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Conserved domains on  [gi|212646167|ref|NP_001129872|]
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C3H1-type domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00121 super family cl31754
MAEBL; Provisional
 258-443 2.25e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  258 KEAKDEKKKSKIQADEKLR--HEERQSTSDYTDDDPIPFTSRRSITGSVSYNYAEQIAERRRVEqqqEDRERQEMLEVER 335
Cdd:PTZ00121 1122 KKAEDARKAEEARKAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE---EVRKAEELRKAED 1198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  336 QRRVLEDRRnsEEEIRKQAELDRVEKDRlRMEQAAAAmEKARKEAELAKRariykhvfrgAEEEGGTEQLEELEQKILGV 415
Cdd:PTZ00121 1199 ARKAEAARK--AEEERKAEEARKAEDAK-KAEAVKKA-EEAKKDAEEAKK----------AEEERNNEEIRKFEEARMAH 1264

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 212646167  416 DIETG-------RRLLKEVSEVEWHKKQDEA----EIRK 443
Cdd:PTZ00121 1265 FARRQaaikaeeARKADELKKAEEKKKADEAkkaeEKKK 1303
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 22-187 5.16e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   22 AESEARSEWFPFGENLTPGGGSPLRKFEPKESVEHSTSESSEKASTSMHQA------PATSTDENPPIESDVPMHHVYPS 95
Cdd:pfam03154 190 GTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQrlpsphPPLQPMTQPPPPSQVSPQPLPQP 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   96 HHHHQHYQLPH-LQQHPHPYSYPLYTFPYPIAPAFHQAQNPPMTSSVASGANGEHHHQP------QQFFAPQYQVIPAGa 168
Cdd:pfam03154 270 SLHGQMPPMPHsLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPpsqsqlQSQQPPREQPLPPA- 348

                         170
                  ....*....|....*....
gi 212646167  169 iPVSTINIDPSQICPVDQM 187
Cdd:pfam03154 349 -PLSMPHIKPPPTTPIPQL 366
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
 258-443 2.25e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  258 KEAKDEKKKSKIQADEKLR--HEERQSTSDYTDDDPIPFTSRRSITGSVSYNYAEQIAERRRVEqqqEDRERQEMLEVER 335
Cdd:PTZ00121 1122 KKAEDARKAEEARKAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE---EVRKAEELRKAED 1198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  336 QRRVLEDRRnsEEEIRKQAELDRVEKDRlRMEQAAAAmEKARKEAELAKRariykhvfrgAEEEGGTEQLEELEQKILGV 415
Cdd:PTZ00121 1199 ARKAEAARK--AEEERKAEEARKAEDAK-KAEAVKKA-EEAKKDAEEAKK----------AEEERNNEEIRKFEEARMAH 1264

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 212646167  416 DIETG-------RRLLKEVSEVEWHKKQDEA----EIRK 443
Cdd:PTZ00121 1265 FARRQaaikaeeARKADELKKAEEKKKADEAkkaeEKKK 1303
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 313-443 3.13e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 47.73  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  313 AERRR---VEQQQEDRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAA------AMEKARKEAELA 383
Cdd:pfam05672  17 AEKRRqarEQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQrkaeeeAEEREQREQEEQ 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  384 KRARIYKhvfrgaeEEGGTEQLEELEQKILgvdiETGRRLLKEVSEVEWHKKQDEaEIRK 443
Cdd:pfam05672  97 ERLQKQK-------EEAEAKAREEAERQRQ----EREKIMQQEEQERLERKKRIE-EIMK 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-446 1.36e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRRVEQQQEDRE------RQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAEL 382
Cdd:COG1196  319 EELEEELAELEEELEELEeeleelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212646167 383 AKRARIYKHVFRGAEE--EGGTEQLEELEQKILGVDIETGRRLLKEVSEVEWHKKQDEAEIRKNAP 446
Cdd:COG1196  399 AAQLEELEEAEEALLErlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 309-411 8.87e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  309 AEQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEEirKQAELdrveKDRLRMEQAAAAMEKARKEAELAKRari 388
Cdd:TIGR02794  49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQA--RQKEL----EQRAAAEKAAKQAEQAAKQAEEKQK--- 119

                          90       100
                  ....*....|....*....|...
gi 212646167  389 ykhvfrgAEEEGGTEQLEELEQK 411
Cdd:TIGR02794 120 -------QAEEAKAKQAAEAKAK 135
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 309-412 2.76e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRRVEQQQEDRERQEMLEVERQ-RRVLEDRRNSEEEIRKQ--AELDRvEKDRLRMEQAAAAMEKARKEAELakr 385
Cdd:cd16269  196 KEKEIEAERAKAEAAEQERKLLEEQQRElEQKLEDQERSYEEHLRQlkEKMEE-ERENLLKEQERALESKLKEQEAL--- 271

                         90       100
                 ....*....|....*....|....*..
gi 212646167 386 ariykhvfrgaEEEGGTEQLEELEQKI 412
Cdd:cd16269  272 -----------LEEGFKEQAELLQEEI 287
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 22-187 5.16e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   22 AESEARSEWFPFGENLTPGGGSPLRKFEPKESVEHSTSESSEKASTSMHQA------PATSTDENPPIESDVPMHHVYPS 95
Cdd:pfam03154 190 GTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQrlpsphPPLQPMTQPPPPSQVSPQPLPQP 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   96 HHHHQHYQLPH-LQQHPHPYSYPLYTFPYPIAPAFHQAQNPPMTSSVASGANGEHHHQP------QQFFAPQYQVIPAGa 168
Cdd:pfam03154 270 SLHGQMPPMPHsLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPpsqsqlQSQQPPREQPLPPA- 348

