067525|ref|XP_036018312|]
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leucine-rich repeat flightless-interacting protein 1 isoform X19 [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 ...
98-396 3.60e-97

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: 294.68  E-value: 3.60e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  98 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSN 168
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 169 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEalerqkeff 248
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE--------- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 249 dsirserddlreetvklkeelkKHGIILNSEIATNGETsdtVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDER 328
Cdd:pfam09738 181 ----------------------KHGLVIVPDENTNGEE---ENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEK 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 329 ECLLEQIKKLKGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 396
Cdd:pfam09738 236 EELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
98-396 3.60e-97

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: 294.68  E-value: 3.60e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  98 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSN 168
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 169 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEalerqkeff 248
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE--------- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 249 dsirserddlreetvklkeelkKHGIILNSEIATNGETsdtVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDER 328
Cdd:pfam09738 181 ----------------------KHGLVIVPDENTNGEE---ENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEK 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 329 ECLLEQIKKLKGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 396
Cdd:pfam09738 236 EELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-471 6.61e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 6.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 197 AESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEALERQKeffDSIRSERDDLREETVKLKEELKKhgiiL 276
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI---ARLEERRRELEERLEELEEELAE----L 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 277 NSEIATNGEtsdtvndvgyqaptkiTKEELNALKSAGEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQKNNKLDLLRA 356
Cdd:COG1196   329 EEELEELEE----------------ELEELEEELEEAEEELEEAEAELAEAEE-ALLEAEAELAEAEEELEELAEELLEA 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 357 EDGILENGTDahvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQREL 436
Cdd:COG1196   392 LRAAAELAAQ------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907067525 437 RSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 471
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-446 1.08e-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: 51.21  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  120 ATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 199
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  200 QRQYEEKNKEFEREKHAHSILQFQFA----EVKEALRQREEMLEALERQKEFFDSIRSERDDLREETVKLKEELKKHGII 275
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  276 LNSEIATNGETSDTVNDV-----GYQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEG-----R 345
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLrerleSLERRIAATERRLEDLEEQIEELSE-DIESLAAEIEELEELIEELESELEAllnerA 883
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  346 QKNNKLDLLRAEDGILE---NGTDAHVMDLQRDANRqisdLKFKLAKSEQEITALEQNVIRLESQVT-RYRSAAENAEKI 421
Cdd:TIGR02168  884 SLEEALALLRSELEELSeelRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEAL 959
                          330       340
                   ....*....|....*....|....*
gi 1907067525  422 EDELKAEKRKLQRELRSALDKTEEL 446
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIKEL 984
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
300-471 5.77e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.27  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  300 KITKEELNALKSAGEGTLDVRLKKLIDEREcllEQIKKLKGQL--EGRQKNNKLDLLRA-EDGIlengtdAHVMDLQRDA 376
Cdd:PRK10929    79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLleKSRQAQQEQDRAREiSDSL------SQLPQQQTEA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  377 NRQISDLKFKL--------AKSEQEITALEQNVIRLESQVTRY--------------RSAAENAEKIEDELKAEKRKL-- 432
Cdd:PRK10929   150 RRQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELelaqlsannrqelaRLRSELAKKRSQQLDAYLQALrn 229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907067525  433 ------QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 471
Cdd:PRK10929   230 qlnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
98-396 3.60e-97

