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Conserved domains on  [gi|188219589|ref|NP_034851|]
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lamin-B1 [Mus musculus]

Protein Classification

intermediate filament family protein( domain architecture ID 11755560)

intermediate filament family protein such as lamins, which are a major component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
32-388 1.26e-100

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 425436 [Multi-domain]  Cd Length: 313  Bit Score: 307.61  E-value: 1.26e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKF 111
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEPSRLYSLYEREIRELRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  112 KAEHDQLLLNYAKKesdlsgaqiklreyeaalnskdaalataLGDKKSLEGDLEDLKdqiaqleaslsaakKQLADETLL 191
Cdd:pfam00038  81 RLAAEDFRQKYEDE----------------------------LNLRQSAEADIVGLR--------------KDLDEATLA 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  192 KVDLENRCQSLTEDLEFRKNMYEEEINETRRKH--ETRLVEVDSGRQIEyeykLAQALHEMREQHDAQVRLYKEELEQTY 269
Cdd:pfam00038 119 RVDLEMKIESLKEELAFLKKNHEEEVRELQSQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAEKNREEAEEWY 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  270 HAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAE 349
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQQ 274
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 188219589  350 IRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEER 388
Cdd:pfam00038 275 IRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
440-544 1.29e-23

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


:

Pssm-ID: 425951 [Multi-domain]  Cd Length: 103  Bit Score: 95.56  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  440 TGNVCIEEIDVDG-----KFIRLKNTSEQDQPMGGWEMIRKIGDTsvsYKYTSRYVLKAGQTVTVWaANAGVTASPPTDL 514
Cdd:pfam00932   4 TGDVVISEVVYDGsggndEFIELYNTGDKAVDLSGWKLSDASGGT---FTFPNGTTLAPGQTVVVW-TGGGAGYWGPLNA 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 188219589  515 IWKNQNSWgtgedvkVILKNSQGEEVAQRS 544
Cdd:pfam00932  80 VWNNGGDA-------VALYDANGELVDSVG 102
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
32-388 1.26e-100

Intermediate filament protein;


Pssm-ID: 425436 [Multi-domain]  Cd Length: 313  Bit Score: 307.61  E-value: 1.26e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKF 111
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEPSRLYSLYEREIRELRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  112 KAEHDQLLLNYAKKesdlsgaqiklreyeaalnskdaalataLGDKKSLEGDLEDLKdqiaqleaslsaakKQLADETLL 191
Cdd:pfam00038  81 RLAAEDFRQKYEDE----------------------------LNLRQSAEADIVGLR--------------KDLDEATLA 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  192 KVDLENRCQSLTEDLEFRKNMYEEEINETRRKH--ETRLVEVDSGRQIEyeykLAQALHEMREQHDAQVRLYKEELEQTY 269
Cdd:pfam00038 119 RVDLEMKIESLKEELAFLKKNHEEEVRELQSQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAEKNREEAEEWY 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  270 HAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAE 349
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQQ 274
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 188219589  350 IRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEER 388
Cdd:pfam00038 275 IRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
440-544 1.29e-23

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 425951 [Multi-domain]  Cd Length: 103  Bit Score: 95.56  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  440 TGNVCIEEIDVDG-----KFIRLKNTSEQDQPMGGWEMIRKIGDTsvsYKYTSRYVLKAGQTVTVWaANAGVTASPPTDL 514
Cdd:pfam00932   4 TGDVVISEVVYDGsggndEFIELYNTGDKAVDLSGWKLSDASGGT---FTFPNGTTLAPGQTVVVW-TGGGAGYWGPLNA 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 188219589  515 IWKNQNSWgtgedvkVILKNSQGEEVAQRS 544
Cdd:pfam00932  80 VWNNGGDA-------VALYDANGELVDSVG 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
24-350 1.60e-15

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: 80.10  E-value: 1.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589    24 SPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvrgreltglkalyetELADARRALDDTARERAK 103
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE---------------ELEQLRKELEELSRQISA 730
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   104 LQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKK 183
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   184 QLADETLLKVDLENRCqsltEDLEFRKNMYEEEINETRRKHETRLVEV-----------DSGRQIEYEYKLAQALHEMRE 252
Cdd:TIGR02168  811 ELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIEELSEDIeslaaeieeleELIEELESELEALLNERASLE 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   253 QHDAQVRLYKEELEQTYH----AKLENARLSSEMNTStVNSAREELMESRMRIESLSSQLSNLQKESracLERIQELEDM 328
Cdd:TIGR02168  887 EALALLRSELEELSEELRelesKRSELRRELEELREK-LAQLELRLEGLEVRIDNLQERLSEEYSLT---LEEAEALENK 962
                          330       340
                   ....*....|....*....|..
gi 188219589   329 LAKERDNSRRMLSDREREMAEI 350
Cdd:TIGR02168  963 IEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
24-367 1.47e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 64.35  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   24 SPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVtereevrgRELTGLKALYETELADARRALDDTARERAK 103
Cdd:COG1196   656 SRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNEL--------RSLEDLLEELRRQLEELERQLEELKRELAA 727
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  104 LQIELGKFKA-------EHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEA 176
Cdd:COG1196   728 LEEELEQLQSrleeleeELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAER 807
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  177 SLSAAKKQLADETLLKVDLENRCQSLTE---DLEFRKNMYEEEINET---RRKHETRLVEVDSGRQiEYEYKLAQALHEm 250
Cdd:COG1196   808 RLDALERELESLEQRRERLEQEIEELEEeieELEEKLDELEEELEELekeLEELKEELEELEAEKE-ELEDELKELEEE- 885
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  251 REQHDAQVRLYKEELEQtyhAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLA 330
Cdd:COG1196   886 KEELEEELRELESELAE---LKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEALG 962
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 188219589  331 KERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDV 367
Cdd:COG1196   963 PVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEV 999
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
29-377 2.34e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  29 SRLQEKEELRELNDRLAVYIDKVRSLETENSalqlqvTEREEVRGReltglkalyeteLADARRALDDTARERAKLQIEL 108
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETE------REREELAEE------------VRDLRERLEELEEERDDLLAEA 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 109 GKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLAD- 187
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDr 382
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 188 -----------ETLLK------VDLENrCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEM 250
Cdd:PRK02224 383 reeieeleeeiEELRErfgdapVDLGN-AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPV 461
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 251 REQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSArEELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLA 330
Cdd:PRK02224 462 EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 188219589 331 KERDNSrrmlSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISA 377
Cdd:PRK02224 541 ELRERA----AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
32-388 1.26e-100