                         170
                  ....*....|....*....
gi 212646167  169 iPVSTINIDPSQICPVDQM 187
Cdd:pfam03154 349 -PLSMPHIKPPPTTPIPQL 366
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
 258-443 2.25e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  258 KEAKDEKKKSKIQADEKLR--HEERQSTSDYTDDDPIPFTSRRSITGSVSYNYAEQIAERRRVEqqqEDRERQEMLEVER 335
Cdd:PTZ00121 1122 KKAEDARKAEEARKAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE---EVRKAEELRKAED 1198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  336 QRRVLEDRRnsEEEIRKQAELDRVEKDRlRMEQAAAAmEKARKEAELAKRariykhvfrgAEEEGGTEQLEELEQKILGV 415
Cdd:PTZ00121 1199 ARKAEAARK--AEEERKAEEARKAEDAK-KAEAVKKA-EEAKKDAEEAKK----------AEEERNNEEIRKFEEARMAH 1264

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 212646167  416 DIETG-------RRLLKEVSEVEWHKKQDEA----EIRK 443
Cdd:PTZ00121 1265 FARRQaaikaeeARKADELKKAEEKKKADEAkkaeEKKK 1303
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 313-443 3.13e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 47.73  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  313 AERRR---VEQQQEDRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAA------AMEKARKEAELA 383
Cdd:pfam05672  17 AEKRRqarEQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQrkaeeeAEEREQREQEEQ 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  384 KRARIYKhvfrgaeEEGGTEQLEELEQKILgvdiETGRRLLKEVSEVEWHKKQDEaEIRK 443
Cdd:pfam05672  97 ERLQKQK-------EEAEAKAREEAERQRQ----EREKIMQQEEQERLERKKRIE-EIMK 144
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 309-445 3.75e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.19  E-value: 3.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQiaERRRVEQQQEDRERQEML-EVERQRRvLEDRRNSEEEIRKQAEldrvEKDRLRMEQAAAAMEKARKEAELAKRAr 387
Cdd:PRK09510  77 AEE--QRKKKEQQQAEELQQKQAaEQERLKQ-LEKERLAAQEQKKQAE----EAAKQAALKQKQAEEAAAKAAAAAKAK- 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 212646167 388 iykhvfrgAEEEggTEQLEELEQKIlgvdietgrRLLKEVSEVEWHKKQDEAEIRKNA 445
Cdd:PRK09510 149 --------AEAE--AKRAAAAAKKA---------AAEAKKKAEAEAAKKAAAEAKKKA 187
PTZ00121 PTZ00121
MAEBL; Provisional
 258-605 3.84e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  258 KEAKDEKK-KSKIQADEKLRHEERQSTSDYTDDDPIPFTSRRSITGSVSYNYAEQI-AERRRVEQQQEDRERQEMLEVER 335
Cdd:PTZ00121 1552 KKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKKAEEE 1631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  336 QRRVLEDRRNSEEEIRKQAELDRVEKD-RLRMEQAAAAMEKARKEAELAKRARiykhvfrgAEEEGGTEQLEELEQKILG 414
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDKKKAEEAKKAE--------EDEKKAAEALKKEAEEAKK 1703

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  415 VDiETGRRLLKEVSEVEWHKKqdEAEIRKNAPPQSDRSAHNLSSLSSGNQSARGRSSSISSPCKPDtsftrnsigrrsvr 494
Cdd:PTZ00121 1704 AE-ELKKKEAEEKKKAEELKK--AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE-------------- 1766

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  495 ttsREKQQESPKSSDQAVQHPLAASTPVRRPPRQPQALPTQDEIHVAREvplANKSTTPSPTRS-EMLRSAAIYCPINRD 573
Cdd:PTZ00121 1767 ---EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE---GGKEGNLVINDSkEMEDSAIKEVADSKN 1840

                         330       340       350
                  ....*....|....*....|....*....|..
gi 212646167  574 plSQREELRAINRSTSNTGAYHNNNNNNNSKF 605
Cdd:PTZ00121 1841 --MQLEEADAFEKHKFNKNNENGEDGNKEADF 1870
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 315-411 4.06e-06

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 47.35  E-value: 4.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  315 RRRVEQQQEDRERQEMLEVERQRRVL--EDRRNSEEEIRKQAELDRVEKDRLRMEQaaaamEKARKEAElaKRARIYKHV 392
Cdd:pfam15346  40 ERRVEEARKIMEKQVLEELEREREAEleEERRKEEEERKKREELERILEENNRKIE-----EAQRKEAE--ERLAMLEEQ 112

                          90
                  ....*....|....*....
gi 212646167  393 FRGAEEEGGTEQLEELEQK 411
Cdd:pfam15346 113 RRMKEERQRREKEEEEREK 131
PTZ00121 PTZ00121
MAEBL; Provisional
 258-445 1.17e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  258 KEAKDEKKKSKIQADEKLRH--EERQSTSDYTDDDPIPFTSRRSITGSVSYNYAEQIAERRRVEQ---QQEDRERQEMLE 332
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKdaEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElkkAEEKKKADEAKK 1297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  333 VERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELAK-RARIYKHVFRGAEEEGGTEQLEELEQK 411
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaEAEAAADEAEAAEEKAEAAEKKKEEAK 1377

                         170       180       190
                  ....*....|....*....|....*....|....
gi 212646167  412 ilgVDIETGRRLLKEVSEVEWHKKQDEaEIRKNA 445
Cdd:PTZ00121 1378 ---KKADAAKKKAEEKKKADEAKKKAE-EDKKKA 1407
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-446 1.36e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRRVEQQQEDRE------RQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAEL 382
Cdd:COG1196  319 EELEEELAELEEELEELEeeleelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212646167 383 AKRARIYKHVFRGAEE--EGGTEQLEELEQKILGVDIETGRRLLKEVSEVEWHKKQDEAEIRKNAP 446
Cdd:COG1196  399 AAQLEELEEAEEALLErlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 309-404 1.61e-05

