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Conserved domains on  [gi|1390249186|ref|NP_001350412|]
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B-cell receptor-associated protein 29 isoform d [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 9.70e-50

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: 160.73  E-value: 9.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186   1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1390249186  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 ...
 185-231 1.13e-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: 47.66  E-value: 1.13e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1390249186 185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQV 231
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQL 43
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-230 4.64e-04

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: 41.63  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 136 VLKTQAENTNKAAKKFMEE--NEKLKRI-LKSHGKdeecVLEAENKKLVEDQEKLKTELRKTsdalskaQNDVMEMKMQS 212
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEleKEKLKNIeLTAHCD----KLLLENKELTQEASDMTLELKKH-------QEDIINCKKQE 529

                          90
                  ....*....|....*...
gi 1390249186 213 ERLSKEYDQLLKEHSELQ 230
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLR 547
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-129 9.70e-50

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: 160.73  E-value: 9.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186   1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1390249186  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 ...
 185-231 1.13e-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: 47.66  E-value: 1.13e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1390249186 185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQV 231
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQL 43
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-230 4.64e-04

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: 41.63  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 136 VLKTQAENTNKAAKKFMEE--NEKLKRI-LKSHGKdeecVLEAENKKLVEDQEKLKTELRKTsdalskaQNDVMEMKMQS 212
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEleKEKLKNIeLTAHCD----KLLLENKELTQEASDMTLELKKH-------QEDIINCKKQE 529

                          90
                  ....*....|....*...
gi 1390249186 213 ERLSKEYDQLLKEHSELQ 230
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLR 547
PTZ00121 PTZ00121
MAEBL; Provisional
 128-228 7.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 7.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186  128 AKELSNKGVLKTQAENTNKAAKKfMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121  1407 ADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKA 1485

                           90       100
                   ....*....|....*....|...
gi 1390249186  206 MEMKMQSERLSKEYDQLLKEHSE 228
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKAAEA 1508
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 126-230 3.36e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 126 QLAKELSNKGVL-KTQAENTNKAAKKFMEEnEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQND 204
Cdd:TIGR04523  82 QQIKDLNDKLKKnKDKINKLNSDLSKINSE-IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK 160

                          90       100
                  ....*....|....*....|....*.
gi 1390249186 205 VMEMKMQSERLSKEYDQLLKEHSELQ 230
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQ 186
COG5374 COG5374
Uncharacterized conserved protein [Function unknown];
98-190 5.67e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227666 [Multi-domain]  Cd Length: 192  Bit Score: 37.09  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186  98 FRSQRNLYISGFSLFFWLVLRRLVTLITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAEN 177
Cdd:COG5374    98 FYAQRNMYLSGSALFLSIVVMRVMSIVEEMLEENAKKGGKIDKMEADSTDLKARLRKAQILLEGLQKNQEELFKLLDKYN 177

                          90
                  ....*....|....*
gi 1390249186 178 KK--LVEDQEKLKTE 190
Cdd:COG5374   178 ELreQVQKESSKKKE 192
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-129 9.70e-50

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: 160.73  E-value: 9.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186   1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1390249186  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 ...
 185-231 1.13e-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: 47.66  E-value: 1.13e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1390249186 185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQV 231
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQL 43
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-230 4.64e-04

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: 41.63  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 136 VLKTQAENTNKAAKKFMEE--NEKLKRI-LKSHGKdeecVLEAENKKLVEDQEKLKTELRKTsdalskaQNDVMEMKMQS 212
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEleKEKLKNIeLTAHCD----KLLLENKELTQEASDMTLELKKH-------QEDIINCKKQE 529

                          90
                  ....*....|....*...
gi 1390249186 213 ERLSKEYDQLLKEHSELQ 230
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLR 547
PTZ00121 PTZ00121
MAEBL; Provisional
 128-228 7.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 7.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186  128 AKELSNKGVLKTQAENTNKAAKKfMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121  1407 ADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakKA 1485

                           90       100
                   ....*....|....*....|...
gi 1390249186  206 MEMKMQSERLSKEYDQLLKEHSE 228
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKAAEA 1508
PTZ00121 PTZ00121
MAEBL; Provisional
 128-228 1.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186  128 AKELSNKGVLKTQAENTNK---AAKKFMEENEKLKRILKSHGKDEECVLEAENKKlVEDQEKLKTELRKTSDALSKAQND 204
Cdd:PTZ00121  1311 AEEAKKADEAKKKAEEAKKkadAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEE 1389

