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Conserved domains on  [gi|190014612|ref|NP_001121696|]
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transmembrane and coiled-coil domains protein 1 isoform c [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 ...
116-524 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: 581.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  116 TKAAIAHLQQKILKLTEQIKIAQTARDDNVAEYLKLANSADKQQAARIKQVFEKKNQKSAQTILQLQKKLEHYHRKLREV 195
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  196 EQNGIP-----RQPKDVFRDMHQGLKDVGAkvtgfsegvvdSVKGGFSSFSQAThsaAGAVVSKPREIASLIRNKFGSAD 270
Cdd:pfam10267  81 ENGEQSsvtshRQPKEVLRDVGQGLRDVGG-----------NIRDGISGLSGGP---PPTVFSKPREFAHLIKNKFGSAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  271 NIPNLKDSLEEGQVDDAGKALG-VISNFQSSPKYGSEEDCSSATSGSVGANSTTGGIAVGASSSKTNTLDMQSSGFDALL 349
Cdd:pfam10267 147 NINSLKSSLETSHDEGGGRKLSgSTFSTVTKPKYPSDDECSSSSVESISAGSNGNPPPHGADNGGQQAESDSQNGLAAIL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  350 HEIQEIRETQARLEESFETLKEHYQRDYSLIMQTLQEERYRCERLEEQLNDLTELHQNEILNLKQELASMEEKIAYQSYE 429
Cdd:pfam10267 227 EELQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  430 RARDIQEALEACQTRISKMELQQQQQQVVQLEGLENATARNLLGKLINILLAVMAVLLVFVSTVANCVVPLMKTRNRTFS 509
Cdd:pfam10267 307 RARDIQEALESCQTRISKMELQQQQQQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILT 386
                         410
                  ....*....|....*
gi 190014612  510 TLFLVVFIAFLWKHW 524
Cdd:pfam10267 387 TILLVLLLIIFWKNW 401
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
116-524 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: 581.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  116 TKAAIAHLQQKILKLTEQIKIAQTARDDNVAEYLKLANSADKQQAARIKQVFEKKNQKSAQTILQLQKKLEHYHRKLREV 195
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  196 EQNGIP-----RQPKDVFRDMHQGLKDVGAkvtgfsegvvdSVKGGFSSFSQAThsaAGAVVSKPREIASLIRNKFGSAD 270
Cdd:pfam10267  81 ENGEQSsvtshRQPKEVLRDVGQGLRDVGG-----------NIRDGISGLSGGP---PPTVFSKPREFAHLIKNKFGSAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  271 NIPNLKDSLEEGQVDDAGKALG-VISNFQSSPKYGSEEDCSSATSGSVGANSTTGGIAVGASSSKTNTLDMQSSGFDALL 349
Cdd:pfam10267 147 NINSLKSSLETSHDEGGGRKLSgSTFSTVTKPKYPSDDECSSSSVESISAGSNGNPPPHGADNGGQQAESDSQNGLAAIL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  350 HEIQEIRETQARLEESFETLKEHYQRDYSLIMQTLQEERYRCERLEEQLNDLTELHQNEILNLKQELASMEEKIAYQSYE 429
Cdd:pfam10267 227 EELQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  430 RARDIQEALEACQTRISKMELQQQQQQVVQLEGLENATARNLLGKLINILLAVMAVLLVFVSTVANCVVPLMKTRNRTFS 509
Cdd:pfam10267 307 RARDIQEALESCQTRISKMELQQQQQQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILT 386
                         410
                  ....*....|....*
gi 190014612  510 TLFLVVFIAFLWKHW 524
Cdd:pfam10267 387 TILLVLLLIIFWKNW 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
348-520 2.75e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612 348 LLHEIQEIRETQARLEESFETLKEHYQRdyslIMQTLQEERYRCERLEEQLNDLTELHQNEILNLKQELASMEEKIAYQS 427
Cdd:COG4717  130 LYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612 428 yERARDIQEALEACQTRISKMElqqqqqqvVQLEGLENATARNLLGKLIN---ILLAVMAVLLVFVSTVANcvvpLMKTR 504
Cdd:COG4717  206 -QRLAELEEELEEAQEELEELE--------EELEQLENELEAAALEERLKearLLLLIAAALLALLGLGGS----LLSLI 272
                        170
                 ....*....|....*.
gi 190014612 505 NRTFSTLFLVVFIAFL 520
Cdd:COG4717  273 LTIAGVLFLVLGLLAL 288
mukB PRK04863
chromosome partition protein MukB;
351-444 8.35e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  351 EIQEIRETQARLEESFETLKEHYQRDYSLIMQTLQEERYR--CERLEEQLNDltelhQNEILNLKQE-LASMEEK--IAY 425
Cdd:PRK04863  315 ELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQadLEELEERLEE-----QNEVVEEADEqQEENEARaeAAE 389
                          90       100
                  ....*....|....*....|...
