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Conserved domains on  [gi|662236743|ref|NP_001284542|]
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transmembrane and coiled-coil domains protein 2 isoform 4 [Homo sapiens]

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 ...
45-455 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: 567.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743   45 TKAAIDHLHQKILKITEQIKIEQEARDDNVAEYLKLANNADKQQVSRIKQVFEKKNQKSAQTIAQLHKKLEHYRRRLKEI 124
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  125 EQNGPS-----RQPKDVLRDMQQGLKDVGANVRAGISgfgggvvegvkgslsGLSQATHTAVVSKPREFASLIRNKFGSA 199
Cdd:pfam10267  81 ENGEQSsvtshRQPKEVLRDVGQGLRDVGGNIRDGIS---------------GLSGGPPPTVFSKPREFAHLIKNKFGSA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  200 DNIAHLKDPLEDGPPEEAARALSGS-ATLVSSPKYGSDDECSSASASSAGAGSNSGAGPGGALGSPKSNALyGAPGNLDA 278
Cdd:pfam10267 146 DNINSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSVESISAGSNGNPPPHGADNGGQQAES-DSQNGLAA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  279 LLEELREIKEGQSHLEDSMEDLKTQLQRDYTYMTQCLQEERYRYERLEEQLNDLTELHQNEMTNLKQELASMEEKVAYQS 358
Cdd:pfam10267 225 ILEELQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQS 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  359 YERARDIQEAVESCLTRVTKLELQQQQQQVVQLEGVENANARALLGKFINVILALMAVLLVFVSTIANFITPLMKTRLRI 438
Cdd:pfam10267 305 YERARDIQEALESCQTRISKMELQQQQQQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRI 384
                         410
                  ....*....|....*..
gi 662236743  439 TSTTLLVLVLFLLWKHW 455
Cdd:pfam10267 385 LTTILLVLLLIIFWKNW 401
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
45-455 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: 567.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743   45 TKAAIDHLHQKILKITEQIKIEQEARDDNVAEYLKLANNADKQQVSRIKQVFEKKNQKSAQTIAQLHKKLEHYRRRLKEI 124
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  125 EQNGPS-----RQPKDVLRDMQQGLKDVGANVRAGISgfgggvvegvkgslsGLSQATHTAVVSKPREFASLIRNKFGSA 199
Cdd:pfam10267  81 ENGEQSsvtshRQPKEVLRDVGQGLRDVGGNIRDGIS---------------GLSGGPPPTVFSKPREFAHLIKNKFGSA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  200 DNIAHLKDPLEDGPPEEAARALSGS-ATLVSSPKYGSDDECSSASASSAGAGSNSGAGPGGALGSPKSNALyGAPGNLDA 278
Cdd:pfam10267 146 DNINSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSVESISAGSNGNPPPHGADNGGQQAES-DSQNGLAA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  279 LLEELREIKEGQSHLEDSMEDLKTQLQRDYTYMTQCLQEERYRYERLEEQLNDLTELHQNEMTNLKQELASMEEKVAYQS 358
Cdd:pfam10267 225 ILEELQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQS 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  359 YERARDIQEAVESCLTRVTKLELQQQQQQVVQLEGVENANARALLGKFINVILALMAVLLVFVSTIANFITPLMKTRLRI 438
Cdd:pfam10267 305 YERARDIQEALESCQTRISKMELQQQQQQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRI 384
                         410
                  ....*....|....*..
gi 662236743  439 TSTTLLVLVLFLLWKHW 455
Cdd:pfam10267 385 LTTILLVLLLIIFWKNW 401
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
269-371 4.24e-04