                           90       100
                   ....*....|....*....|....*..
gi 1390249186  205 VM---EMKMQSERLSKEYDQLLKEHSE 228
Cdd:PTZ00121  1390 KKkadEAKKKAEEDKKKADELKKAAAA 1416
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 120-225 1.58e-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: 38.65  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 120 LVTLITQLAKELSNKGVLKTQAENtnkAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRktsDALS 199
Cdd:pfam07798  27 LRDLLNDSLENVSKDLVTKEDLEN---ETYLQKADLAELRSELQILEKSEFAALRSENEKLRRELEKLKQRLR---EEIT 100

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1390249186 200 KAQNDVmEMKMQSER-----LSKEYDQLLKE 225
Cdd:pfam07798 101 KLKADV-RLDLNLEKgrireELKAQELKIQE 130
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
113-229 1.60e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 113 FWLVLRRLVTL---ITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHG----------------------- 166
Cdd:PRK03918  527 YEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleerlkelepfyneyle 606

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390249186 167 -KDEECVLEAENKKLvedqEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEYDQllKEHSEL 229
Cdd:PRK03918  607 lKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEEL 664
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 118-228 1.84e-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: 39.74  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 118 RRLVTLITQLAKELSNkgVLKTQAENTNKAAKKFMEENEkLKRILKSHGKDEEcvLEAENKKLVED-QEKLKTELRKTSD 196
Cdd:pfam09731 301 KKLAELKKREEKHIER--ALEKQKEELDKLAEELSARLE-EVRAADEAQLRLE--FEREREEIRESyEEKLRTELERQAE 375

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1390249186 197 ALSKAQNDVmeMKMQSERLSKEYDQLLKEHSE 228
Cdd:pfam09731 376 AHEEHLKDV--LVEQEIELQREFLQDIKEKVE 405
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 139-230 2.69e-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: 38.81  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 139 TQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQNDVMEMKMQ-SERLSK 217
Cdd:pfam02841 200 TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQeQEELLK 279

                          90
                  ....*....|....*...
gi 1390249186 218 E-----YDQLLKEHSELQ 230
Cdd:pfam02841 280 EgfkteAESLQKEIQDLK 297
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 126-230 3.36e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 126 QLAKELSNKGVL-KTQAENTNKAAKKFMEEnEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQND 204
Cdd:TIGR04523  82 QQIKDLNDKLKKnKDKINKLNSDLSKINSE-IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK 160

                          90       100
                  ....*....|....*....|....*.
gi 1390249186 205 VMEMKMQSERLSKEYDQLLKEHSELQ 230
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQ 186
PTZ00121 PTZ00121
MAEBL; Provisional
 128-224 3.76e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186  128 AKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAqndvmE 207
Cdd:PTZ00121  1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA-----E 1454

                           90
                   ....*....|....*..
gi 1390249186  208 MKMQSERLSKEYDQLLK 224
Cdd:PTZ00121  1455 EAKKAEEAKKKAEEAKK 1471
COG5374 COG5374
Uncharacterized conserved protein [Function unknown];
98-190 5.67e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227666 [Multi-domain]  Cd Length: 192  Bit Score: 37.09  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186  98 FRSQRNLYISGFSLFFWLVLRRLVTLITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAEN 177
Cdd:COG5374    98 FYAQRNMYLSGSALFLSIVVMRVMSIVEEMLEENAKKGGKIDKMEADSTDLKARLRKAQILLEGLQKNQEELFKLLDKYN 177

                          90
                  ....*....|....*
gi 1390249186 178 KK--LVEDQEKLKTE 190
Cdd:COG5374   178 ELreQVQKESSKKKE 192
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
117-231 8.88e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.19  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249186 117 LRRLVTLITQLAKELSNKGVLKTQAENTNKAAKkfmEENEKLKRILKSHGKdEECVLEAENKKLVEDQEKLKTELRKTSD 196
Cdd:COG4372    75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQ---EEAEELQEELEELQK-ERQDLEQQRKQLEAQIAELQSEIAEREE 150

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1390249186 197 ALSKAQNDVMEMKMQSERLSKEYDQLLKEHSELQV 231
Cdd:COG4372   151 ELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
 
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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