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Conserved domains on  [gi|56549093|ref|NP_001008405|]
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B-cell receptor-associated protein 29 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-129 5.79e-47

Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This family also contains the Bap29 protein that forms a heterodimer with Bap 31.


:

Pssm-ID: 461673  Cd Length: 137  Bit Score: 155.73  E-value: 5.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093     1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56549093    81 KSSTSR-PDAYEHTQMKLFRSQRNLYISGFSLFFWLVLRRLVTLITQLAK 129
Cdd:pfam05529  80 KANAHQhPSARMEVQARKFYAQRNLYICGFTLFLSLVLRRTVTLISELAT 129
Bap31_Bap29_C pfam18035
Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the ...
 185-230 1.98e-07

Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This entry represents the cytoplasmic domain which forms a heterodimeric coiled-coil with Bap29. This Bap29 and Bap31 are homologous to each other and this entry includes both proteins.


:

Pssm-ID: 465623 [Multi-domain]  Cd Length: 52  Bit Score: 47.27  E-value: 1.98e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 56549093   185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQ 230
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQ 42
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-278 2.12e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   136 VLKTQAENTNKAAKKFMEE--NEKLKRI-LKSHGKdeecVLEAENKKLVEDQEKLKTELRKTsdalskaQNDVMEMKMQS 212
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEleKEKLKNIeLTAHCD----KLLLENKELTQEASDMTLELKKH-------QEDIINCKKQE 529

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   213 ERLSKEYDQLLKEHSELQ---HSSFGEFLSKRSHKNGSIGK-QTGSRKGSFRKRQQEKTVNFIKDTCNIL 278
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRdelESVREEFIQKGDEVKCKLDKsEENARSIEYEVLKKEKQMKILENKCNNL 599
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-129 5.79e-47

Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This family also contains the Bap29 protein that forms a heterodimer with Bap 31.


Pssm-ID: 461673  Cd Length: 137  Bit Score: 155.73  E-value: 5.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093     1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56549093    81 KSSTSR-PDAYEHTQMKLFRSQRNLYISGFSLFFWLVLRRLVTLITQLAK 129
Cdd:pfam05529  80 KANAHQhPSARMEVQARKFYAQRNLYICGFTLFLSLVLRRTVTLISELAT 129
Bap31_Bap29_C pfam18035
Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the ...
 185-230 1.98e-07

Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This entry represents the cytoplasmic domain which forms a heterodimeric coiled-coil with Bap29. This Bap29 and Bap31 are homologous to each other and this entry includes both proteins.


Pssm-ID: 465623 [Multi-domain]  Cd Length: 52  Bit Score: 47.27  E-value: 1.98e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 56549093   185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQ 230
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQ 42
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-278 2.12e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   136 VLKTQAENTNKAAKKFMEE--NEKLKRI-LKSHGKdeecVLEAENKKLVEDQEKLKTELRKTsdalskaQNDVMEMKMQS 212
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEleKEKLKNIeLTAHCD----KLLLENKELTQEASDMTLELKKH-------QEDIINCKKQE 529

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   213 ERLSKEYDQLLKEHSELQ---HSSFGEFLSKRSHKNGSIGK-QTGSRKGSFRKRQQEKTVNFIKDTCNIL 278
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRdelESVREEFIQKGDEVKCKLDKsEENARSIEYEVLKKEKQMKILENKCNNL 599
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
113-242 5.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093  113 FWLVLRRLVTL---ITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHG----------------------- 166
Cdd:PRK03918 527 YEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleerlkelepfyneyle 606

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56549093  167 -KDEECVLEAENKKLvedqEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEYDQllKEHSELQhssfGEFLSKRS 242
Cdd:PRK03918 607 lKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELR----EEYLELSR 673
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-231 4.44e-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: 4.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093 117 LRRLVTLITQLAKELsnkGVLKTQAEntnkAAKKFMEENEKLKRI--------LKSHGKDEEcVLEAENKKLVEDQEKLK 188
Cdd:COG1196 188 LERLEDILGELERQL---EPLERQAE----KAERYRELKEELKELeaellllkLRELEAELE-ELEAELEELEAELEELE 259

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 56549093 189 TELRKTSDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSELQH 231
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-129 5.79e-47

Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This family also contains the Bap29 protein that forms a heterodimer with Bap 31.


Pssm-ID: 461673  Cd Length: 137  Bit Score: 155.73  E-value: 5.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093     1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56549093    81 KSSTSR-PDAYEHTQMKLFRSQRNLYISGFSLFFWLVLRRLVTLITQLAK 129
Cdd:pfam05529  80 KANAHQhPSARMEVQARKFYAQRNLYICGFTLFLSLVLRRTVTLISELAT 129
Bap31_Bap29_C pfam18035
Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the ...
 185-230 1.98e-07

Bap31/Bap29 cytoplasmic coiled-coil domain; Bap31 is a polytopic integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Bap31 is cleaved within its cytosolic domain, generating pro-apoptotic p20 Bap31. This entry represents the cytoplasmic domain which forms a heterodimeric coiled-coil with Bap29. This Bap29 and Bap31 are homologous to each other and this entry includes both proteins.