Intermediate filament protein;


Pssm-ID: 425436 [Multi-domain]  Cd Length: 313  Bit Score: 307.61  E-value: 1.26e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKF 111
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEPSRLYSLYEREIRELRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  112 KAEHDQLLLNYAKKesdlsgaqiklreyeaalnskdaalataLGDKKSLEGDLEDLKdqiaqleaslsaakKQLADETLL 191
Cdd:pfam00038  81 RLAAEDFRQKYEDE----------------------------LNLRQSAEADIVGLR--------------KDLDEATLA 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  192 KVDLENRCQSLTEDLEFRKNMYEEEINETRRKH--ETRLVEVDSGRQIEyeykLAQALHEMREQHDAQVRLYKEELEQTY 269
Cdd:pfam00038 119 RVDLEMKIESLKEELAFLKKNHEEEVRELQSQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAEKNREEAEEWY 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  270 HAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAE 349
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQQ 274
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 188219589  350 IRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEER 388
Cdd:pfam00038 275 IRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
440-544 1.29e-23

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 425951 [Multi-domain]  Cd Length: 103  Bit Score: 95.56  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  440 TGNVCIEEIDVDG-----KFIRLKNTSEQDQPMGGWEMIRKIGDTsvsYKYTSRYVLKAGQTVTVWaANAGVTASPPTDL 514
Cdd:pfam00932   4 TGDVVISEVVYDGsggndEFIELYNTGDKAVDLSGWKLSDASGGT---FTFPNGTTLAPGQTVVVW-TGGGAGYWGPLNA 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 188219589  515 IWKNQNSWgtgedvkVILKNSQGEEVAQRS 544
Cdd:pfam00932  80 VWNNGGDA-------VALYDANGELVDSVG 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
24-350 1.60e-15

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: 80.10  E-value: 1.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589    24 SPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvrgreltglkalyetELADARRALDDTARERAK 103
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE---------------ELEQLRKELEELSRQISA 730
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   104 LQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKK 183
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   184 QLADETLLKVDLENRCqsltEDLEFRKNMYEEEINETRRKHETRLVEV-----------DSGRQIEYEYKLAQALHEMRE 252
Cdd:TIGR02168  811 ELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIEELSEDIeslaaeieeleELIEELESELEALLNERASLE 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   253 QHDAQVRLYKEELEQTYH----AKLENARLSSEMNTStVNSAREELMESRMRIESLSSQLSNLQKESracLERIQELEDM 328
Cdd:TIGR02168  887 EALALLRSELEELSEELRelesKRSELRRELEELREK-LAQLELRLEGLEVRIDNLQERLSEEYSLT---LEEAEALENK 962
                          330       340
                   ....*....|....*....|..
gi 188219589   329 LAKERDNSRRMLSDREREMAEI 350
Cdd:TIGR02168  963 IEDDEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-361 1.15e-10

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: 64.69  E-value: 1.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589    34 KEELRELndRLAVYIDKVRSLETENSALQLQVTEREEVRgRELTGLKALYETELADARRALDDTARERAKLQIELGKFKA 113
Cdd:TIGR02168  219 KAELREL--ELALLVLRLEELREELEELQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   114 EhdqlllnYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKV 193
Cdd:TIGR02168  296 E-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   194 DLENRCQSLTEDLEFRKNmyeeeinetrrkhetrlvevdsgrqieyeyKLAQALHEMrEQHDAQVRLYKEELEQtyhAKL 273
Cdd:TIGR02168  369 ELESRLEELEEQLETLRS------------------------------KVAQLELQI-ASLNNEIERLEARLER---LED 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   274 ENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKEsracLERIQELEDMLAKERDNSRRMLSDREREMAEIR-- 351
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQar 490
                          330
                   ....*....|....
gi 188219589   352 ----DQMQQQLSDY 361
Cdd:TIGR02168  491 ldslERLQENLEGF 504
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
24-367 1.47e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 64.35  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   24 SPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVtereevrgRELTGLKALYETELADARRALDDTARERAK 103
Cdd:COG1196   656 SRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNEL--------RSLEDLLEELRRQLEELERQLEELKRELAA 727
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  104 LQIELGKFKA-------EHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEA 176
Cdd:COG1196   728 LEEELEQLQSrleeleeELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAER 807
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  177 SLSAAKKQLADETLLKVDLENRCQSLTE---DLEFRKNMYEEEINET---RRKHETRLVEVDSGRQiEYEYKLAQALHEm 250
Cdd:COG1196   808 RLDALERELESLEQRRERLEQEIEELEEeieELEEKLDELEEELEELekeLEELKEELEELEAEKE-ELEDELKELEEE- 885
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  251 REQHDAQVRLYKEELEQtyhAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLA 330
Cdd:COG1196   886 KEELEEELRELESELAE---LKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEALG 962
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 188219589  331 KERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDV 367
Cdd:COG1196   963 PVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEV 999
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
34-327 2.20e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.50  E-value: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   34 KEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALyETELADARRALDDTARERAKLQIELGKFKA 113
Cdd:COG1196   750 EEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEEL-EEELEEAERRLDALERELESLEQRRERLEQ 828
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  114 EHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLAdetllkv 193
Cdd:COG1196   829 EIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELA------- 901
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  194 dlenRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQhdaqvrlyKEELEQtyhakl 273
Cdd:COG1196   902 ----ELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEE--------IEALGP------ 963
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 188219589  274 enarlssemntstVNS-AREELMESRMRIESLSSQLSNLQKESRACLERIQELED 327
Cdd:COG1196   964 -------------VNLrAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDK 1005
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
71-387 1.67e-08

