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Conserved domains on  [gi|1700611620|ref|NP_001358284|]
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B-cell receptor-associated protein 29 isoform c [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 5.21e-48

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: 158.04  E-value: 5.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620   1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1700611620  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 5.46e-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: 45.73  E-value: 5.46e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1700611620 185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQ 230
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQ 42
PTZ00121 super family cl31754
MAEBL; Provisional
 128-271 3.99e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  128 AKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121  1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakKA 1459

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1700611620  206 MEMKMQSERlSKEYDQLLKEHSELQKQREIlpHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAK 271
Cdd:PTZ00121  1460 EEAKKKAEE-AKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-129 5.21e-48

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: 158.04  E-value: 5.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620   1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1700611620  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 5.46e-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: 45.73  E-value: 5.46e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1700611620 185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQ 230
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQ 42
PTZ00121 PTZ00121
MAEBL; Provisional
 128-271 3.99e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  128 AKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121  1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakKA 1459

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1700611620  206 MEMKMQSERlSKEYDQLLKEHSELQKQREIlpHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAK 271
Cdd:PTZ00121  1460 EEAKKKAEE-AKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 115-273 2.71e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 115 LVLRRLVTLITQLAKELSNKGVLKTQAENTNKAakkfmEENEKLKRilkshgKDEECVLEAENKKLVEDQEKLKTELRKT 194
Cdd:pfam07888  24 LVVPRAELLQNRLEECLQERAELLQAQEAANRQ-----REKEKERY------KRDREQWERQRRELESRVAELKEELRQS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 195 SDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSELQ---KQREILPHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAK 271
Cdd:pfam07888  93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEariRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE 172


                  ..
gi 1700611620 272 NR 273
Cdd:pfam07888 173 RK 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-270 2.35e-03

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: 40.04  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  152 MEENEKLKRILKSH---GKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSE 228
Cdd:TIGR02168  679 IEELEEKIEELEEKiaeLEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1700611620  229 LQKQREILPHRRGEST---VTTEAEIGVMEPQQRNA-DSHQKLEEA 270
Cdd:TIGR02168  759 LEAEIEELEERLEEAEeelAEAEAEIEELEAQIEQLkEELKALREA 804
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-273 2.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 117 LRRLVTLITQLAKELsnkGVLKTQAEntnkAAKKFMEENEKLKRI--------LKSHGKDEEcVLEAENKKLVEDQEKLK 188
Cdd:COG1196   188 LERLEDILGELERQL---EPLERQAE----KAERYRELKEELKELeaellllkLRELEAELE-ELEAELEELEAELEELE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 189 TELRKTSDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSELQKQREILPHRRGESTVT---TEAEIGVMEpqQRNADSHQ 265
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERleeLEEELAELE--EELEELEE 337


                  ....*...
gi 1700611620 266 KLEEAKNR 273
Cdd:COG1196   338 ELEELEEE 345
 
Name Accession Description Interval E-value
Bap31 pfam05529
Bap31/Bap29 transmembrane region; Bap31 is a polytopic integral protein of the endoplasmic ...
 1-129 5.21e-48

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: 158.04  E-value: 5.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620   1 MTLQWAAVATFLYAEIGLILIFCLPFIPPQRwQKIFSFNVWGKIATFWNKAFLTIIILLIVLFLDAVREVRKYSSVHTIE 80
Cdd:pfam05529   1 MTLQWTLVFGFLYAEMAVFLLLVLPLPSPVR-QKIFKSRSESPLSAKFQIGFKITIIFLLILFLDAVRRVRKYSAELESA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1700611620  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 5.46e-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: 45.73  E-value: 5.46e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1700611620 185 EKLKTELRKtsdalskAQNDVMEMKMQSERLSKEYDQLLKEHSELQ 230
Cdd:pfam18035   4 EKLKKELKK-------KKSDIEALKKQAEGLQREYDRLSDEHAKLQ 42
PTZ00121 PTZ00121
MAEBL; Provisional
 128-271 3.99e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  128 AKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121  1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakKA 1459