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 45.94  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  309 AEQIAERRRVEQQQEDRERQE-MLEVERQRRVLE-DRRNSEEEIRKQAEldRVEKDRLRMEQAAAAMEKARkeaELAKRA 386
Cdd:pfam15236  62 KKQLEEKERQKKLEEERRRQEeQEEEERLRREREeEQKQFEEERRKQKE--KEEAMTRKTQALLQAMQKAQ---ELAQRL 136

                          90
                  ....*....|....*...
gi 212646167  387 RIYKHVFRGAEEEGGTEQ 404
Cdd:pfam15236 137 KQEQRIRELAEKGHDTSQ 154
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 309-443 2.40e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.61  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  309 AEQIAERRRVEQQQEDRERQEMLEVERQRRvlEDRRNSEEEIRKQAELDRVEKDRLrMEQAAAAMEKARKEAElAKRARI 388
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQELQQARE--EQIELKERRLAEEAEREEEEFERM-LRKQAEDEEIEQEEAE-KRRMKR 288

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 212646167  389 YKHvfrGAEEEggtEQLEELEQKilgvdietgRRLLKEVSEVEWHKKQDEAEIRK 443
Cdd:pfam13868 289 LEH---RRELE---KQIEEREEQ---------RAAEREEELEEGERLREEEAERR 328
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-426 2.75e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 308 YAEQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAM-EKARKEAELAKRA 386
Cdd:COG1196  652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLeEELEEEALEEQLE 731

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 212646167 387 RIYKHVFRGAEEEGGTEQLEELEQKILGVDIETGRRLLKE 426
Cdd:COG1196  732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
PTZ00121 PTZ00121
MAEBL; Provisional
 259-443 3.52e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  259 EAKDEKKKSKIQADEKLRHEERQSTSDYTDDDPIPFTSRRSITGSVSYNYAEQIAERRRVEQQQEDRERQEMLEVERQRR 338
Cdd:PTZ00121 1050 EDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARK 1129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  339 VLEDRRnsEEEIRKQAELDRVEKDRlRMEQAAAAmEKARKeAELAKRARIYKHV--FRGAEEEGGTEQLEELEQkilGVD 416
Cdd:PTZ00121 1130 AEEARK--AEDARKAEEARKAEDAK-RVEIARKA-EDARK-AEEARKAEDAKKAeaARKAEEVRKAEELRKAED---ARK 1201

                         170       180       190
                  ....*....|....*....|....*....|.
gi 212646167  417 IETGRRlLKEVSEVEWHKKQDEA----EIRK 443
Cdd:PTZ00121 1202 AEAARK-AEEERKAEEARKAEDAkkaeAVKK 1231
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 309-443 4.48e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  309 AEQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNS-------EEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAE 381
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIarlraqqEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212646167  382 laKRARIYKHVFRGAEEEggTEQLEELEQKILGVDIETGRRLLKEVSEVEWHKKQDEAEIRK 443
Cdd:pfam13868 229 --KKARQRQELQQAREEQ--IELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM 286
PTZ00121 PTZ00121
MAEBL; Provisional
 258-443 5.80e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 5.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  258 KEAKDEKKKSKIQADEKLR--HEERQSTSDYTDDDPIPFTSRRsitgsvsynyAEQI--AERRRVEQQQEDRERQEMLEV 333
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRK----------AEEAkkAEEARIEEVMKLYEEEKKMKA 1609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  334 ERQRRVLEDRRNSE-----EEIRKQAEL--DRVEKDRLRMEQAAAAMEKAR-KEAELAKRARIYKhvfRGAEEeggTEQL 405
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEelkkaEEEKKKVEQlkKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDK---KKAEE---AKKA 1683

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 212646167  406 EELEQKilgvDIETGRRLLKEVSEVEWHKKQDEAEIRK 443
Cdd:PTZ00121 1684 EEDEKK----AAEALKKEAEEAKKAEELKKKEAEEKKK 1717
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-456 6.76e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 6.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAmEKARKEAELAKRARI 388
Cdd:COG1196  351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEA 429

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212646167 389 YKHVFRGAEEEggTEQLEELEQKILGVDIETGRRLLKEVSEVEWHKKQDEAEIRKNAPPQSDRSAHNL 456
Cdd:COG1196  430 LAELEEEEEEE--EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 259-445 7.12e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 259 EAKDEKKKSKIQADEKLRHEERQStsdytdddpipftsRRSITGSVSynyAEQIAERRRVEQQQEDRERQEMLEVERQRR 338
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAE--------------EYELLAELA---RLEQDIARLEERRRELEERLEELEEELAEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 339 VLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELAKRARIyKHVFRGAEEEGGTEQLEELEQKILGVDIE 418
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-EELEELAEELLEALRAAAELAAQLEELEE 407

                        170       180
                 ....*....|....*....|....*..
gi 212646167 419 TGRRLLKEVSEVEWHKKQDEAEIRKNA 445
Cdd:COG1196  408 AEEALLERLERLEEELEELEEALAELE 434
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 309-411 8.87e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  309 AEQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEEirKQAELdrveKDRLRMEQAAAAMEKARKEAELAKRari 388
Cdd:TIGR02794  49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQA--RQKEL----EQRAAAEKAAKQAEQAAKQAEEKQK--- 119

