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Conserved domains on  [gi|1327850616|ref|NP_001346690|]
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transmembrane and coiled-coil domain protein 3 isoform b [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 ...
33-432 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: 585.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616  33 VKLNADSLRQKILKVTEQIKIEQTSRDGNVAEYLKLVSSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 112
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 113 E---QNGVTRSSKdiSKDSLKEIHHSLKDAHVKSRtaphclesskSSMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 189
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRDVGGNIR----------DGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 190 AHLKNSLEEFRPEASPRAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGTSTLDSQGKIAKIMEE 262
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 263 LREIKVTQTQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTELHQHETANLKQELASAEEKVAYQAYERS 342
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 343 RDIQEALESCQTRISKLELHQQEQQTLQTDAV---NAKVLLGKCINVVLAFMTVILVCVSTLAKFVSPMMKSRSHILGTF 419
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 1327850616 420 FAVTLLAIFCKNW 432
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 ...
33-432 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: 585.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616  33 VKLNADSLRQKILKVTEQIKIEQTSRDGNVAEYLKLVSSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 112
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 113 E---QNGVTRSSKdiSKDSLKEIHHSLKDAHVKSRtaphclesskSSMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 189
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRDVGGNIR----------DGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 190 AHLKNSLEEFRPEASPRAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGTSTLDSQGKIAKIMEE 262
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 263 LREIKVTQTQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTELHQHETANLKQELASAEEKVAYQAYERS 342
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 343 RDIQEALESCQTRISKLELHQQEQQTLQTDAV---NAKVLLGKCINVVLAFMTVILVCVSTLAKFVSPMMKSRSHILGTF 419
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 1327850616 420 FAVTLLAIFCKNW 432
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-379 1.34e-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: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616  251 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR------------EYGFISQTLQEERYRYERLEDQLHDLTELHQh 318
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDAlqerrealqrlaEYSWDEIDVASAEREIAELEAELERLDASSD- 685
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327850616  319 ETANLKQELASAEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQTLQTDAVNAKVL 379
Cdd:COG4913    686 DLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
251-360 9.73e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 9.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 251 DSQGKIAKIMEELREIKVTQTQLAEDIEALKvqfkreygfisqTLQEERYRYERLEDQLHDLTEL--HQHETANLKQEL- 327
Cdd:PRK02224  472 EDRERVEELEAELEDLEEEVEEVEERLERAE------------DLVEAEDRIERLEERREDLEELiaERRETIEEKRERa 539
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1327850616 328 -----------ASAEEK--VAYQAYERSRDIQEALESCQTRISKLE 360
Cdd:PRK02224  540 eelreraaeleAEAEEKreAAAEAEEEAEEAREEVAELNSKLAELK 585
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
251-360 2.60e-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: 40.44  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616  251 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLTElhqhETANLKQEL 327
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKA----KLEALEEEL 933
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1327850616  328 ASAEEKVAYQAYERS-----RDIQEALESCQTRISKLE 360
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 ...
33-432 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: 585.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616  33 VKLNADSLRQKILKVTEQIKIEQTSRDGNVAEYLKLVSSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 112
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 113 E---QNGVTRSSKdiSKDSLKEIHHSLKDAHVKSRtaphclesskSSMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 189
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRDVGGNIR----------DGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 190 AHLKNSLEEFRPEASPRAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGTSTLDSQGKIAKIMEE 262
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 263 LREIKVTQTQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTELHQHETANLKQELASAEEKVAYQAYERS 342
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 343 RDIQEALESCQTRISKLELHQQEQQTLQTDAV---NAKVLLGKCINVVLAFMTVILVCVSTLAKFVSPMMKSRSHILGTF 419
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 1327850616 420 FAVTLLAIFCKNW 432
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-379 1.34e-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: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616  251 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR------------EYGFISQTLQEERYRYERLEDQLHDLTELHQh 318
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDAlqerrealqrlaEYSWDEIDVASAEREIAELEAELERLDASSD- 685
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327850616  319 ETANLKQELASAEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQTLQTDAVNAKVL 379
Cdd:COG4913    686 DLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
255-360 5.05e-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: 41.45  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 255 KIAKIMEELREIKVTQTQLAEDIEALKVQ---FKREYGFISQTLQEERYRYERLEDQLHDLT---ELH--QHETANLKQE 326
Cdd:COG1579    25 RLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkEYEalQKEIESLKRR 104
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1327850616 327 LASAEEKVAyQAYERSRDIQEALESCQTRISKLE 360
Cdd:COG1579   105 ISDLEDEIL-ELMERIEELEEELAELEAELAELE 137
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
251-360 9.73e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 9.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 251 DSQGKIAKIMEELREIKVTQTQLAEDIEALKvqfkreygfisqTLQEERYRYERLEDQLHDLTEL--HQHETANLKQEL- 327
Cdd:PRK02224  472 EDRERVEELEAELEDLEEEVEEVEERLERAE------------DLVEAEDRIERLEERREDLEELiaERRETIEEKRERa 539
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1327850616 328 -----------ASAEEK--VAYQAYERSRDIQEALESCQTRISKLE 360
Cdd:PRK02224  540 eelreraaeleAEAEEKreAAAEAEEEAEEAREEVAELNSKLAELK 585
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
251-360 2.60e-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: 40.44  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616  251 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLTElhqhETANLKQEL 327
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKA----KLEALEEEL 933
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1327850616  328 ASAEEKVAYQAYERS-----RDIQEALESCQTRISKLE 360
Cdd:TIGR02169  934 SEIEDPKGEDEEIPEeelslEDVQAELQRVEEEIRALE 971
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
255-373 3.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 255 KIAKIMEELREIKVTQTQLAEDIEALKVQFKReygfISQTLQEERYRYERLEDQLHDLtelhQHETANLKQELASAEEKV 334
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEA----QAEEYELLAELARLEQDI 304
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1327850616 335 AYQAyERSRDIQEALESCQTRISKLELHQQEQQTLQTDA 373
Cdd:COG1196   305 ARLE-ERRRELEERLEELEEELAELEEELEELEEELEEL 342
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
293-372 6.52e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 293 QTLQEERYRYERLEDQLHDLTELH---QHETANLKQELASAEEKV-AYQAYERSRDIQEALESCQTRISKLELHQQEQQT 368
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELeelEAELEELREELEKLEKLLqLLPLYQELEALEAELAELPERLEELEERLEELRE 160

                  ....
gi 1327850616 369 LQTD 372
Cdd:COG4717   161 LEEE 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
253-376 9.67e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 9.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327850616 253 QGKIAKIMEELREIKVTQTQLAEDIEALKVQFKREygfiSQTLQEERYRYERLEDQLHDLTELHQHETA---NLKQELAS 329
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEE 320
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1327850616 330 AEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQTLQTDAVNA 376
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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