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1700611620  206 MEMKMQSERlSKEYDQLLKEHSELQKQREIlpHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAK 271
Cdd:PTZ00121  1460 EEAKKKAEE-AKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
PRK12704 PRK12704
phosphodiesterase; Provisional
 134-273 1.52e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 134 KGVLKTQAENTNKAAKKFMEENEKLKRILKshgkdEECVLEA--ENKKLVEDQEKlktELRKTSDALSKAQNDVMEmkmQ 211
Cdd:PRK12704   26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIK-----KEALLEAkeEIHKLRNEFEK---ELRERRNELQKLEKRLLQ---K 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 212 SERLSKEYDQLLKEHSELQKQREILPHRRGESTVtTEAEIGVMEPQQRnadshQKLE--------EAKNR 273
Cdd:PRK12704   95 EENLDRKLELLEKREEELEKKEKELEQKQQELEK-KEEELEELIEEQL-----QELErisgltaeEAKEI 158
PTZ00121 PTZ00121
MAEBL; Provisional
 128-282 8.08e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  128 AKELSNKGVLKTQAENTNKAAKKfMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAqndvmE 207
Cdd:PTZ00121  1446 ADEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA-----E 1519

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1700611620  208 MKMQSERLSKEYDQllKEHSELQKQREIlphRRGESTVTTEaEIGVMEpQQRNADSHQKLEEAKNRFFPRASSSR 282
Cdd:PTZ00121  1520 EAKKADEAKKAEEA--KKADEAKKAEEK---KKADELKKAE-ELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAK 1587
PTZ00121 PTZ00121
MAEBL; Provisional
 67-273 2.30e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620   67 VREVRKYSSVHTIE---KSSTSRPDAYEHTQMKLFRSqrNLYISGFSLFFWLVLRRLVTLI----TQLAKELsNKGVLKT 139
Cdd:PTZ00121  1214 AEEARKAEDAKKAEavkKAEEAKKDAEEAKKAEEERN--NEEIRKFEEARMAHFARRQAAIkaeeARKADEL-KKAEEKK 1290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  140 QAENTNKAAKKfmEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEY 219
Cdd:PTZ00121  1291 KADEAKKAEEK--KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1700611620  220 DQLLKEhsELQKQREILPHRRGESTVTTEAEIGVMEPQQRnADSHQKLEEAKNR 273
Cdd:PTZ00121  1369 AEKKKE--EAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKK 1419
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 115-273 2.71e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 115 LVLRRLVTLITQLAKELSNKGVLKTQAENTNKAakkfmEENEKLKRilkshgKDEECVLEAENKKLVEDQEKLKTELRKT 194
Cdd:pfam07888  24 LVVPRAELLQNRLEECLQERAELLQAQEAANRQ-----REKEKERY------KRDREQWERQRRELESRVAELKEELRQS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 195 SDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSELQ---KQREILPHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAK 271
Cdd:pfam07888  93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEariRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE 172


                  ..
gi 1700611620 272 NR 273
Cdd:pfam07888 173 RK 174
PTZ00121 PTZ00121
MAEBL; Provisional
 137-273 3.74e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  137 LKTQAENTNKA--AKKFMEENEKlkrilkshgKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQN--DVMEMKMQS 212
Cdd:PTZ00121  1383 AKKKAEEKKKAdeAKKKAEEDKK---------KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakKADEAKKKA 1453

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1700611620  213 ERlSKEYDQLLKEHSELQKQREIlpHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAKNR 273
Cdd:PTZ00121  1454 EE-AKKAEEAKKKAEEAKKADEA--KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
PTZ00121 PTZ00121
MAEBL; Provisional
 128-273 4.05e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  128 AKELSNKGVLKtQAENTNKAAKKFMEENEKLKRILKSH-GKDEECVLEAENKKLVEDQEKLKTE-LRKTSDALSKAQndv 205
Cdd:PTZ00121  1548 ADELKKAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEeAKKAEEARIEEVMKLYEEEKKMKAEeAKKAEEAKIKAE--- 1623