gi 190014612  426 QSYERAR----DIQEALEACQTR 444
Cdd:PRK04863  390 EEVDELKsqlaDYQQALDVQQTR 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
352-446 9.54e-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: 38.90  E-value: 9.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612   352 IQEIRETQARLEESFETLKEHyQRDYSLIM----QTLQEERYRCERLEEQLNDLTELHQnEILNLKQELASMEEKIAYQS 427
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDA-SRKIGEIEkeieQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELKELEARIEELE 771
                           90
                   ....*....|....*....
gi 190014612   428 yERARDIQEALEACQTRIS 446
Cdd:TIGR02169  772 -EDLHKLEEALNDLEARLS 789
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
116-524 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: 581.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  116 TKAAIAHLQQKILKLTEQIKIAQTARDDNVAEYLKLANSADKQQAARIKQVFEKKNQKSAQTILQLQKKLEHYHRKLREV 195
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  196 EQNGIP-----RQPKDVFRDMHQGLKDVGAkvtgfsegvvdSVKGGFSSFSQAThsaAGAVVSKPREIASLIRNKFGSAD 270
Cdd:pfam10267  81 ENGEQSsvtshRQPKEVLRDVGQGLRDVGG-----------NIRDGISGLSGGP---PPTVFSKPREFAHLIKNKFGSAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  271 NIPNLKDSLEEGQVDDAGKALG-VISNFQSSPKYGSEEDCSSATSGSVGANSTTGGIAVGASSSKTNTLDMQSSGFDALL 349
Cdd:pfam10267 147 NINSLKSSLETSHDEGGGRKLSgSTFSTVTKPKYPSDDECSSSSVESISAGSNGNPPPHGADNGGQQAESDSQNGLAAIL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  350 HEIQEIRETQARLEESFETLKEHYQRDYSLIMQTLQEERYRCERLEEQLNDLTELHQNEILNLKQELASMEEKIAYQSYE 429
Cdd:pfam10267 227 EELQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  430 RARDIQEALEACQTRISKMELQQQQQQVVQLEGLENATARNLLGKLINILLAVMAVLLVFVSTVANCVVPLMKTRNRTFS 509
Cdd:pfam10267 307 RARDIQEALESCQTRISKMELQQQQQQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILT 386
                         410
                  ....*....|....*
gi 190014612  510 TLFLVVFIAFLWKHW 524
Cdd:pfam10267 387 TILLVLLLIIFWKNW 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
348-520 2.75e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612 348 LLHEIQEIRETQARLEESFETLKEHYQRdyslIMQTLQEERYRCERLEEQLNDLTELHQNEILNLKQELASMEEKIAYQS 427
Cdd:COG4717  130 LYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612 428 yERARDIQEALEACQTRISKMElqqqqqqvVQLEGLENATARNLLGKLIN---ILLAVMAVLLVFVSTVANcvvpLMKTR 504
Cdd:COG4717  206 -QRLAELEEELEEAQEELEELE--------EELEQLENELEAAALEERLKearLLLLIAAALLALLGLGGS----LLSLI 272
                        170
                 ....*....|....*.
gi 190014612 505 NRTFSTLFLVVFIAFL 520
Cdd:COG4717  273 LTIAGVLFLVLGLLAL 288
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
346-449 5.44e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  346 DALLHEIQEIRETQARLEESFETLKEhyqrdyslIMQTLQEERYRCERLEEQLNDLTEL--HQNEILNLKQELASMEE-- 421
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEA--------ELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDAss 684
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 190014612  422 ---KIAYQSYERAR----DIQEALEACQTRISKME 449
Cdd:COG4913   685 ddlAALEEQLEELEaeleELEEELDELKGEIGRLE 719
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
347-439 7.49e-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: 7.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612 347 ALLHEIQEIRETQARLEESFETLK---EHYQRDYSLIMQTLQEERYRCERLEEQLNDLtelhQNEILNLKQELASMEEKI 423
Cdd:COG1196  229 LLLLKLRELEAELEELEAELEELEaelEELEAELAELEAELEELRLELEELELELEEA----QAEEYELLAELARLEQDI 304
                         90
                 ....*....|....*.
gi 190014612 424 AYQSyERARDIQEALE 439
Cdd:COG1196  305 ARLE-ERRRELEERLE 319
mukB PRK04863
chromosome partition protein MukB;
351-444 8.35e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612  351 EIQEIRETQARLEESFETLKEHYQRDYSLIMQTLQEERYR--CERLEEQLNDltelhQNEILNLKQE-LASMEEK--IAY 425
Cdd:PRK04863  315 ELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQadLEELEERLEE-----QNEVVEEADEqQEENEARaeAAE 389
                          90       100
                  ....*....|....*....|...
gi 190014612  426 QSYERAR----DIQEALEACQTR 444
Cdd:PRK04863  390 EEVDELKsqlaDYQQALDVQQTR 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
352-446 9.54e-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: 38.90  E-value: 9.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190014612   352 IQEIRETQARLEESFETLKEHyQRDYSLIM----QTLQEERYRCERLEEQLNDLTELHQnEILNLKQELASMEEKIAYQS 427
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDA-SRKIGEIEkeieQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELKELEARIEELE 771
                           90
                   ....*....|....*....
gi 190014612   428 yERARDIQEALEACQTRIS 446
Cdd:TIGR02169  772 -EDLHKLEEALNDLEARLS 789
 
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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