                          90       100
                  ....*....|....*....|...
gi 212646167  389 ykhvfrgAEEEGGTEQLEELEQK 411
Cdd:TIGR02794 120 -------QAEEAKAKQAAEAKAK 135
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
258-388 1.09e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 45.63  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 258 KEAKDEKKKSKIQADEKLRHEERQSTSDytdddpipftsrrsitgsVSYNYAEQIAERRrVEQQQEDRERQEMLEVErQR 337
Cdd:COG2268  238 RIAEAEAELAKKKAEERREAETARAEAE------------------AAYEIAEANAERE-VQRQLEIAEREREIELQ-EK 297

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212646167 338 RVLEDRRNSEEEIRKQAELDRvEKDRLRME-QAAAAMEKARKEAElAKRARI 388
Cdd:COG2268  298 EAEREEAELEADVRKPAEAEK-QAAEAEAEaEAEAIRAKGLAEAE-GKRALA 347
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 259-431 1.30e-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: 45.83  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   259 EAKDEKKKSKIQADEKLRHEERQSTSDYTDDDPIPFTSR-RSITGSVSyNYAEQIAERrrvEQQQEDRERQEMLEVERQR 337
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIA-SLERSIAEK---ERELEDAEERLAKLEAEID 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   338 RVLEDRRNSEEEIRKQaeldRVEKDRL--RMEQAAAAMEKARKEA-ELAKRARIYKHVFRGAEE--EGGTEQLEELeQKI 412
Cdd:TIGR02169  333 KLLAEIEELEREIEEE----RKRRDKLteEYAELKEELEDLRAELeEVDKEFAETRDELKDYREklEKLKREINEL-KRE 407

                          170
                   ....*....|....*....
gi 212646167   413 LGVDIETGRRLLKEVSEVE 431
Cdd:TIGR02169  408 LDRLQEELQRLSEELADLN 426
PTZ00121 PTZ00121
MAEBL; Provisional
 309-445 1.57e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  309 AEQIAERRRVEQQ---QEDRERQEMLEVERQRRVLEDRRNSEEEirKQAELDRVEKDRLRMEQAAAAMEKARKEAELAKR 385
Cdd:PTZ00121 1199 ARKAEAARKAEEErkaEEARKAEDAKKAEAVKKAEEAKKDAEEA--KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE 1276

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  386 ARIYKHVfRGAEEEGGTEQLEELEQKilgVDIETGRRLLKEVSEVEWHKKQDEaEIRKNA 445
Cdd:PTZ00121 1277 ARKADEL-KKAEEKKKADEAKKAEEK---KKADEAKKKAEEAKKADEAKKKAE-EAKKKA 1331
PTZ00121 PTZ00121
MAEBL; Provisional
 258-580 1.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  258 KEAKDEKKKS--KIQADEKLRHEERQSTSDYTDDdpipftsrrsitgsvsynyAEQI--AERRRVEQQQEDRERQEMLEV 333
Cdd:PTZ00121 1353 EAAADEAEAAeeKAEAAEKKKEEAKKKADAAKKK-------------------AEEKkkADEAKKKAEEDKKKADELKKA 1413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  334 ERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELAKRA---RIYKHVFRGAEEEGGTEQL----E 406
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeaKKADEAKKKAEEAKKADEAkkkaE 1493

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  407 ELEQKILGV-DIETGRRLLKEVSEVEWHKKQDE---AEIRKNA----PPQSDRSAHNLSSLSSGNQSARGRSSSISSPCK 478
Cdd:PTZ00121 1494 EAKKKADEAkKAAEAKKKADEAKKAEEAKKADEakkAEEAKKAdeakKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  479 PDtsftRNSIGRRSVRTTSREKQQESPKSSDQAVQHPLAASTPVRRPPRQPQALPTQDEIHVAREVPLANKSTTPSPTRS 558
Cdd:PTZ00121 1574 ED----KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649

                         330       340
                  ....*....|....*....|..
gi 212646167  559 EMLRSAAIYCPINRDPLSQREE 580
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAE 1671
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 309-445 1.99e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  309 AEQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELAKRArI 388
Cdd:pfam13868  25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQ-M 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 212646167  389 YKHVFRGAEEEGGTEQLEELEQKILGVDIETGRRLLKEVSEVEwhKKQDEAEIRKNA 445
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE--KEEEREEDERIL 158
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 313-443 2.00e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  313 AERRRVEQQQEDRERQEMLEVERQRRVLEDRRNsEEEIRKQAELDRVEKDRLRMEQAAAAM---EKARKEAELAKRARIY 389
Cdd:pfam13868  51 EERERALEEEEEKEEERKEERKRYRQELEEQIE-EREQKRQEEYEEKLQEREQMDEIVERIqeeDQAEAEEKLEKQRQLR 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 212646167  390 KHVFRGAEE-----EGGTEQLEELEQKILGVDIEtgrrllKEVSEVEWHKKQDEAEIRK 443
Cdd:pfam13868 130 EEIDEFNEEqaewkELEKEEEREEDERILEYLKE------KAEREEEREAEREEIEEEK 182
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-413 2.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 308 YAEQIAERRRVEQQQEDRERQEmleverQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELAKRAR 387
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAE------EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                         90       100
                 ....*....|....*....|....*.
gi 212646167 388 IYKHVFRGAEEEGGTEQLEELEQKIL 413
Cdd:COG1196  462 LELLAELLEEAALLEAALAELLEELA 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-442 2.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRRVEQQQEDRERQEM-LEVERQRRVLEDRRNSEEEIrkQAELDRVEKDRLRMEQAAAAMEKARKEAELAKRAR 387
Cdd:COG1196  251 LEAELEELEAELAELEAELEELrLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 212646167 388 IYKHVFRGAEEEGGTEQLEELEQKIlgvdietgRRLLKEVSEVEWHKKQDEAEIR 442
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEEL--------EEAEAELAEAEEALLEAEAELA 375
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
259-442 3.45e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 259 EAKDEKKKSKIQADEKL-RHEERQSTSDYTDDDPIPFTSRRSITGSVSYNYAEQIAERRRVEQQQEDR------------ 325
Cdd:PRK02224 227 EQREQARETRDEADEVLeEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeagldd 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 326 -------ERQEMLEVERQ--RRVLEDRRNSEEEIRKQAELDRVEKDRLRmEQAAAAMEKAR---KEAELAKRARiykhvf 393
Cdd:PRK02224 307 adaeaveARREELEDRDEelRDRLEECRVAAQAHNEEAESLREDADDLE-ERAEELREEAAeleSELEEAREAV------ 379