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1700611620  206 mEMKmQSERLSKEYDQLLKEHSELQKQREILPHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAKNR 273
Cdd:PTZ00121  1624 -ELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
PTZ00121 PTZ00121
MAEBL; Provisional
 128-287 4.74e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  128 AKELSNKGVLKTQAENTNKAAKKfMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQndvmE 207
Cdd:PTZ00121  1433 ADEAKKKAEEAKKADEAKKKAEE-AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA----E 1507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  208 MKMQSERLSKEYDQllKEHSELQKQREilpHRRGESTVTTEAEIGVMEPQQ----RNADSHQKLEEAKnrffpRASSSRS 283
Cdd:PTZ00121  1508 AKKKADEAKKAEEA--KKADEAKKAEE---AKKADEAKKAEEKKKADELKKaeelKKAEEKKKAEEAK-----KAEEDKN 1577


                   ....
gi 1700611620  284 MALQ 287
Cdd:PTZ00121  1578 MALR 1581
PTZ00121 PTZ00121
MAEBL; Provisional
 118-273 7.51e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 7.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  118 RRLVTLITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEECVLEAENKKLVEDQEKLKT-------- 189
Cdd:PTZ00121  1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAaeeakkae 1671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  190 ELRKTSDALSKAQND---VMEMKMQSERLSKEYDQLLKEHSELQKQREILPHRRGESTVTTEAEIGVMEPQQRNADSHQK 266
Cdd:PTZ00121  1672 EDKKKAEEAKKAEEDekkAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751


                   ....*..
gi 1700611620  267 LEEAKNR 273
Cdd:PTZ00121  1752 DEEEKKK 1758
PTZ00121 PTZ00121
MAEBL; Provisional
 137-271 1.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  137 LKTQAENTNKAAKKFMEENEKLKRilkshgKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQND----VMEMKMQS 212
Cdd:PTZ00121  1666 EAKKAEEDKKKAEEAKKAEEDEKK------AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEA 1739

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1700611620  213 ERLSKEYDQLLKEHSELQKQREILPHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAK 271
Cdd:PTZ00121  1740 EEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-270 2.35e-03

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: 40.04  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  152 MEENEKLKRILKSH---GKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSE 228
Cdd:TIGR02168  679 IEELEEKIEELEEKiaeLEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1700611620  229 LQKQREILPHRRGEST---VTTEAEIGVMEPQQRNA-DSHQKLEEA 270
Cdd:TIGR02168  759 LEAEIEELEERLEEAEeelAEAEAEIEELEAQIEQLkEELKALREA 804
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-234 2.61e-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: 39.70  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 136 VLKTQAENTNKAAKKFMEE--NEKLKRI-LKSHGKdeecVLEAENKKLVEDQEKLKTELRKTsdalskaQNDVMEMKMQS 212
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEleKEKLKNIeLTAHCD----KLLLENKELTQEASDMTLELKKH-------QEDIINCKKQE 529

                          90       100
                  ....*....|....*....|..
gi 1700611620 213 ERLSKEYDQLLKEHSELQKQRE 234
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELE 551
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-273 2.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 117 LRRLVTLITQLAKELsnkGVLKTQAEntnkAAKKFMEENEKLKRI--------LKSHGKDEEcVLEAENKKLVEDQEKLK 188
Cdd:COG1196   188 LERLEDILGELERQL---EPLERQAE----KAERYRELKEELKELeaellllkLRELEAELE-ELEAELEELEAELEELE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 189 TELRKTSDALSKAQNDVMEMKMQSERLSKEYDQLLKEHSELQKQREILPHRRGESTVT---TEAEIGVMEpqQRNADSHQ 265
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERleeLEEELAELE--EELEELEE 337