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: 57.77  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589    71 VRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLlnyakkeSDLSGAQIKLREYEAALNskdaal 150
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS-------QELSDASRKIGEIEKEIE------ 726
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   151 atalgdkkSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLefrkNMYEEEINETRRKhetrlve 230
Cdd:TIGR02169  727 --------QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEAR------- 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   231 vDSGRQIEYEYKLAQALHEMREQHDAQV---------RLYKEELEQTYHAKLENARLSSEMNtstVNSAREELMESRMRI 301
Cdd:TIGR02169  788 -LSHSRIPEIQAELSKLEEEVSRIEARLreieqklnrLTLEKEYLEKEIQELQEQRIDLKEQ---IKSIEKEIENLNGKK 863
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   302 ESLSSQLSNLQKESRaclERIQELEDmLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKL 381
Cdd:TIGR02169  864 EELEEELEELEAALR---DLESRLGD-LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939

                   ....*.
gi 188219589   382 LEGEEE 387
Cdd:TIGR02169  940 KGEDEE 945
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
96-389 1.75e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.42  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   96 DTARERAKLQIELgkFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLE 175
Cdd:COG1196   210 EKAERYQELKAEL--RELELALLLAKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQ 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  176 ASLSAAKKQLADETLLKVDLENRCqsltEDLEFRKNMYEEEINETRRKHETR--LVEVDSGRQIEYEYKLAQaLHEMREQ 253
Cdd:COG1196   288 EELLELKEEIEELEGEISLLRERL----EELENELEELEERLEELKEKIEALkeELEERETLLEELEQLLAE-LEEAKEE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  254 HDAQVRLYKEELEqtyhaklenarlssemntSTVNSAREELMESRMRIESLSSQLSNLQKEsraclerIQELEDmlakER 333
Cdd:COG1196   363 LEEKLSALLEELE------------------ELFEALREELAELEAELAEIRNELEELKRE-------IESLEE----RL 413
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 188219589  334 DNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERL 389
Cdd:COG1196   414 ERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELEREL 469
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
34-354 5.91e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 55.88  E-value: 5.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   34 KEELRELndRLAVYIDKVRSLETENSALQLQVTEREEvRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKA 113
Cdd:COG1196   219 KAELREL--ELALLLAKLKELRKELEELEEELSRLEE-ELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKE 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  114 EHDQLLLN-------YAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLA 186
Cdd:COG1196   296 EIEELEGEisllrerLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELE 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  187 DETLlkvdlenRCQSLTEDLEFRKNMYEEEINETRrkhetrlvevdsgRQIEYEYKLAQALHEMREQHDAQVRLYKEELE 266
Cdd:COG1196   376 ELFE-------ALREELAELEAELAEIRNELEELK-------------REIESLEERLERLSERLEDLKEELKELEAELE 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  267 QTyHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDMlAKERDNSRRMLSDRERE 346
Cdd:COG1196   436 EL-QTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAE-QRASQGVRAVLEALESG 513

                  ....*...
gi 188219589  347 MAEIRDQM 354
Cdd:COG1196   514 LPGVYGPV 521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
111-364 7.76e-08

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: 55.45  E-value: 7.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   111 FKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETL 190
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   191 LKVDLENRCQSL---TEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEykLAQALHEMREQHDAQVRLYKEELEQ 267
Cdd:TIGR02168  317 QLEELEAQLEELeskLDELAEELAELEEKLEELKEELESLEAELEELEAELEE--LESRLEELEEQLETLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   268 TYHAKLENARLSSEMNTSTVNSAREelmesRMRIESLSSQLSNLQ-KESRACLERIQELEDMLAKERDNSRRMLSDRERE 346
Cdd:TIGR02168  395 IASLNNEIERLEARLERLEDRRERL-----QQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREE 469
                          250
                   ....*....|....*...
gi 188219589   347 MAEIRDQMQQQLSDYEQL 364
Cdd:TIGR02168  470 LEEAEQALDAAERELAQL 487
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
81-390 7.95e-08

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: 55.46  E-value: 7.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589    81 ALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSgAQIKLREYEAALnskdaalatalgdkksL 160
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYE----------------L 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   161 EGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFR----KNMYEEEINETRRKHETRLVEVDSGRQ 236
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASLER 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   237 IEYEYKL-AQALHEMREQHDAQVRLYKEELEQtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKES 315
Cdd:TIGR02169  309 SIAEKEReLEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219589   316 RACLERIQELEDMLAKERDNSRRMLSDRER---EMAEIRDQMQQQLSDYEQLLDVKLALDMEISAyrklLEGEEERLK 390
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDRLQEELQRlseELADLNAAIAGIEAKINELEEEKEDKALEIKK----QEWKLEQLA 461
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
32-214 8.33e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 55.49  E-value: 8.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKF 111
Cdd:COG1196   323 ERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEEL 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  112 KAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLL 191
Cdd:COG1196   403 KREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKE 482
                         170       180
                  ....*....|....*....|...
gi 188219589  192 KVDLENRCQSLTEDLEFRKNMYE 214
Cdd:COG1196   483 LSSLEARLDRLEAEQRASQGVRA 505
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
26-326 1.92e-07