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: 43.13  E-value: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743   269 LYGAPGNLDALLEELREIKEGQSHLEDSMEDLKTQLQRDYTYMTQCLQEERYRYERLEEQLNDLTELHQnEMTNLKQELA 348
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELK 761
                           90       100
                   ....*....|....*....|...
gi 662236743   349 SMEEKVAYQSyERARDIQEAVES 371
Cdd:TIGR02169  762 ELEARIEELE-EDLHKLEEALND 783
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
276-431 2.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743 276 LDALLEELREIKEGQSHLEDSMEDLKTQLQRDYTYMTQC-----LQEERYRYERLEEQLNDLTELHQ------NEMTNLK 344
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleaeLAELPERLEELEERLEELRELEEeleeleAELAELQ 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743 345 QELASMEEKVAYQSYERARDIQEAVESCLTRVT------------KLELQQQQQQVVQLEGVENANARALLGKFINVILA 412
Cdd:COG4717  177 EELEELLEQLSLATEEELQDLAEELEELQQRLAeleeeleeaqeeLEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
                        170
                 ....*....|....*....
gi 662236743 413 LMAVLLVFVSTIANFITPL 431
Cdd:COG4717  257 ALLALLGLGGSLLSLILTI 275
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
45-455 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: 567.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743   45 TKAAIDHLHQKILKITEQIKIEQEARDDNVAEYLKLANNADKQQVSRIKQVFEKKNQKSAQTIAQLHKKLEHYRRRLKEI 124
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  125 EQNGPS-----RQPKDVLRDMQQGLKDVGANVRAGISgfgggvvegvkgslsGLSQATHTAVVSKPREFASLIRNKFGSA 199
Cdd:pfam10267  81 ENGEQSsvtshRQPKEVLRDVGQGLRDVGGNIRDGIS---------------GLSGGPPPTVFSKPREFAHLIKNKFGSA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  200 DNIAHLKDPLEDGPPEEAARALSGS-ATLVSSPKYGSDDECSSASASSAGAGSNSGAGPGGALGSPKSNALyGAPGNLDA 278
Cdd:pfam10267 146 DNINSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSVESISAGSNGNPPPHGADNGGQQAES-DSQNGLAA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  279 LLEELREIKEGQSHLEDSMEDLKTQLQRDYTYMTQCLQEERYRYERLEEQLNDLTELHQNEMTNLKQELASMEEKVAYQS 358
Cdd:pfam10267 225 ILEELQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQS 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743  359 YERARDIQEAVESCLTRVTKLELQQQQQQVVQLEGVENANARALLGKFINVILALMAVLLVFVSTIANFITPLMKTRLRI 438
Cdd:pfam10267 305 YERARDIQEALESCQTRISKMELQQQQQQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRI 384
                         410
                  ....*....|....*..
gi 662236743  439 TSTTLLVLVLFLLWKHW 455
Cdd:pfam10267 385 LTTILLVLLLIIFWKNW 401
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
269-371 4.24e-04

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: 43.13  E-value: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743   269 LYGAPGNLDALLEELREIKEGQSHLEDSMEDLKTQLQRDYTYMTQCLQEERYRYERLEEQLNDLTELHQnEMTNLKQELA 348
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELK 761
                           90       100
                   ....*....|....*....|...
gi 662236743   349 SMEEKVAYQSyERARDIQEAVES 371
Cdd:TIGR02169  762 ELEARIEELE-EDLHKLEEALND 783
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
276-431 2.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743 276 LDALLEELREIKEGQSHLEDSMEDLKTQLQRDYTYMTQC-----LQEERYRYERLEEQLNDLTELHQ------NEMTNLK 344
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleaeLAELPERLEELEERLEELRELEEeleeleAELAELQ 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236743 345 QELASMEEKVAYQSYERARDIQEAVESCLTRVT------------KLELQQQQQQVVQLEGVENANARALLGKFINVILA 412
Cdd:COG4717  177 EELEELLEQLSLATEEELQDLAEELEELQQRLAeleeeleeaqeeLEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
                        170
                 ....*....|....*....
gi 662236743 413 LMAVLLVFVSTIANFITPL 431
Cdd:COG4717  257 ALLALLGLGGSLLSLILTI 275
 
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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