                  ....*...
gi 1700611620 266 KLEEAKNR 273
Cdd:COG1196   338 ELEELEEE 345
PTZ00121 PTZ00121
MAEBL; Provisional
 128-273 2.91e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  128 AKELSNKGVLKtQAENTNKAAKKFMEENEK----LKRILKSHGKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQn 203
Cdd:PTZ00121  1350 AEAEAAADEAE-AAEEKAEAAEKKKEEAKKkadaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA- 1427

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  204 dvmEMKMQSERLSKEYDQlLKEHSELQKQREilPHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAKNR 273
Cdd:PTZ00121  1428 ---EEKKKADEAKKKAEE-AKKADEAKKKAE--EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 118-231 3.19e-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: 39.35  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 118 RRLVTLITQLAKELSNkgVLKTQAENTNKAAKKFMEENEkLKRILKSHGKDEEcvLEAENKKLVED-QEKLKTELRKTSD 196
Cdd:pfam09731 301 KKLAELKKREEKHIER--ALEKQKEELDKLAEELSARLE-EVRAADEAQLRLE--FEREREEIRESyEEKLRTELERQAE 375

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1700611620 197 ALSKAQNDVmeMKMQSERLSKEYDQLLKEHSELQK 231
Cdd:pfam09731 376 AHEEHLKDV--LVEQEIELQREFLQDIKEKVEEER 408
PTZ00121 PTZ00121
MAEBL; Provisional
 138-273 4.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  138 KTQAENTNKAAKKFMEENEKLKRILKshgKDEECVLEAENKKLVEDQEKLKTELRKTSDALSKAQndvmEMKMQSERlSK 217
Cdd:PTZ00121  1373 KEEAKKKADAAKKKAEEKKKADEAKK---KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD----EAKKKAEE-AK 1444

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1700611620  218 EYDQLLKEHSELQKQREIlpHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAKNR 273
Cdd:PTZ00121  1445 KADEAKKKAEEAKKAEEA--KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
113-242 4.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 113 FWLVLRRLVTL---ITQLAKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHG----------------------- 166
Cdd:PRK03918  527 YEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleerlkelepfyneyle 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 167 -KDEECVLEAENKKLvedqEKLKTELRKTSDALSKAQNDVMEMKMQSERLSKEYDQ------------LLKEHSELQKQR 233
Cdd:PRK03918  607 lKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeelreeyleLSRELAGLRAEL 682


                  ....*....
gi 1700611620 234 EILPHRRGE 242
Cdd:PRK03918  683 EELEKRREE 691
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 141-234 8.46e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 37.38  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620 141 AENTNKAAKKFMEENEKLKRILKShgkdeecvLEAENKKLVEDQEKLKTELRKTSDALSKAQN------DVMEMKMQSER 214
Cdd:pfam15294 128 SALLHMEIERLKEENEKLKERLKT--------LESQATQALDEKSKLEKALKDLQKEQGAKKDvksnlkEISDLEEKMAA 199

                          90       100
                  ....*....|....*....|
gi 1700611620 215 LSKEYDQLLKEHSELQKQRE 234
Cdd:pfam15294 200 LKSDLEKTLNASTALQKSLE 219
PTZ00121 PTZ00121
MAEBL; Provisional
 128-271 9.81e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 9.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611620  128 AKELSNKGVLKTQAENTNKAAKKFMEENEKLKRILKSHGKDEEcVLEAENKKLVEdqEKLKTELRKTSDALSKAQN--DV 205
Cdd:PTZ00121  1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKKAD--EAKKAEEAKKADEAKKAEEkkKA 1548

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1700611620  206 MEMKmQSERLSKEYDQLLKEHSELQKQREILPHRRGESTVTTEAEIGVMEPQQRNADSHQKLEEAK 271
Cdd:PTZ00121  1549 DELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
 
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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