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: 294.68  E-value: 3.60e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  98 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSN 168
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 169 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEalerqkeff 248
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE--------- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 249 dsirserddlreetvklkeelkKHGIILNSEIATNGETsdtVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDER 328
Cdd:pfam09738 181 ----------------------KHGLVIVPDENTNGEE---ENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEK 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 329 ECLLEQIKKLKGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 396
Cdd:pfam09738 236 EELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-471 6.61e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 6.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 197 AESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEALERQKeffDSIRSERDDLREETVKLKEELKKhgiiL 276
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI---ARLEERRRELEERLEELEEELAE----L 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 277 NSEIATNGEtsdtvndvgyqaptkiTKEELNALKSAGEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQKNNKLDLLRA 356
Cdd:COG1196   329 EEELEELEE----------------ELEELEEELEEAEEELEEAEAELAEAEE-ALLEAEAELAEAEEELEELAEELLEA 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 357 EDGILENGTDahvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQREL 436
Cdd:COG1196   392 LRAAAELAAQ------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907067525 437 RSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 471
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-446 1.08e-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: 51.21  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  120 ATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 199
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  200 QRQYEEKNKEFEREKHAHSILQFQFA----EVKEALRQREEMLEALERQKEFFDSIRSERDDLREETVKLKEELKKHGII 275
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  276 LNSEIATNGETSDTVNDV-----GYQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEG-----R 345
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLrerleSLERRIAATERRLEDLEEQIEELSE-DIESLAAEIEELEELIEELESELEAllnerA 883
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  346 QKNNKLDLLRAEDGILE---NGTDAHVMDLQRDANRqisdLKFKLAKSEQEITALEQNVIRLESQVT-RYRSAAENAEKI 421
Cdd:TIGR02168  884 SLEEALALLRSELEELSeelRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEAL 959
                          330       340
                   ....*....|....*....|....*
gi 1907067525  422 EDELKAEKRKLQRELRSALDKTEEL 446
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
225-470 6.17e-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: 6.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  225 AEVKEALRQREEMLEALERQKEFFDSIRSERDDLREETVKLKEELKKhgiiLNSEIATngetsdtvndvgYQAPTKITKE 304
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE----LEARIEE------------LEEDLHKLEE 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  305 ELNALKSAgegTLDVRLKKLIDERECLLEQIKKLKGQL-EGRQKNNKLDLLRAedgILEngtdahvmDLQRDANRQISDL 383
Cdd:TIGR02169  780 ALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKE---YLE--------KEIQELQEQRIDL 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  384 KFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKAN 463
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925

                   ....*..
gi 1907067525  464 RSALLSQ 470
Cdd:TIGR02169  926 LEALEEE 932
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
234-462 1.46e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  234 REEMLE------ALERQKEFFDSIRSERDDLR--EETVKLKEELKKHGiilnSEIATNGETSDTVNDVGYQAPTKITKEE 305
Cdd:COG4913    214 REYMLEepdtfeAADALVEHFDDLERAHEALEdaREQIELLEPIRELA----ERYAAARERLAELEYLRAALRLWFAQRR 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  306 LNALKSAGEgTLDVRLKKLIDERECLLEQIKKLKGQLEG------RQKNNKLDLLRAEdgiLENGTD--AHVMDLQRDAN 377
Cdd:COG4913    290 LELLEAELE-ELRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLERE---IERLERelEERERRRARLE 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  378 RQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEkieDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 457
Cdd:COG4913    366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442

                   ....*
gi 1907067525  458 EKMKA 462
Cdd:COG4913    443 LALRD 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
155-447 1.89e-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: 44.28  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  155 AEVEEKYK--KAMVSNAQLD---NEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKE 229
Cdd:TIGR02168  209 AEKAERYKelKAELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  230 ALRQREEMLEALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGE--TSDTVNDVGYQAPTKITKEELN 307
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEklEELKEELESLEAELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  308 ALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENGTDAhvmdLQRDANRQISDLKFKL 387
Cdd:TIGR02168  369 ELESR-LEELEEQLETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIEEL----LKKLEEAELKELQAEL 442
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  388 AKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 447
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
320-467 4.46e-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: 43.12  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  320 RLKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGI--------LENGTDAHVMDLQRDANRQISDLKFKLAKSE 391
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleeriaQLSKELTELEAEIEELEERLEEAEEELAEAE 781
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067525  392 QEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 467
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
219-467 5.20e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 5.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 219 ILQFQFAEVKEALRQREEMLEALERQKEffdSIRSERDDLREETVKLKEELKKhgiiLNSEIAtngETSDTVNDvgyqap 298
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAA----LERRIA---ALARRIRA------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 299 tkiTKEELNALKSagegtldvRLKKLIDERECLLEQIKKLKGQLEGR----QKNNKLDLLRaedgILENGTDAhvmdlqR 374
Cdd:COG4942    74 ---LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPLA----LLLSPEDF------L 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 375 DANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLV 454
Cdd:COG4942   133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
                         250
                  ....*....|...
gi 1907067525 455 KRLEKMKANRSAL 467
Cdd:COG4942   213 AELAELQQEAEEL 225
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
223-471 8.88e-04

