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Conserved domains on  [gi|1700611665|ref|NP_001358286|]
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B-cell receptor-associated protein 29 isoform f [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 1.78e-49

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: 158.42  E-value: 1.78e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665   1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1700611665  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 ...
 185-235 1.17e-06

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: 44.57  E-value: 1.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1700611665 185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQDIDPG 235
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQLDEGE 47
PTZ00121 super family cl31754
MAEBL; Provisional
 128-233 1.51e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665  128 AKELSNKGVLKTQAENTNKAAKKfMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121  1407 ADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKA 1485

                           90       100
                   ....*....|....*....|....*...
gi 1700611665  206 MEMKMQSERLSKEYDQLLKEHSELQDID 233
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-129 1.78e-49

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: 158.42  E-value: 1.78e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665   1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1700611665  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 ...
 185-235 1.17e-06

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: 44.57  E-value: 1.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1700611665 185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQDIDPG 235
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQLDEGE 47
PTZ00121 PTZ00121
MAEBL; Provisional
 128-233 1.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665  128 AKELSNKGVLKTQAENTNKAAKKfMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121  1407 ADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKA 1485

                           90       100
                   ....*....|....*....|....*...
gi 1700611665  206 MEMKMQSERLSKEYDQLLKEHSELQDID 233
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-231 2.15e-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: 38.93  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665 136 VLKTQAENTNKAAKKFMEE--NEKLKRI-LKSHGKdeecVLEAENKKLVEDQEKLKTELRKTsdalskaQNDVMEMKMQS 212
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEleKEKLKNIeLTAHCD----KLLLENKELTQEASDMTLELKKH-------QEDIINCKKQE 529

                          90
                  ....*....|....*....
gi 1700611665 213 ERLSKEYDQLLKEHSELQD 231
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRD 548
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-129 1.78e-49

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: 158.42  E-value: 1.78e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665   1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1700611665  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 ...
 185-235 1.17e-06

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: 44.57  E-value: 1.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1700611665 185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQDIDPG 235
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQLDEGE 47
PTZ00121 PTZ00121
MAEBL; Provisional
 128-233 1.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665  128 AKELSNKGVLKTQAENTNKAAKKfMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121  1407 ADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKA 1485

                           90       100
                   ....*....|....*....|....*...
gi 1700611665  206 MEMKMQSERLSKEYDQLLKEHSELQDID 233
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-231 2.15e-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: 38.93  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665 136 VLKTQAENTNKAAKKFMEE--NEKLKRI-LKSHGKdeecVLEAENKKLVEDQEKLKTELRKTsdalskaQNDVMEMKMQS 212
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEleKEKLKNIeLTAHCD----KLLLENKELTQEASDMTLELKKH-------QEDIINCKKQE 529

                          90
                  ....*....|....*....
gi 1700611665 213 ERLSKEYDQLLKEHSELQD 231
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRD 548
PTZ00121 PTZ00121
MAEBL; Provisional
 128-233 2.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665  128 AKELSNKGVLKTQAENTNK---AAKKFMEENEKLKRILKSHGKDEECVLEAENKKlVEDQEKLKTELRKTSDALSKAQND 204
Cdd:PTZ00121  1311 AEEAKKADEAKKKAEEAKKkadAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEE 1389

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1700611665  205 VM---EMKMQSERLSKEYDQLLKEHSELQDID 233
Cdd:PTZ00121  1390 KKkadEAKKKAEEDKKKADELKKAAAAKKKAD 1421
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 118-228 6.14e-03

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: 37.43  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665 118 RRLVTLITQLAKELSNkgVLKTQAENTNKAAKKFMEENEkLKRILKSHGKDEEcvLEAENKKLVED-QEKLKTELRKTSD 196
Cdd:pfam09731 301 KKLAELKKREEKHIER--ALEKQKEELDKLAEELSARLE-EVRAADEAQLRLE--FEREREEIRESyEEKLRTELERQAE 375

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1700611665 197 ALSKAQNDVmeMKMQSERLSKEYDQLLKEHSE 228
Cdd:pfam09731 376 AHEEHLKDV--LVEQEIELQREFLQDIKEKVE 405
PTZ00121 PTZ00121
MAEBL; Provisional
 128-224 7.16e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665  128 AKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAqndvmE 207
Cdd:PTZ00121  1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA-----E 1454

                           90
                   ....*....|....*..
gi 1700611665  208 MKMQSERLSKEYDQLLK 224
Cdd:PTZ00121  1455 EAKKAEEAKKKAEEAKK 1471
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
113-231 8.04e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.35  E-value: 8.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665 113 FWLVLRRLVTL---ITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHG----------------------- 166
Cdd:PRK03918  527 YEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleerlkelepfyneyle 606

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1700611665 167 -KDEECVLEAENKKLvedqEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEYDQllKEHSELQD 231
Cdd:PRK03918  607 lKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELRE 666
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 120-225 9.11e-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: 35.95  E-value: 9.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611665 120 LVTLITQLAKELSNKGVLKTQAENtnkAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRktsDALS 199
Cdd:pfam07798  27 LRDLLNDSLENVSKDLVTKEDLEN---ETYLQKADLAELRSELQILEKSEFAALRSENEKLRRELEKLKQRLR---EEIT 100

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1700611665 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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