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Conserved domains on  [gi|221378064|ref|NP_649654|]
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dementin, isoform E [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 ...
 208-617 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: 552.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  208 SVQAIDRLNTKIQCTKESIRQEQTARDDNVNEYLKLAASADKQQLQRIKAVFEKKNQKSAHNISQLQKKLDNYTKRAKDL 287
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  288 QNHQFQTKSQHRQPREVLRDVGQGLRNVGGNIRDGITGFSGS----VMSKPREFAHLIKNKFGSADNINQMSEAELQGMQ 363
Cdd:pfam10267  81 ENGEQSSVTSHRQPKEVLRDVGQGLRDVGGNIRDGISGLSGGppptVFSKPREFAHLIKNKFGSADNINSLKSSLETSHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  364 SANADVLGSerlqqvpgagtstgsggggqnnnTGGAGSGTGKFNSDNGSECSSVTSESI--------PGGSGKSQSGASQ 435
Cdd:pfam10267 161 EGGGRKLSG-----------------------STFSTVTKPKYPSDDECSSSSVESISAgsngnpppHGADNGGQQAESD 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  436 YHIVLKTLLTELAERKAENEKLKERIERLET-GQKEFNNLTATLESERYRAEGLEEQINDLTELHQNEIENLKQTIADME 514
Cdd:pfam10267 218 SQNGLAAILEELQEIKEAQVQLEEKLERLKTqFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASME 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  515 EKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQ-QYVTVEGIDNSNARALVVKLINVVLTILQVVLLLVATAAGIIMPF 593
Cdd:pfam10267 298 EKVAYQSYERARDIQEALESCQTRISKMELQQQQqQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPL 377

                         410       420
                  ....*....|....*....|....
gi 221378064  594 LKTRVRVLTTFLSICFVIFVIRQW 617
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 ...
 208-617 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: 552.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  208 SVQAIDRLNTKIQCTKESIRQEQTARDDNVNEYLKLAASADKQQLQRIKAVFEKKNQKSAHNISQLQKKLDNYTKRAKDL 287
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  288 QNHQFQTKSQHRQPREVLRDVGQGLRNVGGNIRDGITGFSGS----VMSKPREFAHLIKNKFGSADNINQMSEAELQGMQ 363
Cdd:pfam10267  81 ENGEQSSVTSHRQPKEVLRDVGQGLRDVGGNIRDGISGLSGGppptVFSKPREFAHLIKNKFGSADNINSLKSSLETSHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  364 SANADVLGSerlqqvpgagtstgsggggqnnnTGGAGSGTGKFNSDNGSECSSVTSESI--------PGGSGKSQSGASQ 435
Cdd:pfam10267 161 EGGGRKLSG-----------------------STFSTVTKPKYPSDDECSSSSVESISAgsngnpppHGADNGGQQAESD 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  436 YHIVLKTLLTELAERKAENEKLKERIERLET-GQKEFNNLTATLESERYRAEGLEEQINDLTELHQNEIENLKQTIADME 514
Cdd:pfam10267 218 SQNGLAAILEELQEIKEAQVQLEEKLERLKTqFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASME 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  515 EKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQ-QYVTVEGIDNSNARALVVKLINVVLTILQVVLLLVATAAGIIMPF 593
Cdd:pfam10267 298 EKVAYQSYERARDIQEALESCQTRISKMELQQQQqQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPL 377

                         410       420
                  ....*....|....*....|....
gi 221378064  594 LKTRVRVLTTFLSICFVIFVIRQW 617
Cdd:pfam10267 378 LKTRLRILTTILLVLLLIIFWKNW 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
440-617 9.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 9.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 440 LKTLLTELAERKAENEKLKERIERLETGQ------KEFNNLTATLESERYRAEGLEEQINDLTELHQ------NEIENLK 507
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPERLEELEERLEELRELEEeleeleAELAELQ 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 508 QTIADMEEKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEG----IDNSNARALVVKLINVV--LTILQVVLL 581
Cdd:COG4717  177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEleeeLEQLENELEAAALEERLkeARLLLLIAA 256

