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Conserved domains on  [gi|78771620|ref|NP_742048|]
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transmembrane and coiled-coil domain protein 3 isoform a [Mus musculus]

Protein Classification

transmembrane and coiled-coil domain protein( domain architecture ID 11186040)

transmembrane and coiled-coil domain protein may be involved in the regulation of the proteolytic processing of the amyloid precursor protein (APP) possibly also implicating APOE

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
64-463 0e+00

Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil containing proteins is conserved from worms to humans. Its function is unknown.


:

Pssm-ID: 463036  Cd Length: 401  Bit Score: 590.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620    64 VKLNADSLRQKILKVTEQIKIEQTSRDGNVAEYLKLVSSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 143
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   144 E---QNGVTRSSKdiSKDSLKEIHHSLKDAHVKSRtaphclesskSSMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 220
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRDVGGNIR----------DGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   221 AHLKNSLEEFRPEASPRAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGTSTLDSQGKIAKIMEE 293
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   294 LREIKVTQTQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTELHQHETANLKQELASAEEKVAYQAYERS 373
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   374 RDIQEALESCQTRISKLELHQQEQQTLQTDAV---NAKVLLGKCINVVLAFMTVILVCVSTLAKFVSPMMKSRSHILGTF 450
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 78771620   451 FAVTLLAIFCKNW 463
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
64-463 0e+00

Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil containing proteins is conserved from worms to humans. Its function is unknown.


Pssm-ID: 463036  Cd Length: 401  Bit Score: 590.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620    64 VKLNADSLRQKILKVTEQIKIEQTSRDGNVAEYLKLVSSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 143
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   144 E---QNGVTRSSKdiSKDSLKEIHHSLKDAHVKSRtaphclesskSSMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 220
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRDVGGNIR----------DGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   221 AHLKNSLEEFRPEASPRAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGTSTLDSQGKIAKIMEE 293
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   294 LREIKVTQTQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTELHQHETANLKQELASAEEKVAYQAYERS 373
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   374 RDIQEALESCQTRISKLELHQQEQQTLQTDAV---NAKVLLGKCINVVLAFMTVILVCVSTLAKFVSPMMKSRSHILGTF 450
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 78771620   451 FAVTLLAIFCKNW 463
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
282-410 1.42e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620  282 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR------------EYGFISQTLQEERYRYERLEDQLHDLTELHQh 349
Cdd:COG4913  607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDAlqerrealqrlaEYSWDEIDVASAEREIAELEAELERLDASSD- 685
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78771620  350 ETANLKQELASAEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQTLQTDAVNAKVL 410
Cdd:COG4913  686 DLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
282-391 1.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620  282 DSQGKIAKIMEELREIKVTQTQLAEDIEALKvqfkreygfisqTLQEERYRYERLEDQLHDLTEL--HQHETANLKQEL- 358
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAE------------DLVEAEDRIERLEERREDLEELiaERRETIEEKRERa 539
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 78771620  359 -----------ASAEEK--VAYQAYERSRDIQEALESCQTRISKLE 391
Cdd:PRK02224 540 eelreraaeleAEAEEKreAAAEAEEEAEEAREEVAELNSKLAELK 585
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
282-391 1.73e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620    282 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLTElhqhETANLKQEL 358
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKA----KLEALEEEL 933
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 78771620    359 ASAEEKVAYQAYERS-----RDIQEALESCQTRISKLE 391
Cdd:TIGR02169  934 SEIEDPKGEDEEIPEeelslEDVQAELQRVEEEIRALE 971
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
64-463 0e+00

Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil containing proteins is conserved from worms to humans. Its function is unknown.


Pssm-ID: 463036  Cd Length: 401  Bit Score: 590.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620    64 VKLNADSLRQKILKVTEQIKIEQTSRDGNVAEYLKLVSSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 143
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   144 E---QNGVTRSSKdiSKDSLKEIHHSLKDAHVKSRtaphclesskSSMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 220
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRDVGGNIR----------DGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   221 AHLKNSLEEFRPEASPRAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGTSTLDSQGKIAKIMEE 293
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   294 LREIKVTQTQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTELHQHETANLKQELASAEEKVAYQAYERS 373
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620   374 RDIQEALESCQTRISKLELHQQEQQTLQTDAV---NAKVLLGKCINVVLAFMTVILVCVSTLAKFVSPMMKSRSHILGTF 450
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 78771620   451 FAVTLLAIFCKNW 463
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
282-410 1.42e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620  282 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR------------EYGFISQTLQEERYRYERLEDQLHDLTELHQh 349
Cdd:COG4913  607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDAlqerrealqrlaEYSWDEIDVASAEREIAELEAELERLDASSD- 685
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78771620  350 ETANLKQELASAEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQTLQTDAVNAKVL 410
Cdd:COG4913  686 DLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
286-391 2.51e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 2.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620 286 KIAKIMEELREIKVTQTQLAEDIEALKVQ---FKREYGFISQTLQEERYRYERLEDQLHDLT---ELH--QHETANLKQE 357
Cdd:COG1579  25 RLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkEYEalQKEIESLKRR 104
                        90       100       110
                ....*....|....*....|....*....|....
gi 78771620 358 LASAEEKVAyQAYERSRDIQEALESCQTRISKLE 391
Cdd:COG1579 105 ISDLEDEIL-ELMERIEELEEELAELEAELAELE 137
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
282-391 1.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620  282 DSQGKIAKIMEELREIKVTQTQLAEDIEALKvqfkreygfisqTLQEERYRYERLEDQLHDLTEL--HQHETANLKQEL- 358
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAE------------DLVEAEDRIERLEERREDLEELiaERRETIEEKRERa 539
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 78771620  359 -----------ASAEEK--VAYQAYERSRDIQEALESCQTRISKLE 391
Cdd:PRK02224 540 eelreraaeleAEAEEKreAAAEAEEEAEEAREEVAELNSKLAELK 585
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
282-391 1.73e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620    282 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLTElhqhETANLKQEL 358
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKA----KLEALEEEL 933
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 78771620    359 ASAEEKVAYQAYERS-----RDIQEALESCQTRISKLE 391
Cdd:TIGR02169  934 SEIEDPKGEDEEIPEeelslEDVQAELQRVEEEIRALE 971
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
286-404 2.16e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620 286 KIAKIMEELREIKVTQTQLAEDIEALKVQFKReygfISQTLQEERYRYERLEDQLHDLtelhQHETANLKQELASAEEKV 365
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEA----QAEEYELLAELARLEQDI 304
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 78771620 366 AYQAyERSRDIQEALESCQTRISKLELHQQEQQTLQTDA 404
Cdd:COG1196 305 ARLE-ERRRELEERLEELEEELAELEEELEELEEELEEL 342
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
324-403 3.76e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620 324 QTLQEERYRYERLEDQLHDLTElhqhETANLKQELASAEEKV--------AYQAYERSRDIQEALESCQTRISKLELHQQ 395
Cdd:COG4717  81 KEAEEKEEEYAELQEELEELEE----ELEELEAELEELREELeklekllqLLPLYQELEALEAELAELPERLEELEERLE 156

                ....*...
gi 78771620 396 EQQTLQTD 403
Cdd:COG4717 157 ELRELEEE 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
284-407 7.30e-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: 7.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78771620 284 QGKIAKIMEELREIKVTQTQLAEDIEALKVQFKREygfiSQTLQEERYRYERLEDQLHDLTELHQHETA---NLKQELAS 360
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEE 320
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 78771620 361 AEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQTLQTDAVNA 407
Cdd:COG1196 321 LEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
 
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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