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: 54.30  E-value: 1.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589    26 TRLSRLQ----EKEELRELNDRLAVY-----IDKVRSLETENSALQLQVTEREEvrgrELTGLKALYE---TELADARRA 93
Cdd:TIGR02169  198 QQLERLRrereKAERYQALLKEKREYegyelLKEKEALERQKEAIERQLASLEE----ELEKLTEEISeleKRLEEIEQL 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589    94 LDDTAR--------ERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAalatalgDKKSLEGDLE 165
Cdd:TIGR02169  274 LEELNKkikdlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-------EIEELEREIE 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   166 DLKDQIAQLEASLSAAKKQLADetllkvdLENRCQSLTEDLE--FRKNM-YEEEINETRRKHEtrlvevDSGRQIEYEYK 242
Cdd:TIGR02169  347 EERKRRDKLTEEYAELKEELED-------LRAELEEVDKEFAetRDELKdYREKLEKLKREIN------ELKRELDRLQE 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   243 LAQALHEMREQHDAQVRLYKEELEQtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERI 322
Cdd:TIGR02169  414 ELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492

                   ....
gi 188219589   323 QELE 326
Cdd:TIGR02169  493 AEAE 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
34-328 3.00e-07

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: 53.53  E-value: 3.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589    34 KEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKAL------YETELADARRALDDTARERAKLQIE 107
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlssLEQEIENVKSELKELEARIEELEED 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   108 LGKFKAEHDQLLLNYAKKESDLSGAQIK------------LREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLE 175
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSRIPEIQAELSkleeevsriearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   176 ASLSAAKKQLAD------ETLLKV-DLENRCQSLTEDLEFRKNMYEE------EINETRRKHETRLVEVDSGRQIEyEYK 242
Cdd:TIGR02169  854 KEIENLNGKKEEleeeleELEAALrDLESRLGDLKKERDELEAQLRElerkieELEAQIEKKRKRLSELKAKLEAL-EEE 932
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   243 LAQALHEMRE-QHDAQVRLYKEELEQTYHAKLENARLSSEMNtstvNSAREELMESRMRIESLSSQLSNLQKESRACLER 321
Cdd:TIGR02169  933 LSEIEDPKGEdEEIPEEELSLEDVQAELQRVEEEIRALEPVN----MLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008

                   ....*..
gi 188219589   322 IQELEDM 328
Cdd:TIGR02169 1009 IEEYEKK 1015
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
29-377 2.34e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  29 SRLQEKEELRELNDRLAVYIDKVRSLETENSalqlqvTEREEVRGReltglkalyeteLADARRALDDTARERAKLQIEL 108
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETE------REREELAEE------------VRDLRERLEELEEERDDLLAEA 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 109 GKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLAD- 187
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDr 382
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 188 -----------ETLLK------VDLENrCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEM 250
Cdd:PRK02224 383 reeieeleeeiEELRErfgdapVDLGN-AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPV 461
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 251 REQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSArEELMESRMRIESLSSQLSNLQKESRACLERIQELEDMLA 330
Cdd:PRK02224 462 EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 188219589 331 KERDNSrrmlSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISA 377
Cdd:PRK02224 541 ELRERA----AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
29-390 2.38e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  29 SRLQE-KEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYEtelaDARRALDDTARERAKLQIE 107
Cdd:PRK03918 338 ERLEElKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE----ELEKAKEEIEEEISKITAR 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 108 LGKFKAEHDQLL-----LNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAK 182
Cdd:PRK03918 414 IGELKKEIKELKkaieeLKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 183 KQLADETLLK--VDLENRCQSLT-EDLEFRKNMYEEEINETRR-KHETRLVEVDSGRQIEYEYKLAQALHEMREqhdaqv 258
Cdd:PRK03918 494 ELIKLKELAEqlKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlKGEIKSLKKELEKLEELKKKLAELEKKLDE------ 567
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 259 rlyKEELEQTYHAKLENARLSSEmntstvnsarEELMESRMRIESLSSQLSNLqKESRACLERIQELEDMLAKERDNSRR 338
Cdd:PRK03918 568 ---LEEELAELLKELEELGFESV----------EELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 188219589 339 MLSDREREMAEIRDQMQQQLS-----DYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRRE 690
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
33-387 2.57e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   33 EKEELRELNDRLAVYIDKVRSLETENSALQLQVTE----REEVRG--RELTGLKALYETELADARRALDDT-------AR 99
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekiAEELKGkeQELIFLLQAREKEIHDLEIQLTAIktseehyLK 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  100 ERAKLQIELGKFK-------AEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIA 172
Cdd:pfam05483 472 EVEDLKTELEKEKlknieltAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE 551
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  173 QLEASLsaakKQLADETLLKVD----------------------LENRCQSLTEDLEfRKNMYEEEINETRRKHETRlVE 230
Cdd:pfam05483 552 SVREEF----IQKGDEVKCKLDkseenarsieyevlkkekqmkiLENKCNNLKKQIE-NKNKNIEELHQENKALKKK-GS 625
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  231 VDSGRQIEYEYKLAQALHEMreqhdAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSN 310
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELEL-----ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH 700
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219589  311 LQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYE-QLLDVKLALDMEISAYRKLLEGEEE 387
Cdd:pfam05483 701 KIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKaELLSLKKQLEIEKEEKEKLKMEAKE 778
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
32-389 4.16e-05