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 221378064 582 LVATAAGIIMPFLKTRVRVLTTFLSICFVIFVIRQW 617
Cdd:COG4717  257 ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
440-517 3.38e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.38e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221378064 440 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRAEGLEEQINDLTElhqnEIENLKQTIADMEEKV 517
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE----RIEELKKEIEELEEKV 282
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 440-561 1.77e-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: 41.57  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064   440 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRA-EGLEEQINDLTELHQNEIENLKQTIADMEEKVQ 518
Cdd:TIGR00606  250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 221378064   519 YQSDER--LRDVNEVLENCQTRISKMEHMSQQQYVTVEGIDNSNA 561
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 ...
 208-617 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: 552.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  208 SVQAIDRLNTKIQCTKESIRQEQTARDDNVNEYLKLAASADKQQLQRIKAVFEKKNQKSAHNISQLQKKLDNYTKRAKDL 287
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  288 QNHQFQTKSQHRQPREVLRDVGQGLRNVGGNIRDGITGFSGS----VMSKPREFAHLIKNKFGSADNINQMSEAELQGMQ 363
Cdd:pfam10267  81 ENGEQSSVTSHRQPKEVLRDVGQGLRDVGGNIRDGISGLSGGppptVFSKPREFAHLIKNKFGSADNINSLKSSLETSHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  364 SANADVLGSerlqqvpgagtstgsggggqnnnTGGAGSGTGKFNSDNGSECSSVTSESI--------PGGSGKSQSGASQ 435
Cdd:pfam10267 161 EGGGRKLSG-----------------------STFSTVTKPKYPSDDECSSSSVESISAgsngnpppHGADNGGQQAESD 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  436 YHIVLKTLLTELAERKAENEKLKERIERLET-GQKEFNNLTATLESERYRAEGLEEQINDLTELHQNEIENLKQTIADME 514
Cdd:pfam10267 218 SQNGLAAILEELQEIKEAQVQLEEKLERLKTqFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASME 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  515 EKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQ-QYVTVEGIDNSNARALVVKLINVVLTILQVVLLLVATAAGIIMPF 593
Cdd:pfam10267 298 EKVAYQSYERARDIQEALESCQTRISKMELQQQQqQLVQLEGLENANARALLGKLINIVLAILTVILVLVSTAAKFVAPL 377

                         410       420
                  ....*....|....*....|....
gi 221378064  594 LKTRVRVLTTFLSICFVIFVIRQW 617
Cdd:pfam10267 378 LKTRLRILTTILLVLLLIIFWKNW 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
440-617 9.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 9.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 440 LKTLLTELAERKAENEKLKERIERLETGQ------KEFNNLTATLESERYRAEGLEEQINDLTELHQ------NEIENLK 507
Cdd:COG4717   97 LEELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPERLEELEERLEELRELEEeleeleAELAELQ 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 508 QTIADMEEKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEG----IDNSNARALVVKLINVV--LTILQVVLL 581
Cdd:COG4717  177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEleeeLEQLENELEAAALEERLkeARLLLLIAA 256

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 221378064 582 LVATAAGIIMPFLKTRVRVLTTFLSICFVIFVIRQW 617
Cdd:COG4717  257 ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 440-543 1.66e-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: 46.46  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 440 LKTLLTELAERKAENEKLKERIERLE------TGQKEFNNLTATLESERYRAEGLEEQINDLTElhqnEIENLKQTIADM 513
Cdd:COG1579   54 LEDLEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKEYEALQKEIESLKRRISDLEDEILELME----RIEELEEELAEL 129

                         90       100       110
                 ....*....|....*....|....*....|
gi 221378064 514 EEKVqyqsDERLRDVNEVLENCQTRISKME 543
Cdd:COG1579  130 EAEL----AELEAELEEKKAELDEELAELE 155
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 439-543 7.57e-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: 44.53  E-value: 7.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 439 VLKTLLTELAERKAENEKLKERIERLETG----QKEFNNLTATLESERYRAEGLEEQINDLT---ELH--QNEIENLKQT 509
Cdd:COG1579   25 RLKELPAELAELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkEYEalQKEIESLKRR 104

                         90       100       110
                 ....*....|....*....|....*....|....
gi 221378064 510 IADMEEKVQyQSDERLRDVNEVLENCQTRISKME 543
Cdd:COG1579  105 ISDLEDEIL-ELMERIEELEEELAELEAELAELE 137
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
440-517 3.38e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.38e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221378064 440 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRAEGLEEQINDLTElhqnEIENLKQTIADMEEKV 517
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE----RIEELKKEIEELEEKV 282
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
442-542 1.17e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 442 TLLTELAERKAENEKLKERIERLET---GQKEFNNLT--------------ATLESERYRAEGLEEQINDL--------- 495
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEDlveAEDRIERLEerredleeliaerrETIEEKRERAEELRERAAELeaeaeekre 558

