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Conserved domains on  [gi|281361234|ref|NP_001163531|]
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dementin, isoform H [Drosophila melanogaster]

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 ...
 249-658 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: 555.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  249 SVQAIDRLNTKIQCTKESIRQEQTARDDNVNEYLKLAASADKQQLQRIKAVFEKKNQKSAHNISQLQKKLDNYTKRAKDL 328
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  329 QNHQFQTKSQHRQPREVLRDVGQGLRNVGGNIRDGITGFSGS----VMSKPREFAHLIKNKFGSADNINQMSEAELQGMQ 404
Cdd:pfam10267  81 ENGEQSSVTSHRQPKEVLRDVGQGLRDVGGNIRDGISGLSGGppptVFSKPREFAHLIKNKFGSADNINSLKSSLETSHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  405 SANADVLGSerlqqvpgagtstgsggggqnnnTGGAGSGTGKFNSDNGSECSSVTSESI--------PGGSGKSQSGASQ 476
Cdd:pfam10267 161 EGGGRKLSG-----------------------STFSTVTKPKYPSDDECSSSSVESISAgsngnpppHGADNGGQQAESD 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  477 YHIVLKTLLTELAERKAENEKLKERIERLET-GQKEFNNLTATLESERYRAEGLEEQINDLTELHQNEIENLKQTIADME 555
Cdd:pfam10267 218 SQNGLAAILEELQEIKEAQVQLEEKLERLKTqFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASME 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  556 EKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQ-QYVTVEGIDNSNARALVVKLINVVLTILQVVLLLVATAAGIIMPF 634
Cdd:pfam10267 298 EKVAYQSYERARDIQEALESCQTRISKMELQQQQqQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPL 377

                         410       420
                  ....*....|....*....|....
gi 281361234  635 LKTRVRVLTTFLSICFVIFVIRQW 658
Cdd:pfam10267 378 LKTRLRILTTILLVLLLIIFWKNW 401
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
 249-658 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: 555.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  249 SVQAIDRLNTKIQCTKESIRQEQTARDDNVNEYLKLAASADKQQLQRIKAVFEKKNQKSAHNISQLQKKLDNYTKRAKDL 328
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  329 QNHQFQTKSQHRQPREVLRDVGQGLRNVGGNIRDGITGFSGS----VMSKPREFAHLIKNKFGSADNINQMSEAELQGMQ 404
Cdd:pfam10267  81 ENGEQSSVTSHRQPKEVLRDVGQGLRDVGGNIRDGISGLSGGppptVFSKPREFAHLIKNKFGSADNINSLKSSLETSHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  405 SANADVLGSerlqqvpgagtstgsggggqnnnTGGAGSGTGKFNSDNGSECSSVTSESI--------PGGSGKSQSGASQ 476
Cdd:pfam10267 161 EGGGRKLSG-----------------------STFSTVTKPKYPSDDECSSSSVESISAgsngnpppHGADNGGQQAESD 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  477 YHIVLKTLLTELAERKAENEKLKERIERLET-GQKEFNNLTATLESERYRAEGLEEQINDLTELHQNEIENLKQTIADME 555
Cdd:pfam10267 218 SQNGLAAILEELQEIKEAQVQLEEKLERLKTqFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASME 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  556 EKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQ-QYVTVEGIDNSNARALVVKLINVVLTILQVVLLLVATAAGIIMPF 634
Cdd:pfam10267 298 EKVAYQSYERARDIQEALESCQTRISKMELQQQQqQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPL 377

                         410       420
                  ....*....|....*....|....
gi 281361234  635 LKTRVRVLTTFLSICFVIFVIRQW 658
Cdd:pfam10267 378 LKTRLRILTTILLVLLLIIFWKNW 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
481-658 5.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 481 LKTLLTELAERKAENEKLKERIERLETGQ------KEFNNLTATLESERYRAEGLEEQINDLTELHQ------NEIENLK 548
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPERLEELEERLEELRELEEeleeleAELAELQ 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 549 QTIADMEEKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEG----IDNSNARALVVKLINVV--LTILQVVLL 622
Cdd:COG4717  177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEleeeLEQLENELEAAALEERLkeARLLLLIAA 256

