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Conserved domains on  [gi|2462578525|ref|XP_054200525|]
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leucine-rich repeat flightless-interacting protein 1 isoform X43 [Homo sapiens]

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

 Zoom to residue level

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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 ...
42-351 4.46e-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: 313.17  E-value: 4.46e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  42 MKELERQQKEEDserysrrsrrntsasDEDERMSVGSRGSLRVeerpekdfTEKGSRNMPGLSAATLASLGGTSSRRGSG 121
Cdd:pfam09738  20 MRELERQQKEVE---------------ENADRVFDMSSSSGAD--------TASGSPTASTTSAGTLNSLGGTSSRRSSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525 122 DTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKH 201
Cdd:pfam09738  77 DSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525 202 AHSILQFQFAEVKEALKQREEMLEKHGIILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLKKLVD 281
Cdd:pfam09738 157 NLRRLQFQLAELKEQLKQRDELIEKHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLAD 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578525 282 ERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 351
Cdd:pfam09738 234 EKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
DUF3450 super family cl26418
Protein of unknown function (DUF3450); This family of proteins are functionally ...
367-426 9.70e-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: 9.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525 367 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 426
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 ...
42-351 4.46e-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: 313.17  E-value: 4.46e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  42 MKELERQQKEEDserysrrsrrntsasDEDERMSVGSRGSLRVeerpekdfTEKGSRNMPGLSAATLASLGGTSSRRGSG 121
Cdd:pfam09738  20 MRELERQQKEVE---------------ENADRVFDMSSSSGAD--------TASGSPTASTTSAGTLNSLGGTSSRRSSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525 122 DTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKH 201
Cdd:pfam09738  77 DSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525 202 AHSILQFQFAEVKEALKQREEMLEKHGIILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLKKLVD 281
Cdd:pfam09738 157 NLRRLQFQLAELKEQLKQRDELIEKHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLAD 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578525 282 ERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 351
Cdd:pfam09738 234 EKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
157-425 3.25e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  157 LDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEKHGIILNSEIA 236
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  237 TNGETSDTLNNVgyqgptkmtKEELNALKstgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVL 316
Cdd:TIGR02169  766 RIEELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ--KLNRLTLEKEYL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  317 EngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALD 396
Cdd:TIGR02169  832 E--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
                          250       260
                   ....*....|....*....|....*....
gi 2462578525  397 KTEELEVSNGHLVKRLEKMKANRSALLSQ 425
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSELKAKLEALEEE 932
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
255-426 8.63e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.50  E-value: 8.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  255 KMTKEELNALKSTGDGTLDIRLKKLVDEREcllEQIKKLKGQLEE--RQKIGKLDNLRSEDDVLEngtdmHVMDLQRDAN 332
Cdd:PRK10929    79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLLEksRQAQQEQDRAREISDSLS-----QLPQQQTEAR 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  333 RQISDLKFKL--------AKSEQEITALEQNVIRLESQVSRYKSA--------------AENAEKIEDELKAEKRKL--- 387
Cdd:PRK10929   151 RQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELELAqlsannrqelarlrSELAKKRSQQLDAYLQALrnq 230
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462578525  388 -----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 426
Cdd:PRK10929   231 lnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
367-426 9.70e-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: 9.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525 367 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 426
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 ...
42-351 4.46e-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: 313.17  E-value: 4.46e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  42 MKELERQQKEEDserysrrsrrntsasDEDERMSVGSRGSLRVeerpekdfTEKGSRNMPGLSAATLASLGGTSSRRGSG 121
Cdd:pfam09738  20 MRELERQQKEVE---------------ENADRVFDMSSSSGAD--------TASGSPTASTTSAGTLNSLGGTSSRRSSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525 122 DTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKH 201
Cdd:pfam09738  77 DSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525 202 AHSILQFQFAEVKEALKQREEMLEKHGIILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLKKLVD 281
Cdd:pfam09738 157 NLRRLQFQLAELKEQLKQRDELIEKHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLAD 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462578525 282 ERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 351
Cdd:pfam09738 234 EKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
157-425 3.25e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  157 LDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEKHGIILNSEIA 236
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  237 TNGETSDTLNNVgyqgptkmtKEELNALKstgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVL 316
Cdd:TIGR02169  766 RIEELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ--KLNRLTLEKEYL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  317 EngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALD 396
Cdd:TIGR02169  832 E--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
                          250       260
                   ....*....|....*....|....*....
gi 2462578525  397 KTEELEVSNGHLVKRLEKMKANRSALLSQ 425
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
106-425 8.71e-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: 8.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  106 ATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 185
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  186 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEKHGIILNSEIATNGETSDTLNNVgyQGPTKMTKEELNALK 265
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKEELKALR 802
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  266 STGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKldnlRSEDDVLEngtdmhvmdlqrdANRQISDLK 339
Cdd:TIGR02168  803 EALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE----ELSEDIES-------------LAAEIEELE 865
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  340 FKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANR 419
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLELRLEGLEVRI 938

                   ....*.
gi 2462578525  420 SALLSQ 425
Cdd:TIGR02168  939 DNLQER 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
127-401 5.06e-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: 5.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  127 IDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSIL 206
Cdd:TIGR02168  722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  207 QFQFAEVKEALKQREEMLEKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKEELNALKSTGDgTLDIRLKKLVDERECL 286
Cdd:TIGR02168  802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELEAL 878
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  287 LEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-R 365
Cdd:TIGR02168  879 LNERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeE 948
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462578525  366 YKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 401
Cdd:TIGR02168  949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
255-426 8.63e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.50  E-value: 8.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  255 KMTKEELNALKSTGDGTLDIRLKKLVDEREcllEQIKKLKGQLEE--RQKIGKLDNLRSEDDVLEngtdmHVMDLQRDAN 332
Cdd:PRK10929    79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLLEksRQAQQEQDRAREISDSLS-----QLPQQQTEAR 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525  333 RQISDLKFKL--------AKSEQEITALEQNVIRLESQVSRYKSA--------------AENAEKIEDELKAEKRKL--- 387
Cdd:PRK10929   151 RQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELELAqlsannrqelarlrSELAKKRSQQLDAYLQALrnq 230
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462578525  388 -----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 426
Cdd:PRK10929   231 lnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
367-426 9.70e-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: 9.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578525 367 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 426
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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