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 46.68  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRE------LTGLKALYETELADARRALDDTARERAKLQ 105
Cdd:COG0419  414 ELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGekcpvcGQELPEEHEKELLELYELELEELEEELSRE 493
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 106 IELGKFKAEHDQLL--LNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKK 183
Cdd:COG0419  494 KEEAELREEIEELEkeLRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLEDRLQELKE 573
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 184 QLADETLL--KVDLENRCQSLTEDLEFRKNMYEE---EINETRRKHETRLVEVDSGRQIEyEYKLAQALHEMREQHDAQV 258
Cdd:COG0419  574 LLEELRLLrtRKEELEELRERLKELKKKLKELEErlsQLEELLQSLELSEAENELEEAEE-ELESELEKLNLQAELEELL 652
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 259 RLYKEELEQTYHAKLE--NARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKEsracLERIQELEDMLAKERDNS 336
Cdd:COG0419  653 QAALEELEEKVEELEAeiRRELQRIENEEQLEEKLEELEQLEEELEQLREELEELLKK----LGEIEQLIEELESRKAEL 728
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 188219589 337 RRMLSDREremaeirdQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERL 389
Cdd:COG0419  729 EELKKELE--------KLEKALELLEELREKLGKAGLRADILRNLLAQIEAEA 773
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
121-206 7.72e-05

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 45.10  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  121 NYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQL-EASLSAAKKQLADETLLKVDLENRC 199
Cdd:TIGR04320 262 KLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAALANAEARLAKAKEAL 341