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 212646167 394 rgaeeEGGTEQLEELEQKI---------LGVDIETGRRLLKEVSEVEWHKKQDEAEIR 442
Cdd:PRK02224 380 -----EDRREEIEELEEEIeelrerfgdAPVDLGNAEDFLEELREERDELREREAELE 432
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 311-443 3.51e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 43.87  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  311 QIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELAKR--ARI 388
Cdd:pfam15558  28 QQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDqeNQR 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 212646167  389 YKHVFRGAEEEGGTEQLEELEQKILgvdiETGRRLLKEVSEVEWHKKQDEAEIRK 443
Cdd:pfam15558 108 QEKLERARQEAEQRKQCQEQRLKEK----EEELQALREQNSLQLQERLEEACHKR 158
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 311-384 5.82e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.57  E-value: 5.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  311 QIAERRRVEQQQedRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRL-RMEQAAA------AMEKARKEAELA 383
Cdd:PTZ00266  453 KILEKKRIERLE--REERERLERERMERIERERLERERLERERLERDRLERDRLdRLERERVdrlerdRLEKARRNSYFL 530


                  .
gi 212646167  384 K 384
Cdd:PTZ00266  531 K 531
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 313-388 6.74e-04

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 40.76  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  313 AERRRVE-QQQEDRERQEMLEVERQRRVLedRRNSEEEIRKQAE--LDRVEKDRLRMEQAAAA-MEKARKEAELAKRARI 388
Cdd:pfam00430  42 AEERRKDaAAALAEAEQQLKEARAEAQEI--IENAKKRAEKLKEeiVAAAEAEAERIIEQAAAeIEQEKDRALAELRQQV 119
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 259-443 8.20e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  259 EAKDEKKKSKIQADEKLRHEERQSTsdytdddpipftsRRSItgsvsynyAEQIAERRR---VEQQQEDRERQEMLEV-- 333
Cdd:pfam13868  50 EEERERALEEEEEKEEERKEERKRY-------------RQEL--------EEQIEEREQkrqEEYEEKLQEREQMDEIve 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  334 --------------ERQRRVLEDRRNSEEE--IRKQAELDRVEKDRLRMEQAA-------AAMEKARKEAELAKRARIYK 390
Cdd:pfam13868 109 riqeedqaeaeeklEKQRQLREEIDEFNEEqaEWKELEKEEEREEDERILEYLkekaereEEREAEREEIEEEKEREIAR 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 212646167  391 HVFRGAEEEGGTEQLEELEQKilgvdietgrrLLKEVSEVEWHKKQDEAEIRK 443
Cdd:pfam13868 189 LRAQQEKAQDEKAERDELRAK-----------LYQEEQERKERQKEREEAEKK 230
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-443 8.95e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 8.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQiAERRRvEQQQEDRERqemlevERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELAKRARI 388
Cdd:COG1196  209 AEK-AERYR-ELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 212646167 389 YKHVFRGAEEEGGTEQLEELEQKILgVDIETGRRLLKEVSEVEWHKKQDEAEIRK 443
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIA-RLEERRRELEERLEELEEELAELEEELEE 334
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 309-498 9.00e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.53  E-value: 9.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  309 AEQIAERRRVEQQQEDRERQ------EMLEVERQRRVLEDRRNSEEEIRKQAELDRV---EKDRLRMEQAAAA----MEK 375
Cdd:TIGR02794  77 AEEAEKQRAAEQARQKELEQraaaekAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKakaEAEAERKAKEEAAkqaeEEA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  376 ARKEAELAKRARiyKHVFRGAEEEggTEQLEELEQKILGVDIETGRRLLKEVSEVEWHKK-------QDEAEIRKNAPPQ 448
Cdd:TIGR02794 157 KAKAAAEAKKKA--EEAKKKAEAE--AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKaeaeaaaAAAAEAERKADEA 232

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 212646167  449 SDRSAHNLSSLSSGNQSARGRSSSISSPCKPDTSFTRNSIGRRSVRTTSR 498
Cdd:TIGR02794 233 ELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLYDDPSF 282
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 308-388 1.09e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  308 YAEQIAERRRVEQQQEDRERQEMLEVERQRRVLE--DRRNSEEEIRKQAELDR------VEKDRLRMEQAAAAMEKARKE 379
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEeiEQEEAEKRRMKRLEHRRelekqiEEREEQRAAEREEELEEGERL 320