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221378064 496 --TELHQnEIENLKQTIADMEEKVQYQSD--ERLRDVNEVL---ENCQTRISKM 542
Cdd:PRK02224 559 aaAEAEE-EAEEAREEVAELNSKLAELKEriESLERIRTLLaaiADAEDEIERL 611
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 440-561 1.77e-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: 41.57  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064   440 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRA-EGLEEQINDLTELHQNEIENLKQTIADMEEKVQ 518
Cdd:TIGR00606  250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 221378064   519 YQSDER--LRDVNEVLENCQTRISKMEHMSQQQYVTVEGIDNSNA 561
Cdd:TIGR00606  330 KLNKERrlLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLA 374
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
445-569 3.62e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 445 TELAERKAE----NEKLKERIERLETGQKEFNNLTATLESERYRAEGLEEQINDLtelhQNEIENLKQTIADMEEKVQyQ 520
Cdd:COG4372   66 EELEQARSEleqlEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIA-E 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 221378064 521 SDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEGIDNSNARALVVKLI 569
Cdd:COG4372  141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 440-533 3.96e-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: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 440 LKTLLTELAERKAENEKLKERIERLetgQKEFNNLTATLESERYRAEGLEEQINDLTE---LHQNEIENLKQTIADMEEK 516
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQAeeyELLAELARLEQDIARLEER 310

                         90
                 ....*....|....*..
gi 221378064 517 VQYQSDERLRDVNEVLE 533
Cdd:COG1196  311 RRELEERLEELEEELAE 327
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 446-568 4.63e-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: 40.05  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064   446 ELAERKAENEKLKERIERLEtgqKEFNNLTATLESERYRAEGLEEQINDLTE---LHQNEIENLKQTIADMEEKVQ---- 518
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIE---QKLNRLTLEKEYLEKEIQELQEQRIDLKEqikSIEKEIENLNGKKEELEEELEelea 875

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 221378064   519 --YQSDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEgIDNSNARALVVKL 568
Cdd:TIGR02169  876 alRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRLSELKAKL 926
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 443-557 5.73e-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: 40.05  E-value: 5.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064   443 LLTELAERKAENEKLKERIERLEtgqKEFNNLTATLESERYRAEGLEEQINDL-----------TELHQnEIENLKQTIA 511
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELkreldrlqeelQRLSE-ELADLNAAIA 430

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 221378064   512 DMEEKVQyQSDERLRDVNEVLE----NCQTRISKMEHMSQQQYVTVEGID 557
Cdd:TIGR02169  431 GIEAKIN-ELEEEKEDKALEIKkqewKLEQLAADLSKYEQELYDLKEEYD 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 433-542 5.74e-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: 5.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064   433 ASQYHIVLKTLLTELAERKAENEKLKERIERLETGQKEFN--NLTAT--LESERYRAEGLEEQINDLTElhqnEIENLKQ 508
Cdd:TIGR02168  946 SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvNLAAIeeYEELKERYDFLTAQKEDLTE----AKETLEE 1021

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 221378064   509 TIADMEEKVQyqsdERLRDV-NEVLENCQTRISKM 542
Cdd:TIGR02168 1022 AIEEIDREAR----ERFKDTfDQVNENFQRVFPKL 1052
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 440-524 5.84e-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: 5.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064   440 LKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESeryRAEGLEEQINDLT----------ELHQNEIENLKQT 509
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELES---RLEELEEQLETLRskvaqlelqiASLNNEIERLEAR 408

                           90
                   ....*....|....*
gi 221378064   510 IADMEEKVQYQSDER 524
Cdd:TIGR02168  409 LERLEDRRERLQQEI 423
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
444-540 7.71e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 7.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 444 LTELAERKAENEKLKERIERLEtgqKEFNNLTATLESERYRAEGLEEQINDL---TELHQNEIENLKQTIADMEEKvqyq 520
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETE---REREELAEEVRDLRERLEELEEERDDLlaeAGLDDADAEAVEARREELEDR---- 322

                         90       100
                 ....*....|....*....|
gi 221378064 521 sDERLRDvneVLENCQTRIS 540
Cdd:PRK02224 323 -DEELRD---RLEECRVAAQ 338
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 429-548 7.91e-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: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064  429 SQSGASQYHIVLKTLLTELAERKAENEKLKERIERLetgqkefNNLTATLESER----YRAEGLEEQINDLTELHQN--- 501
Cdd:pfam15905 196 SKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITEL-------SCVSEQVEKYKldiaQLEELLKEKNDEIESLKQSlee 268

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 221378064  502 EIENLKQTIADMEEKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQ 548
Cdd:pfam15905 269 KEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEK 315
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
439-543 9.97e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 9.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378064 439 VLKTLLTELAERKAENEK----LKERI----ERLETGQKEFNNLTATLESERYRAEGLEEQINDLTE------------- 497
Cdd:PRK02224 255 TLEAEIEDLRETIAETERereeLAEEVrdlrERLEELEEERDDLLAEAGLDDADAEAVEARREELEDrdeelrdrleecr 334

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 221378064 498 ----LHQNEIENLKQTIADMEEKVQyQSDERLRDVNEVLENCQTRISKME 543
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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