                  ....*..
gi 188219589  200 QSLTEDL 206
Cdd:TIGR04320 342 ANLNADL 348
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
34-360 1.54e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  34 KEELRELNDRLAVYIDKVRSLETENSALQLQV----TEREEVRGRELTGLKALYE-TELADARRALDDTARERAK-LQIE 107
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARReeleDRDEELRDRLEECRVAAQAhNEEAESLREDADDLEERAEeLREE 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 108 LGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLAD 187
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 188 -ETLLK----------------VDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEM 250
Cdd:PRK02224 445 aEALLEagkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEEL 524
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 251 REQHDAQVRLYKEELEQTYHAKLEnarLSSEMNTstvnsAREELMESRMRIESLSSQLSNLQKESRACLERIQELE---D 327
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAE---LEAEAEE-----KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirT 596
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 188219589 328 MLAKERDNSRRMLSDRER--EMAEIRDQMQQQLSD 360
Cdd:PRK02224 597 LLAAIADAEDEIERLREKreALAELNDERRERLAE 631
PRK11281 PRK11281
mechanosensitive channel MscK;
172-384 1.70e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  172 AQLEASLSAAKKQ---LADETLLKVDLENrcqslTEDLEFRKNMYEEEINETRRKhetrlvevdsgrqieyeykLAQALH 248
Cdd:PRK11281   39 ADVQAQLDALNKQkllEAEDKLVQQDLEQ-----TLALLDKIDRQKEETEQLKQQ-------------------LAQAPA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  249 EMREQHDAQVRLYKEELEQTY--HAKLENARLSSEMN--TSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQE 324
Cdd:PRK11281   95 KLRQAQAELEALKDDNDEETRetLSTLSLRQLESRLAqtLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  325 LEDMLAKERDNSRRMLSDReremaeiRDQMQQQLSdyeqlldvklALDMEISAYRKLLEG 384
Cdd:PRK11281  175 IRNLLKGGKVGGKALRPSQ-------RVLLQAEQA----------LLNAQNDLQRKSLEG 217
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
3-339 1.81e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 44.71  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589     3 TATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLavyidkvRSLETENSALQLQVTERE---EVRGRELTGL 79
Cdd:pfam15921  502 TASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHL-------RNVQTECEALKLQMAEKDkviEILRQQIENM 574
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589    80 KALyeteLADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESdlsgaqiKLREYEAA---LNSKDAALATALGD 156
Cdd:pfam15921  575 TQL----VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA-------KIRELEARvsdLELEKVKLVNAGSE 643
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   157 KKSLEGDLEDLKDQIA-QLEASLSAAKKQLADETLLKVDLENRCQSL---TEDLEFRKNMYEEEINETRRKHETrlVEVD 232
Cdd:pfam15921  644 RLRAVKDIKQERDQLLnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMettTNKLKMQLKSAQSELEQTRNTLKS--MEGS 721
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   233 SGRQIEYEYKLAQALHEMREQHDA---QVRLYKEEL----EQTYHAKLENARLSSEMNT--STVNSAREELMESRMRIES 303
Cdd:pfam15921  722 DGHAMKVAMGMQKQITAKRGQIDAlqsKIQFLEEAMtnanKEKHFLKEEKNKLSQELSTvaTEKNKMAGELEVLRSQERR 801
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 188219589   304 LSSQLSNLQKESRACLERIQELEDMLAKERDNSRRM 339
Cdd:pfam15921  802 LKEKVANMEVALDKASLQFAECQDIIQRQEQESVRL 837
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
116-390 4.38e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 43.21  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 116 DQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDL 195
Cdd:COG0419  203 DLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERL 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 196 ENRCQSLTEDLEFRKNMYEEEINEtrrkhetrlvevdsgrqieyEYKLAQALHEMREQHDAQVRLykEELEQTYHAKLEN 275
Cdd:COG0419  283 LEELEEKIERLEELEREIEELEEE--------------------LEGLRALLEELEELLEKLKSL--EERLEKLEEKLEK 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 276 ARLSSEMNTSTVNSAREELmesRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERdNSRRMLSDREREMAEIRDQMQ 355
Cdd:COG0419  341 LESELEELAEEKNELAKLL---EERLKELEERLEELEKELEKALERLKQLEEAIQELK-EELAELSAALEEIQEELEELE 416
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 188219589 356 QQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:COG0419  417 KELEELERELEELEEEIKKLEEQINQLESKELMIA 451
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
164-391 4.47e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.29  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   164 LEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSgrqieyeyKL 243
Cdd:pfam12128  246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA--------AV 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   244 AQALHEMrEQHDAQVRLYKEELEQTYHAKLENA-RLSSEMNtsTVNSAREELMESRMRIESLSSQLSnlQKESRACLERI 322
Cdd:pfam12128  318 AKDRSEL-EALEDQHGAFLDADIETAAADQEQLpSWQSELE--NLEERLKALTGKHQDVTAKYNRRR--SKIKEQNNRDI 392
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188219589   323 QELEDMLAKERDnsrrmlsDREREMAEIRDQMQQQLSDYEQLLDVKLaLDMEISAYRKLLEGEEERLKL 391
Cdd:pfam12128  393 AGIKDKLAKIRE-------ARDRQLAVAEDDLQALESELREQLEAGK-LEFNEEEYRLKSRLGELKLRL 453
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
160-382 5.04e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.29  E-value: 5.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   160 LEGDLEDLKDQIAQLEASLSAAKKQL----ADETLLKVDLEN---RCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVD 232
Cdd:pfam12128  609 AEEALQSAREKQAAAEEQLVQANGELekasREETFARTALKNarlDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLE 688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   233 sGRQIEYEYKLAQALHEMREQ---HDAQVRLYKEELEQTYHAKLenARLSSEMNTSTVNSARE--ELMESRMR------- 300
Cdd:pfam12128  689 -AQLKQLDKKHQAWLEEQKEQkreARTEKQAYWQVVEGALDAQL--ALLKAAIAARRSGAKAElkALETWYKRdlaslgv 765
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   301 -----------IESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEqlLDVKl 369
Cdd:pfam12128  766 dpdviaklkreIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTK--LRRA- 842
                          250
                   ....*....|...
gi 188219589   370 ALDMEISAYRKLL 382
Cdd:pfam12128  843 KLEMERKASEKQQ 855
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
32-390 6.22e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 42.83  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  32 QEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREevrgRELTGLKALYETELADARRALDDTARERAKLQIELGKF 111
Cdd:COG0419  326 SLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERL----KELEERLEELEKELEKALERLKQLEEAIQELKEELAEL 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 112 KAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEgdledlkdQIAQLEASLSAAKKQLADETLL 191
Cdd:COG0419  402 SAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIA--------ELAGAGEKCPVCGQELPEEHEK 473
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 192 KVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEyKLAQALHEMREQHDA---QVRLYKEELEQT 268
Cdd:COG0419  474 ELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIELLE-LEEALKEELEEKLEKlenLLEELEELKEKL 552
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 269 YHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSqLSNLQKESRACLERIQELedMLAKERDNSRRMLSDREREMA 348
Cdd:COG0419  553 QLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELEE-LRERLKELKKKLKELEER--LSQLEELLQSLELSEAENELE 629
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 188219589 349 EIRdqmqQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:COG0419  630 EAE----EELESELEKLNLQAELEELLQAALEELEEKVEELE 667
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-331 9.95e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 9.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  33 EKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEvrgrELTGLKALYEtELADARRALDDTaRERAKLQIELGKFK 112
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE----RIEELKKEIE-ELEEKVKELKEL-KEKAEEYIKLSEFY 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 113 AEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLK------DQIAQLEASLSAAKKQLA 186
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLT 382
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 187 DETLLKVDLEnrcqslTEDLEFRKNMYEEEINE-TRRKHETRLVEVDSGRQIEyEYKLAQAL-----HEMREQHdaqvrl 260
Cdd:PRK03918 383 GLTPEKLEKE------LEELEKAKEEIEEEISKiTARIGELKKEIKELKKAIE-ELKKAKGKcpvcgRELTEEH------ 449
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219589 261 yKEELEQTYHAKLENarLSSEMntSTVNSAREELMESRMRIESLSSQLSNLQKEsRACLERIQELEDMLAK 331
Cdd:PRK03918 450 -RKELLEEYTAELKR--IEKEL--KEIEEKERKLRKELRELEKVLKKESELIKL-KELAEQLKELEEKLKK 514
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
78-346 1.29e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 41.25  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  78 GLKALYETELADARRaLDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDK 157
Cdd:COG4942   25 AVLAAAFSAAADDKQ-LKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 158 KSLEGDLEDLKDQIAQLeasLSAAKKQLADETLLKVDLENRCQSltedlEFRKNMYEEEINETRRKHETRLVEVDSGRQi 237
Cdd:COG4942  104 NALEVQEREQRRRLAEQ---LAALQRSGRNPPPALLVSPEDAQR-----SVRLAIYYGALNPARAERIDALKATLKQLA- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 238 eyeyKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTstvnsareELMESRMRIESLSSQLSNLQKE-SR 316
Cdd:COG4942  175 ----AVRAEIAAEQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNS--------ELSADQKKLEELRANESRLKNEiAS 242
                        250       260       270
                 ....*....|....*....|....*....|
gi 188219589 317 ACLERIQELEDMLAKERDNSRRMLSDRERE 346
Cdd:COG4942  243 AEAAAAKAREAAAAAEAAAARARAAEAKRT 272
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
235-399 1.68e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 235 RQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYH--AKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQ 312
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 313 KESRACLERIQELEDMLAKERDNSRRmLSDREREMAEIRDQMQQQL---SDYEQLLDVKLALDMEISAYRKLLEGEEERL 389
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
                        170
                 ....*....|
gi 188219589 390 KLSPSPSSRV 399
Cdd:PRK03918 331 KELEEKEERL 340
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
29-368 1.74e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 429718 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   29 SRLQEKeeLRELNDRLAVYIDKVRSLETENSALQlQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIEL 108
Cdd:pfam07888  34 NRLEEC--LQERAELLQAQEAANRQREKEKERYK-RDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  109 GKFKAEHDQLLLNYAKKESdlsgaqiKLREYEAALnskdAALATALGDKkslEGDLEDLKDQIAQLEASLsaaKKQLADE 188
Cdd:pfam07888 111 EELAEEKDALLAQRAESEA-------RIRELEEDI----KTLTQRVLER---ETELERMKERVKKAGAQR---KEEEAER 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  189 TLLKVDL---ENRCQSLTEDLEFRKNMYEEEINETRRKHE-----TRLVEVDSGRQIEYEYKLAQ--ALHEMREQHDAQV 258
Cdd:pfam07888 174 KQLQAKLqqtEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittlTQKLTTAHRKEAENEALLEElrSLQERLNASERKV 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  259 RLYKEELEQTY------HAKLENARLSSEMNTSTVNSAREELMESRM------------------RIESLSSQLsnLQKE 314
Cdd:pfam07888 254 EGLGEELSSMAaqrdrtQAELHQARLQAAQLTLQLADASLALREGRArwaqeretlqqsaeadkdRIEKLSAEL--QRLE 331
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 188219589  315 SRACLERIQ--ELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVK 368
Cdd:pfam07888 332 ERLQEERMEreKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
157-390 1.92e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.24  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  157 KKSLEGDLEDLKDQIAQLE--ASLSAAKKQLaDETLLKVDLENRCQSLtEDLEFRKNMYEEEINETRRKHETRLVEVDSg 234
Cdd:COG1196   195 LEELEKQLEKLERQAEKAEryQELKAELREL-ELALLLAKLKELRKEL-EELEEELSRLEEELEELQEELEEAEKEIEE- 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  235 rqieyeykLAQALHEMREQ-HDAQVRLYKEELE-QTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQ 312
Cdd:COG1196   272 --------LKSELEELREElEELQEELLELKEEiEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERE 343
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219589  313 KESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:COG1196   344 TLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLE 421
COG4913 COG4913
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown];
89-364 2.28e-03