                          90
                  ....*....|.
gi 212646167  380 AELAK--RARI 388
Cdd:pfam13868 321 REEEAerRERI 331
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
309-413 1.36e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.96  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRRVEQQ-------QEDRERQEMLEVERQ-----RRVLEDRRNSEEEIRK-QAELDRVEKDRLRMEQAAAAME- 374
Cdd:COG1842   47 AQVIANQKRLERQleeleaeAEKWEEKARLALEKGredlaREALERKAELEAQAEAlEAQLAQLEEQVEKLKEALRQLEs 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 212646167 375 -----KARKEAELA--KRARIYKHV---FRGAEEEGGTEQLEELEQKIL 413
Cdd:COG1842  127 kleelKAKKDTLKAraKAAKAQEKVneaLSGIDSDDATSALERMEEKIE 175
fliH PRK06669
flagellar assembly protein H; Validated
 264-429 1.53e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 41.54  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 264 KKKSKIQADEKLRHEERQSTSDYTDDDPIPFTSRRSITGSVSYNY-AEQIAERRRVEQQQEDRERQEMLE---VERQRRV 339
Cdd:PRK06669   7 KRSNVINKEKLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQLREeANDEAKEIIEEAEEDAFEIVEAAEeeaKEELLKK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 340 LEDRRNSEEEIRKQAELDRVEKDRLR---MEQAAA-----AMEKARKEA--ELAKRARIYKHVFRGAEEEgGTEQLEELE 409
Cdd:PRK06669  87 TDEASSIIEKLQMQIEREQEEWEEELerlIEEAKAegyeeGYEKGREEGleEVRELIEQLNKIIEKLIKK-REEILESSE 165

                        170       180
                 ....*....|....*....|
gi 212646167 410 QKILGVDIETGRRLLKEVSE 429
Cdd:PRK06669 166 EEIVELALDIAKKVIKEISE 185
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
309-443 2.32e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRRVEQQ-QEDRERQEML-EVERQRR-VLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKE-AEL-A 383
Cdd:PRK02224 595 RTLLAAIADAEDEiERLREKREALaELNDERReRLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKlDELrE 674

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212646167 384 KRARIYKHVfRGAEEEggTEQLEEL--EQKILGVDIETGRRLLKEVSEVEWHKKQDEAEIRK 443
Cdd:PRK02224 675 ERDDLQAEI-GAVENE--LEELEELreRREALENRVEALEALYDEAEELESMYGDLRAELRQ 733
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 308-426 2.32e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  308 YAEQIAERRRVEQQQEDRERQEMLEVERQRRVL--EDRRNSEEEIRKQAELDRVE-----KDRLRMEQAAAAMEKARKEA 380
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEaeREEEEFERMLRKQAEDEEIEqeeaeKRRMKRLEHRRELEKQIEER 302

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 212646167  381 ELAKRARiykhvfRGAEEEGGTEQLEELEQKILGVDIETgRRLLKE 426
Cdd:pfam13868 303 EEQRAAE------REEELEEGERLREEEAERRERIEEER-QKKLKE 341
PTZ00491 PTZ00491
major vault protein; Provisional
 309-388 2.42e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 41.54  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRrvEQQQEDR-ERQEML---EVERQRRVL-------------------EDRRNSEEEIRKQAELD----RVEK 361
Cdd:PTZ00491 668 ARHQAELL--EQEARGRlERQKMHdkaKAEEQRTKLlelqaesaavessgqsraeALAEAEARLIEAEAEVEqaelRAKA 745

                         90       100
                 ....*....|....*....|....*..
gi 212646167 362 DRLRMEqAAAAMEKARKEAELAKRARI 388
Cdd:PTZ00491 746 LRIEAE-AELEKLRKRQELELEYEQAQ 771
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 309-412 2.76e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRRVEQQQEDRERQEMLEVERQ-RRVLEDRRNSEEEIRKQ--AELDRvEKDRLRMEQAAAAMEKARKEAELakr 385
Cdd:cd16269  196 KEKEIEAERAKAEAAEQERKLLEEQQRElEQKLEDQERSYEEHLRQlkEKMEE-ERENLLKEQERALESKLKEQEAL--- 271

                         90       100
                 ....*....|....*....|....*..
gi 212646167 386 ariykhvfrgaEEEGGTEQLEELEQKI 412
Cdd:cd16269  272 -----------LEEGFKEQAELLQEEI 287
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 258-444 3.17e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   258 KEAKDEKKKSKIQADEKLR------HEERQSTSDYTDDDPIPFTSRRSITGSVS--YNYAEQIAERRRVEQQQEDRERQE 329
Cdd:pfam02463  204 EQAKKALEYYQLKEKLELEeeyllyLDYLKLNEERIDLLQELLRDEQEEIESSKqeIEKEEEKLAQVLKENKEEEKEKKL 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   330 M----------LEVERQRRVLEDRR---------NSEEEIRK---------------QAELDRVEKDRLRMEQAAAAMEK 375
Cdd:pfam02463  284 QeeelkllakeEEELKSELLKLERRkvddeeklkESEKEKKKaekelkkekeeieelEKELKELEIKREAEEEEEEELEK 363

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212646167   376 ARKEAELAKRARIYKHVFRGAEEEGGTEQLEELEQKILgvDIETGRRLLKEVSEvewhKKQDEAEIRKN 444
Cdd:pfam02463  364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS--EEEKEAQLLLELAR----QLEDLLKEEKK 426
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 310-442 3.22e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.09  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  310 EQIAERRR--VEQQQEDRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELA---K 384
Cdd:pfam15709 340 AERAEMRRleVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQaaqE 419

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  385 RARIYKHVFR---------GAEEEGGTEQLEELEQKILGVDIETGRRLLKEVSE---VEWHKKQDEAEIR 442
Cdd:pfam15709 420 RARQQQEEFRrklqelqrkKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEeerLEYQRQKQEAEEK 489
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
308-469 3.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  308 YAEQIAERRRVEQQQEDRERQEMLEVERQRRVLEdrrnsEEEIRKQAELDRVEKDRlrmEQAAAAMEKARKEAELAKRAR 387
Cdd:COG4913   261 AERYAAARERLAELEYLRAALRLWFAQRRLELLE-----AELEELRAELARLEAEL---ERLEARLDALREELDELEAQI 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  388 iykhvfRGAeeegGTEQLEELEQKI--LGVDIETGRRLLKEVSE----VEWHKKQDEAEIRKNApPQSDRSAHNLSSLSS 461
Cdd:COG4913   333 ------RGN----GGDRLEQLEREIerLERELEERERRRARLEAllaaLGLPLPASAEEFAALR-AEAAALLEALEEELE 401