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: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 223 QFAEVKEALRQREEMLEALERqkeffDSIRSERDDLREETVKLKEELKKhgiiLNSEIATngetsdtvndvgyqaptkiT 302
Cdd:COG1196   214 RYRELKEELKELEAELLLLKL-----RELEAELEELEAELEELEAELEE----LEAELAE-------------------L 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 303 KEELNALKSAGEgTLDVRLKKLIDERECLLEQIKKLKGQL---EGRQKNNKLDLLRAEDGILENGTDahvmdlQRDANRQ 379
Cdd:COG1196   266 EAELEELRLELE-ELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELEEELAELEEE------LEELEEE 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 380 ISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEK 459
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
                         250
                  ....*....|..
gi 1907067525 460 MKANRSALLSQQ 471
Cdd:COG1196   419 LEEELEELEEAL 430
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
137-470 9.82e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 9.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  137 TSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMlleleeqlaesqRQYEEKNKEFEREKHA 216
Cdd:pfam15921  485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL------------KNEGDHLRNVQTECEA 552
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  217 hsiLQFQFAE---VKEALRQR-EEMLEALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVND 292
Cdd:pfam15921  553 ---LKLQMAEkdkVIEILRQQiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD 629
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  293 VgyqaptkitkeELNALKSAGEGTLDVR-LKKLIDERECLLEQIKKLKGQLEGRQKNNKL--DLLRAEDGILENGTDAHV 369
Cdd:pfam15921  630 L-----------ELEKVKLVNAGSERLRaVKDIKQERDQLLNEVKTSRNELNSLSEDYEVlkRNFRNKSEEMETTTNKLK 698
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  370 MDLqRDANRQISDLKFKLAKSE--------------QEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRE 435
Cdd:pfam15921  699 MQL-KSAQSELEQTRNTLKSMEgsdghamkvamgmqKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1907067525  436 LRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 470
Cdd:pfam15921  778 LSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
142-434 3.10e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  142 DTEASIREIKDSLAEVEEKYKKamvSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFERE-KHAHSIL 220
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEK---LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEiASLERSI 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  221 QFQFAEVKEALRQREEMLEALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSdtvndvgyqAPTK 300
Cdd:TIGR02169  311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD---------KEFA 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  301 ITKEELNALKsagegtldVRLKKLIDERECLLEQIKKL---KGQLEGRQKNNKLDLLRAEDGILENGTDAhvmdlqrdan 377
Cdd:TIGR02169  382 ETRDELKDYR--------EKLEKLKREINELKRELDRLqeeLQRLSEELADLNAAIAGIEAKINELEEEK---------- 443
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067525  378 rqiSDLKFKLAKSEQEitaLEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQR 434
Cdd:TIGR02169  444 ---EDKALEIKKQEWK---LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
300-471 5.77e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.27  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  300 KITKEELNALKSAGEGTLDVRLKKLIDEREcllEQIKKLKGQL--EGRQKNNKLDLLRA-EDGIlengtdAHVMDLQRDA 376
Cdd:PRK10929    79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLleKSRQAQQEQDRAREiSDSL------SQLPQQQTEA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  377 NRQISDLKFKL--------AKSEQEITALEQNVIRLESQVTRY--------------RSAAENAEKIEDELKAEKRKL-- 432
Cdd:PRK10929   150 RRQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELelaqlsannrqelaRLRSELAKKRSQQLDAYLQALrn 229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907067525  433 ------QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 471
Cdd:PRK10929   230 qlnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
316-445 7.18e-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: 37.98  E-value: 7.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 316 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 382
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067525 383 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 445
Cdd:COG1579    94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
171-447 7.97e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 7.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  171 LDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEALERQKeffDS 250
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL---KE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  251 IRSERDDLREETVKLKEEL-----------------------KKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELN 307
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALndlearlshsripeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  308 ALKSAGEGTLDVRLKKLIDERECLLEQIKKLKG---QLEGRQKN--NKLDLLRAEDGILENGTDAHVMDLQRdANRQISD 382
Cdd:TIGR02169  843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrDLESRLGDlkKERDELEAQLRELERKIEELEAQIEK-KRKRLSE 921
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525  383 LKFKLAKSEQEITALEQNVIRLES---QVTRYRSAAENAEKIE------------------------DELKAEKRKLQRE 435
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEeeiralepvnmlaiqeyeevlkrlDELKEKRAKLEEE 1001
                          330
                   ....*....|..
gi 1907067525  436 LRSALDKTEELE 447
Cdd:TIGR02169 1002 RKAILERIEEYE 1013
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
198-420 8.49e-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: 38.21  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 198 ESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEALERQkefFDSIRSERDDLREETVKLKEELKkhgiiln 277
Cdd:COG4942    31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAELRAELE------- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067525 278 seiatngETSDTVNDVGYQAPTKITKEELNALKSAGEGTLDVR----LKKLIDERECLLEQIKKLKGQLEGRQKNNKLDL 353
Cdd:COG4942   101 -------AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrlqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067525 354 LRAEDGILENGTDAHVMDLQRDANRQ-ISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEK 420
Cdd:COG4942   174 AELEALLAELEEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
 
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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