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


Pssm-ID: 227250 [Multi-domain]  Cd Length: 1104  Bit Score: 41.16  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   89 DARRALDDTARER------AKLQIELGKFKAEHDQLLLnYAKKESDLSGAQIKLREYEAALNsKDAALATALGDKKSLEG 162
Cdd:COG4913   597 DDRRKLGDRSTYRlgstndAKVETLRETVKAMLSREDF-YMIKIMRQQGEYIKLQEQANALA-HIQALNFASIDLPSAQR 674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  163 DLEDLKDQIAQLEASLSA---AKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEY 239
Cdd:COG4913   675 QIAELQARLERLTHTQSDiaiAKAALDAAQTRQKVLERQYQQEVTECAGLKKDLKRAAMLSRKVHSIAKQGMTGALQALG 754
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  240 EyklAQALHEMREQHDAQVRLYKEELEQTYHAKL--ENARL-----------SSEMNTSTVNSA---------------- 290
Cdd:COG4913   755 A---AHFPQVAPEQHDDIVDIERIEHRRQLQKRIdaVNARLrrlreeiigrmSDAKKEDTAALSevgaelddipeylarl 831
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  291 ----REELME---------SRMRIESLSSQLSNLQKESRACLERIQELEDMLAKERDNSRRMLSDREREMAEIRDQMQQQ 357
Cdd:COG4913   832 qtltEDALPEflarfqellNRSSDDGVTQLLSHLDHERALIEERIEAINDSLRRVDFNSGRYLHIDIAKQPVPHDSMRTF 911