Pssm-ID: 465623 [Multi-domain]  Cd Length: 52  Bit Score: 47.27  E-value: 1.98e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 56549093   185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQ 230
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQ 42
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-278 2.12e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.25  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   136 VLKTQAENTNKAAKKFMEE--NEKLKRI-LKSHGKdeecVLEAENKKLVEDQEKLKTELRKTsdalskaQNDVMEMKMQS 212
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEleKEKLKNIeLTAHCD----KLLLENKELTQEASDMTLELKKH-------QEDIINCKKQE 529

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   213 ERLSKEYDQLLKEHSELQ---HSSFGEFLSKRSHKNGSIGK-QTGSRKGSFRKRQQEKTVNFIKDTCNIL 278
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRdelESVREEFIQKGDEVKCKLDKsEENARSIEYEVLKKEKQMKILENKCNNL 599
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 118-256 1.63e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 43.59  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   118 RRLVTLITQLAKELSNkgVLKTQAENTNKAAKKFMEENEkLKRILKSHGKDEEcvLEAENKKLVED-QEKLKTELRKTSD 196
Cdd:pfam09731 301 KKLAELKKREEKHIER--ALEKQKEELDKLAEELSARLE-EVRAADEAQLRLE--FEREREEIRESyEEKLRTELERQAE 375

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   197 ALSKAQNDVmeMKMQSERLSKEYDQLLKEHSELQHSSFGEFLSKRSHKNGSIGKQTGSRK 256
Cdd:pfam09731 376 AHEEHLKDV--LVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEKATSSHS 433
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
113-242 5.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093  113 FWLVLRRLVTL---ITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHG----------------------- 166
Cdd:PRK03918 527 YEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleerlkelepfyneyle 606

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56549093  167 -KDEECVLEAENKKLvedqEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEYDQllKEHSELQhssfGEFLSKRS 242
Cdd:PRK03918 607 lKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELR----EEYLELSR 673
PTZ00121 PTZ00121
MAEBL; Provisional
 128-228 1.59e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   128 AKELSNKGVLKTQAENTNKAAKKfMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121 1407 ADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKA 1485

                          90       100
                  ....*....|....*....|...
gi 56549093   206 MEMKMQSERLSKEYDQLLKEHSE 228
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEA 1508
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 125-228 2.65e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 37.38  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   125 TQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRilkshgkdeecvLEAENKKLVEDQEKLKTELRK---TSDALSKA 201
Cdd:pfam04871   8 SEASSLKNENTELKAELQELSKQYNSLEQKESQAKE------------LEAEVKKLEEALKKLKAELSEekqKEKEKQSE 75

                          90       100
                  ....*....|....*....|....*..
gi 56549093   202 QNDVMEMKMQSERLSKEYDQLLKEHSE 228
Cdd:pfam04871  76 LDDLLLLLGDLEEKVEKYKARLKELGE 102
PTZ00121 PTZ00121
MAEBL; Provisional
 128-228 2.66e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   128 AKELSNKGVLKTQAENTNK---AAKKFMEENEKLKRILKSHGKDEECVLEAENKKlVEDQEKLKTELRKTSDALSKAQND 204
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKkadAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEE 1389

                          90       100
                  ....*....|....*....|....*..
gi 56549093   205 VM---EMKMQSERLSKEYDQLLKEHSE 228
Cdd:PTZ00121 1390 KKkadEAKKKAEEDKKKADELKKAAAA 1416
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 137-267 3.11e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.32  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   137 LKTQAENTNKAAKKFMEENEKLKRilksHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQNDVMEMKMQSERLS 216
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKK----KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL 674

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56549093   217 KEY-------DQLLKEHSEL----QH--SSFGEFLSKRSHKNGSIGKQTGSRKGSFRKRQQEKT 267
Cdd:pfam05483 675 EEVekakaiaDEAVKLQKEIdkrcQHkiAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQS 738
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-231 4.44e-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: 4.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093 117 LRRLVTLITQLAKELsnkGVLKTQAEntnkAAKKFMEENEKLKRI--------LKSHGKDEEcVLEAENKKLVEDQEKLK 188
Cdd:COG1196 188 LERLEDILGELERQL---EPLERQAE----KAERYRELKEELKELeaellllkLRELEAELE-ELEAELEELEAELEELE 259

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 56549093 189 TELRKTSDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSELQH 231
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 139-230 5.79e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 38.04  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   139 TQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQNDVMEMKMQ-SERLSK 217
Cdd:pfam02841 200 TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQeQEELLK 279

                          90
                  ....*....|....*...
gi 56549093   218 E-----YDQLLKEHSELQ 230
Cdd:pfam02841 280 EgfkteAESLQKEIQDLK 297
PTZ00121 PTZ00121
MAEBL; Provisional
 137-283 6.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 6.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   137 LKTQAENTNKAAKKFMEENEKLKRilkshgKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQND----VMEMKMQS 212
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKK------AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEA 1739

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56549093   213 ERLSKEYDQLLKEHSE---LQHSSFGEFLSK---RSHKNGSIgKQTGSRKGSFRKRQQEKTVNFIKDTCNILCQNDN 283
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEkkkIAHLKKEEEKKAeeiRKEKEAVI-EEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
PTZ00121 PTZ00121
MAEBL; Provisional
 128-224 7.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   128 AKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAqndvmE 207
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA-----E 1454

                          90
                  ....*....|....*..
gi 56549093   208 MKMQSERLSKEYDQLLK 224
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKK 1471
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 120-225 8.35e-03

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 36.72  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549093   120 LVTLITQLAKELSNKGVLKTQAENtnkAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRktsDALS 199
Cdd:pfam07798  27 LRDLLNDSLENVSKDLVTKEDLEN---ETYLQKADLAELRSELQILEKSEFAALRSENEKLRRELEKLKQRLR---EEIT 100

                          90       100       110
                  ....*....|....*....|....*....|.
gi 56549093   200 KAQNDVmEMKMQSER-----LSKEYDQLLKE 225
Cdd:pfam07798 101 KLKADV-RLDLNLEKgrireELKAQELKIQE 130
 
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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