                  ....*...
gi 212646167  462 GNQSARGR 469
Cdd:COG4913   402 ALEEALAE 409
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 309-440 3.51e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 40.01  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  309 AEQIAERRRVEQQQEDRER-QEML---------------EVERQRRVLEDRRNSEEEirKQAELDRVEKDRLRMEQAAAA 372
Cdd:pfam00261  36 AEVAALNRRIQLLEEELERtEERLaealekleeaekaadESERGRKVLENRALKDEE--KMEILEAQLKEAKEIAEEADR 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  373 --MEKARKEAELakRARIYKHVFRGAEEEGGTEQLEElEQKILGVDIetgRRLlkEVSEVEWHKKQDEAE 440
Cdd:pfam00261 114 kyEEVARKLVVV--EGDLERAEERAELAESKIVELEE-ELKVVGNNL---KSL--EASEEKASEREDKYE 175
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 308-384 3.77e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 40.78  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  308 YAEQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEEirkqaELDR----VEKDRLRMEQAAAAMEKARKEAELA 383
Cdd:pfam05701  29 HRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLE-----ELEStkrlIEELKLNLERAQTEEAQAKQDSELA 103


                  .
gi 212646167  384 K 384
Cdd:pfam05701 104 K 104
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
309-445 3.80e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRrveQQQEDRERQEMLEVERQrrvleDRRNSEEEIRKQAELDrvekdrlRMEQAAAAMEKARKEAEL---AKR 385
Cdd:COG2268  195 AEIIRDAR---IAEAEAERETEIAIAQA-----NREAEEAELEQEREIE-------TARIAEAEAELAKKKAEErreAET 259

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212646167 386 ARIYkhvfrgAEEEGGTEQlEELEQKILgVDIETGRRlLKEV----SEVEWHKKQDEAEIRKNA 445
Cdd:COG2268  260 ARAE------AEAAYEIAE-ANAEREVQ-RQLEIAER-EREIelqeKEAEREEAELEADVRKPA 314
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 332-440 3.88e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.98  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  332 EVERQRRVLEDR-RNSEEEIRK-QAEL-------DRVEKDRLRMEQAAAAMEKARKEAELAKRaRIYKHVFRGAEEEggt 402
Cdd:pfam20492   3 EAEREKQELEERlKQYEEETKKaQEELeeseetaEELEEERRQAEEEAERLEQKRQEAEEEKE-RLEESAEMEAEEK--- 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 212646167  403 eqlEELEQKILGVDIETgrRLLKEVSEvewhKKQDEAE 440
Cdd:pfam20492  79 ---EQLEAELAEAQEEI--ARLEEEVE----RKEEEAR 107
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-440 3.89e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEE--IRKQAELDRVEKDRLRMEQAAAAmEKARKEAELAKRA 386
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELelEEAQAEEYELLAELARLEQDIAR-LEERRRELEERLE 319

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212646167 387 RIykhvfrGAEEEGGTEQLEELEQKILGVDIEtGRRLLKEVSEVEWHKKQDEAE 440
Cdd:COG1196  320 EL------EEELAELEEELEELEEELEELEEE-LEEAEEELEEAEAELAEAEEA 366
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 310-445 3.90e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 310 EQIAERRRVEQQQEDR--ERQEMLEVERQRR-VLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAM---EKARKEAELA 383
Cdd:PRK09510  95 KQAAEQERLKQLEKERlaAQEQKKQAEEAAKqAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKkaaAEAKKKAEAE 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212646167 384 KRARIYKHVFRGAEEEGGTEQLEELEQKILGVDIETGRRLLKEVSEVEWHKKQDEAEIRKNA 445
Cdd:PRK09510 175 AAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
324-445 4.53e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  324 DRERQEMLEVERQRRVLED-RRNSEEEIRKQAELD---------RVEKDRLRMEQAAAAMEKARKEAELAKRARiykhVF 393
Cdd:COG4913   238 ERAHEALEDAREQIELLEPiRELAERYAAARERLAeleylraalRLWFAQRRLELLEAELEELRAELARLEAEL----ER 313

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 212646167  394 RGAEEEGGTEQLEELEQKILGVDietGRRL--LKEvsEVEwHKKQDEAEIRKNA 445
Cdd:COG4913   314 LEARLDALREELDELEAQIRGNG---GDRLeqLER--EIE-RLERELEERERRR 361
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 338-445 4.68e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 38.62  E-value: 4.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 338 RVLEDRRnseEEIRKqaELDRVEKDRLRMEQAAAAMEKARKEAElAKRARIYKHvfrgAEEEgGTEQLEELEQKilgVDI 417
Cdd:COG0711   27 KALDERQ---EKIAD--GLAEAERAKEEAEAALAEYEEKLAEAR-AEAAEIIAE----ARKE-AEAIAEEAKAE---AEA 92

                         90       100
                 ....*....|....*....|....*...
gi 212646167 418 ETGRRLLKEVSEVEWHKKQDEAEIRKNA 445
Cdd:COG0711   93 EAERIIAQAEAEIEQERAKALAELRAEV 120
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
309-444 4.82e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 309 AEQIAE-RRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKE-AELAKRA 386
Cdd:PRK03918 237 KEEIEElEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElREIEKRL 316