                  ....*..
gi 188219589  358 LSDYEQL 364
Cdd:COG4913   912 QQALRAL 918
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
167-390 2.57e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.85  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  167 LKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEdlEFRKNMYEEEINETRRKHEtrlvevdsGRQIEYEYKLAQA 246
Cdd:COG1196   170 YKERKEEAERKLERTEENLERLEDLLEELEKQLEKLER--QAEKAERYQELKAELRELE--------LALLLAKLKELRK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  247 LhemREQHDAQVRLYKEELEQTYhAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELE 326
Cdd:COG1196   240 E---LEELEEELSRLEEELEELQ-EELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELE 315
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219589  327 DMLAKERDNSRRMLSDREREMAEIRDQmQQQLSDYEQLLDVKLALDMEISAYRKLLEGEEERLK 390
Cdd:COG1196   316 NELEELEERLEELKEKIEALKEELEER-ETLLEELEQLLAELEEAKEELEEKLSALLEELEELF 378
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
85-389 3.89e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 40.25  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589   85 TELADARRALDDTARERAKLQIELGKFKAEHD------QLLLN-------YAKKESDLSGAQIKLREYEAALNSKDAALA 151
Cdd:COG3096   300 QQLAAEQYRHVDMSRELAELNGAEGDLEADYQaasdhlNLVQTalrqqekIERYQADLEELTIRLEEQNEVVEEANERQE 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  152 TALGDKKSLEGDLEDLKDQIAQLEASLSAAK----------------KQLADETLLKVD--------LENRCQSLTED-L 206
Cdd:COG3096   380 ENEARAEAAELEVDELKSQLADYQQALDVQQtraiqyqqaiaaleraKELCHLPDLTADsaeewletFQAKEEEATEKlL 459
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  207 EFRKNMYEEEINETRRKHETRLV-----EV------DSGRQIEYEYKLAQALhemrEQHDAQVRLYKEELEQTYHAKLEN 275
Cdd:COG3096   460 SLEQKMSMAQAAHSQFEQAYQLVvaiagELarseawDVARELLREGPDQRHL----AEQVQPLRMRLSELEQRLRQQQSA 535
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  276 ARLSSEMNTSTVNSAREELMES-----RMRIESLSSQLSNlQKESRACLEriQELEDMLAKERDNSRRM---------LS 341
Cdd:COG3096   536 ERLLADFCKRQGKNLDAEELEAlhqelEALIESLSDSVSN-AREQRMALR--QEQEQLQSRIQSLMQRApvwlaaqnaLE 612
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 188219589  342 DREREMAEIRDQMQQQLSDYEQLLDVKLALDME---ISAYRKLLEGEEERL 389
Cdd:COG3096   613 QLSEQSGEEFTDSQDVTEYMQQLLEREREATVErdeLGARKNALDEEIERL 663
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-331 4.41e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  21 TPLSPTRLSRLQEKEELR--ELNDRLAVYIDKVRSLETENSALQLQVTEREEVR------GRELT-----GLKALYETEL 87
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAkeEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTeehrkELLEEYTAEL 461
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  88 ADARRALDDTARERAKLQ---IELGKFKAEHDQLLLNYAK-----------KESDLSGAQIKLREYE------AALNSKD 147
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRkelRELEKVLKKESELIKLKELaeqlkeleeklKKYNLEELEKKAEEYEklkeklIKLKGEI 541
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 148 AALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKV-DLENRCQSL----TEDLEFRKNMYEEEINETRR 222
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELepfyNEYLELKDAEKELEREEKEL 621
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 223 KHETRLVEvdsgRQIEYEYKLAQALHEMREQHDAQVRLYKEEleqtYHAKLENARLSSEMNTSTVNSAREELMESRMRIE 302
Cdd:PRK03918 622 KKLEEELD----KAFEELAETEKRLEELRKELEELEKKYSEE----EYEELREEYLELSRELAGLRAELEELEKRREEIK 693
                        330       340
                 ....*....|....*....|....*....
gi 188219589 303 SLSSQLSNLQKESRACLERIQELEDMLAK 331
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEKLEKALER 722
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
29-356 6.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 6.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  29 SRLQEKEElRELNDRLAvyidkvrSLETENSALQLQVTEREEVRGREltglkalyetelADARRALDDTARERAKLQIEL 108
Cdd:PRK02224 194 AQIEEKEE-KDLHERLN-------GLESELAELDEEIERYEEQREQA------------RETRDEADEVLEEHEERREEL 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 109 GKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADE 188
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 189 TLLKVDLENRCQSLTE---DLEFRKNMYEEEINE----------TRRKHETRLVEVDSG-RQIEYEYKLAQALHEMREQH 254
Cdd:PRK02224 334 RVAAQAHNEEAESLREdadDLEERAEELREEAAEleseleeareAVEDRREEIEELEEEiEELRERFGDAPVDLGNAEDF 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589 255 DAQVRLYKEEL---EQTYHAKLENARLSSEMNTSTVNSAR--------------EELMESRMRIESLSSQLSNLQKESRA 317
Cdd:PRK02224 414 LEELREERDELrerEAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEE 493
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 188219589 318 CLERIQELEDM---------LAKERDNSRRMLSDREREMAEIRDQMQQ 356
Cdd:PRK02224 494 VEERLERAEDLveaedrierLEERREDLEELIAERRETIEEKRERAEE 541
HlyD pfam00529
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ...
104-268 6.75e-03

HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 38.94  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  104 LQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGdkksLEGDLEDLKDQIAQLEASLSAAKK 183
Cdd:pfam00529  49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDG----ATAQLRAAQAAVKAAQAQLAQAQI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  184 QLAD-ETLLKVDLENRCQSLTEDLEFRKNmyEEEINETRRKHETRLVEVDSGRQieyeyKLAQALHEMREQHDAQVRLYK 262
Cdd:pfam00529 125 DLARrRVLAPIGGISRESLVTAGALVAQA--QANLLATVAQLDQIYVQITQSAA-----ENQAEVRSELSGAQLQIAEAE 197

                  ....*.
gi 188219589  263 EELEQT 268
Cdd:pfam00529 198 AELKLA 203
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
168-387 8.12e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 428520 [Multi-domain]  Cd Length: 660  Bit Score: 38.94  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  168 KDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKheTRLVEVDSGRQIEYEYKLAQAl 247
Cdd:pfam05557  26 KRARIELERKASALARQLERESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK--KKNLEALNKKLNEKESQLADA- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219589  248 hemreqHDAQVRLYKEELEqtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLE---RIQE 324
Cdd:pfam05557 103 ------REVISCLKNELSE--LRRQIQRQELELSSTNSELEELQERLDLQKAKAQEAEQLRQNLEAQQSSLAEaeqRIKE 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219589  325 LEDMLAKERDNSRRMLSDRER--EMAEIRDQMQQQLSDYEQL---LDVKLALDMEISAYRKLLEGEEE 387
Cdd:pfam05557 175 LEFEIQSQEQDSEIVKNSKSElaRIPELERELERLREHNKHLnenIENKLLLKEEVEDLKRKLEREEG 242
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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