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 281361234 623 LVATAAGIIMPFLKTRVRVLTTFLSICFVIFVIRQW 658
Cdd:COG4717  257 ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
481-558 2.70e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281361234 481 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRAEGLEEQINDLTElhqnEIENLKQTIADMEEKV 558
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE----RIEELKKEIEELEEKV 282
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 481-602 1.57e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234   481 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRA-EGLEEQINDLTELHQNEIENLKQTIADMEEKVQ 559
Cdd:TIGR00606  250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 281361234   560 YQSDER--LRDVNEVLENCQTRISKMEHMSQQQYVTVEGIDNSNA 602
Cdd:TIGR00606  330 KLNKERrlLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLA 374
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
 249-658 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: 555.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  249 SVQAIDRLNTKIQCTKESIRQEQTARDDNVNEYLKLAASADKQQLQRIKAVFEKKNQKSAHNISQLQKKLDNYTKRAKDL 328
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  329 QNHQFQTKSQHRQPREVLRDVGQGLRNVGGNIRDGITGFSGS----VMSKPREFAHLIKNKFGSADNINQMSEAELQGMQ 404
Cdd:pfam10267  81 ENGEQSSVTSHRQPKEVLRDVGQGLRDVGGNIRDGISGLSGGppptVFSKPREFAHLIKNKFGSADNINSLKSSLETSHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  405 SANADVLGSerlqqvpgagtstgsggggqnnnTGGAGSGTGKFNSDNGSECSSVTSESI--------PGGSGKSQSGASQ 476
Cdd:pfam10267 161 EGGGRKLSG-----------------------STFSTVTKPKYPSDDECSSSSVESISAgsngnpppHGADNGGQQAESD 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  477 YHIVLKTLLTELAERKAENEKLKERIERLET-GQKEFNNLTATLESERYRAEGLEEQINDLTELHQNEIENLKQTIADME 555
Cdd:pfam10267 218 SQNGLAAILEELQEIKEAQVQLEEKLERLKTqFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASME 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  556 EKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQ-QYVTVEGIDNSNARALVVKLINVVLTILQVVLLLVATAAGIIMPF 634
Cdd:pfam10267 298 EKVAYQSYERARDIQEALESCQTRISKMELQQQQqQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPL 377

                         410       420
                  ....*....|....*....|....
gi 281361234  635 LKTRVRVLTTFLSICFVIFVIRQW 658
Cdd:pfam10267 378 LKTRLRILTTILLVLLLIIFWKNW 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
481-658 5.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 481 LKTLLTELAERKAENEKLKERIERLETGQ------KEFNNLTATLESERYRAEGLEEQINDLTELHQ------NEIENLK 548
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPERLEELEERLEELRELEEeleeleAELAELQ 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 549 QTIADMEEKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEG----IDNSNARALVVKLINVV--LTILQVVLL 622
Cdd:COG4717  177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEleeeLEQLENELEAAALEERLkeARLLLLIAA 256

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 281361234 623 LVATAAGIIMPFLKTRVRVLTTFLSICFVIFVIRQW 658
Cdd:COG4717  257 ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 481-584 1.07e-05

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: 47.23  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 481 LKTLLTELAERKAENEKLKERIERLE------TGQKEFNNLTATLESERYRAEGLEEQINDLTElhqnEIENLKQTIADM 554
Cdd:COG1579   54 LEDLEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKEYEALQKEIESLKRRISDLEDEILELME----RIEELEEELAEL 129

                         90       100       110
                 ....*....|....*....|....*....|
gi 281361234 555 EEKVqyqsDERLRDVNEVLENCQTRISKME 584
Cdd:COG1579  130 EAEL----AELEAELEEKKAELDEELAELE 155
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 480-584 4.74e-05

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: 45.30  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 480 VLKTLLTELAERKAENEKLKERIERLETG----QKEFNNLTATLESERYRAEGLEEQINDLT---ELH--QNEIENLKQT 550
Cdd:COG1579   25 RLKELPAELAELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkEYEalQKEIESLKRR 104

                         90       100       110
                 ....*....|....*....|....*....|....
gi 281361234 551 IADMEEKVQyQSDERLRDVNEVLENCQTRISKME 584
Cdd:COG1579  105 ISDLEDEIL-ELMERIEELEEELAELEAELAELE 137
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
481-558 2.70e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281361234 481 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRAEGLEEQINDLTElhqnEIENLKQTIADMEEKV 558
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE----RIEELKKEIEELEEKV 282
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
483-583 1.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 483 TLLTELAERKAENEKLKERIERLET---GQKEFNNLT--------------ATLESERYRAEGLEEQINDL--------- 536
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEDlveAEDRIERLEerredleeliaerrETIEEKRERAEELRERAAELeaeaeekre 558

