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Conserved domains on  [gi|1907075454|ref|XP_036011708|]
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transmembrane and coiled-coil domain protein 3 isoform X2 [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 ...
48-447 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: 585.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454  48 VKLNADSLRQKILKVTEQIKIEQTSRDGNVAEYLKLVSSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 127
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 128 E---QNGVTRSSKdiSKDSLKEIHHSLKDAHVKSRtaphclesskSSMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 204
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRDVGGNIR----------DGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 205 AHLKNSLEEFRPEASPRAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGTSTLDSQGKIAKIMEE 277
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 278 LREIKVTQTQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTELHQHETANLKQELASAEEKVAYQAYERS 357
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 358 RDIQEALESCQTRISKLELHQQEQQTLQTDAV---NAKVLLGKCINVVLAFMTVILVCVSTLAKFVSPMMKSRSHILGTF 434
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 1907075454 435 FAVTLLAIFCKNW 447
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 ...
48-447 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: 585.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454  48 VKLNADSLRQKILKVTEQIKIEQTSRDGNVAEYLKLVSSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 127
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 128 E---QNGVTRSSKdiSKDSLKEIHHSLKDAHVKSRtaphclesskSSMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 204
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRDVGGNIR----------DGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 205 AHLKNSLEEFRPEASPRAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGTSTLDSQGKIAKIMEE 277
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 278 LREIKVTQTQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTELHQHETANLKQELASAEEKVAYQAYERS 357
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 358 RDIQEALESCQTRISKLELHQQEQQTLQTDAV---NAKVLLGKCINVVLAFMTVILVCVSTLAKFVSPMMKSRSHILGTF 434
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 1907075454 435 FAVTLLAIFCKNW 447
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
266-394 1.40e-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: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454  266 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR------------EYGFISQTLQEERYRYERLEDQLHDLTELHQh 333
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDAlqerrealqrlaEYSWDEIDVASAEREIAELEAELERLDASSD- 685
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075454  334 ETANLKQELASAEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQTLQTDAVNAKVL 394
Cdd:COG4913    686 DLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
266-375 1.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 266 DSQGKIAKIMEELREIKVTQTQLAEDIEALKvqfkreygfisqTLQEERYRYERLEDQLHDLTEL--HQHETANLKQEL- 342
Cdd:PRK02224  472 EDRERVEELEAELEDLEEEVEEVEERLERAE------------DLVEAEDRIERLEERREDLEELiaERRETIEEKRERa 539
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907075454 343 -----------ASAEEK--VAYQAYERSRDIQEALESCQTRISKLE 375
Cdd:PRK02224  540 eelreraaeleAEAEEKreAAAEAEEEAEEAREEVAELNSKLAELK 585
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
266-375 2.85e-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: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454  266 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLTElhqhETANLKQEL 342
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKA----KLEALEEEL 933
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907075454  343 ASAEEKVAYQAYERS-----RDIQEALESCQTRISKLE 375
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 ...
48-447 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: 585.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454  48 VKLNADSLRQKILKVTEQIKIEQTSRDGNVAEYLKLVSSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 127
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 128 E---QNGVTRSSKdiSKDSLKEIHHSLKDAHVKSRtaphclesskSSMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 204
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRDVGGNIR----------DGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 205 AHLKNSLEEFRPEASPRAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGTSTLDSQGKIAKIMEE 277
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 278 LREIKVTQTQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTELHQHETANLKQELASAEEKVAYQAYERS 357
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 358 RDIQEALESCQTRISKLELHQQEQQTLQTDAV---NAKVLLGKCINVVLAFMTVILVCVSTLAKFVSPMMKSRSHILGTF 434
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 1907075454 435 FAVTLLAIFCKNW 447
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
266-394 1.40e-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: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454  266 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR------------EYGFISQTLQEERYRYERLEDQLHDLTELHQh 333
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDAlqerrealqrlaEYSWDEIDVASAEREIAELEAELERLDASSD- 685
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075454  334 ETANLKQELASAEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQTLQTDAVNAKVL 394
Cdd:COG4913    686 DLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
270-375 5.24e-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: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 270 KIAKIMEELREIKVTQTQLAEDIEALKVQ---FKREYGFISQTLQEERYRYERLEDQLHDLT---ELH--QHETANLKQE 341
Cdd:COG1579    25 RLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkEYEalQKEIESLKRR 104
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907075454 342 LASAEEKVAyQAYERSRDIQEALESCQTRISKLE 375
Cdd:COG1579   105 ISDLEDEIL-ELMERIEELEEELAELEAELAELE 137
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
266-375 1.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 266 DSQGKIAKIMEELREIKVTQTQLAEDIEALKvqfkreygfisqTLQEERYRYERLEDQLHDLTEL--HQHETANLKQEL- 342
Cdd:PRK02224  472 EDRERVEELEAELEDLEEEVEEVEERLERAE------------DLVEAEDRIERLEERREDLEELiaERRETIEEKRERa 539
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907075454 343 -----------ASAEEK--VAYQAYERSRDIQEALESCQTRISKLE 375
Cdd:PRK02224  540 eelreraaeleAEAEEKreAAAEAEEEAEEAREEVAELNSKLAELK 585
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
266-375 2.85e-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: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454  266 DSQGKIAKIMEELREIKVTQTQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLTElhqhETANLKQEL 342
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKA----KLEALEEEL 933
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907075454  343 ASAEEKVAYQAYERS-----RDIQEALESCQTRISKLE 375
Cdd:TIGR02169  934 SEIEDPKGEDEEIPEeelslEDVQAELQRVEEEIRALE 971
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
270-388 3.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 270 KIAKIMEELREIKVTQTQLAEDIEALKVQFKReygfISQTLQEERYRYERLEDQLHDLtelhQHETANLKQELASAEEKV 349
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEA----QAEEYELLAELARLEQDI 304
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907075454 350 AYQAyERSRDIQEALESCQTRISKLELHQQEQQTLQTDA 388
Cdd:COG1196   305 ARLE-ERRRELEERLEELEEELAELEEELEELEEELEEL 342
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
308-387 6.33e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075454 308 QTLQEERYRYERLEDQLHDLTELH---QHETANLKQELASAEEKV-AYQAYERSRDIQEALESCQTRISKLELHQQEQQT 383
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELeelEAELEELREELEKLEKLLqLLPLYQELEALEAELAELPERLEELEERLEELRE 160

                  ....
gi 1907075454 384 LQTD 387
Cdd:COG4717   161 LEEE 164
 
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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