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212646167 387 RIYKHVFRGAEE-----EGGTEQLEELEQKIlgvdietgRRLLKEVSEVE-WHKKQDEAEIRKN 444
Cdd:PRK03918 317 SRLEEEINGIEErikelEEKEERLEELKKKL--------KELEKRLEELEeRHELYEEAKAKKE 372
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 22-187 5.16e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   22 AESEARSEWFPFGENLTPGGGSPLRKFEPKESVEHSTSESSEKASTSMHQA------PATSTDENPPIESDVPMHHVYPS 95
Cdd:pfam03154 190 GTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQrlpsphPPLQPMTQPPPPSQVSPQPLPQP 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167   96 HHHHQHYQLPH-LQQHPHPYSYPLYTFPYPIAPAFHQAQNPPMTSSVASGANGEHHHQP------QQFFAPQYQVIPAGa 168
Cdd:pfam03154 270 SLHGQMPPMPHsLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPpsqsqlQSQQPPREQPLPPA- 348

                         170
                  ....*....|....*....
gi 212646167  169 iPVSTINIDPSQICPVDQM 187
Cdd:pfam03154 349 -PLSMPHIKPPPTTPIPQL 366
atpF CHL00019
ATP synthase CF0 B subunit
 334-410 5.86e-03

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 38.69  E-value: 5.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212646167 334 ERQRRVLEDRRNSEEeIRKQAeLDRVEKDRLRMEQAAAAMEKARKEAELAKRaRIYKHVFRGAEEEggTEQLEELEQ 410
Cdd:CHL00019  55 NRKQTILNTIRNSEE-RREEA-IEKLEKARARLRQAELEADEIRVNGYSEIE-REKENLINQAKED--LERLENYKN 126
PRK12704 PRK12704
phosphodiesterase; Provisional
 258-400 6.40e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 258 KEAKDEKKKSKIQADEKLrHEERQStsdytdddpipftsrrsitgsvsynyAEQIAERRRVE-QQQEDR--ERQEMLE-- 332
Cdd:PRK12704  49 KEAEAIKKEALLEAKEEI-HKLRNE--------------------------FEKELRERRNElQKLEKRllQKEENLDrk 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 333 ---VERQRRVLEDRRNS----EEEI-RKQAELDR-VEKDRLRMEQAAA---------AMEKARKEAElAKRARIYKHVFR 394
Cdd:PRK12704 102 lelLEKREEELEKKEKEleqkQQELeKKEEELEElIEEQLQELERISGltaeeakeiLLEKVEEEAR-HEAAVLIKEIEE 180


                 ....*.
gi 212646167 395 GAEEEG 400
Cdd:PRK12704 181 EAKEEA 186
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-440 7.42e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 7.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 310 EQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRnseEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELAKRARiy 389
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-- 309

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 212646167 390 KHVFRGAEEEGGTEQLEELEQKILGvDIETGRRLLKEVSEVEwhKKQDEAE 440
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEE-LEEELEELEEELEEAE--EELEEAE 357
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 321-407 7.62e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.21  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  321 QQEDRERQEM-LEVERQRRVLEDRRNSEEEIRKQAELdrvEKDRLRMEQAAAAMEKARKEAELA-KRARIYKHVFRGAEE 398
Cdd:pfam20492  26 QEELEESEETaEELEEERRQAEEEAERLEQKRQEAEE---EKERLEESAEMEAEEKEQLEAELAeAQEEIARLEEEVERK 102


                  ....*....
gi 212646167  399 EGGTEQLEE 407
Cdd:pfam20492 103 EEEARRLQE 111
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 310-461 8.06e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167  310 EQIAERRRVEQQQEDRERQEM--LEVERQRrvlEDRRNSEEEIRKQAELDRVEKDRLRMEQAAAAMEKARKEAELAKRAR 387
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVrrLEEERAR---EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR 493

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212646167  388 iyKHVFRGAEEEGGTEQLEE-LEQKILGVDIETGRRLLKEVSE----VEWHKKQDEAEIRKNAPPQSDRSAHNLSSLSS 461
Cdd:pfam17380 494 --RKILEKELEERKQAMIEEeRKRKLLEKEMEERQKAIYEEERrreaEEERRKQQEMEERRRIQEQMRKATEERSRLEA 570
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-387 8.95e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 8.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212646167 309 AEQIAERRRVEQQQEDRERQEMLEVERQRRVLEDRRNSEEEIRKQAELDrvEKDRLRMEQAAAAMEKARKEAELAKRAR 387
Cdd:COG1196  700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL--EEEALEELPEPPDLEELERELERLEREI 776
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 313-386 9.38e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.42  E-value: 9.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 313 AERRRVEQQQEDRERQEMLE---VERQRRVLEDRRNSE---EEIRKQAEldrvekdrlrmEQAAAAMEKARKEAELAKRA 386
Cdd:cd06503   42 AEKAKEEAEELLAEYEEKLAearAEAQEIIEEARKEAEkikEEILAEAK-----------EEAERILEQAKAEIEQEKEK 110
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
308-469 9.59e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 308 YAEQIAERRRVEQQQED---------RERQEMLE-VERQRRVLEDRRNSEEEIRKQAELDRVEKDRL------------- 364
Cdd:PRK02224 246 HEERREELETLEAEIEDlretiaeteREREELAEeVRDLRERLEELEEERDDLLAEAGLDDADAEAVearreeledrdee 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212646167 365 ---RMEQAAAAMEKARKEAELAkRARIYKHVFRGAEEEggtEQLEELEQKI--LGVDIETGRrllKEVSEVEwhKKQDEA 439
Cdd:PRK02224 326 lrdRLEECRVAAQAHNEEAESL-REDADDLEERAEELR---EEAAELESELeeAREAVEDRR---EEIEELE--EEIEEL 396

                        170       180       190
                 ....*....|....*....|....*....|.
gi 212646167 440 EIR-KNAPPQSDRSAHNLSSLSSGNQSARGR 469
Cdd:PRK02224 397 RERfGDAPVDLGNAEDFLEELREERDELRER 427
 
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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