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 281361234 537 --TELHQnEIENLKQTIADMEEKVQYQSD--ERLRDVNEVL---ENCQTRISKM 583
Cdd:PRK02224 559 aaAEAEE-EAEEAREEVAELNSKLAELKEriESLERIRTLLaaiADAEDEIERL 611
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 481-602 1.57e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234   481 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRA-EGLEEQINDLTELHQNEIENLKQTIADMEEKVQ 559
Cdd:TIGR00606  250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 281361234   560 YQSDER--LRDVNEVLENCQTRISKMEHMSQQQYVTVEGIDNSNA 602
Cdd:TIGR00606  330 KLNKERrlLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLA 374
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
486-610 2.28e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 486 TELAERKAE----NEKLKERIERLETGQKEFNNLTATLESERYRAEGLEEQINDLtelhQNEIENLKQTIADMEEKVQyQ 561
Cdd:COG4372   66 EELEQARSEleqlEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIA-E 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 281361234 562 SDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEGIDNSNARALVVKLI 610
Cdd:COG4372  141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 481-574 3.53e-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: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 481 LKTLLTELAERKAENEKLKERIERLetgQKEFNNLTATLESERYRAEGLEEQINDLTE---LHQNEIENLKQTIADMEEK 557
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAeeyELLAELARLEQDIARLEER 310

                         90
                 ....*....|....*..
gi 281361234 558 VQYQSDERLRDVNEVLE 574
Cdd:COG1196  311 RRELEERLEELEEELAE 327
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 487-609 3.63e-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: 40.82  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234   487 ELAERKAENEKLKERIERLEtgqKEFNNLTATLESERYRAEGLEEQINDLTE---LHQNEIENLKQTIADMEEKVQ---- 559
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIE---QKLNRLTLEKEYLEKEIQELQEQRIDLKEqikSIEKEIENLNGKKEELEEELEelea 875

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 281361234   560 --YQSDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEgIDNSNARALVVKL 609
Cdd:TIGR02169  876 alRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRLSELKAKL 926
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 484-598 4.38e-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: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234   484 LLTELAERKAENEKLKERIERLEtgqKEFNNLTATLESERYRAEGLEEQINDL-----------TELHQnEIENLKQTIA 552
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELkreldrlqeelQRLSE-ELADLNAAIA 430

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 281361234   553 DMEEKVQyQSDERLRDVNEVLE----NCQTRISKMEHMSQQQYVTVEGID 598
Cdd:TIGR02169  431 GIEAKIN-ELEEEKEDKALEIKkqewKLEQLAADLSKYEQELYDLKEEYD 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 474-583 5.11e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234   474 ASQYHIVLKTLLTELAERKAENEKLKERIERLETGQKEFN--NLTA--TLESERYRAEGLEEQINDLTElhqnEIENLKQ 549
Cdd:TIGR02168  946 SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvNLAAieEYEELKERYDFLTAQKEDLTE----AKETLEE 1021

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 281361234   550 TIADMEEKVQyqsdERLRDV-NEVLENCQTRISKM 583
Cdd:TIGR02168 1022 AIEEIDREAR----ERFKDTfDQVNENFQRVFPKL 1052
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 481-565 5.62e-03

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234   481 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESeryRAEGLEEQINDLT----------ELHQNEIENLKQT 550
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELES---RLEELEEQLETLRskvaqlelqiASLNNEIERLEAR 408

                           90
                   ....*....|....*
gi 281361234   551 IADMEEKVQYQSDER 565
Cdd:TIGR02168  409 LERLEDRRERLQQEI 423
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
485-581 6.87e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 485 LTELAERKAENEKLKERIERLEtgqKEFNNLTATLESERYRAEGLEEQINDL---TELHQNEIENLKQTIADMEEKvqyq 561
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETE---REREELAEEVRDLRERLEELEEERDDLlaeAGLDDADAEAVEARREELEDR---- 322

                         90       100
                 ....*....|....*....|
gi 281361234 562 sDERLRDvneVLENCQTRIS 581
Cdd:PRK02224 323 -DEELRD---RLEECRVAAQ 338
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 470-589 7.83e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.02  E-value: 7.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234  470 SQSGASQYHIVLKTLLTELAERKAENEKLKERIERLetgqkefNNLTATLESER----YRAEGLEEQINDLTELHQN--- 542
Cdd:pfam15905 196 SKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITEL-------SCVSEQVEKYKldiaQLEELLKEKNDEIESLKQSlee 268

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 281361234  543 EIENLKQTIADMEEKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQ 589
Cdd:pfam15905 269 KEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEK 315
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
480-584 8.87e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361234 480 VLKTLLTELAERKAENEK----LKERI----ERLETGQKEFNNLTATLESERYRAEGLEEQINDLTE------------- 538
Cdd:PRK02224 255 TLEAEIEDLRETIAETERereeLAEEVrdlrERLEELEEERDDLLAEAGLDDADAEAVEARREELEDrdeelrdrleecr 334

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 281361234 539 ----LHQNEIENLKQTIADMEEKVQyQSDERLRDVNEVLENCQTRISKME 584
Cdd:PRK02224 335 vaaqAHNEEAESLREDADDLEERAE-ELREEAAELESELEEAREAVEDRR 383
 
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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